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Database: UniProt
Entry: C8RZ39_9RHOB
LinkDB: C8RZ39_9RHOB
Original site: C8RZ39_9RHOB 
ID   C8RZ39_9RHOB            Unreviewed;      1147 AA.
AC   C8RZ39;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 72.
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   ORFNames=Rsw2DRAFT_1067 {ECO:0000313|EMBL:EEW25996.1};
OS   Rhodobacter sp. SW2.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodobacter.
OX   NCBI_TaxID=371731 {ECO:0000313|EMBL:EEW25996.1, ECO:0000313|Proteomes:UP000010121};
RN   [1] {ECO:0000313|EMBL:EEW25996.1, ECO:0000313|Proteomes:UP000010121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SW2 {ECO:0000313|EMBL:EEW25996.1,
RC   ECO:0000313|Proteomes:UP000010121};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Emerson D.;
RT   "The draft genome of Rhodobacter sp. SW2.";
RL   Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
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}.
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:EEW25996.1}.
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DR   EMBL; ACYY01000005; EEW25996.1; -; Genomic_DNA.
DR   RefSeq; WP_008028810.1; NZ_ACYY01000005.1.
DR   AlphaFoldDB; C8RZ39; -.
DR   STRING; 371731.Rsw2DRAFT_1067; -.
DR   eggNOG; COG1197; Bacteria.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000010121; Unassembled WGS sequence.
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; 3.40.50.11140; -; 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; IPR048635; MFD_D3.
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; PF21132; MFD_D3; 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:UP000010121}.
FT   DOMAIN          612..773
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          794..950
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1147 AA;  125558 MW;  714C63DE4D83DC47 CRC64;
     MAAADRITLG GAPKGYDARL LARELARGVP VIHVARDDKR MALMRAALAV MAPEAVVLDL
     PAWDCLPYDR VSPNPEICAR RMATLAALAQ GVAGPFVLLT TVSAATQRLP TRAVLAASSF
     SARVGDRVDE GALRGFLSRM GFSLVTTVTE PGDYALRGGI IDIYPPGPGG PVRLDFFGDV
     LDGARRFDPA TQRTIQKLSH VDLAPVSEVI LDEAAITRFR QAYRIEFGAA GVDDPLYEAV
     SAGRKHQGME HWLPLFHARL ETLFDYLPQA SVMLDDAVTA VRLSRWDGIA DQYDARREAL
     TAKGRMDTVY KPAAPALLYL DDADWEAALA PHRVVQLSPL PQSPGPGVLD AGGRAGRSFS
     AERQLESVSL FGALAAHIKA LREERQVVIA SWSEGARERL QGLLEDQGLR GAAHLKDMRD
     LPEGRGGLFL VVWALEQGFT APGLAVISEQ DVLGDRLISK PRKRRKAENF LAEVNSLSPG
     DLVVHVEHGV GRFRGLETIM ALGAPHECLA LEYAENARLY LPVENIELLS RYGHEEGLLD
     RLGGGAWQAK KAKLKDRIRE IAERLMRIAA ERHLRHAPIL EAPHAMWEAF AARFPYQETD
     DQLAAIADVV ADLEAGSPMD RLIVGDVGFG KTEVAMRAAF VAALAGMQVA VVCPTTLLAR
     QHYRSFHDRF RGFPIEIRPL SRFVTAKDAA ATRAGLADGT VDICIGTHAL LAKAIRFKSL
     GLLVIDEEQH FGVTHKERLK EMRAEVHVLT LTATPIPRTL QLSLTGVRDL SIIATPPVDR
     LAIRTYVSEF DGITVREALL RERFRGGQSF YVVPRISDLP EIEAFLRDHV PEVTHVIAHG
     QLAAHDLDER MNAFYDGKYD VLLATSIVES GLDIPAANTM IVHRADMFGL GQLYQIRGRV
     GRAKTRAYCY LTTKPRSPLT PQATKRLHLL GSLDSLGAGF NLASHDLDLR GAGNLLGEEQ
     SGHIQEVGYE LYQAMLEETI SKIKSGELQG LSRMDDQWAP QINLGVPVLI PEAFVPDLDI
     RLGLYRRLSA LSTKVELEGF AAELIDRFGA LPKEVNTLLL VVRIKSMCKR AGISRLDAGP
     KGATVQFHND KFANPAGLVD FIRAQTGARI KDNKIVLAAD WKTEAERIKG AFGIARDLAE
     KVVRPNG
//
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