ID   A0A0P0IY26_9CAUD        Unreviewed;       899 AA.
AC   A0A0P0IY26;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Membrane alanine aminopeptidase N {ECO:0000313|EMBL:ALJ98964.1};
DE            EC=3.4.11.2 {ECO:0000313|EMBL:ALJ98964.1};
OS   Acinetobacter phage Ab105-3phi.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes.
OX   NCBI_TaxID=1718842 {ECO:0000313|EMBL:ALJ98964.1, ECO:0000313|Proteomes:UP000257267};
RN   [1] {ECO:0000313|EMBL:ALJ98964.1, ECO:0000313|Proteomes:UP000257267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lopez M., Rueda A., Blasco L., Gato E., Barbosa B., Fernandez-Cuenca F.,
RA   Martinez-Martinez L., Vila J., Cisneros J.M., Pachon J., Rodriguez-Bano J.,
RA   Pascual A., Tomas M.;
RT   "Molecular evolution of Acinetobacter baumannii strains (belonging to ST-2
RT   clone) in a decade: Role of phages.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR634016-3};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3};
CC   -!- SIMILARITY: Belongs to the peptidase M1 family.
CC       {ECO:0000256|ARBA:ARBA00010136}.
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DR   EMBL; KT588073; ALJ98964.1; -; Genomic_DNA.
DR   Proteomes; UP000257267; Genome.
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; cd09601; M1_APN-Q_like; 1.
DR   Gene3D; 1.25.50.20; -; 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; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR   PANTHER; PTHR11533:SF174; PUROMYCIN-SENSITIVE AMINOPEPTIDASE-RELATED; 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|ARBA:ARBA00022438,
KW   ECO:0000313|EMBL:ALJ98964.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ALJ98964.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR634016-3};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT   DOMAIN          43..222
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          265..472
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          562..880
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
FT   BINDING         335
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         339
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         358
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
SQ   SEQUENCE   899 AA;  100581 MW;  E5F602B0EF8BBDB8 CRC64;
     MLVKPSFKKR LLLTTLLSLS ATQIFASNNS EQIPIGKLPE WVVPESYDLD FKIDPAQKGY
     TGKTTIHLKL AQATDHIWIH GKSLTVKDVN ITSAEGVKTK AKYEQASEID GVSKIKFAKT
     LPAGQYQLVL DFNAAYDQQL DGIYKIEFEG KPYVMTQMEA ISARQSFPSF DEPRFKTPFN
     IRLTIPSKYS GFANTQQTSE QIEKSGWKTL SFAQTKPLPT YLLALAVGPW QLQKGPDIGA
     TSWRKQPIQL RGIAPDTKAE KMQQALSETP AILKTLEDYF AFGYPFDKLD LLAAPDFAAG
     AMENPGLITF RDYLMLLDKD SPVFFVQNSF NVNAHELAHQ WFGDVVTMPW WDDLWLNESF
     ATWMQSKITQ KLHPEFNADL ERITDTADAM KSDSLVSVRR IRQPILSNAD IQTAFDGITY
     QKGAAVLNMF ESYLGEEKFK QGVRNYINKH QYGNATANDL ISALAEQSGQ GERFTRAMKS
     FLDQPGVPLI NTALQQEGNK VFLNVKQSRY LPVGSKGDAR SLWGVPLCVR YEVPNAGSKV
     QCELVDQAEA KIELKGASLG SWYIPNADAA GYYQFSLPQK EFTRLTAATE KLSNTEQLAY
     AYAISAAFNH GDINLLAVVD AAKKFANSNS RQISTALFSQ LSTIHRHVLK TEAERERFRK
     VLANLYLPKL NQLGYVSKTD ESAEDSLWRS ELVRFLALDI QVPEVRTQLL KQSDALFAQK
     QLNFAQVTPE LLPTILAVRV QEKGQPAFDR LSGELQRVTQ PTQRLAILTA LGSANQEATR
     QQARQLILNP RVKVGEVRTV VNSINSYGDE QGGLWSWFKV NHDAVFDRLG KSSAGRFPAM
     FSGAACTQQQ AAQLNDFFAP RTKELVGVER GLKQTKERIQ LCESLVAKQD GSIVQQLKL
//