ID A0A0Q4Q455_9SPHN Unreviewed; 1152 AA.
AC A0A0Q4Q455;
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=ASE90_02685 {ECO:0000313|EMBL:KQN91709.1};
OS Sphingomonas sp. Leaf67.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736230 {ECO:0000313|EMBL:KQN91709.1, ECO:0000313|Proteomes:UP000051342};
RN [1] {ECO:0000313|EMBL:KQN91709.1, ECO:0000313|Proteomes:UP000051342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf67 {ECO:0000313|EMBL:KQN91709.1,
RC ECO:0000313|Proteomes:UP000051342};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN91709.1, ECO:0000313|Proteomes:UP000051342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf67 {ECO:0000313|EMBL:KQN91709.1,
RC ECO:0000313|Proteomes:UP000051342};
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:KQN91709.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMLP01000001; KQN91709.1; -; Genomic_DNA.
DR RefSeq; WP_055995560.1; NZ_LMLP01000001.1.
DR AlphaFoldDB; A0A0Q4Q455; -.
DR STRING; 1736230.ASE90_02685; -.
DR Proteomes; UP000051342; 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}.
FT DOMAIN 621..782
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 803..957
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1152 AA; 126590 MW; 5D57E9DD4562AE66 CRC64;
MPDLSKILSA PRSLTLSGVP AGFLPALLAD LARGSKGDLV YIAPDEATMR AIATTAPFFA
PDLSVLQFPA WDCLPYDRAS PTLRSMAERL SALHTLQSKA KGPRLIVTTV NAATQRTLTP
FRIRQLVARL APGERISLPR LSTLLQANGY NRVDTVHDAG EFAVRGGLVD LWPSGSDSGL
RLDFFGDEIE TVRTFSPEDQ RTTGRVDGFT LLPASEALLD EESIKRFRTR YREKFGATAT
GDPIYQAISD GRRLSGMEHW LPFFEERLET FFDHLSPEAV IVRDAGVPAA AEQRFESIAD
YHTNRVRAQT SDPGSYRPLL PAALYLSADE WVERLSDTAA HQVTPFHAPD SATSVDFEVD
GPRDFTPERT QQANIYEAVV DHIAALRKQG RKPILASYSE GARERLMGLL ADHDLTGVST
VETWQQALGG AKSTVSFVVL PLDHGFTAAD VAVLTEQDML GDRLVRRAKR RKNTDAFLQE
LATLSPGDLV VHADHGIGRY VGLTQVPVAK APHDCVQLEY AGGDKLYVPV ENLEVLSRYG
AGEEGASLDR LGGEAWQRRK ARMKDRIREI AGDLIATAAK RAMRPADIAE PDSGGYPAFV
DRFPYQETDD QERAIADVLE DLGAGRPMDR LVVGDVGFGK TEVALRAAFV AAMAGMQVAI
VCPTTLLARQ HYNNFKARFE GFPIEIGRLS RLVTATEAKK VRDGLTDGTI DVVVGTHAVL
SKQVDFKRLG LVIVDEEQRF GVTHKERLKA MKADVHVLTL TATPIPRTLQ MAMSGLRELS
VIQTPPVDRL AVRTYIMPWD PVVLREALLR EHYRGGQAYF VTPRIADLPD IEKFLTEEIP
EIRYVVAHGQ MAPTEVEERM SAFYDKRYDL LVSTTIVESG LDIPSANTLI INRADKFGLA
QLYQLRGRVG RSKTRAYAYM TTPPERLVSE AAEKRLKVLS DLESLGAGFQ LASHDLDIRG
AGNMLGDEQS GHIKEVGFEL YQSMLEEAIL DAKAGGIRDD KPKDFSPAIT VDAPILIPED
YVPDLDLRMG LYRRLNDVED RAGIDAFATE LIDRFGKLPL ATANLLQLIE AKLNAKKACV
AKIDIGAKGA IVSFHEDKFP SVEGLLAYVD KLAGTAKLRP DMKLVISRSF GDPQARLNAA
LQISRGLAKA AG
//
