ID A0A2D8PAK9_9RHOB Unreviewed; 1157 AA.
AC A0A2D8PAK9;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
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:MAM62409.1};
GN ORFNames=CMH11_13045 {ECO:0000313|EMBL:MAM62409.1};
OS Maritimibacter sp.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Maritimibacter.
OX NCBI_TaxID=2003363 {ECO:0000313|EMBL:MAM62409.1, ECO:0000313|Proteomes:UP000224593};
RN [1] {ECO:0000313|Proteomes:UP000224593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tully B.J., Graham E.D., Heidelberg J.F.;
RT "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from the
RT Global Oceans.";
RL Submitted (SEP-2017) 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:MAM62409.1}.
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DR EMBL; NZNT01000021; MAM62409.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2D8PAK9; -.
DR Proteomes; UP000224593; 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; 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}.
FT DOMAIN 613..774
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 795..949
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1157 AA; 127130 MW; DFA57A15173C0F3C CRC64;
MASRDHITLS GAPEGFDALL VSRELEKSGG PVVHVARDDK RLAAMQAALA FLAPRVTVLT
FPGWDCLPYD RVSPNPDVSA ARMATLAALA HGVPGPFVLL TTLNAATQRL PAREVLAEAS
WSASVDNRID VDGLRSFLVR MGFSQAPTVT EPGDFAVRGG IIDIFPPGEA GPVRLDLFGD
VLDGARRFDP VTQLTTETLS AVELAPVSEI ILDETAIARF RRNYRVEFGA GGADDPLYEA
VSAGRKHAGM EHWLPFFHER LETLFDYVPG ASVMLDDQTG PARIARWEGI ADQYDTRAAA
MKDRNRLDTV YKPCPPEQLY LDEEAWTGAL ADLRVLQLTE LPQPTGAGVL DGGGRIGRNF
APERQQEKIN LFEVLAEHIR VRRDVGPVVV ASYSEGARER VGGLLADEGL TAQTEIADFR
DVPLDKGGLY LAVWPLEHGF EAPGLTVISE QDVLGDRLIR APKRKRRAEN FLTEHQSLSP
GELIVHVDHG VGIYRGLETV EALGAPHDCV LLEYAGGDRL YLPVENIELL SKYGHEQGLL
DKLGGGAWQA KKARLKERIR EIADKLIRLA AERALRKAPV LEAPHHAWEE FAARFPYTET
DDQLSAIADV IEDLSAGSPM DRLICGDVGF GKTEVAMRAA FVAAMTGMQV AVIAPTTLLA
RQHYKSFAER FRGFPIQVGQ LSRFVGQAES TRTREGMKDG SVDIVVGTHA LLSKGTRFKN
LGLLVIDEEQ RFGVTHKERL KELRSDVHVL TLSATPIPRT LQMSLTGVRD LSIIGTPPVD
RLSIRTYVSP FDTVTIREAL LREHYRGGQS FFVVPRVKDL PEIEDFLKTQ VPEVTYVVAT
GQMAAGELDD RMNAFYDGKF DVLVATTIVE SGLDIPTANT MVIWRADMFG LAQLYQIRGR
VGRAKTRAYC YLTTKPRVPL TPGAEKRLKV LGSLDSLGAG FALASQDLDI RGAGNLLGEE
QSGNMNEVGY ELYQNMLEEA ISKIRSGELE GLTEANETWA PQINLGVPVM IPESYVPDLD
VRLGLYRRLS DLTTKVELEG FAAELIDRFG KLPKEVNTLL LIVRIKGMCK RAGIARLDGG
PKGATIQFHN DKFASPTGLV EFMQAQNGLA KVKDNKIIVR RDWKRDSDKI KGAFAIARDL
AEKVVAEKKK AKARKNA
//
