ID A9HIY2_GLUDA Unreviewed; 1131 AA.
AC A9HIY2;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 103.
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:CAP55829.1};
GN OrderedLocusNames=GDI1886 {ECO:0000313|EMBL:CAP55829.1};
OS Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / CCUG 37298
OS / CIP 103539 / LMG 7603 / PAl5).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconacetobacter.
OX NCBI_TaxID=272568 {ECO:0000313|EMBL:CAP55829.1, ECO:0000313|Proteomes:UP000001176};
RN [1] {ECO:0000313|EMBL:CAP55829.1, ECO:0000313|Proteomes:UP000001176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49037 / DSM 5601 / CCUG 37298 / CIP 103539 / LMG 7603 /
RC PAl5 {ECO:0000313|Proteomes:UP000001176};
RX PubMed=19775431; DOI=10.1186/1471-2164-10-450;
RA Bertalan M., Albano R., Padua V., Rouws L., Rojas C., Hemerly A.,
RA Teixeira K., Schwab S., Araujo J., Oliveira A., Franca L., Magalhaes V.,
RA Alqueres S., Cardoso A., Almeida W., Loureiro M.M., Nogueira E., Cidade D.,
RA Oliveira D., Simao T., Macedo J., Valadao A., Dreschsel M., Freitas F.,
RA Vidal M., Guedes H., Rodrigues E., Meneses C., Brioso P., Pozzer L.,
RA Figueiredo D., Montano H., Junior J., Filho G., Flores V., Ferreira B.,
RA Branco A., Gonzalez P., Guillobel H., Lemos M., Seibel L., Macedo J.,
RA Alves-Ferreira M., Sachetto-Martins G., Coelho A., Santos E., Amaral G.,
RA Neves A., Pacheco A.B., Carvalho D., Lery L., Bisch P., Rossle S.C.,
RA Urmenyi T., Kruger W.V., Martins O., Baldani J.I., Ferreira P.C.;
RT "Complete genome sequence of the sugarcane nitrogen-fixing endophyte
RT Gluconacetobacter diazotrophicus Pal5.";
RL BMC Genomics 10:450-450(2009).
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; AM889285; CAP55829.1; -; Genomic_DNA.
DR AlphaFoldDB; A9HIY2; -.
DR KEGG; gdi:GDI1886; -.
DR Proteomes; UP000001176; 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:UP000001176}.
FT DOMAIN 594..755
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 776..930
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1131 AA; 124971 MW; 62B5513A65B177EA CRC64;
MARRAREHDG PVLHVARDDA GMARIGELLS FVAPNAEILR FPSWDCLPYD RVSPNPAIVA
ERVATLTRLL EPATAPRIVL TTVGGLVQRV APRAAFRGQS LTLAAGDSLD QALLIDLLVA
AGYNRTDTVM EPGEFATRGG IFDIFPSGEA EPVRLDLFGD EVENIRRFDP ATQRSSDRLD
RFVMRPVADF TLDQASISRF RTGWRDLFGP AAASDPLYEH VSDGRRHAGL EHWLPLFHEH
LETLVDYLPG VSIILAHQVE DVLAARLEMI ADHFEARRQP VREGEVPYRA LPPHLMYLDR
KGWDGILSGH PVMLFSPFAR PDNAGGVDAG GRPGILFASV AGGGARENVF AMLDTQVRQW
AETGRRAYVS AWTRGSRERI ATLLREHGMR VETFDGWARA QDLPPGTVGL LTLGLERGFI
ADNLAFVSEQ DLLGERISRP PRRRKKADQF IAEASEIAEG DLVVHQDYGI GRYDGLETIG
VGTAPHDCLR LIYDGNEKLF LPVENIELLS RFGSDQAGVA LDKLGGASWQ NRKARMKQRI
RDMAGELIRT AALRALREAP SMTPAEGMWD EFCARFPFVE TEDQSRAIAD VLEDMGSGRP
MDRLVCGDVG FGKTEVALRA AFVAALSGAQ VAVVVPTTLL ARQHFRTFSA RFSGLPITVA
QLSRMVTPKE ATAVRKGLAD GTINIVIGTH ALLAKGVQFA DLELLIIDEE QHFGVAHKEK
LKALREDVHV LTLSATPLPR TLQLALTGVR EMSLIATPPT DRLAVRTFIM PFDSVVIREA
IQRERFRGGQ IFCVVPRIED LDRMAARLQD IVPDARLVQA HGRLTPTELE RVMTEFSDGK
YDILLSTNIV ESGLDMPAVN TLIIHRADMF GLGQLYQLRG RVGRGKQRGY AYLTWPQTHV
LSAAAEKRLE VMQTLDTLGA GFTLASHDLD LRGAGNLLGD EQSGHIREVG IELYQQMLED
AVAELRVEKG RRKAQDRDWT PNIILGLPVL IPETYVPDLP VRLGLYRRIA GLANDAEIEA
MEAELVDRFG TMPDEVRNLL DVVAIKRLCR EAGVERLEAG PKGMVIQFRG NSFANPGGLV
TWIAAHKEGN VRLRPDHKLA LVREMTNAQR IRLAKDTVQT LGRLAGQEKA A
//
