ID A0A127A2J6_9MICC Unreviewed; 851 AA.
AC A0A127A2J6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=SA2016_2345 {ECO:0000313|EMBL:AMM33014.1};
OS Sinomonas atrocyanea.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Sinomonas.
OX NCBI_TaxID=37927 {ECO:0000313|EMBL:AMM33014.1, ECO:0000313|Proteomes:UP000070134};
RN [1] {ECO:0000313|EMBL:AMM33014.1, ECO:0000313|Proteomes:UP000070134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 3377 {ECO:0000313|EMBL:AMM33014.1,
RC ECO:0000313|Proteomes:UP000070134};
RA Kim K.M.;
RT "Complete genome of Sinomonas atrocyanea KCTC 3377.";
RL Submitted (FEB-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; CP014518; AMM33014.1; -; Genomic_DNA.
DR RefSeq; WP_066498196.1; NZ_CP014518.1.
DR AlphaFoldDB; A0A127A2J6; -.
DR STRING; 37927.SA2016_2345; -.
DR KEGG; satk:SA2016_2345; -.
DR PATRIC; fig|37927.3.peg.2414; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000070134; Chromosome.
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:SF304; AMINOPEPTIDASE N; 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:0000313|EMBL:AMM33014.1};
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:UP000070134};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 81..192
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 237..448
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 531..842
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 851 AA; 93687 MW; CE1D543140C60F96 CRC64;
MPGTNLTRSE AVERAECIRH VEDYHVELDL TRGERVFGSR TTVRFSAAEG ASSFIDAITD
TVRSVTLNGV ELHVEKASDG VRIQLPSLAA ENVLVVDADA PYMNTGEGLH RFVDPVDGEA
YLYTQFEVPD SRRMFAVFEQ PDLKASFRFT VTAPSHWEVV SNSPTPEPVR VPGQEARSTW
DFAPTPRISS YVTALVAGPY QKVADELVNA EGRTIPLGIF ARKSLMQYLD AENIFALTKE
GFAFYEREFG CGYPFEKYDQ LFVPEFNAGA MENAGAVTIL ESYVFRSKPT QATVERRAIT
VLHELAHMWF GDLVTMRWWD DLWLNESFAE FMSHLAAAEA TDFRHAWTTF ASVEKSWAYR
QDQLPTTHPI FADISDLADV EVNFDGITYA KGASVLKQLV AWVGQDHFME GVRRYFAKHA
WGNTVLADLM AELEAASGRD LTAWGQAWLE TAGVNTLSPE IETDDDGRIL RFAVRQSAVP
DYPQIRPHRL AIAFYDRDGA GELVRTHRAE LDVDGELTEV PELVGRPRPA LVLLNDDDLA
YAKVRLDPVS LATATSCLKD ISESLPRALV WGSAWDGARD GETPARAYVD LVLGNIGAES
DASVVQTLLR QLATTLDYYV AADAQPEAKR SAAERLWALV HEAAPGSDSQ LQFVKSFSAL
ASSEEHLDAV AGLLDGSAPI PGLDVDQDLR WELVASLACG GRIERARIED ELARDTTSTG
QCAAALATAA LPTPEAKAEA WESIVVKGTL SNAMQQAAIN GFARVHDAAL LAPFAEKYFE
AVPRIVAERT HALAQQVVVG LYPARQTTQA MLERTDEFLA SLGPDQAALR RMTLENRDGV
QRALRAQAAD R
//
