ID A1K635_AZOSB Unreviewed; 1150 AA.
AC A1K635;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 110.
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:CAL94290.1};
GN OrderedLocusNames=azo1673 {ECO:0000313|EMBL:CAL94290.1};
OS Azoarcus sp. (strain BH72).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Azoarcus.
OX NCBI_TaxID=418699 {ECO:0000313|EMBL:CAL94290.1, ECO:0000313|Proteomes:UP000002588};
RN [1] {ECO:0000313|EMBL:CAL94290.1, ECO:0000313|Proteomes:UP000002588}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH72 {ECO:0000313|EMBL:CAL94290.1,
RC ECO:0000313|Proteomes:UP000002588};
RX PubMed=17057704; DOI=10.1038/nbt1243;
RA Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J.,
RA Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C.,
RA Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J.,
RA Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.;
RT "Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp.
RT strain BH72.";
RL Nat. Biotechnol. 24:1385-1391(2006).
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; AM406670; CAL94290.1; -; Genomic_DNA.
DR RefSeq; WP_011765406.1; NC_008702.1.
DR AlphaFoldDB; A1K635; -.
DR STRING; 62928.azo1673; -.
DR KEGG; azo:azo1673; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_3_4; -.
DR Proteomes; UP000002588; 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:UP000002588}.
FT DOMAIN 622..783
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 804..958
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1150 AA; 127923 MW; 339423929A885EC8 CRC64;
MPRSFDSLLP AIARLAFPKP GTRLDLPALA GSADALAIAQ LAGQGRMIAV ITANPIDAQR
LQDELAWVAP DLRSHLLPDW ETLPYDSFSP HQDLISERLS TLYAVSRGEV DVVLVPAPTA
LYRLAPPAYL AAYTFFMKQG DRLDVEALRK QMALAGYAHV TQVVSPGEFS VRGGLVDLYP
MGSALPYRID LFDDEVESIK TFDPDSQRTV YPTKEIRLLP AREFPLDDKG RTHFRSRFRE
SFEGDPTRAA VYKDVSNGIA PAGIEYYLPL FFDETATLFD YLPTDVPVLL HRDVPGAIAE
FWRDTRSRYD LLKGDRSRPV MPPEQLFLSE EAFFLALKDR PRIAIGADSK LADAALPLPE
LAVERKATDP LHKFKAFQAG EWGRDGGRIL LLADSPGRRE TMAEFLAEYG LKPAASADFA
GFLDTDAPLA LGVAPLAAGF LLPDAKIAVV TEAELYATTA RSRARRESKK AATMEGWLRD
LSELKLGDPV VHVSHGIGRY LGLIHMNLGE GDTEFLHLEY NGGDKLYVPV SQLHVITRYA
GADPEAVDLH RLGSGQWEKA KKKAAMQVRD TAAELLALYA QRAARPGHRF DFKQHDLEAF
AEAFGFETTP DQQAAIDAVV GDMKSGRPMD RLVCGDVGFG KTEVALRAAF IAVADGKQVV
VLCPTTLLAE QHYQTFADRF ADWPIKIAEL SRFKSAKEQA EALKQLGEGK VDIIIGTHRL
LQKDVLFKRL GLVIIDEEHR FGVRQKEALK QLRSEVDILT LTATPIPRTL GLAMEGLREF
SVIATAPQKR LAIKTFVQRW SKGIVREAVL REFKRGGQVY FLHNEVDTIE NVRNELAELL
PEARIVVGHG QLPERELERV MRDFTQQRAN LLLCTTIIET GINIPTANTI VINRADRFGL
AQLHQLRGRV GRSHHQAYAY LLTDAHAKPT AQAQKRLEAI SMMEELGSGF YLAMHDLEIR
GAGEVLGENQ SGEIQQVGFS LYTEMLKRAV KDLQAGKEPD LSQPLEVVSE INLHTPALLP
TDYCPDVQER LTLYKRLANC ESEDDLRALQ EELIDRFGEL PPQTVALIET HRLRLLVQSR
GVQKLDASEA QISVQFGPNP PIDPAKVIFL IQKDKSTKMA GPDKLIRRAN LPDLRQRVKA
VRELLDAVKL
//
