ID R7TCZ0_CAPTE Unreviewed; 929 AA.
AC R7TCZ0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=CAPTEDRAFT_224136 {ECO:0000313|EMBL:ELT91342.1};
OS Capitella teleta (Polychaete worm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC Sedentaria; Scolecida; Capitellidae; Capitella.
OX NCBI_TaxID=283909 {ECO:0000313|EMBL:ELT91342.1};
RN [1] {ECO:0000313|Proteomes:UP000014760}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=I ESC-2004 {ECO:0000313|Proteomes:UP000014760};
RA Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ELT91342.1, ECO:0000313|Proteomes:UP000014760}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=I ESC-2004 {ECO:0000313|EMBL:ELT91342.1,
RC ECO:0000313|Proteomes:UP000014760};
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
RN [3] {ECO:0000313|EnsemblMetazoa:CapteP224136}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
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DR EMBL; AMQN01002941; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KB310543; ELT91342.1; -; Genomic_DNA.
DR AlphaFoldDB; R7TCZ0; -.
DR STRING; 283909.R7TCZ0; -.
DR EnsemblMetazoa; CapteT224136; CapteP224136; CapteG224136.
DR HOGENOM; CLU_003705_2_0_1; -.
DR OMA; NIRWRRD; -.
DR Proteomes; UP000014760; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 2.60.40.1910; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF276; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|RuleBase:RU364040};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU364040};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU364040};
KW Reference proteome {ECO:0000313|Proteomes:UP000014760};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 52..244
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 291..493
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 596..894
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 20..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 358
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 357
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 361
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 380
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 444
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 929 AA; 106553 MW; 00C23FE469623985 CRC64;
MQSIIRMSLT SYIVSGLPGT PPCDGEVTGS STPLPTAQPD RPEDYLLPDD LVPVHYDIEL
RPDIYGSDAD DFAFTGYSVM HFWCRTATDT VVMHINYLSI DNSSIVVRSS SGSIIPVTQT
RHRPEFYFYD IVLGESLIVG ENYTISTNFS GPLSQNMAGM YWSSYPEEGQ TKYMIATQFE
APDARRAFPC MDEPALKATF NVTLHHQSHM TALTNMPEHE QIPGENNWVA TVFEKTSVVM
PTYLLAFAVA DYSFVNSTST GGLTEKFSRY WARHEYIDEG YADYVSQGYS DNVFDYFETY
FNHSYLLPKQ DQIAIPDFAA GAMENWGLIT YREERLLWNP QMSTLYEKQR MAGTVAHELL
HQWLGNVVTC AWWSDIWLQE GMARVHQHLA LAEAEPTWIS DELFQAQVLY RALSYDQMGS
AHPIHNPTIH TYRDPDSVFT VISYDKAGSF IRMIAETVLG LDSYERSMQV YVDRMQYGSA
VYGDLFKAWD DQALADGITL NKNLSQACLT WIMQSGYPVL NFARTSASQF LITQELFLIE
PERDLVEWYD TPYDYTWDIP IKYKSSVETE VKTEWFYREN NDKTINLDQD LGDGDWLLAN
VGHSGLFRVN YDLENWNALI GQLKTDHLVN IITIIMSIST YLLYWRLSIE IPLGIAEYLR
DEREFLPWYA LLQGWPHINR LFDSHSNYAA LRSFIRNITS DAYAELGWDE DVADELPTIY
LRTLILNTAC ENGHSDCQAM AQTLFRDWRA DPSALHSIIR PDVRESVYCS AIEAGSAEDW
EFLFEQYQES FSYFGAEPQR RADGLICTTQ AWLINRMLGL AANGDESIRS SDRTRFLTGI
SLSSYGHSLA WHYLNEHHTT MAASHVRSMT EALVEKFSTT YDLEKLDSFL ESFDEAAEDW
KDSLRTTVNA NIVWRMGNEE PLFNYLDVY
//
