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Database: UniProt
Entry: A0A1I5RYA8_9SPHN
LinkDB: A0A1I5RYA8_9SPHN
Original site: A0A1I5RYA8_9SPHN 
ID   A0A1I5RYA8_9SPHN        Unreviewed;      1153 AA.
AC   A0A1I5RYA8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=SAMN04488241_104187 {ECO:0000313|EMBL:SFP62986.1};
OS   Sphingomonas rubra.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=634430 {ECO:0000313|EMBL:SFP62986.1, ECO:0000313|Proteomes:UP000199586};
RN   [1] {ECO:0000313|EMBL:SFP62986.1, ECO:0000313|Proteomes:UP000199586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.9113 {ECO:0000313|EMBL:SFP62986.1,
RC   ECO:0000313|Proteomes:UP000199586};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOXP01000004; SFP62986.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5RYA8; -.
DR   STRING; 634430.SAMN04488241_104187; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000199586; 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; 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};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:SFP62986.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000199586}.
FT   DOMAIN          623..784
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          805..959
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1153 AA;  126041 MW;  64702195BAE8D11B CRC64;
     MPDLKTILSA KASLTLAGVP TGFQPSLLAD LARAAGRVVF VAADDAAMRA IAATAPFFAP
     ELEVVTFPAW DCLPYDRASP TLRVMAERVA ALHRLQAKAK GPQLVLATAN AATQRVLTPF
     RIRQLVASLA PGERIGRDDL ATLLQANGYV RTETVHDHGE YAVRGGIVDL YPSGEEHALR
     LDFFGDEIES VRSFDPADQR TIGRVDGFTL LPASEALLDA ESIKRFRTRY REKFGATATG
     DPLYQAVSDG RRLAGMEHWL PLFEDKLATL FDHLGDALVV RDAGVAAAAE GRFEAIADYY
     ENRMRAEGQQ PGSYRPLPAK ALYLDAEEWA TRLGETTAHV TTAFHEPESA RVVDFGVDGP
     RDFAPERANQ ANVYEAVVDH LEKLRKDGRK PVLASYSGGS RDRLASLLKD HGLKGGKPVD
     TWQEARGHAD TTRSFGVAMV VLPLDHGFTA PGIAVLTEQD MLGDRLIRRN KRKKSADAFL
     AELATLSPGD LVVHADHGIG RYEGLTSIPV GKSPHDCVAL SYAGGDKLYV PVENLEVLTR
     YGSGEDGASL DRLGGEAWQR RKSKMKERIR EIAGELIATA AERALRPGEV AEPDSSGYPS
     FVDRFPYEPT DDQDRAIDDV LGDLSAGRPM DRLIVGDVGF GKTEVALRAA FVAAMGGMQV
     AVVCPTTLLA RQHYNNFCQR FEGFPIKVGR MSRLVGTAEI KMVKEGAASG DLDVVIGTHA
     LLAKNVSFKR LGLVIVDEEQ RFGVTHKERL KALKADVHML TLTATPIPRT LQMAMSGLRE
     LSVIQTPPVD RLAVRTYVMP WDPVVLREAL LREHYRGGQS FLVTPRVADL TDIEEFLAKE
     VPEIRYVIAH GQMSASEVEE RMSAFYEKRF EVLVSTTIIE SGIDIPSANT MIVNRADRFG
     LAQLYQLRGR VGRSKTRAYA YMVTPPERQM TEAADKRLKV LSDLDTLGAG FQLASHDLDI
     RGAGNLLGDE QSGHIKEVGY ELYQSMLEEA IMDAKAGGLA SRPRDFSPQI TVDAPILIPE
     EYVPDLDLRM GLYRRLNDVD DAGEVAAFAA EMIDRFGPLP DATENLIRVI EIKLNAKRAC
     IAKMDVGAKG VLVSFHGDKP PNVEGLLAYV DRLGGVAKLR PDAKLVLQRA WPDAKARLHG
     ALQLSKGLAK AMG
//
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