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Database: UniProt
Entry: A0A136KTT9_9CHLR
LinkDB: A0A136KTT9_9CHLR
Original site: A0A136KTT9_9CHLR 
ID   A0A136KTT9_9CHLR        Unreviewed;      1141 AA.
AC   A0A136KTT9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
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   ECO:0000313|EMBL:KXK12782.1};
GN   ORFNames=UZ14_CFX002002018 {ECO:0000313|EMBL:KXK12782.1};
OS   Chloroflexi bacterium OLB14.
OC   Bacteria; Chloroflexota; Tepidiformia.
OX   NCBI_TaxID=1617415 {ECO:0000313|EMBL:KXK12782.1, ECO:0000313|Proteomes:UP000070321};
RN   [1] {ECO:0000313|EMBL:KXK12782.1, ECO:0000313|Proteomes:UP000070321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB14 {ECO:0000313|EMBL:KXK12782.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT   "Genome based microbial ecology of anammox granules in a full-scale
RT   wastewater treatment system.";
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:KXK12782.1}.
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DR   EMBL; LMZR01000048; KXK12782.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136KTT9; -.
DR   STRING; 1617415.UZ14_CFX002002018; -.
DR   PATRIC; fig|1617415.3.peg.2038; -.
DR   Proteomes; UP000070321; 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}.
FT   DOMAIN          602..763
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          784..938
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1141 AA;  129258 MW;  66450B5855A81B15 CRC64;
     MKQLLESFRA LPQYQNLLKD INASQSISGL GLPRSARLPV LATLHADINQ PILLITDRAD
     HALSMFDELG FWVKSARYLF AEPNPLFYED AAWGVTTRRE RLQVLTALSS YHLPFVKKPE
     TPPIIVTSVR ALMTRTLPRR DFLKACKKLS VNSINQTDSL MREWARIGYQ RVNTVLEPGQ
     FSSRGGILDV WATTELHPVR LDFFGDEIET IRTFDPATQR TLEKLENILI TPAREFLADT
     TETETQLSEF HIPLIHSQPA SLLDYLPQKT FVLVDDFSLI DVMANEVEEQ AIKFKSESIK
     EGTLAESFPV PYIPWSELND SVSEFTNVEL SSSSVETREL ENSFTQVFGH DERFGGRLKP
     FIDYLFPIIE KGEQVFIVSR QSQRLQELWF EHYPESDFTN LEFIESSLSE GFTFALGGVP
     AAEYGGLSKL HLITDSEIFG WERPQPRARQ RKTADTPESL YADLQAGDYV VHVDHGIGRF
     GGLIQRQMDG HEREYLTVEY DREDILYVPV HQADRLTRYV GADGGKPSLD NLGGQAWAET
     KSKVKEAVQK VAEDLLDLYA RRQVVEGFAF DVDTQWQKEL EDSFPYVETD DQKRAIADIK
     RDMERARPMD RLLCGDVGYG KTEVALRAAF KAVMNGKQTA VLVPTTVLAQ QHYETFSQRL
     AAFPVKVEML SRFRTPREQT EILHKLAIGE VDIIIGTHRL ISADVSFKDL GLVVIDEEQR
     FGVTHKEHLK KLRTEVDVLT LTATPIPRTL YMALTGVRDI SNLNTPPEER LPIITHVGPY
     SPRLVRQAIL RELERGGQIF FVHNRVQTIE AMKAHLEKLV PEASVDIGHG QMPENQLSAV
     MHRFNTGEID ILLSTTIIES GLDIPNANTL IVDRADTFGL AQLYQLRGRV GRGAMRAYAY
     FFRHNKMSPT QDGQQRLEVI AENTQLGAGY SIAMRDLEIR GAGELLGTRQ HGFIQAVGFH
     LYTRMLADAV RRLRKIANDV LKVDSEKLDN ALSTFNLPLS MPVNVELPLA VGIPATYISD
     SDLRLRLYRR MADLRDETEL DALGSEFRDR FGIIPEMLQN LLYQMRVKLR AEKIGLASVN
     WEAGQILLKY PVTNNGQEEK RLADLENGVR GGKSAYWITL SKDEVWTVKL LDVLAQLGDK
     T
//
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