ID Q7MU01_PORGI Unreviewed; 1122 AA.
AC Q7MU01;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 139.
DE RecName: Full=Transcription-repair-coupling factor {ECO:0000256|HAMAP-Rule:MF_00969};
DE Short=TRCF {ECO:0000256|HAMAP-Rule:MF_00969};
DE EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_00969};
GN Name=mfd {ECO:0000256|HAMAP-Rule:MF_00969,
GN ECO:0000313|EMBL:AAQ66775.1};
GN OrderedLocusNames=PG_1774 {ECO:0000313|EMBL:AAQ66775.1};
OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=242619 {ECO:0000313|EMBL:AAQ66775.1, ECO:0000313|Proteomes:UP000000588};
RN [1] {ECO:0000313|EMBL:AAQ66775.1, ECO:0000313|Proteomes:UP000000588}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-308 / W83 {ECO:0000313|Proteomes:UP000000588};
RX PubMed=12949112; DOI=10.1128/JB.185.18.5591-5601.2003;
RA Nelson K., Fleishmann R., DeBoy R., Paulsen I., Fouts D., Eisen J.,
RA Daugherty S., Dodson R., Durkin A., Gwinn M., Haft D., Kolonay J.,
RA Nelson W., White O., Mason T., Tallon L., Gray J., Granger D., Tettelin H.,
RA Dong H., Galvin J., Duncan M., Dewhirst F., Fraser C.;
RT "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT gingivalis strain W83.";
RL J. Bacteriol. 185:5591-5601(2003).
CC -!- FUNCTION: Couples transcription and DNA repair by recognizing RNA
CC polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent
CC release of RNAP and its truncated transcript from the DNA, and
CC recruitment of nucleotide excision repair machinery to the damaged
CC site. {ECO:0000256|HAMAP-Rule:MF_00969}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00969}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the helicase family.
CC RecG subfamily. {ECO:0000256|HAMAP-Rule:MF_00969}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the UvrB family.
CC {ECO:0000256|HAMAP-Rule:MF_00969}.
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DR EMBL; AE015924; AAQ66775.1; -; Genomic_DNA.
DR RefSeq; WP_005873725.1; NC_002950.2.
DR AlphaFoldDB; Q7MU01; -.
DR STRING; 242619.PG_1774; -.
DR EnsemblBacteria; AAQ66775; AAQ66775; PG_1774.
DR KEGG; pgi:PG_1774; -.
DR PATRIC; fig|242619.8.peg.1641; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_3_10; -.
DR BioCyc; PGIN242619:G1G02-1655-MONOMER; -.
DR Proteomes; UP000000588; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProtKB-UniRule.
DR GO; GO:0000716; P:transcription-coupled nucleotide-excision repair, DNA damage recognition; IEA:UniProtKB-UniRule.
DR CDD; cd17991; DEXHc_TRCF; 1.
DR Gene3D; 2.40.10.170; -; 1.
DR Gene3D; 3.40.50.11180; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.30.2060.10; Penicillin-binding protein 1b domain; 1.
DR Gene3D; 3.90.1150.50; Transcription-repair-coupling factor, D7 domain; 1.
DR HAMAP; MF_00969; TRCF; 1.
DR InterPro; IPR003711; CarD-like/TRCF_RID.
DR InterPro; IPR036101; CarD-like/TRCF_RID_sf.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR004576; Mfd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR047112; RecG/Mfd.
DR InterPro; IPR037235; TRCF-like_C_D7.
DR InterPro; IPR005118; TRCF_C.
DR InterPro; IPR041471; UvrB_inter.
DR NCBIfam; TIGR00580; mfd; 1.
DR PANTHER; PTHR47964; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR PANTHER; PTHR47964:SF1; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR Pfam; PF02559; CarD_TRCF_RID; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF03461; TRCF; 1.
DR Pfam; PF17757; UvrB_inter; 1.
DR SMART; SM01058; CarD_TRCF; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00982; TRCF; 1.
DR SUPFAM; SSF141259; CarD-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
DR SUPFAM; SSF143517; TRCF domain-like; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00969}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00969};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_00969};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_00969};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00969}; Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00969};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00969}; Reference proteome {ECO:0000313|Proteomes:UP000000588}.
FT DOMAIN 570..731
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 751..906
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1122 AA; 126747 MW; B1009D3D0047B9C3 CRC64;
MIKSPQPIDI LSLFRRHNGV QALMKALDRE KCVALDGLCG SSAALIVKLL HESGRPVLCI
ASDMEEAGYL FSDLEQLGGE GSALFFPSSY KRAIKYGHTD AAQQVLRAEA LAALSMEGSC
PLVVSYPEAV AERVVAGDIL EKEMHSIRQG DRLDRDFLRD LLLEWGFERT DYVYEPGQFA
VRGSLLDVFS FSRELPVRID FFDDEIESIR LFEVESQLSV GTLSEVVLMP DVAGDVRAEE
CLLGLFPKNT IIVLPDRPFL EDRLQMVFTD APLFDDGEGF ESLVAMQERL TSPKELMDKL
NDFTTIATGS GRSGNYRIGF KTQPQPLFHK NFDLLIDQLE QWRDAGYRML LATASDKQYE
RVEEILSERG SSSLLPKRVS LTLHEGFSDE ALRIVLLTDH QLFDRYHKYN LKSDKARSGK
VTLSLKELNQ FSQGDYIVHI DHGIGRFGGL ITTDVGGKRQ EVIKLIYRNN DIIFVNLHSL
HKLSKYKGGD SDAQVELSRL GTGAWQKLKE RTKKRVKDIA RDLIRLYAQR KEERGFAFSP
DSYLQHELEA SFLYEDTPDQ ERATAEVKAD MESDRPMDRL ICGDVGFGKT EVAVRAAFKA
ATDGKQVAIL VPTTVLAYQH YQTFRDRLQN FPVRIEYISR ARSAKDIKAI LHDLAEGRID
IIIGTHRLVS NDIRFHDLGL LVIDEEQKFG VAVKEKLRKL QVNVDTLTMS ATPIPRTLQF
SLMGARDLSN INTPPPNRYP VATELARFSP DIVREAVNFE MSRNGQVFIV HNRIDNIEEI
AGIVQREVPD ARVAVGHGRM SPTELERLIL DFVHYEYDVL VATTIIENGI DVPNANTIII
DDAHRYGLSE LHQLRGRVGR SNRKAFCYLL SPPLSVLSDD SRRRLQAIEN FSDLGSGIRI
ALQDLDIRGA GNVLGAEQSG FIADLGYETY SKVFNEAVSE LKADEFADLY AESQEAIPSA
SRFVVETTVE SDLELSFPEE YVPLDSERIL LYRELDNLST DEELDAFRRR MQDRFGKIPP
EGEELIRVPR LRRLGRSLGI EKIVLRGDQM SFHLVGKEDS PYYQSEVFGM LLEYIAAHTR
RCEIRQSGGK RIVRLREVPD VLTACELCTA ISTRSSAERI EL
//
