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Database: UniProt/TrEMBL
Entry: D5ES86_PRER2
LinkDB: D5ES86_PRER2
Original site: D5ES86_PRER2 
ID   D5ES86_PRER2            Unreviewed;       802 AA.
AC   D5ES86;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Transglutaminase-like protein {ECO:0000313|EMBL:ADE83547.1};
GN   OrderedLocusNames=PRU_1170 {ECO:0000313|EMBL:ADE83547.1};
OS   Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Xylanibacter.
OX   NCBI_TaxID=264731 {ECO:0000313|EMBL:ADE83547.1, ECO:0000313|Proteomes:UP000000927};
RN   [1] {ECO:0000313|EMBL:ADE83547.1, ECO:0000313|Proteomes:UP000000927}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19189 / JCM 8958 / 23 {ECO:0000313|Proteomes:UP000000927};
RX   PubMed=20585943; DOI=10.1007/s00248-010-9692-8;
RG   North American Consortium for Rumen Bacteria;
RA   Purushe J., Fouts D.E., Morrison M., White B.A., Mackie R.I.,
RA   Coutinho P.M., Henrissat B., Nelson K.E.;
RT   "Comparative genome analysis of Prevotella ruminicola and Prevotella
RT   bryantii: insights into their environmental niche.";
RL   Microb. Ecol. 60:721-729(2010).
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DR   EMBL; CP002006; ADE83547.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5ES86; -.
DR   STRING; 264731.PRU_1170; -.
DR   KEGG; pru:PRU_1170; -.
DR   eggNOG; COG1305; Bacteria.
DR   HOGENOM; CLU_325905_0_0_10; -.
DR   Proteomes; UP000000927; Chromosome.
DR   Gene3D; 3.10.620.30; -; 1.
DR   Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR002931; Transglutaminase-like.
DR   PANTHER; PTHR35532:SF5; CARB-BD_DOM_FAM9 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR35532; SIMILAR TO POLYHYDROXYALKANOATE DEPOLYMERASE; 1.
DR   Pfam; PF01841; Transglut_core; 1.
DR   SMART; SM00460; TGc; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000927};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..802
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003071382"
FT   DOMAIN          137..196
FT                   /note="Transglutaminase-like"
FT                   /evidence="ECO:0000259|SMART:SM00460"
SQ   SEQUENCE   802 AA;  91406 MW;  96F9015C8F962326 CRC64;
     MYKTLTIFTI LLSAMCLPAS AQTRDSYVDY LYQFMPQPDK TDYSREFYQQ NVALSLKARA
     EMPWGKTIPE REFRHFVVPV RVNNENLDNS REVFYKALKP RVEKLSMQEA ILEVNHWCHE
     HVTYRPSDGR TSSPLATLRT AYGRCGEQST FTVAALRAVG IPARQVYTPR WAHTDDNHAW
     VEAWADGKWY FLGACEPEPV LNLGWFNESA SRGMLMHTKA FGNYDGPEEV MSQTPCYTEI
     NVVDNYAPTA QVNVQVVNAK GKPVSGARVE FKLYNYAEFY TVANKTTDKL GHASLTAGKG
     DMLLWVSKGG LVATRKVSFG KDKQVKIVLN SKELPDLVDL DIVPPPVSGQ LPLVTAEQRA
     ENNRRSAYED SIRHAYEATM PVEDWRGNHR TIQQFLDEAP NQLMAEKLLG VLAKKDLRDI
     ELAVLKDNQV AAVDTSDIYL KYVLCPRVEL EWLTPYKAFF REHMGSIKSP AQLEAWCNQN
     IRIDNDHNPQ GLRMQPMSVY REKLTDDLGR NIFFVSVARS LGMPARINEV NGKPQYYADG
     RWVDVFAKAQ NAKQGNTAKL KLDYKLSAHN DNPKYYIHFT LSKVVDGQLQ LQTFPEDATQ
     QDFVNGQEID KGEYILTTGV RMASGKVLAR MQRFTLNGDT TISYALRENQ EDVQVIGSIN
     AEDIYHDKAT DSDKSLLSTT GRGYYVLAIV APNQEPTNHA MRDISVYKQQ FEEWGRKMIF
     LFQNDDEAQR FNFAEFDKLP NTVVWGTDVE GKIKQEVWQQ MKLQSPALPV FLICDSFNRV
     VFVQQGYTIN LGEQLIKVIR QL
//
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