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Database: UniProt
Entry: A0A1F8MJQ3_9CHLR
LinkDB: A0A1F8MJQ3_9CHLR
Original site: A0A1F8MJQ3_9CHLR 
ID   A0A1F8MJQ3_9CHLR        Unreviewed;       552 AA.
AC   A0A1F8MJQ3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Peptidase M28 domain-containing protein {ECO:0000259|Pfam:PF04389};
GN   ORFNames=A2Z71_04080 {ECO:0000313|EMBL:OGN98826.1};
OS   Chloroflexi bacterium RBG_13_50_21.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1797623 {ECO:0000313|EMBL:OGN98826.1, ECO:0000313|Proteomes:UP000177581};
RN   [1] {ECO:0000313|EMBL:OGN98826.1, ECO:0000313|Proteomes:UP000177581}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGN98826.1}.
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DR   EMBL; MGMQ01000009; OGN98826.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8MJQ3; -.
DR   STRING; 1797623.A2Z71_04080; -.
DR   Proteomes; UP000177581; Unassembled WGS sequence.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR008969; CarboxyPept-like_regulatory.
DR   InterPro; IPR045175; M28_fam.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR   PANTHER; PTHR12147:SF59; PEPTIDASE_M28 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF13620; CarboxypepD_reg; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..552
FT                   /note="Peptidase M28 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009537360"
FT   DOMAIN          246..437
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   552 AA;  59939 MW;  898D692497EBD304 CRC64;
     MKKRIFSYIL LLILLIFLTG NVQATPHTTI DPKALVFVNL KYPDDLSRFS LTQLPLYSML
     DGGLLTGANL RDQHKLRDAG LSFQVIDPDL QAGTYFLAEI RPSRPAPGFT AYGRVLLSTA
     NGVLLRMDSS QADALTQAGV ELRTITITPK PLPTALTQEV FPEVVVPNPI IQMMIDQVIL
     DTVHTYDRQL AGELPVWVDG AWYTILSRHT YSGIPIQKTT SYAGQHMENL GLDVEYHTWS
     GSTYPNVIGE ITGLIHPDKI FIIGAHIDDI QGTPGADDNA SGSVATLLAA DILAQYLWDC
     TVRFALWTGE EQGLNGSHAY AQRSYTAGEN IVGYLNLDMI AWNTPNSAPA IDIYYSNSVP
     GSLAFAQLFS DVVGAYNLNL IPGLGTGVSG SDHASFWQFG YNSILAIEDK GDFNPYYHGP
     GDTPAHTDLS YFTDFVKASI ATFVHKSECL SPNGYGFLDG HVTASSGGAP IEGAIVSAED
     SQGRSYPART DSTGYYKRTL AADTYTITST AHGYLPATIS GVEVVTDTVT TQDFSLVSAP
     PNYYIYQPLV SR
//
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