ID A0A0M2LKG6_9SPHN Unreviewed; 1062 AA.
AC A0A0M2LKG6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=XM50_17850 {ECO:0000313|EMBL:KKI18035.1};
OS Sphingomonas sp. Ag1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1642949 {ECO:0000313|EMBL:KKI18035.1, ECO:0000313|Proteomes:UP000033997};
RN [1] {ECO:0000313|EMBL:KKI18035.1, ECO:0000313|Proteomes:UP000033997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ag1 {ECO:0000313|EMBL:KKI18035.1,
RC ECO:0000313|Proteomes:UP000033997};
RA Pei D., Yu W., Kukutla P., Xu J.;
RT "Draft Genome Sequences of Sphingomonas sp. Ag1 from Mosquito Anopheles
RT gambiae.";
RL Submitted (APR-2015) 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:KKI18035.1}.
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DR EMBL; LAZX01000094; KKI18035.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M2LKG6; -.
DR STRING; 1642949.XM50_17850; -.
DR PATRIC; fig|1642949.3.peg.1279; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000033997; 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 Gene3D; 2.40.10.170; -; 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 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};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KKI18035.1};
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 553..713
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 734..888
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1062 AA; 112922 MW; 1AFF6EA69D1B1479 CRC64;
MRPRSEAEIA VMTPRADVPA PTLSIAEASA AVAELLADAN VIVAVADETR ALALTRMVAA
LVPDATTMFC PGSDALPGDN APASPANVGQ RVSALRAIRR ALEAEAPGRI ALITSGEALA
RAYPAPAAFD AEPPSVAVGQ PCDLAQLHDD LLSLGYVADE RVDEPGEVAL RGQVLDVFPA
DSDLPLRIEV VDGVIAGIRG YDPADQRSTD EMERHELGRV MEPPLDGDRT TLLDHLPGAL
VVVTAAADER RRRLLLLSAD TAKRGSRRAP ADMIADAAWQ KALAARDAAS LDRAGEPPAR
FVEQRAPLAA FARAAQAAIA DGERVVLIGG ERDVRFLTRR IEQRLKLTAE AVADWAGVGA
AAPGTLLTLT GPADQGFRRD GVLAIAAADL IGSRAEREDG SAHRVDLSLV HSAEIRVGDT
VIHEDHGIGV VDGIEPLPAG EGVGGDTIKL IYAKDAVRLV PVAEADRLWR YGAEDDAVTL
DTLDGKSWHD RRGEIAAAIA ETARGLTELA EKRATRTAPV LDPPVAAYER FAAGFPFSET
PDQLAAIEAV RNDLSSGRPM DRLVIGDVGF GKTEVALRAA ALAALAGKQV AIAAPTTVLA
RQHLESFTAR FEGTDVVVAG LSRLTSAADK RRVKAGLADG SIHIVIGTGA VAGKGVAYKD
LALVIIDEEQ RFGTADKNKL QALSAGHVLT LSATPIPRTL QAALVGLRQL SVIATPPARR
QPIRTAVSAF APETLRAALL RERARGGQSF VVVPRIADMA PLAEKLATLV PELEILHAHG
KMPAADIDDT MVRFGHGDGD VLLATNIIEA GLDVPRANTM AIIHADRFGL SQLHQLRGRV
GRGHRRGQVL LFTEADDAIA PRTLKRLRTL EAFDRLGAGF AISARDLDMR GAGDLLGDTQ
AGHMRLIGVE LYQQLLEDAL RTARGETVER WTPDLRLGID GRLPAEWIPD EDLRISLYAR
LGRLRSDADL DAFEAELEDR FGELPEEAAL LLSIARVRER ARALGIARID AGPAAIALTP
RRDAPPALGE IDGLVEKDGR LLLKEPHEDA AERLERLAAL LA
//
