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Database: UniProt
Entry: A0A1Q3TRI4_9SPHI
LinkDB: A0A1Q3TRI4_9SPHI
Original site: A0A1Q3TRI4_9SPHI 
ID   A0A1Q3TRI4_9SPHI        Unreviewed;       653 AA.
AC   A0A1Q3TRI4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Peptidase M1 {ECO:0000313|EMBL:OJW05056.1};
GN   ORFNames=BGO52_21490 {ECO:0000313|EMBL:OJW05056.1};
OS   Sphingobacteriales bacterium 44-61.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX   NCBI_TaxID=1895838 {ECO:0000313|EMBL:OJW05056.1, ECO:0000313|Proteomes:UP000186208};
RN   [1] {ECO:0000313|EMBL:OJW05056.1, ECO:0000313|Proteomes:UP000186208}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=44-61 {ECO:0000313|EMBL:OJW05056.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-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:OJW05056.1}.
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DR   EMBL; MKTW01000001; OJW05056.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3TRI4; -.
DR   STRING; 1895838.BGO52_21490; -.
DR   Proteomes; UP000186208; Unassembled WGS sequence.
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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..653
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012208206"
FT   DOMAIN          381..552
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
SQ   SEQUENCE   653 AA;  74982 MW;  F92C886750A9378A CRC64;
     MRKFILFIAV SLNTVLAFAQ SNYDAKEAFN PQFYPYPGNE FRSASGEPGP RYWQNRADYK
     INCTLDTTNH RLSGEVEINY TNNSPDNLKF LWLQLDQNIY KKDSRASATT TEAGGRWANG
     EFTQGDVIKS IAVEYNGKKY TAQYNITDTR MQVWLQEALK SAGGKIKLSI PFEFEIPQYG
     TDRMGRLNTQ NGWIYETAQW FPRLCVYDDI QGWNVLPYLG AGEFYLEYGD IEYAVTAPAN
     MIVVGSGELL NPHECFTGEQ LKRYNEAKTS DKTITIRSDK DINDRNAQPK KASSTWKFRI
     LNARDVAWGA SRAFVLDAAR INLPDGKKSL AVSAYPVESM KDKKGNDWRR STEMVKASIE
     HYSEKWFEFP YPAATNVAGI VGGMEYPGIV FCSYTSVGAG LWGVTDHEFG HTWFPMIVGS
     NERKYAWMDE GFNTFINDLS TDAFHNGEFK DKSFFNDPTS PFMIKYTFGD KMDGLYTVPD
     AIQQDNLGIA AYMKPSQMLH ALRDIVLGPE RFDRAFREYV QRWAFKHPTP WDFFHSMENV
     AGESLDWFWR SWVLNTWKLD QSVKEVKYVK NDPAKGAEIT LENLEKMPMP VTIVIKETNG
     KEYRMDLPVE IWQRGALYTL GVPSTTEIKE VVLDPDKKLP DWNRENNKWK KAF
//
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