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Database: UniProt
Entry: K7YPT2_9PROT
LinkDB: K7YPT2_9PROT
Original site: K7YPT2_9PROT 
ID   K7YPT2_9PROT            Unreviewed;      1167 AA.
AC   K7YPT2;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 56.
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:AFX99542.1};
GN   ORFNames=A1OE_1371 {ECO:0000313|EMBL:AFX99542.1};
OS   Candidatus Endolissoclinum faulkneri L2.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Endolissoclinum.
OX   NCBI_TaxID=1193729 {ECO:0000313|EMBL:AFX99542.1, ECO:0000313|Proteomes:UP000010077};
RN   [1] {ECO:0000313|EMBL:AFX99542.1, ECO:0000313|Proteomes:UP000010077}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L2 {ECO:0000313|EMBL:AFX99542.1,
RC   ECO:0000313|Proteomes:UP000010077};
RX   PubMed=23185008; DOI=10.1073/pnas.1213820109;
RA   Kwan J.C., Donia M.S., Han A.W., Hirose E., Haygood M.G., Schmidt E.W.;
RT   "Genome streamlining and chemical defense in a coral reef symbiosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:20655-20660(2012).
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; CP003539; AFX99542.1; -; Genomic_DNA.
DR   RefSeq; WP_015089040.1; NC_019566.1.
DR   AlphaFoldDB; K7YPT2; -.
DR   STRING; 1193729.A1OE_1371; -.
DR   KEGG; thal:A1OE_1371; -.
DR   PATRIC; fig|1193729.4.peg.709; -.
DR   eggNOG; COG1197; Bacteria.
DR   HOGENOM; CLU_005122_3_2_5; -.
DR   Proteomes; UP000010077; Chromosome.
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; 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          635..796
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          817..971
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1167 AA;  130881 MW;  159DF9A9D350C56E CRC64;
     MNMVGNFNQL FANFPIDVGR VAIASAPEGV EAEAISFLAR SHGLLLHVTC DDTVSNELKR
     AVAFFDPELQ VMQLPPWDCL PYDRFSPNKE IMGQRIETLS MLALRKLSAK PALVITTVNA
     VLQRVPPKSF FIDSTMALKV GQIISLAKIT DFFVSNGYYR SDMVQECGEY AVHGGTIDVF
     PTGTAWPVRL DFFGDTLEEI RCFDPISQRT INNRKDILFL PAREVQLNAV TIQRFRSSYR
     SLFGAEVIDD PVYESISAGR FYSGMEHWLP LFYQTISTVL DYVGDAPITL GYQVEKSINN
     RFEQITEYHN TRMQMLHCSD TEADNRYRPL DPCAMYLMPD EWDLLMSTRV VGIFTPFAIP
     SSADSVIDLG ARSGISLAEA RALGGSAVYD AVRHAVMDEN SQGRRVVIAA YSKSSCELIA
     RLFHDHSIDN VDLVANLQAV LALPIATVAT VVLPLKHGYR RGKLTIVSEC EIFGQRLLRQ
     SKLGKRRGKH LLREISALTE GDYVVHYEHG IGRYLGLETL EINDALHDVL CLEYLGGDKL
     FVLVENIDVL SRYGDHEFKV QLDKLGGLSW RSRKAKVKKR LFDMAEKLIN IAANRELRKT
     QPLCLPVANY DKFCSRFPFI ETEDQLKAID DVLADMESSR PMDRLICGDV GFGKTEVALR
     AAFVATGQGY QVAVVVPTTL LCRQHYVSFV NRFEGFPIKV AQISRLISTK EANDVRDGLR
     NGNINIVVGT HALLSNHNHF DNLGLVIIDE EQHFGVSQKE LLKDMRNAVH VLTMTATPIP
     RTTQMALSGL REMSLITTPP VDRLAVQTFV IPYDGMVVRD ALLRERHRGG QTFYVCPRID
     DLVHVHEQLL KLILDLRIGV AHGRMASNDL EDVITSFIDG NYDVLISTNI LESGLDIPAA
     NTIIIHRSDM FGLAQLYQLR GRVGRSKAQA YAYLTTHPTK LLPPAAKRRL EVLQTFNNLG
     ACLSLASHDI EIRGAGNLLG DQQSGQVKEV GIELYHEMLR EAVEVARAGD HIKTKNDTSW
     TPQITINMPV LIPPTYISNI SMRMSLYRRI AMLINQEEID GFIVELVDRF GPLPVEVDNL
     LKIMTIKLLC RVAGVEKIDA GSKGAIIAFR NNSFAYPDKL ITFMQQQADF VQFRPDHRMI
     YRCTWNDSDK LLRGLIGLMK KLAAVVV
//
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