ID I3YTI1_AEQSU Unreviewed; 646 AA.
AC I3YTI1;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Aminopeptidase N {ECO:0000313|EMBL:AFL80299.1};
GN OrderedLocusNames=Aeqsu_0794 {ECO:0000313|EMBL:AFL80299.1};
OS Aequorivita sublithincola (strain DSM 14238 / LMG 21431 / ACAM 643 / 9-3).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aequorivita.
OX NCBI_TaxID=746697 {ECO:0000313|EMBL:AFL80299.1, ECO:0000313|Proteomes:UP000006049};
RN [1] {ECO:0000313|EMBL:AFL80299.1, ECO:0000313|Proteomes:UP000006049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14238 / LMG 21431 / ACAM 643 / 9-3
RC {ECO:0000313|Proteomes:UP000006049};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Peters L.,
RA Munk A.C.C., Kyrpides N., Mavromatis K., Pagani I., Ivanova N.,
RA Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA Faehnrich R., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Aequorivita sublithincola DSM 14238.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP003280; AFL80299.1; -; Genomic_DNA.
DR RefSeq; WP_014781557.1; NC_018013.1.
DR AlphaFoldDB; I3YTI1; -.
DR KEGG; asl:Aeqsu_0794; -.
DR PATRIC; fig|746697.3.peg.796; -.
DR eggNOG; COG0308; Bacteria.
DR HOGENOM; CLU_015077_0_0_10; -.
DR OrthoDB; 9814383at2; -.
DR Proteomes; UP000006049; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd09604; M1_APN_like; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF303; AMINOPEPTIDASE N; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 4: Predicted;
KW Aminopeptidase {ECO:0000313|EMBL:AFL80299.1};
KW Hydrolase {ECO:0000313|EMBL:AFL80299.1};
KW Protease {ECO:0000313|EMBL:AFL80299.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..646
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003684077"
FT DOMAIN 355..550
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 646 AA; 73936 MW; 420780AEB6BC1100 CRC64;
MKYSKSSFLL SLLLFTFCFA AISQVQEVKQ DNQQLFDNFS YRQGNVYRSA SGKPGPEYWQ
NSADYKLEAT LDDKNHTVSG NVNIHYTNNS PETLDFIWLY LEQDRFTENS RGTLTTPVQG
NRYNGDVEGG FELTNVSAKT KTGTSSKYLI TDTRMQLWLD KPLAAKGGEV DIKMNFKFKV
PVEGMDRMGR LEVKDGTIYA IAQWYPRVAV FDDVVGWNTD PYLGAGEFYC EYGNYDVKIT
APADQTVVCS GVLQNPKDVL TAEQQKRWSQ AEKSDKTVYI IQPDEVGKPV AHAKTSGTIT
WHFKMENTRD VAWASSKTFI WDAARMNLGD GKSGLAQSVY PKESAGDKAW KRSTEFTKAS
IEFYSKTYFT YPYQNAINVA ASVGGMEYPG VSFCHYQSHD ADLWDVTDHE FGHNWFPMIV
GSNERRYPWM DEGFNTFINH YSTKAFNNGE FPTSTDKPKS IVRYLSFDQR EGIDTYPDVA
HPFNLAYTAY YKPAAGLYML REYILGPERF DNAFKSYIST WAYKHPQPND FFNHIENVAG
EDLSWFWKGW FYGNGNIDLG ISEVKPYNGN YLITVENDGQ IPMPVQLQVI YTDNTTENIN
LPVEIWQRGN SWEHLLKTTK QVQRVVLDPD KMLPDVNPLN DTWNKL
//
