ID A0A1A0MU45_9MYCO Unreviewed; 860 AA.
AC A0A1A0MU45;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=A5662_02365 {ECO:0000313|EMBL:OBA88927.1};
OS Mycobacteriaceae bacterium 1482268.1.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae.
OX NCBI_TaxID=1834080 {ECO:0000313|EMBL:OBA88927.1, ECO:0000313|Proteomes:UP000091934};
RN [1] {ECO:0000313|EMBL:OBA88927.1, ECO:0000313|Proteomes:UP000091934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1482268.1 {ECO:0000313|EMBL:OBA88927.1,
RC ECO:0000313|Proteomes:UP000091934};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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}.
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:OBA88927.1}.
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DR EMBL; LZSH01000477; OBA88927.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A0MU45; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000091934; 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: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:OBA88927.1};
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 Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 63..193
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 532..850
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 860 AA; 94720 MW; 70287CD194D667DB CRC64;
MVLPNLTRDQ AIERAALVTI DRYGIDLDLT DGAGAPGEKT FRSITTVEFS ALPGADTYID
IAAETVHKAT LNGIDLDVSA YDEENGIALP GLQERNTLVV DAQCLYSNTG EGLHRFVDPV
DNEVYLYSQF ETADAKRMFA CFDQPDLKAT FDIAVTAPEH WEVVSNGAPV NAQVTGNAKT
VTFATTPKMS TYLVALIAGP YAVWRDSYTD EHGEIPLGLF CRKSLQEFMD ADRLFTETKQ
GFDFYHRNFG QPYAFGKYDQ LFVPEFNAGA MENAGAVTFL EDYVFRSKVT RASYERRAET
VLHEMAHMWF GDLVTMRWWD DLWLNESFAT FASVLCQAEA TEYTEAWTTF ANAEKSWAYR
QDQLPSTHPV AADIPDLAAV EVNFDGITYA KGASVLKQLV AYVGLEAFLA GLRDYFRDHA
FDNATFGDLL GALEKSSGRD LSHWGQQWLK TTGLNTLRAD FDVDPDGKFS RFAISQSGAA
PGAGETRVHR LAVGIYDDDG SGKLVRLHRE ELDIEGASTE VPALQAIPRG KLILVNDDDL
TYCSLRLDPE SLQTVLTRIA DIAEPLPRTL AWSAAWEMTR EAELKARDFV ALVVNGVHAE
TEVGVAQRLL LQAQTALRSY ADPDWACSDG WPTFADRLLE LARAAEPGSD HQLAYINALC
TSVLALRHVA VLAALLDTDP AEHGLPGLTI DTDLRWRIVT ALAAAGDIDN DGEATPFIDA
EVERDPTAAG KRNAARAAAA RPQDAVKKTA WQLVIEDDTL PNIVGRSIID GFVQPGQQAL
LQPFTAKYFD AIPGVWQRRS SEVAQTVVIG LYPTWDISED ALKAADRFLE GDMQPSLRRL
VVEGRAGVER ALRARAFDIS
//
