ID A3SPK2_ROSNI Unreviewed; 1153 AA.
AC A3SPK2;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 85.
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=ISM_16040 {ECO:0000313|EMBL:EAP76392.1};
OS Roseovarius nubinhibens (strain ATCC BAA-591 / DSM 15170 / ISM).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=89187 {ECO:0000313|EMBL:EAP76392.1, ECO:0000313|Proteomes:UP000005954};
RN [1] {ECO:0000313|EMBL:EAP76392.1, ECO:0000313|Proteomes:UP000005954}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-591 / DSM 15170 / ISM
RC {ECO:0000313|Proteomes:UP000005954};
RA Moran M.A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (DEC-2005) 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:EAP76392.1}.
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DR EMBL; AALY01000002; EAP76392.1; -; Genomic_DNA.
DR RefSeq; WP_009815217.1; NZ_CH724156.1.
DR AlphaFoldDB; A3SPK2; -.
DR STRING; 89187.ISM_16040; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_3_5; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000005954; 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; 3.40.50.11140; -; 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; 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; 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:UP000005954}.
FT DOMAIN 611..772
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 793..947
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1153 AA; 126778 MW; A9EC9C3F1F614A98 CRC64;
MAEQFKFTVG GAPEGFDARL ILQESDKSGG PVIHVARDDK RMVAMQAALR FFAPDLPVIT
FPGWDCLPYD RVSPNADISA TRMATLAALA HGMSGRFVLL TTLNAATQKL PAREVLQSAA
FAAQVGERID EEALRAFLVR MGFTQAPTVT EPGDYAIRGG IIDIYSPGDA GPVRLDLFGD
VLDGVRRFDP ATQRTVAKLD QIELAPVSEV ILDEAAITRF RQNYRIEFGA AGTDDPLYEA
VSAGRKHQGI EHWLPFFHAR LETLFDYLPG ASVTLDDQSA AMRDARWVSV VDQYETRQHA
LKTKGRDETI YKPVPPGQLY LDGAGWDAAV AGRRVLAFSP LPQAPGPGII DAGARVGRNF
SPERQQEDVN LFAALKTHVE ARMSAGPVLI AAYSEGARER LEGLVEDEGL LGAVSVTDAK
GLRGQGLYLT VWGLEHGFET PDLTVIAEQD ILGDRLIRAP KRRRKAENFL TEAQSLSPGD
LVVHVDHGIG RYHGMEVISA AGAAHECLLL EYAENARLYL PVENIELLSR YGHDEGLLDR
LGGGAWQAKK AKLKERIREM ADRLIRVAAE RALRKAPVLE PEHHAWEAFS ARFPYQETDD
QLGAISDVME DLGSGRPMDR LICGDVGFGK TEVAMRAAFV AAMSGQQVAV IAPTTLLARQ
HYQSFAERFR GFPVNVAPLS RFVSAGEATK TREGLARGKV DIVVGTHALL AKSVRFENLG
LLIIDEEQRF GVAHKERLKQ MRSDVHVLTL SATPIPRTLQ LSLSGVRDLS IIGTPPVDRL
SIRTYVSEFD RVTVREALLR EHYRGGQSFY VVPRVSDLPE IEEFLRNEVP EVTFAVAHGQ
MAAGELDARM NAFYDGKYDV LLATTIVESG LDIPRANTMI VHRADMFGLA QLYQIRGRVG
RSKLRAYAYL TTKPRVKLTP AAEKRLRVLS SLDTLGAGFT LASQDLDIRG AGNLLGEEQS
GQMRDVGYEL YQSMLEEAIA KIKSGDLEGL SEADGQWAPQ INLGVPVLIP EDYVPDLDVR
LGLYRRLSGL ETKVELEGFA AELIDRFGKL PREVNTLLLV VRIKAMCKKA GIAKLDGGPK
GATIQFHNDK FASPQGLVEF VQAQDGLAKI RDNKIVVRRD WRKDGDKIKG AFAIARDLAE
KVVAEKKRTS AQK
//
