he structure 2ACE has in total 1 chains. Out of these 1 are sequence-unique. Currently viewing unique chains only.

[show all chains] [ Show 3D in Jmol]

Chain Display

Chain A (polymer 1) [help] [fasta] [sequence & DSSP] Description Chain Type UniProtKB reference Length scop domain assignment
[hide] [reference]

ACETYLCHOLINESTERASE polypeptide(L) P04058 537 residues d2acea_ Acetylcholinesterase: 527 residues

dssp secondary structure 37% helical (26 helices; 202 residues) [hide] [reference] 16% beta sheet (24 strands; 87 residues)

Simple Modular Architecture Research Tool

SMART MODE:
NORMALGENOMIC

Schultz et al. (1998) Proc. Natl. Acad. Sci. USA 95, 5857-5864 Letunic et al. (2008) Nucleic Acids Res , doi:10.1093/nar/gkn808

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WHAT'S NEW FEEDBACK

Domains within the query sequence of 537 residues

Mouse over domain / undefined region for more info; click on it to go to detailed annotation; right-click to save whole protein as PNG image Transmembrane segments as predicted by the TMHMM2 program ( ), coiled coil regions determined by the Coils2 program ( ), segments of low

compositional complexity determined by the SEG program ( position in AA.

). Intron positions are indicated with vertical lines showing the intron phase and exact

You can save the results of your search for easy access in the future by bookmarking this page. It will be available for one month.

The SMART diagram above represents a summary of the results shown below. Domains with scores less significant than established cutoffs are not shown in the diagram. Features are also not shown when two or more occupy the same piece of sequence; the priority for display is given by SMART > PFAM > PROSPERO repeats > Signal peptide > Transmembrane > Coiled coil > Unstructured regions > Low complexity. In either case, features not shown in the above diagram are marked as 'overlap' in the second table below. No domains, repeats, motifs or features could be predicted with confidence

These features and domains are not shown in the diagram, either because their scores are less significant than the required threshold, or because they overlap with some other source of annotation:

Name Begin End E-value Reason DM16 5 46 3.35e+03 threshold RNB 184 434 7.79e+04 threshold MHC_II_beta 220 279 5.93e+04 threshold POU 297 383 5.97e+02 threshold LY 353 393 2.45e+03 threshold
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PYRUVATE PHOSPHATE DIKINASE

Sequence / Structure Details

1DIK

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Redundancy Reduction and Sequence Clustering View the clustering results for 1DIK.

Sequence Display The structure 1DIK has in total 1 chains. Out of these 1 are sequence-unique. Currently viewing unique chains only. [show all chains] [ Show 3D in Jmol]

Chain Display

Chain A (polymer 1) [help] [fasta] [sequence & DSSP] Description Chain Type UniProtKB reference Length scop domain assignment PYRUVATE PHOSPHATE DIKINASE polypeptide(L) P22983 874 residues d1dika1 Pyruvate phosphate dikinase, C-terminal domain: 365 [hide] [reference] residues d1dika2 Pyruvate phosphate dikinase, central domain: 129 residues d1dika3 Pyruvate phosphate dikinase, N-terminal domain: 375 residues dssp secondary structure 46% helical (41 helices; 406 residues) [hide] [reference] 16% beta sheet (35 strands; 148 residues)
Simple Modular Architecture Research Tool
SMART MODE:
NORMALGENOMIC

Schultz et al. (1998) Proc. Natl. Acad. Sci. USA 95, 5857-5864 Letunic et al. (2008) Nucleic Acids Res , doi:10.1093/nar/gkn808

HOME SETUP FAQ ABOUT GLOSSARY

WHAT'S NEW FEEDBACK

Domains within the query sequence of 1091 residues

Mouse over domain / undefined region for more info; click on it to go to detailed annotation; right-click to save whole protein as PNG image Transmembrane segments as predicted by the TMHMM2 program ( compositional complexity determined by the SEG program ( position in AA. ), coiled coil regions determined by the Coils2 program ( ), segments of low

). Intron positions are indicated with vertical lines showing the intron phase and exact

You can save the results of your search for easy access in the future by bookmarking this page. It will be available for one month.

