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Database: UniProt
Entry: A0A1K1RYA5_9BACT
LinkDB: A0A1K1RYA5_9BACT
Original site: A0A1K1RYA5_9BACT 
ID   A0A1K1RYA5_9BACT        Unreviewed;       499 AA.
AC   A0A1K1RYA5;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE            EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN   ORFNames=SAMN05661012_04458 {ECO:0000313|EMBL:SFW77049.1};
OS   Chitinophaga sancti.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=1004 {ECO:0000313|EMBL:SFW77049.1, ECO:0000313|Proteomes:UP000183788};
RN   [1] {ECO:0000313|EMBL:SFW77049.1, ECO:0000313|Proteomes:UP000183788}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 784 {ECO:0000313|EMBL:SFW77049.1,
RC   ECO:0000313|Proteomes:UP000183788};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a
CC         peptide, amide or arylamide. Xaa is preferably Ala, but may be most
CC         amino acids including Pro (slow action). When a terminal hydrophobic
CC         residue is followed by a prolyl residue, the two may be released as
CC         an intact Xaa-Pro dipeptide.; EC=3.4.11.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000098};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M1 family.
CC       {ECO:0000256|ARBA:ARBA00010136}.
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DR   EMBL; FPIZ01000015; SFW77049.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1K1RYA5; -.
DR   STRING; 1004.SAMN05661012_04458; -.
DR   Proteomes; UP000183788; Unassembled WGS sequence.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09603; M1_APN_like; 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; IPR001930; Peptidase_M1.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR11533:SF174; ALANINE/ARGININE AMINOPEPTIDASE-RELATED; 1.
DR   PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 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|ARBA:ARBA00022438};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          14..177
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          230..414
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
SQ   SEQUENCE   499 AA;  56828 MW;  723CD76707C09AF6 CRC64;
     MFTGIRAQQV DVQSYAISLN LQDTTDQIKA SVSITLKYLQ STRRLKFDLA GMKVKEVFTG
     PKKYSFEQDA NALYINVDGK AGEQGIYTIT YGGTPKDGLI ISRNKYGHRT FFTDHWPDRA
     HQWFPCIDHP SDKAIFRISV AAPDHYTVVA NGVKKEEVNM GGHMKMTSWE EKVPLATKVM
     AFAAADFSVT HSGDVGNIPV DSYVFREDSL HQGYARATQI LPYFIQLVGP FQFEKLANIQ
     SKTIFGGMEN AGAIFYAEES PGHEKLESLL AHEIAHQWFG DAVTETDWRH LWLSEGFATY
     FTLLYMEHTY STDTLKASLK ADREKIIAFA KRRKTPVVDT TVHSNYMQLL NANSYERGGW
     VLHMLRRKIG DERFRAGIRQ YFRDYNGRNA STDDFRAEME RAGGENLKGF FTQWLYTAAI
     PELQVNLNYN ESTHTVKMEV IQNQLPLFEF PLEYTLDKTK PLQKLMIKDK VTTVMIPAAA
     KPAGIWLDPD INLLAEFAR
//
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