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Database: UniProt
Entry: A0A3L8PXA6_9GAMM
LinkDB: A0A3L8PXA6_9GAMM
Original site: A0A3L8PXA6_9GAMM 
ID   A0A3L8PXA6_9GAMM        Unreviewed;       850 AA.
AC   A0A3L8PXA6;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, 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=D5018_08970 {ECO:0000313|EMBL:RLV60036.1};
OS   Parashewanella curva.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Parashewanella.
OX   NCBI_TaxID=2338552 {ECO:0000313|EMBL:RLV60036.1, ECO:0000313|Proteomes:UP000281474};
RN   [1] {ECO:0000313|EMBL:RLV60036.1, ECO:0000313|Proteomes:UP000281474}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C51 {ECO:0000313|EMBL:RLV60036.1,
RC   ECO:0000313|Proteomes:UP000281474};
RA   Wang G.;
RT   "Phylogeny of the Shewanellaceae, and recommendation for two new genera,
RT   Pseudoshewanella and Parashewanella.";
RL   Submitted (SEP-2018) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RLV60036.1}.
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DR   EMBL; QZEI01000022; RLV60036.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3L8PXA6; -.
DR   OrthoDB; 100605at2; -.
DR   Proteomes; UP000281474; 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:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09600; M1_APN; 1.
DR   Gene3D; 2.60.40.1840; -; 1.
DR   Gene3D; 3.30.2010.30; -; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   Gene3D; 1.25.50.10; Peptidase M1, alanyl aminopeptidase, C-terminal domain; 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; IPR038438; PepN_Ig-like_sf.
DR   InterPro; IPR001930; Peptidase_M1.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR012779; Peptidase_M1_pepN.
DR   InterPro; IPR024601; Peptidase_M1_pepN_C.
DR   InterPro; IPR037144; Peptidase_M1_pepN_C_sf.
DR   InterPro; IPR035414; Peptidase_M1_pepN_Ig-like.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   NCBIfam; TIGR02414; pepN_proteo; 1.
DR   PANTHER; PTHR46322; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR46322:SF1; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR   Pfam; PF11940; DUF3458; 1.
DR   Pfam; PF17432; DUF3458_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:0000313|EMBL:RLV60036.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000281474};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          20..184
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          224..434
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          442..532
FT                   /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT                   /evidence="ECO:0000259|Pfam:PF11940"
FT   DOMAIN          535..849
FT                   /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17432"
SQ   SEQUENCE   850 AA;  96270 MW;  9FEA840DD5FA690F CRC64;
     MSELQAKYLK DYQQSDFTIN HLSLDFQLNI PTTKVVAISQ VERQSKQATE LVLDGEDLDL
     VSVKVNSQPA SHQVKDKQLY IQADLDNFEL EIITHIKPAE NTALEGLYMS DGAYCTQCEA
     EGFRRITYYL DRPDVLAKFD VRVEADKTEF PFLLSNGNLI SSGDAVNGRH FATWQDPFPK
     PSYLFALVAG DFDLLEDQFT TRSGRDVKLQ VFVDKGNLHK AHHAMASLKK SMKWDEDRFD
     LEYDLDIYMI VAVDFFNMGA MENKGLNVFN TKYVLADKES ATDDDYHGIE SVIGHEYFHN
     WTGNRVTCRD WFQLSLKEGL TVFRDQEFSS DVGSRPVNRI QAIQVIRNHQ FAEDAGPMAH
     PIRPESVIEM NNFYTVTVYN KGAEVIRMMH TLLGEKNFQA GMKLYFERHD GQAVTCDDFV
     SAMEDASGVD LQQFRLWYSQ AGTPSVAVSE NFEDGQYQLT LTQSRPTVAG NNDLPMHIPF
     DVELIDLDGK SITSKVLNFT ERQQTFTFDG LTQKPVVSLL QDFSAPVKLE YQYEDEHLAH
     LMRYASSEVA RWEASVSLFS KSVWDNVKAL VAGKSMQLSD IVKDAFKGVI LDEKLDEELI
     AEIMSVPSIS ALVEQTESVD LDSLITARSF VKDELALACE DEVVARYHTS KDKDIASARA
     LKNECLSWAC VANEEHEALV NAQYESATNM TDSLGALKVA SDLNLSNRES LMTHFENRWV
     DTPLVMDKWF TLQAIQDSEQ VIDKIKALTS HKAFSFNNPN RVRSLIGSFA AGNIKHFHKS
     DGSGYQYLTD ILKKMNIINP QVAARIITPL IQFSKFDLAR QQKIKESLQE LIELPDLSKD
     LYEKVSRALS
//
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