The SMART diagram above represents a summary of the results shown below. Domains with scores less significant than established cutoffs are not shown in the diagram. Features are also not shown when two or more occupy the same piece of sequence; the priority for display is given by SMART > PFAM > PROSPERO repeats > Signal peptide > Transmembrane > Coiled coil > Unstructured regions > Low complexity. In either case, features not shown in the above diagram are marked as 'overlap' in the second table below. Confidently predicted domains, repeats, motifs and features:

Name Begin End E-value low complexity 393 405 low complexity 710 732 low complexity 749 761 low complexity 862 871 These features and domains are not shown in the diagram, either because their scores are less significant than the required threshold, or because they overlap with some other source of annotation:

Name Begin End E-value Reason GuKc 14 191 2.72e+03 threshold Elp3 37 225 2.19e+03 threshold Aamy 45 341 1.29e+03 threshold 35EXOc 63 223 3.66e+03 threshold FCD 64 182 5.86e+04 threshold PMEI 76 221 6.07e+04 threshold BTB 103 195 1.18e+03 threshold SWAP 104 142 3.90e+03 threshold HPT 122 216 1.94e+03 threshold HMG 125 189 4.70e+02 threshold WGR 130 194 2.79e+04 threshold IPPc 138 374 1.73e+03 threshold SecA_DEAD 152 486 1.13e+05 threshold Aamy_C 215 290 4.18e+03 threshold DYNc 226 465 1.92e+03 threshold FCH 275 376 2.42e+02 threshold Malic_M 281 418 1.02e+04 threshold SecA_PP_bind 294 369 1.32e+05 threshold DM15 296 336 3.60e+03 threshold HTH_DTXR 304 385 7.11e+02 threshold SPEC 313 430 1.57e+03 threshold PepX_C 330 527 7.59e+04 threshold Pro_CA 331 464 1.07e+05 threshold DoH 350 473 3.69e+03 threshold TOPRIM 355 454 3.50e+03 threshold ETF 365 546 9.75e+03 threshold SAF 374 430 3.73e+04 threshold BMC 378 433 1.25e+05 threshold BAR 475 734 5.22e+03 threshold MR_MLE 522 674 7.66e+04 threshold

OmpH IL10 CTLH TFS2N HOX Tubulin_C H4 Flu_M1_C DSRM DM PHD RING LY

557 562 568 569 607 617 629 663 807 824 827 828 907

729 705 637 654 657 733 690 740 875 875 855 862 947

4.83e+04 threshold 1.18e+03 threshold 2.66e+03 threshold 1.11e+03 threshold 2.48e+03 threshold 1.08e+05 threshold 6.89e+02 threshold 4.14e+06 threshold 3.98e+02 threshold 1.31e+03 threshold 2.09e+03 threshold 1.72e+03 threshold 2.45e+03 threshold
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ADDA - Automatic Domain Decomposition Algorithm

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Description Identifier Length Created Sequence

ACETYLCHOLINESTERASE PRECURSOR (EC 3.1.1.7) (ACHE) ACES_TORCA Acccessionnumber P04058 586 Rsdb 491208=90 329750=40 this(854)=100 2000/04/12 Updated 2000-06-04 23:29:26 >854 MNLLVTSSLGVLLHLVVLCQADDHSELLVNTKSGKVMGTRVPVLSSHISAFLGIPFAEPPVGNMRFRRPEPKKPWSGVWN ASTYPNNCQQYVDEQFPGFSGSEMWNPNREMSEDCLYLNIWVPSPRPKSTTVMVWIYGGGFYSGSSTLDVYNGKYLAYTE EVVLVSLSYRVGAFGFLALHGSQEAPGNVGLLDQRMALQWVHDNIQFFGGDPKTVTIFGESAGGASVGMHILSPGSRDLF RRAILQSGSPNCPWASVSVAEGRRRAVELGRNLNCNLNSDEELIHCLREKKPQELIDVEWNVLPFDSIFRFSFVPVIDGE FFPTSLESMLNSGNFKKTQILLGVNKDEGSFFLLYGAPGFSKDSESKISREDFMSGVKLSVPHANDLGLDAVTLQYTDWM DDNNGIKNRDGLDDIVGDHNVICPLMHFVNKYTKFGNGTYLYFFNHRASNLVWPEWMGVIHGYEIEFVFGLPLVKELNYT AEEEALSRRIMHYWATFAKTGNPNEPHSQESKWPLFTTKEQKFIDLNTEPMKVHQRLRVQMCVFWNQFLPKLLNATACDG ELSSSGTSSSKGIIFYVLFSILYLIF References Database Accessionnumber Identifier swall P04058 ACES_TORCA Masked Regions There are no regions masked in this sequence. Repeats RADAR did not find repeats in sequence 854. GO assignments None

