ID A0A2V4NF84_9RHOB Unreviewed; 854 AA.
AC A0A2V4NF84;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=DI396_06285 {ECO:0000313|EMBL:PYC48570.1};
OS Litorivita pollutaquae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Litorivita.
OX NCBI_TaxID=2200892 {ECO:0000313|EMBL:PYC48570.1, ECO:0000313|Proteomes:UP000248012};
RN [1] {ECO:0000313|EMBL:PYC48570.1, ECO:0000313|Proteomes:UP000248012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSX-11 {ECO:0000313|EMBL:PYC48570.1,
RC ECO:0000313|Proteomes:UP000248012};
RA Hetharua B.H., Min D., Liao H., Tian Y.;
RT "Oceanovita maritima gen. nov., sp. nov., a marine bacterium in the family
RT Rhodobacteraceae isolated from surface seawater of Lundu port Xiamen,
RT China.";
RL Submitted (MAY-2018) 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:PYC48570.1}.
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DR EMBL; QFVT01000003; PYC48570.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V4NF84; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000248012; 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; cd09600; M1_APN; 1.
DR Gene3D; 2.60.40.1840; -; 1.
DR Gene3D; 3.30.2010.30; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 1.25.50.10; Peptidase M1, alanyl aminopeptidase, C-terminal domain; 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; IPR038438; PepN_Ig-like_sf.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR012779; Peptidase_M1_pepN.
DR InterPro; IPR024601; Peptidase_M1_pepN_C.
DR InterPro; IPR037144; Peptidase_M1_pepN_C_sf.
DR InterPro; IPR035414; Peptidase_M1_pepN_Ig-like.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR NCBIfam; TIGR02414; pepN_proteo; 1.
DR PANTHER; PTHR46322; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR PANTHER; PTHR46322:SF1; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR Pfam; PF11940; DUF3458; 1.
DR Pfam; PF17432; DUF3458_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:PYC48570.1};
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:UP000248012};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 108..183
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 222..436
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 441..532
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 537..852
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 854 AA; 94459 MW; DFDE0A853E35B9F2 CRC64;
MLDARATHPN PTIYLKDYTP PAYLVDSVAL TFRLAPKATR VVSRIQFRPN PDHENRDFFL
EGEELKLIWA KIDGVDITPH VTDKGLSCEV PDAPFLFEAE VEIAPEDNTA LEGLYMSSGM
YCTQCEAQGF RKITYYPDRP DVMSVFSVRI EGDLPVLLSN GNPTGSGTGF AEWHDPWPKP
AYLFALVAGD LIAHPDRFTT MSGKDVALNI YVRPGDEDKC AFGMEALKAS MRWDETAYGR
EYDLDIFNIV AVDDFNMGAM ENKGLNIFNS SCVLASPETS TDANFERIEA IIAHEYFHNW
TGNRITCRDW FQLCLKEGLT VYRDSQFTSD MRSGPVKRIG DVIDLRARQF REDGGPLAHP
VRPESFQEIN NFYTATVYEK GAELIGMLKT LVGDDAYAKA LDLYFARHDG EAATIEDWLK
VFEDTTGRDL SQFKRWYSDA GTPRVSVCED FNDGTYTLTF KQQTPPTPGQ DVKPPRVIPI
AVGLLSPNGD EVHSTTVLEM TETEQSFTFE GLGARPIPSI LRGFSAPVIL ERDSSAEERA
FLLAHDTDPF NRWEAGAEIA RQLRMDMARS GGAPDSAYLD ALLDIARDDS LDPAYRALML
QPPAQEDIAQ ALHANGTTPD PQTIYDVAET VAQTIAEHFG NTAPRLYAEM DTPAPYSPDA
DAAGKRALQA RMLGMITRLD GGKTAAAQYA GADNMTQQYG ALCALLSQDF GGDENAAFYQ
QWKHDRLVID KWFAAQIAFT APEETAEAAA RMTHHADFNA KNPNRFRAVF GALAGHHGGF
HHASGAGYAL LADHLIALDP VNPQTTARMM SAFSTWTRYD ADRQTLARAA LERIAATDGL
SPDTSEMVGR ILSI
//
