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
//