ADDA

Family # Domains # Sequences Range 3 12214 11063 12-556

Radar JNet Neighbourhood Near neighbourhood Neighbours nrdb100 in pairsdb.nrdb90 16 nrdb100 in pairsdb.nrdb40 78 Remote neighbourhood Neighbours BLASTP neighbourhood in pairsdb.pairsdb_40x40 for 329750 388 PSIBLAST neighbourhood in pairsdb.psiblast_40x40 for 329750 529 ( No BLASTP/PSIBLAST alignments available for this sequence. Please go to representative sequence 491208. )

Domains

Level Database Identifier Range Id Description nrdb ADDA 3 12-556 329750 na

ADDA - Automatic Domain Decomposition Algorithm

Home Sequence Family Browse Genomes Statistics Download Help

Contents of ADDA family 3 on level nrdb40

Summary Top of Form
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Members

Domains Sequences Residues Length

Bottom of Form 4002 Top of Form

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3659 1115705

279

Structural coverage Domains Sequences Chains

Bottom of Form 62 Top of Form

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63

468

Associated families Families

Bottom of Form 1359 Taxonomic spread Archaea Bacteria Eukaryota

(domains in nrdb) Top of Form Top of Form

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120

3396

3327

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Sequence G88555|G88555 P33894|STE13_YEAST P42658|DPP6_HUMAN Q40863|EMB8_PICGL P81429|EST1_SCHGA

Q28017|PAFA_BOVIN

P55577|Y4NA_RHISN P55627|Y4QF_RHISN Q10614|Y1288_MYCTU P53219|YG1L_YEAST Q50599|Y1834_MYCTU P0A5F5|Y1835_MYCTU P0A5F5|Y1835_MYCTU P64304|DHMA2_MYCBO P64304|DHMA2_MYCBO S44807|S44807 Q50658|Y2307_MYCTU P42840|YN60_YEAST P81171|Y174_RICPR P56161|ACES_ANOST P36196|ACES_CHICK P36196|ACES_CHICK Q01109|BAH_STRHY P39058|CEFG_CEPAC O67988|CLCD_RHOOP

