ID S2VK17_9ACTO Unreviewed; 1239 AA.
AC S2VK17;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 50.
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=HMPREF9237_01620 {ECO:0000313|EMBL:EPD26340.1};
OS Actinotignum schaalii FB123-CNA-2.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinotignum.
OX NCBI_TaxID=883067 {ECO:0000313|EMBL:EPD26340.1, ECO:0000313|Proteomes:UP000014393};
RN [1] {ECO:0000313|EMBL:EPD26340.1, ECO:0000313|Proteomes:UP000014393}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FB123-CNA-2 {ECO:0000313|EMBL:EPD26340.1,
RC ECO:0000313|Proteomes:UP000014393};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Saerens B., Vaneechoutte M.,
RA Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Actinobaculum schaalii FB123-CNA2.";
RL Submitted (MAY-2013) 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:EPD26340.1}.
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DR EMBL; AGWM01000012; EPD26340.1; -; Genomic_DNA.
DR RefSeq; WP_016443224.1; NZ_KE150263.1.
DR AlphaFoldDB; S2VK17; -.
DR STRING; 59505.FB03_04565; -.
DR PATRIC; fig|883067.3.peg.1592; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_2_2_11; -.
DR Proteomes; UP000014393; 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; 3.
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:UP000014393}.
FT DOMAIN 683..844
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 869..1019
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 50..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1239 AA; 134116 MW; F3D8E6FE3F66D326 CRC64;
MQLESLLPLI GADPALSRAA ASTATRLDIP MPRGVVPPAL AYLAGSGGPG GPGGFSGPGG
PTGPSGSSGP TGSTAAHPLH VAITASGREA EILEGAMRAY LPAEQIAVFP SWETLPHERL
SPRSDTVARR LLTLRRLAHP EEFEPLRLLI MPVRALLQPI TRGLGDLAPV RLRLREDAPM
EEVENALVNA AYTRVDMVER RGQFAVRGGI LDVFPPTERH PIRVEFFGDT VDEIRTFSVG
DQRSMEEREE IYAPPCREIL LTESVRTRAR SLISELPGAT DMLDKIAAGI APEGMESLTP
VLVDGMDAVV DVLPADARLL IIEPERVDQR AESLIATTEE FLAAAWSAAA AGGTPPVQAN
AASFASVAAT REAALTRGQA WWTLGGFSGN ALSGNALPGN VTSTAGTFKN DDAGAAVAAR
EPRKFLGKVD EALAAIGEQA RRGVRQVLVV DGPGLARRYA EQLGELDVPA SAVAEVPTHL
DSGVVYVVAA PIAEGFVLEG QQLGVYAGAD LTGRGGSSTR DMRALPKRRR KNAVDPLSLT
PGDFVVHDRH GVGRFVRMEK RAIGGKGGQR EYIVLEYAPS RRGGPPDQLW VPTDQLDQVS
KYSGGESPSL NKMGGADWEK TKSKARAATR KIAAELIRLY AQRMATPGIA FSPDTPWQRE
LEDAFAYVET PDQLHTIDEV KADMEKPVPM DRLISGDVGY GKTEIAVRAA FKAVQDGRQV
AVLVPTTLLV EQHRETFEER YAGFPVRVAA LSRFQNARES EEVIAGLADG TIDVVIGTHR
LLTGNVRFKA LGLVVIDEEQ RFGVEHKETL KQMYPNIDVL SMSATPIPRT LEMAVTGVRE
MSTLATPPEE RHPILTYVGA RENRQISAAI RRELLRDGQV FYVHNRVGDM GRVAAQLGEL
VPEARIAVAH GKMSERDLEN VIQNFWEHEI DVLICTTIVE TGLDISNANT LIVDNADKLG
LSQLHQLRGR VGRGRERAYA YFLYDPDRAL TETSLERLRT IAANTDLGAG TQVAMKDLEI
RGAGNMLGGE QSGHIEGVGF DLYVRMVSEA VAKIRGEIPS DDDASSDVRI ELPVEAYLPE
DYVPSERLRL EIYTKLAASR GEDQREEIRA ELRDRYGEIP EVAARLFRIA QLRDLARSAG
LEEITQMGRN VRFAPVALPD SRQARLKRLY PGAMLKPAVR VLMVPVPPAQ VGGAMSARPG
VMGAAQTSAR LGTGAPMEGD ELLEWVSRLV TAVFISSVG
//
