ID A0A238KQA8_9RHOB Unreviewed; 1159 AA.
AC A0A238KQA8;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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:SMX44918.1};
GN ORFNames=MAA8898_03093 {ECO:0000313|EMBL:SMX44918.1};
OS Maliponia aquimaris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Maliponia.
OX NCBI_TaxID=1673631 {ECO:0000313|EMBL:SMX44918.1, ECO:0000313|Proteomes:UP000207598};
RN [1] {ECO:0000313|EMBL:SMX44918.1, ECO:0000313|Proteomes:UP000207598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8898 {ECO:0000313|EMBL:SMX44918.1,
RC ECO:0000313|Proteomes:UP000207598};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-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}.
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DR EMBL; FXYF01000008; SMX44918.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238KQA8; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000207598; 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}; Reference proteome {ECO:0000313|Proteomes:UP000207598}.
FT DOMAIN 619..780
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 801..955
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1159 AA; 127594 MW; 63984210FBC69FAF CRC64;
MTNERIIMGG APEGHDARLL LREVERAGGP VVHVARDDRR LAALRDALAF FAPNMPVVIF
PAWDCLPYDR VSPNADISAA RMATLAGLVH GMPARYILLT TLSAAMQYVP ARGVLREVAF
TARVGDRVNE EALRNFLVRM GFSLASTVTE PGDYAIRGGI IDIYPPGEGG PVRLDFFGDV
LDGARRFDPA SQRTTEKLEL VELAPVSEVI LDDSAITRFR QNYRIEFGAA GTDDPLYEAV
SAGRKHAGVE HWLPFFHEKL ETLFDYLPGA PVCLDDQLTP SRLSRWDSIA DQYDARRHAL
NQKKSLGSTV YKPIPPGLLY MDDAAWERAV DGRRVVQFHP LPQASGPGVV DAGGRIGRNF
APERQQESIS LFGALAAHVK ARMQDGPVLI ASYSEGARER LTGLIEDEGL AEAIPVANGT
RIGKRGLHLA VWSLEAGFDA PWEPAGPKGR LTVISEQDVL GDRLIRQPKK RRKAENFLTE
HQSLSPGDLV VHVDHGIGRY HGLEVVTAAG AAHECLTLEY AEGSKLYLPV ENIELLSRYG
HEEGLLDKLG GGAWQAKKAK LKQRIRDMAD RLIRIAAERA LRKAPIMDPP PGAYDSFAAR
FPYQETDDQL KAIEDVMEDM HSGMPMDRLI CGDVGFGKTE VAMRAAFVAA MSGVQVAVIA
PTTLLARQHY NGFAERFRGF PVQVAPLSRF VGSRQAALTR EGIAKGTVDI AVGTHALLAK
GIRFNNLGLL IIDEEQRFGV QHKERLKQLR SDIHVLTLTA TPIPRTLQLS LTGVRDLSII
GTPPVDRLSI RTYVSEFDPV TIREALLREH YRGGQSFFVV PRLTDLPEVE EFLRDQVPEV
TYVVAHGQMA AGDLDERMNA FYDGKYDVLL ATTIVESGLD IPTANTMIVH KADMYGLSQL
YQIRGRVGRA KTRAYCYLTT KPRTKLTVTA EKRLRVLGAI DTLGAGFSLA SQDLDIRGAG
NLLGEEQSGQ MRDVGYELYQ SMLEEAIAKI RAGEMEGLAE ADGQWAPTIN LGVPVLIPED
YVPDLDVRLG LYRRLSNLTT KVELEGFAAE LIDRFGKLPR EVNTLLLVVR IKAMCKKAGI
AKLDGGPKGA VIQFHNDKFA SPQGLVEFLK DQNGLAKVKD NKIVIRRDWT REKDKIQGAF
AIARDLADIL SAAKKQAKA
//
