ID A0A1I7IEW0_9BACT Unreviewed; 1123 AA.
AC A0A1I7IEW0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=SAMN04487941_2156 {ECO:0000313|EMBL:SFU71390.1};
OS Pontibacter akesuensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Pontibacter.
OX NCBI_TaxID=388950 {ECO:0000313|EMBL:SFU71390.1, ECO:0000313|Proteomes:UP000182491};
RN [1] {ECO:0000313|Proteomes:UP000182491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18820 {ECO:0000313|Proteomes:UP000182491};
RA Varghese N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FPCA01000002; SFU71390.1; -; Genomic_DNA.
DR RefSeq; WP_068837475.1; NZ_FPCA01000002.1.
DR AlphaFoldDB; A0A1I7IEW0; -.
DR STRING; 388950.GCA_001611675_01385; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000182491; 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; 3.40.50.11180; -; 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; 2.
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:UP000182491}.
FT DOMAIN 576..737
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 758..912
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1123 AA; 128122 MW; 2A86552B7526BC82 CRC64;
MKVKDFLELY RLDGVVQTIA GRLKADEPYR LQIKGLAGSQ DAVLASAVYT LNYGHQLFIM
HDKEEAAYFY TDLKNLLGEE KDILLFPTSY KRPYSFDDTE NANILMRAEV LNRLNQKTGK
GELIVTYPEA LTEKVINKKS LVENTLGAKV GEKLDTAFLS EMLAEYGFER TEFVYEAGQY
AVRGGIVDVY SYANDLPYRI ELFGDEIESI RTFDPETQLS VETKKAISII PNVQTKLLQE
TREAFLDFIP ANTTLWFKDV RLTLDVIDEY FDKAAHNFEK MLATSGGTQI VSDPEQLFQT
QKQFKKLLEK FNVVEIGKRF HFKSSETIQL QAKPQPSFNK DFKRLVKDLH EQQGAGFVNI
IATDSPRQIN RLTMIFDELD HDVRFQHLPV SLREGFIDQT LKITCYTDHQ LFDRFYQHKA
KEGHSKSKAM TLKELRSLQP GDYVTHIDYG IGRFAGLEKV EVGGRLQEAI RLVYRDDDLL
YVSIHALHKI SKYSGKEGGP PSMSKLGSPE WENKKKRVKS KVKDIAHELI SLYAKRKAAP
GYAYTRDGFL QAELESSFIY EDTPDQGKAT EDVKADMEQP HPMDRLVCGD VGFGKTEIAI
RAAFKAACDG KQVAVLVPTT ILAMQHFRTF RDRLEQFPVT VDYVNRFKTA KDTKDTLKRL
AEGKVDILIG THRIVSKDVK FKDLGLMIID EEQKFGVKTK EKLREMKINV DTLTLTATPI
PRTLHFSLMG ARDLSVIATP PPNRQPVKTE LHVFDETLIR DAIVHEMKRG GQVFFVHNRI
KDIEEIAAMI LRHVPDCKVT YAHGQMEPEK LEKRMMKFVN GEYDVLVSTN IIESGLDIEN
ANTIIINRAH MFGLSDLHQM RGRVGRSNKK AYCYLLTPPV AGLPSDARKR LSTLEEFSDL
GEGFKIAMRD LDIRGAGNLL GGEQTGFITD LGFEMYHQVL DDAIKELKET EFRELFLGDN
LEQFIEPVRE CNIETDMEVL IPDWYVNNIS ERLNLYSKLD NVKSLDELEK LRASIVDRFG
ALPEQVQQLV EIVKLRWQAQ QLGFEKLTIK KEVMKGYLPS ENNDAYFQSD VFGNILKYVQ
QHPRRSRLKD AKHKLIVIVE DIQSIADAKE VFEGLGIAAA TSV
//
