ID A0A150X9C5_9BACT Unreviewed; 739 AA.
AC A0A150X9C5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Aminopeptidase {ECO:0000313|EMBL:KYG75339.1};
GN ORFNames=AWW68_11120 {ECO:0000313|EMBL:KYG75339.1};
OS Roseivirga spongicola.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Roseivirgaceae;
OC Roseivirga.
OX NCBI_TaxID=333140 {ECO:0000313|EMBL:KYG75339.1, ECO:0000313|Proteomes:UP000075606};
RN [1] {ECO:0000313|EMBL:KYG75339.1, ECO:0000313|Proteomes:UP000075606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UST030701-084 {ECO:0000313|EMBL:KYG75339.1,
RC ECO:0000313|Proteomes:UP000075606};
RA Selvaratnam C., Thevarajoo S., Goh K.M., Ee R., Chan K.-G., Chong C.S.;
RT "Genome sequencing of Roseivirga spongicola UST030701-084.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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:KYG75339.1}.
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DR EMBL; LRPC01000023; KYG75339.1; -; Genomic_DNA.
DR RefSeq; WP_068221368.1; NZ_LRPC01000023.1.
DR AlphaFoldDB; A0A150X9C5; -.
DR STRING; 333140.AWW68_11120; -.
DR OrthoDB; 9814383at2; -.
DR Proteomes; UP000075606; Unassembled WGS sequence.
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:SF174; ALANINE/ARGININE AMINOPEPTIDASE-RELATED; 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:KYG75339.1};
KW Hydrolase {ECO:0000313|EMBL:KYG75339.1};
KW Protease {ECO:0000313|EMBL:KYG75339.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000075606};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..739
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007574483"
FT DOMAIN 408..564
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT REGION 598..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 739 AA; 84904 MW; B2884FB02C250BA0 CRC64;
MKSTLSIFLM LLAFTATSQT GWQGKFEQMG NMLPTPNQYR TGSGEPGPSY WQQKADYKIK
LELDDENQKI TGSEVVTYYN NSPSALRYLW VQLDQNVRQK DNLSSLTSGT RGIPDNVTSL
RTTQAQSALG DTGFDGGFKL MAVKDTKGND LDYVVNFTMM KINLPEPLES GDSFSFNIDW
WYNINDRGLI GGRSGYEYFK EDDNYLYTIA QFYPRMAVYD DFNGWQNKQF IGSGEFALTF
GDFEVEITVP SDHIVASTGE LQNPKDVLTS KELQRYERAK ESFDKQVFIV TEDEAKKKEK
SRSSKKSTWV YHAENVRDFA FASSRKFIWD AQAVKVGEKT PLAMSYYPKE GNPLWEREST
KAVINTLINY SEMTIDYPYP VAISVHAASI GMEYPMICFN FGRPRPDGTY NDFVKTRMVS
VIVHEVGHNY FPMIINSDER QWAWMDEGLD SFMEYMTMKR FYPDLPYNSN TPEAIIPYMK
GSKDYMRPIM TNPEQSLQLG PEAYSKPSAA LVVLREEVMG PELFDAAFKE YSRRWAFKHP
KPADFFRTME DASAVDLDWF WKGWFFSTDN VDVEVADVKW FKIKGENKSL EGEVKAQAGN
LGGNSQTNED NPFYGQPQEL SLNDDQVRGE YRGEIDNEAI KQRFAGKNVY QITFKNNGGL
ITPITLEWTY KDGSKEIEKI PAEIWRRNEA EVTKLFVKDK EVDNVVFDPF KQLGDVNTEN
NSFPQGESRN SRFDQFKKN
//