Bottom of Form Description HYPOTHETICAL 42.9 KD PROTEIN B0464.7 IN 1-230 na CHROMOSOME III 671Saccharomyces DIPEPTIDYL AMINOPEPTIDASE A (EC 3.4.14.-) (DPAP A) 931 cerevisiae (YSCIV) DIPEPTIDYL PEPTIDASE IV LIKE PROTEIN (DIPEPTIDYL 601Homo sapiens AMINOPEPTIDASE- RELATED PROTEIN) 865 (DIPEPTIDYLPEPTIDASE VI) (DPPX-L/DPPX-S) 71-457 Picea glauca LATE EMBRYOGENESIS ABUNDANT PROTEIN EMB8 ESTERASE SG1 PRECURSOR (EC 3.1.1.1) 1-198 Schizaphis graminum (CARBOXYLIC-ESTER HYDROLASE) (FRAGMENT) PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE PRECURSOR (EC 3.1.1.47) (PAF ACETYLHYDROLASE) 1-444 Bos taurus (PAF 2-ACYLHYDROLASE) (LDL-ASSOCIATED PHOSPHOLIPASE A2) (LDL-PLA(2)) (2-ACETYL-1ALKYLGLYCEROPHOSPHOCHOLINE EST 401Rhizobium sp. NGR234 PROBABLE PEPTIDASE Y4NA (EC 3.4.21.-) 726 451Rhizobium sp. NGR234 PROBABLE PEPTIDASE Y4QF (EC 3.4.21.-) 754 161Mycobacterium HYPOTHETICAL 49.6 KD PROTEIN RV1288 456 tuberculosis Saccharomyces HYPOTHETICAL 38.5 KD PROTEIN IN ERV1-GLS2 1-342 cerevisiae INTERGENIC REGION Mycobacterium 1-288 HYPOTHETICAL 31.7 KD PROTEIN RV1834 tuberculosis Mycobacterium 1-628 HYPOTHETICAL 69.9 KD PROTEIN RV1835C tuberculosis 1-628 Mycobacterium bovis HYPOTHETICAL 69.9 KD PROTEIN RV1835C Mycobacterium 1-286 HYPOTHETICAL 32.2 KD PROTEIN RV1833C tuberculosis 1-286 Mycobacterium bovis HYPOTHETICAL 32.2 KD PROTEIN RV1833C 431HYPOTHETICAL 86.0 KD PROTEIN F44B9.1 IN na 690 CHROMOSOME III Mycobacterium 1-281 HYPOTHETICAL 29.7 KD PROTEIN RV2307C tuberculosis Saccharomyces HYPOTHETICAL 32.3 KD PROTEIN IN KRE1-HXT14 1-284 cerevisiae INTERGENIC REGION 351Rickettsia prowazekii PROBABLE PEPTIDASE RP174 (EC 3.4.21.-) 722 1-664 Anopheles stephensi ACETYLCHOLINESTERASE PRECURSOR (EC 3.1.1.7) 1-330 Gallus gallus ACETYLCHOLINESTERASE PRECURSOR (EC 3.1.1.7) 501Gallus gallus ACETYLCHOLINESTERASE PRECURSOR (EC 3.1.1.7) 767 Streptomyces 41-299 ACETYL-HYDROLASE (EC 3.1.1.-) hygroscopicus ACETYL-COA--DEACETYLCEPHALOSPORIN C Acremonium 1-444 ACETYLTRANSFERASE PRECURSOR (EC 2.3.1.-) chrysogenum (DCPC-ATF) 1-252 Rhodococcus opacus CARBOXYMETHYLENEBUTENOLIDASE (EC 3.1.1.45) Range Organism

(DIENELACTONE HYDROLASE) (DLH) P27120|DCOR1_XENLA O67802|DLHH_AQUAE Q43914|DLHH_AZOBR Q07505|DLHH_YEAST Q59093|ELH1_ACIAD Q49418|ESL2_MYCGE Q49421|ESL3_MYCGE P16854|EST1_CULPI Q51758|EST1_PSEFL P10095|EST5_DROMO P35502|ESTF_MYZPE P18773|EST_ACILW O51900|FES_ERWCH O51900|FES_ERWCH Q56855|FES_YEREN P16218|GUNH_CLOTM 1EDB|1EDB P80048|HYEP_PSEU1 Q06816|HYEP_STIAU P30809|JHEA_TRINI Q02104|LIP1_PSYIM P24484|LIP2_MORS1 P21309|LUXD1_PHOLE T28936|T28936 Q01470|PCD_ARTOX P22635|PCYA_PSEPA P52090|PHA1_PSELE P46541|PIP_BACCO P75092|PIP_MYCPN O64252|PRXH_BPMD2 Q59536|PTRB_MORLA 151526|AAA25978.1 P27100|TCBE_PSESQ P01267|THYG_BOVIN 581380|CAA41963.1 P03518|VGLM_RVFV 421460 1-231 1-231 1-273 1-266 1-268 1-273 1-540 1-218 1-38 1-564 1-303 1-190 191434 1-353 1-50 1-150 1-77 1-232 1-109 1-317 1-433 1-130 1-476 1-493 1-139 1-414 1-288 1-309 1-278 421690 1-231 1-238 21912769 1-220 1-130 Xenopus laevis Aquifex aeolicus ORNITHINE DECARBOXYLASE (EC 4.1.1.17) (ODC)

