ID G5SQE4_9BACT Unreviewed; 1133 AA.
AC G5SQE4;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 54.
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=HMPREF9441_01582 {ECO:0000313|EMBL:EHH00347.1};
OS Paraprevotella clara YIT 11840.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Paraprevotella.
OX NCBI_TaxID=762968 {ECO:0000313|EMBL:EHH00347.1, ECO:0000313|Proteomes:UP000003598};
RN [1] {ECO:0000313|EMBL:EHH00347.1, ECO:0000313|Proteomes:UP000003598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 11840 {ECO:0000313|EMBL:EHH00347.1,
RC ECO:0000313|Proteomes:UP000003598};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (MAR-2011) 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:EHH00347.1}.
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DR EMBL; AFFY01000022; EHH00347.1; -; Genomic_DNA.
DR RefSeq; WP_008619505.1; NZ_JH376597.1.
DR AlphaFoldDB; G5SQE4; -.
DR STRING; 762968.HMPREF9441_01582; -.
DR GeneID; 78582634; -.
DR PATRIC; fig|762968.3.peg.1416; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_3_10; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000003598; 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; 3.40.50.300; 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; 3.
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}.
FT DOMAIN 584..745
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 765..920
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1133 AA; 127669 MW; A1F0814C81398804 CRC64;
MEIQGLQALY AGHKSVKALA KALQDGSART IFAEGLCASA APLLFSSVAA ACPQVMACPY
VFVLDDAEEA GYFYHDLTQI LGEQEVFYFP SSFRRAVKFG QRDAANEILR TEVISRLSAG
HRPLFVVTYP EAVMEKVVSR QKLDEQTLRL HAGERVDITF VEETLRAFGF RRVDYVYEPG
QFAVRGSILD VFSFSSEWPY RVDFFGDEVD SIRTFEVQTQ LSRDKQEEIV IVPELAGYVQ
GKVPFTDFLP PETVLVMKDL FFLRDVADRV YADGFSAQAL MDEQARTEME EAERHEKLRA
DLMLVDGSAL MKGMLDFRRV EVGNKPSATP QATVRFHLTA QPIFHKNFEL VTRTFHEYLE
KGYTLYILAD SAKQTDRLAS IFTEQASGIG FTPVNRTLHA GFADDDLKAC FFTDHQIFDR
FHKYNLRSDK ARSGKVALSL KELQEFNIGD YVVHVDHGVG KFGGLVRIPN GDTMQEVIKI
IYQNDDVVFV SIHSLHKVSK YRGKEGEPPR LNKLGTGAWE RLKERTKTKI KDIARDLIKL
YSLRRQEKGF AFSPDSFMQH ELEASFLYED TPDQLKATQA VKADMERDRP MDRLVCGDVG
FGKTEVAIRA AFKACADNKQ VAVLVPTTVL AYQHFQTFSS RLKGMPVRVD YLSRARSAAK
TKEILRDLAD GKINIIVGTH KLIGKSVKFK DLGLLIIDEE QKFGVATKEK LRQMKVNVDT
LTLTATPIPR TLQFSLMGAR DLSVIQTPPP NRYPVQTEVH TFSAELIAEA VNFEMSRNGQ
VFIVNNRISS LYDLEALLHK HVPDARVCVG HGQMPPEELE NIIFGFVHYD YDVLVSTTII
ESGIDIPNAN TIIINGAQNF GLSDLHQMRG RVGRSNKKAF CYLLAPPLAA LTPEARRRLQ
AIENFSDLGS GIHIAMQDLD IRGAGNLLGA EQSGFIADLG YETYQKILSE AVKELKNDEF
GDLYAEEIRK GNDLGGENFV DECALESDLQ MSFPDDYVPS SSERMLLYRE LDGLERDEDV
EAFRLRMKDR FGEIPEEGEE LIRVVTLRRL GKCLGAEKIF LKAGRMVLYF VQNEKSAYFE
SKAFGQCIAY AAMNAHRSNL REANGRRSMV IQEVRSVKDA VGILRQISEL QAV
//
