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Database: UniProt
Entry: A0A1H4QXC2_9ACTN
LinkDB: A0A1H4QXC2_9ACTN
Original site: A0A1H4QXC2_9ACTN 
ID   A0A1H4QXC2_9ACTN        Unreviewed;       835 AA.
AC   A0A1H4QXC2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE            EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
DE   AltName: Full=Alanine aminopeptidase {ECO:0000256|ARBA:ARBA00029811};
DE   AltName: Full=Lysyl aminopeptidase {ECO:0000256|ARBA:ARBA00031533};
GN   ORFNames=SAMN05216482_2604 {ECO:0000313|EMBL:SEC24198.1};
OS   Streptomyces sp. PAN_FS17.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1855351 {ECO:0000313|EMBL:SEC24198.1, ECO:0000313|Proteomes:UP000199275};
RN   [1] {ECO:0000313|Proteomes:UP000199275}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAN_FS17 {ECO:0000313|Proteomes:UP000199275};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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; FNTN01000001; SEC24198.1; -; Genomic_DNA.
DR   RefSeq; WP_030958937.1; NZ_FNTN01000001.1.
DR   AlphaFoldDB; A0A1H4QXC2; -.
DR   STRING; 1855351.SAMN05216482_2604; -.
DR   Proteomes; UP000199275; 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; cd09602; M1_APN; 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; IPR012778; Pept_M1_aminopeptidase.
DR   InterPro; IPR001930; Peptidase_M1.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   NCBIfam; TIGR02412; pepN_strep_liv; 1.
DR   PANTHER; PTHR11533:SF174; ALANINE/ARGININE AMINOPEPTIDASE-RELATED; 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|ARBA:ARBA00022438,
KW   ECO:0000313|EMBL:SEC24198.1}; 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:UP000199275};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          86..182
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          223..436
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          513..824
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
SQ   SEQUENCE   835 AA;  92524 MW;  22DDCDB5539F2B57 CRC64;
     MSVLTRDEAQ TRAQLLDVHR YTIELDLTTG DETFDSRTVI AFTARTGADT FVEVKPAELR
     SVTLDGRPLD PETLDGNRLP LKDLAAGDHE LRIDAAMRYS RTGEGMHRFT DPTDGETYLY
     TQLFMEDVQR VFAAFDQPDL KAVFELSVTA PEGWSVLANG RTEHTGDGRW QATPTPLIST
     YLVAVAAGPW HSVRTEHGGL PFGLHCRRSL APYLDTDADE LFQVTRQCFD RFHEKFDEPY
     PFDSYDQAFV PEFNAGAMEN PGLVTFRDEF VYRSAVTDTE RQTRAMVIAH EMAHMWFGDL
     VTLRWWDDIW LNESFAEYMG YQTLVEATRF TDTWVDFGVA RKSWGYDADQ RPSTHPVAPE
     NVDDTASAML NFDGISYAKG ASALRQLVAW LGEKDFLAGI NTHFDRHKFA NATLADFIDS
     LASATDRDVH AWADSWLRTT GVDTLTPQVA PGDNGTYSLT VDHAGSRPHR VAVGLYDQDL
     GDDEGRHLTL RRRLEIDVPQ STPLPIGKRP ALLVLNDGDL TYAKVRFDAE SFTTLRERLS
     GLPDPLTRAV VWNALRDAVR DGELAAIAYL EAARAHLPRE TDLAIVQGVL AFAVGQVTDR
     YLPADERPAA LATLSALCRD LIRRTEDGDN PGLRLIAVRH FISVAAHPDT IAAWLADGTV
     PGGPELDPEL RWRVMGRLAV LGAVDEAAIA AELERDQSAS GQEGAARCRA ALPDEEAKAA
     AWEALFTTDE SSDLSNYLFT ATAQGFWQPE QADLVSPYVA RFYKDAVALA ARRGPAIAEA
     AGRYAFPVHA VDAEALSLGE ECLRDGDPIP ALRRRLADQL DDLARALRVR EGRTK
//
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