PUTATIVE CARBOXYMETHYLENEBUTENOLIDASE (EC 3.1.1.45) (DIENELACTONE HYDROLASE) (DLH) PUTATIVE CARBOXYMETHYLENEBUTENOLIDASE (EC Azospirillum brasilense 3.1.1.45) (DIENELACTONE HYDROLASE) (DLH) Saccharomyces PUTATIVE CARBOXYMETHYLENEBUTENOLIDASE (EC cerevisiae 3.1.1.45) (DIENELACTONE HYDROLASE) (DLH) 3-OXOADIPATE ENOL-LACTONASE I (EC 3.1.1.24) Acinetobacter (ENOL-LACTONE HYDROLASE I) (BETA-KETOADIPATE calcoaceticus ENOL-LACTONE HYDROLASE I) Mycoplasma genitalium PUTATIVE ESTERASE/LIPASE 2 (EC 3.1.-.-) Mycoplasma genitalium PUTATIVE ESTERASE/LIPASE 3 (EC 3.1.-.-) Culex pipiens ESTERASE B1 PRECURSOR (EC 3.1.1.1) Pseudomonas CARBOXYLESTERASE 1 (EC 3.1.1.1) (ESTERASE I) fluorescens Drosophila mojavensis ESTERASE 5 (EC 3.1.1.1) (FRAGMENT) ESTERASE FE4 PRECURSOR (EC 3.1.1.1) Myzus persicae (CARBOXYLIC-ESTER HYDROLASE) Acinetobacter lwoffii ESTERASE (EC 3.1.1.-) ENTEROCHELIN ESTERASE (FERRIC ENTEROBACTIN Erwinia chrysanthemi ESTERASE) ENTEROCHELIN ESTERASE (FERRIC ENTEROBACTIN Erwinia chrysanthemi ESTERASE) ENTEROCHELIN ESTERASE (FERRIC ENTEROBACTIN Yersinia enterocolitica ESTERASE) Clostridium ENDOGLUCANASE H PRECURSOR (EC 3.2.1.4) (EGH) thermocellum (ENDO-1,4-BETA-GLUCANASE) (CELLULASE H) Xanthobacter HALOALKANE DEHALOGENASE (EC 3.8.1.5) autotrophicus EPOXIDE HYDROLASE (EC 3.3.2.3) (EPOXIDE Pseudomonas sp. HYDRATASE) (FRAGMENTS) EPOXIDE HYDROLASE (EC 3.3.2.3) (EPOXIDE Stigmatella aurantiaca HYDRATASE) JUVENILE HORMONE ESTERASE, ISOFORM A (EC Trichoplusia ni 3.1.1.59) (JH ESTERASE) (JHE-A) (FRAGMENTS) Psychrobacter LIPASE 1 PRECURSOR (EC 3.1.1.3) immobilis (TRIACYLGLYCEROL LIPASE) Moraxella sp. LIPASE 2 (EC 3.1.1.3) (TRIACYLGLYCEROL LIPASE) Photobacterium ACYL TRANSFERASE (EC 2.3.1.-) (ACT) (MYRISTOYLleiognathi ACP-SPECIFIC THIOESTERASE) PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE na HOMOLOG (EC 3.1.1.47) PHENMEDIPHAM HYDROLASE (EC 3.1.1.-) Arthrobacter oxydans (PHENYLCARBAMATE HYDROLASE) Sphingomonas PROTOCATECHUATE 4,5-DIOXYGENASE ALPHA CHAIN paucimobilis (EC 1.13.11.8) (4,5-PCD) POLY(3-HYDROXYALKANOATE) DEPOLYMERASE C Paucimonas lemoignei PRECURSOR (EC 3.1.1.-) (PHA DEPOLYMERASE) (PHB DEPOLYMERASE) PROLINE IMINOPEPTIDASE (EC 3.4.11.5) (PROLYL Bacillus coagulans AMINOPEPTIDASE) Mycoplasma PUTATIVE PROLINE IMINOPEPTIDASE (EC 3.4.11.5) pneumoniae (PROLYL AMINOPEPTIDASE) Mycobacteriophage PUTATIVE NON-HEME HALOPEROXIDASE (EC 1.11.1.-) D29 Moraxella lacunata na Pseudomonas sp. P51 Bos taurus na Rift Valley fever virus PROTEASE II (EC 3.4.21.83) (OLIGOPEPTIDASE B) QUINOLONE SENSITIVITY PROTEIN CARBOXYMETHYLENEBUTENOLIDASE (EC 3.1.1.45) (DIENELACTONE HYDROLASE) (DLH) THYROGLOBULIN PRECURSOR PUTATIVE THYMIDYLATE SYNTHASE (EC 2.1.1.45) (TS) M POLYPROTEIN PRECURSOR [CONTAINS:

