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Database: UniProt
Entry: A0A3B0C9M6_9FLAO
LinkDB: A0A3B0C9M6_9FLAO
Original site: A0A3B0C9M6_9FLAO 
ID   A0A3B0C9M6_9FLAO        Unreviewed;       692 AA.
AC   A0A3B0C9M6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE            EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN   ORFNames=D7Z94_10140 {ECO:0000313|EMBL:RKN81288.1};
OS   Ulvibacterium marinum.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Ulvibacterium.
OX   NCBI_TaxID=2419782 {ECO:0000313|EMBL:RKN81288.1, ECO:0000313|Proteomes:UP000276603};
RN   [1] {ECO:0000313|EMBL:RKN81288.1, ECO:0000313|Proteomes:UP000276603}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMM003 {ECO:0000313|EMBL:RKN81288.1,
RC   ECO:0000313|Proteomes:UP000276603};
RA   Zhang Z.;
RT   "Ulvibacterium marinum gen. nov., sp. nov., a novel marine bacterium of the
RT   family Flavobacteriaceae, isolated from a culture of the green alga Ulva
RT   prolifera.";
RL   Submitted (OCT-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:RKN81288.1}.
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DR   EMBL; RBCJ01000002; RKN81288.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B0C9M6; -.
DR   OrthoDB; 100605at2; -.
DR   Proteomes; UP000276603; 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; 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:SF303; AMINOPEPTIDASE N; 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   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:UP000276603};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          35..195
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          234..434
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
SQ   SEQUENCE   692 AA;  80668 MW;  477FE53297B7353D CRC64;
     MKQLITVLFL FQSVFVLTQR QDKVNFIHGE AQIVPFAREG RLEGSVIYKF EVFQDVDSVF
     LDARNMEFTS VRLNDRIVKY SNSGNTVSLK KKLKGGKSYK LKLDYTAGPK QTVYFMNWND
     DNPNNDQIWT QGQGKYTSYW LPSFDDMTEK VEFDLNITFD KNYEIIANGK LVAIQEKNSL
     KTWSFDMKDP MSSYLLAFAI GIYEKQQLTS ANGTPIKNYF YPKDSERVEP TYRYTKEIFD
     FLEEEIGVAY PWQNYKQVPV HDFLYAGMEN TGCTIFSDAY VIDSVAFMDK NYVNVNAHEL
     AHQWFGNLVT EKSGSHHWLH EGFATYYAYL TEKELFGEEH FYWKLFETLT ALQNSIEKGQ
     GQSLLDPRAS SLTFYEKGAW AIFMLRDRIG DVAFKKGIQS YLEKYAFANV TVPSFIQEME
     KSSGADLSHY VKVWLEDTAL PFKVAQEKLA EKSEPLKSLF ALQAALKSQE SDDIDYTSYW
     NGTNSIQLKK YMIQNFLRTM PEEIIDRVLD SNTLELRQAL ALSIQDAKDY PKEKFETLLN
     DNSYVTLENT LFKLWMAYPE ERNSYLEKTK ETIGFPNKNV RLMWLTLAIL TEGYEGRNTK
     LYFDELSGYT APEYSFEVRQ GAFQYLNEAF GFKDSNLLDL AEATTHHSWQ FKKFSRNLMV
     ELLKDQVYKE RIMSLLGKLK PEERRYIESK VK
//
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