ID U5T6S0_9GAMM Unreviewed; 1156 AA.
AC U5T6S0;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 53.
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=SPICUR_04695 {ECO:0000313|EMBL:AGY91917.1};
OS Spiribacter curvatus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Spiribacter.
OX NCBI_TaxID=1335757 {ECO:0000313|EMBL:AGY91917.1, ECO:0000313|Proteomes:UP000017640};
RN [1] {ECO:0000313|EMBL:AGY91917.1, ECO:0000313|Proteomes:UP000017640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAH-SP71 {ECO:0000313|EMBL:AGY91917.1,
RC ECO:0000313|Proteomes:UP000017640};
RX PubMed=24225341; DOI=10.1186/1471-2164-14-787;
RA Lopez-Perez M., Ghai R., Leon M.J., Rodriguez-Olmos A., Copa-Patino J.L.,
RA Soliveri J., Sanchez-Porro C., Ventosa A., Rodriguez-Valera F.;
RT "Genomes of "Spiribacter", a streamlined, successful halophilic
RT bacterium.";
RL BMC Genomics 14:787-787(2013).
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; CP005990; AGY91917.1; -; Genomic_DNA.
DR RefSeq; WP_023366555.1; NC_022664.1.
DR AlphaFoldDB; U5T6S0; -.
DR STRING; 1335757.SPICUR_04695; -.
DR KEGG; spiu:SPICUR_04695; -.
DR PATRIC; fig|1335757.3.peg.914; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_3_6; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000017640; 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; 3.40.50.11140; -; 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:UP000017640}.
FT DOMAIN 623..784
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 805..964
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 335..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1156 AA; 128542 MW; A97B6F1A7C406767 CRC64;
MPNTNPLLIH HDLPTRAGTR QDWLGLAGDA GALAIAETAA RHDGPLLLIT TGTAEAEELR
RGLRFFGVED IELMPDWEVL PYDVFSPHQD ITSERLRALH RLPRKQRGVV IVPAATLMQR
IAPPSFLEGT VIRLASGQRL DLEAMRTALQ ASGYRCVSEV LEHGEFAVRG AILDLYPMGA
EAPFRIDLFD DEIDTIRSFD PETQRSIDRL ESVELLPAHE FPTDEAGIKR FRRQYRARFE
GDPTASPVYQ AVSDGHIPNG IEAYLPLFFE ATATLFDYLP AGTLAIRVGA VDEQLAAEWS
QIGERYEQRR HDRERPLLPP ETLYLDPDAV RHGLHAGGQV DLPTDTHREP SRNRDRALSA
RPLPDLRTAP GDDTGVASLQ SFIDGFEGQV LLTAETAGRR EAFRERLQAA GIRVRDVSDW
AAFVADPPAL ALTVAPLDVG FRLEQAGLAV VPESALLGER AEQRRRRKSS PDRDPDAIIR
DLTDLSIGAP VVHEQHGIGR YQGLQTLAVD GIETEFLTLE YAAGDKLYVP VASLHLISRY
TGADDDGAPM HRLGSGQWEK ARKRAAQKAR DVAAELLDIY ARREAQQGEP HIVPAEDYAH
FANQFPFEET PDQQTAIHAV LQDLQQIRPM DRVVCGDVGF GKTEVAMRAA FAGIQSGRQV
AVLVPTTLLC QQHYQNFKDR FADWPVRIEQ LSRFQSARDQ SKTLEAITEG KVDVVIGTHK
LLQQSVRFKR LGLMIIDEEH RFGVRQKEAL KRLRANVDVL TLTATPIPRT LNMSLAGLRD
LSIIATPPAR RLAVKTFVNE WDETTIREAC LRELHRGGQV YFLHNDVDSI QRTAEALATL
IPEARVGTAH GQMPERELER VMLDFYHQRF NILVCTTIIE SGIDVPTANT IIINRADRLG
LAQLHQLRGR VGRSHHRAYA YLIAPPRRSQ TADAVKRLDA ISSLEDLGIG FALASHDLEI
RGAGELLGEG QSGQIHEVGF NLYSDLLDRA VQSLKAGKEP ALEQPLEQSA DVDLHISALL
PEDYLPDVHT RLVMYKRIAN APNAAALREL QVEMIDRFGL LPEPARNLLE IARIRQQVQA
MGISRFEVGP GGGVVQFGAS PQVDASALVR LVQEQPAVYR LEGQERLRIK RETETAEARI
ALVDRLLESM ALREAA
//