NONSTRUCTURAL PROTEIN NS-M; GLYCOPROTEINS G1 AND G2] P21084|VK05_VACCC P26223|XYNB_BUTFI P23553|XYNC_CALSA P51584|XYNY_CLOTM P10478|XYNZ_CLOTM Q57427|Y193_HAEIN Q44510|Y2406_ANASP P73883|Y249_SYNY3 P73879|Y264_SYNY3 146257|AAA23929.1 O14359|YB4E_SCHPO P38139|YB54_YEAST O02485|YDJ1_CAEEL O13912|YDW6_SCHPO O14249|YE63_SCHPO O14249|YE63_SCHPO O14249|YE63_SCHPO O14304|YE88_SCHPO 516608|AAA24151.1 P53208|YG19_YEAST P53264|YG2V_YEAST P53264|YG2V_YEAST P53324|YG5J_YEAST P38796|PPE1_YEAST S28284|S28284 E89453|E89453 P35866|Y967_CORGL P53925|YNL5_YEAST Q02891|YP95_YEAST P54549|YQJL_BACSU P54567|YQKD_BACSU 1-136 371635 1-266 7911077 1-270 1-287 1-250 1-251 Vaccinia virus (strain Copenhagen) Butyrivibrio fibrisolvens Caldicellulosiruptor saccharolyticus Clostridium thermocellum Clostridium thermocellum Haemophilus influenzae Nostoc sp. PCC 7120 PROTEIN K5 ENDO-1,4-BETA-XYLANASE B (EC 3.2.1.8) (XYLANASE B) (1,4-BETA- D-XYLAN XYLANOHYDROLASE B) ACETYL ESTERASE (EC 3.1.-.-) (ACETYLXYLOSIDASE) ENDO-1,4-BETA-XYLANASE Y PRECURSOR (EC 3.2.1.8) (XYLANASE Y) (XYLY) (1,4-BETA-D-XYLAN XYLANOHYDROLASE Y) ENDO-1,4-BETA-XYLANASE Z PRECURSOR (EC 3.2.1.8) (XYLANASE Z) (1,4-BETA-D-XYLAN XYLANOHYDROLASE Z) PUTATIVE ESTERASE/LIPASE HI0193 (EC 3.1.-.-) HYPOTHETICAL 28.7 KD PROTEIN IN ISIB 3'REGION (ORF 2)

