ID A0A0Q8R2Q9_9SPHN Unreviewed; 1162 AA.
AC A0A0Q8R2Q9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=ASE22_18605 {ECO:0000313|EMBL:KRB89658.1};
OS Sphingomonas sp. Root720.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736595 {ECO:0000313|EMBL:KRB89658.1, ECO:0000313|Proteomes:UP000051570};
RN [1] {ECO:0000313|Proteomes:UP000051570}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root720 {ECO:0000313|Proteomes:UP000051570};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB89658.1, ECO:0000313|Proteomes:UP000051570}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root720 {ECO:0000313|EMBL:KRB89658.1,
RC ECO:0000313|Proteomes:UP000051570};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KRB89658.1}.
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DR EMBL; LMID01000013; KRB89658.1; -; Genomic_DNA.
DR RefSeq; WP_056363742.1; NZ_LMID01000013.1.
DR AlphaFoldDB; A0A0Q8R2Q9; -.
DR STRING; 1736595.ASE22_18605; -.
DR Proteomes; UP000051570; 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; IPR048635; MFD_D3.
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; PF21132; MFD_D3; 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:UP000051570}.
FT DOMAIN 632..793
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 814..967
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1162 AA; 127736 MW; 4697364AF42993AA CRC64;
MIDLPRILKA SEALTLSRAP SGFQPWLLAD LARAVAAKDG RVVFVAADDQ AMQAVADAAR
YFLPELSVLM FPAWDCLPYD RASPALRATS ERLAALHALQ AKPLGPTLVA TTVNAVTQRV
LTPFRIRQLV ARLAPGERID RDKLAALLQA NGYLRTDTVT DHGEYAVRGG LVDLFPSGEP
HALRLDFFGD EIESVRQFDA TDQRTIGPID GFTLLPASEA LLDEETIKRF RGRYRERFGA
AATGDPIYQA VSDGRRLAGM DHWLPLFEER LETLFDHLSP DDLIVREAGS IKAAEARFEA
IGDYHANRVR ARSSDPGSYR PLEPDELYLG AGEWQAAIAD RPIHLVTPFA EPESARVIDL
GVDGARDFAP ERNQGVNIYD AVVEHAEALG KAGKRVVLAN YSAGSRDRFA GLLQEHGLDR
VDLVDDWQAA IAQPASGKSL GSGMARVALA VLPLDHGFTS GDIALLTEQD MLGDRLVRRQ
KRKKSADAFL AELATLSPGD LVVHMDHGIG RYEGLTSIPV AKAPHDCVAL SYAGGDKLYV
PVENIDVLSR YGAENEGVQL DKLGGVAWQA RKARMKERIR EIAGELIKTA AERALRPAEA
IEPGSGYNEF VDRFPYQETE DQDRAIADVI EDLAAGKPMD RLICGDVGFG KTEVALRAAF
VAAMGGMQVA LICPTTLLAR QHYRNFVDRF HGMPVNIGHL SRLVTSGEAK RTKDGMADGS
IDIVIGTHAL LAKGIEFKRL GLVIVDEEQR FGVTHKERLK ALKTDVHMLT LTATPIPRTL
QMAMSGLREL SVIQTPPVDR LAVRTYVAPW DGVVIREALL REHYRGGQSF LVTPRIKDLP
DIEEYLRKEV PEVSYVVAHG QMAASEVEER MSAFYDKKFD ILVSTTIIES GLDIPSANTL
IINRADRFGL AQLYQLRGRV GRSKTRAYAY LTTGDKGLTE TAEKRLHILQ NIDTLGAGFQ
IASHDLDIRG AGNLLGDEQS GHIKEVGFEL YQSMLEEAIL EAKAGGLAPL KRESFSPQIN
VDAPILIPEN YVPDLDLRMG LYRRMNEVET RAEIEAFAAE LIDRFGKLPA ATQNLLTVIE
IKLNCRKACV AKIDTGPRGA LVTFHEDNFP DLPGLLAYVD RLKDSARLRP DSKLVITRHW
PDPSHRLHGA LQLSRGLAKI VG
//