Synechocystis sp. PCC HYPOTHETICAL 28.9 KD PROTEIN SLL0249 6803 Synechocystis sp. PCC 1-369 HYPOTHETICAL 41.0 KD PROTEIN SLR0264 6803 HYPOTHETICAL 49.1 KD PROTEIN IN GPT-CRL 1-433 na INTERGENIC REGION Schizosaccharomyces HYPOTHETICAL 27.4 KD PROTEIN C30D10.14 IN 1-249 pombe CHROMOSOME II Saccharomyces PUTATIVE PEROXISOMAL LIPASE IN CDC47-KTR3 1-375 cerevisiae INTERGENIC REGION (EC 3.1.1.-) HYPOTHETICAL 35.6 KD PROTEIN ZK1073.1 IN 1-325 Caenorhabditis elegans CHROMOSOME X 211Schizosaccharomyces HYPOTHETICAL 60.1 KD PROTEIN C23C11.06C IN 535 pombe CHROMOSOME I Schizosaccharomyces HYPOTHETICAL 48.7 KD PROTEIN C6G10.03C IN 1-70 pombe CHROMOSOME I Schizosaccharomyces HYPOTHETICAL 48.7 KD PROTEIN C6G10.03C IN 71-210 pombe CHROMOSOME I 211Schizosaccharomyces HYPOTHETICAL 48.7 KD PROTEIN C6G10.03C IN 428 pombe CHROMOSOME I Schizosaccharomyces HYPOTHETICAL 27.3 KD PROTEIN C9G1.08C IN 1-160 pombe CHROMOSOME I HYPOTHETICAL 26.7 KD PROTEIN IN MEND-MENB 1-180 na INTERGENIC REGION Saccharomyces HYPOTHETICAL 37.9 KD PROTEIN IN MSB2-UGA1 1-328 cerevisiae INTERGENIC REGION Saccharomyces HYPOTHETICAL 52.0 KD PROTEIN IN CLB6-SHY1 1-260 cerevisiae INTERGENIC REGION 261Saccharomyces HYPOTHETICAL 52.0 KD PROTEIN IN CLB6-SHY1 445 cerevisiae INTERGENIC REGION 131Saccharomyces HYPOTHETICAL 48.5 KD PROTEIN IN APL6-MES1 424 cerevisiae INTERGENIC REGION Saccharomyces HYPOTHETICAL 44.9 KD PROTEIN IN ERG7-NMD2 1-400 cerevisiae INTERGENIC REGION HYPOTHETICAL 88.4 KD PROTEIN B0464.7 IN 1-220 na CHROMOSOME III 531HYPOTHETICAL 94.6 KD PROTEIN F35H12.3 IN na 836 CHROMOSOME X 151Corynebacterium HYPOTHETICAL 45.7 KD PROTEIN IN LYSI 3'REGION 426 glutamicum (ORF2) 251Saccharomyces HYPOTHETICAL 74.0 KD PROTEIN IN MLS1-RPC19 460 cerevisiae INTERGENIC REGION Saccharomyces HYPOTHETICAL 51.7 KD PROTEIN IN SEC62-MSY1 1-456 cerevisiae INTERGENIC REGION HYPOTHETICAL 28.2 KD PROTEIN IN GLNQ-ANSR 1-253 Bacillus subtilis INTERGENIC REGION HYPOTHETICAL 34.6 KD PROTEIN IN GLNQ-ANSR 1-305 Bacillus subtilis INTERGENIC REGION

Q7M3K8|Q7M3K8_CAEEL 143185|AAC37015.1 Q18610|YYC5_CAEEL P95915|P95915_SULSO 1JJI-A|1JJI-A O29736|O29736_ARCFU O29582|O29582_ARCFU O30312|O30312_ARCFU

171371 1-120 1-375 271569 1-311 1-187

HYPOTHETICAL 41.4 KD PROTEIN K02A2.1 IN CHROMOSOME II HYPOTHETICAL 21.4 KD PROTEIN IN MEND-MENB na INTERGENIC REGION (ORF3) (ORF5) HYPOTHETICAL 42.3 KD PROTEIN C44C1.5 IN Caenorhabditis elegans CHROMOSOME X na Sulfolobus solfataricus ACYLAMINO-ACID-RELEASING ENZYME

Archaeoglobus fulgidus CARBOXYLESTERASE (ESTA) Archaeoglobus fulgidus HYPOTHETICAL 21.2 KD PROTEIN 2-HYDROXY-6-OXOHEPTA-2,4-DIENOATE HYDROLASE 1-238 Archaeoglobus fulgidus (TODF) 71-140 Archaeoglobus fulgidus CONSERVED HYPOTHETICAL PROTEIN

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CathDB: V3_4_0 (change)

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Domain

1ea5A00

CATH Domain: 1ea5A00

1ea5A00

PDB 1ea5, Chain A, Domain 0

CATH Code

Level Link Descr s iption Alpha Beta 3Layer( aba) Sandw ich Rossm ann fold Gen e3D

3.40

3.40.50

3.40.50.1820 3.40.50.1820.93 3.40.50.1820. 93.1 3.40.50.182 0.93.1.1 3.40.50.18 20.93.1.1.1 3.40.50. 1820.93.1. 1.1.1
Structure

Sequence

History

[top] Segment boundaries for domain 1ea5A00

Domai n 1ea5A 4 00

Start PDB Residue

Stop PDB Residue 535

Hide What is a Structural Neighbour?

The term "structural neighbour" is used here to describe two CATH domains that share a degree of structural similarity. The SSAP algorithm is used to calculate this similarity and works by generating a structure-based pairwise alignment of the two domains then scoring this alignment using a RMSD score which has been normalised by the length of the larger domain divided by the number of aligned residues (SIMAX).

Structural Neighbourhood (3 entries)

There are 3 matching structural neighberhood comparisons for CATH ID 3.40.50.1820.93.1.1.1.1 (SIMAX score < 5) [1] Displaying entries 1 to 3 (page 1 of 1) Matc SSA Match h P Leng Seque Overl RMS SIM Match Match Keywords Superfam Dept scor th nce Id ap D AX ily h e 2h7cB 87.4 00 9 3bixA0 87.4
Metabolic processCarboxylesterase activityLiver carboxylesterase 1Carboxylesterase [EC:3.1.1.1]Metabolic pathways Neuronal ion channel clusteringNeuroliginRattus norvegicusProtein

3.40.50.18 531 20 3.40.50.18 544

32

96

2.62 2.72

33

92

2.80 3.02

Matc SSA Match h P Leng Seque Overl RMS SIM Match Match Keywords Superfam Dept scor th nce Id ap D AX ily h e 0 0
heterotetramerizationProtein targeting EstAAspergillus niger

20 3.40.50.18 513 20 27 90 3.34 3.68

1ukcB 84.4 00 4 [1]

Displaying entries 1 to 3 (page 1 of 1)

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PDBs: 1ea5

Domain: 1ea5A00

Chains: 1ea5A

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CathDB: V3_4_0 (change)

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Domain

1kblA04

CATH Domain: 1kblA04

1kblA04

PDB 1kbl, Chain A, Domain 4

CATH Code Level Lin Descriptio ks n Alpha Beta Alpha-Beta Barrel TIM Barrel Phosphoeno lpyruvate- Gen binding e3D domains

3 3.20 3.20.20

3.20.20.60

3.20.20.60. 11

CATH Code

Level Lin Descriptio ks n

3.20.20.6 0.11.1 3.20.20. 60.11.1.1 3.20.2 0.60.11. 1.1.1 3.20 .20.60 .11.1. 1.1.1
Structure

Sequence

History
[top]

Segment boundaries for domain 1kblA04

Doma in 1kblA 2 01

Start PDB Residue

Stop PDB Residue 109

1kblA 199 01

243

1kblA 342 02 1kblA 510 02 1kblA 383 03 1kblA 532 04 1kblA 110 05 1kblA 244 06

382

531

507

873

198

341

Hide What is a Structural Neighbour?

The term "structural neighbour" is used here to describe two CATH domains that share a degree of structural similarity. The SSAP algorithm is used to calculate this similarity and works by generating a structure-based pairwise alignment of the two domains then scoring this alignment using a RMSD score which has been normalised by the length of the larger domain divided by the number of aligned residues (SIMAX).

Structural Neighbourhood (1 entries)

There are 1 matching structural neighberhood comparisons for CATH ID 3.20.20.60.11.1.1.1.1 (SIMAX score < 5) [1] Displaying entries 1 to 1 (page 1 of 1)

Matc SSA h Matc P Match Keywords Dept h scor h e 2olsA 82.8 04 2 [1] Displaying entries 1 to 1 (page 1 of 1)
Neisseria meningitidis serogroup BPhosphoenolpyruvate synthasePyruvate, water dikinase [EC:2.7.9.2]Pyruvate metabolismMetabolic pathways

Match Leng Seque Overl RMS SIM Superfa th nce Id ap D AX mily

3.20.20.6 312 0

23

84

3.34 3.94

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Related CATH Data Files

Domain: 1kblA04

See Also

Internal Links
PDBs: 1kbl

Chains: 1kblA

External Links

<="" a="" style="border-topstyle: none; borderright-style: none; border-bottom-style: none; border-left-

style: none; borderwidth: initial; bordercolor: initial; ">

<="" a="" style="bordertop-style: none; border-right-style: none; border-bottomstyle: none; borderleft-style: none; border-width: initial; border-color: initial; ">

University College London - Gower Street - London - WC1E 6BT - Telephone: +44 (0)20 7679 2000 - Copyright 1999-2008 UCL