ID A0A136MY98_9BACT Unreviewed; 1122 AA.
AC A0A136MY98;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=UZ09_BCD002001238 {ECO:0000313|EMBL:KXK38865.1};
OS Bacteroidetes bacterium OLB9.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1617420 {ECO:0000313|EMBL:KXK38865.1, ECO:0000313|Proteomes:UP000070267};
RN [1] {ECO:0000313|EMBL:KXK38865.1, ECO:0000313|Proteomes:UP000070267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB9 {ECO:0000313|EMBL:KXK38865.1};
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:KXK38865.1}.
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DR EMBL; LNBW01000040; KXK38865.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136MY98; -.
DR STRING; 1617420.UZ09_BCD002001238; -.
DR PATRIC; fig|1617420.3.peg.1325; -.
DR Proteomes; UP000070267; 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; 3.40.50.300; 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; 2.
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 576..737
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 758..912
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1122 AA; 128601 MW; 090F8DA19BA484C1 CRC64;
MSNIRELINI YSTNQQIHEL NAWTHGDDAV KIQVRGLSGA MDCFALAGAF LAQKQSHIYI
ASDKEEAAYV LNTLQSILEE KTIHFFPDSF KRPLQYEELD KNNVLTRTEA INKIHTVQGK
NQIMVSYPEA IFEKAVDPGF LEKDKIFIQK NHTLDIDTII ELLVMYGFQR VDFVYQPGQF
SIRGGIVDIF SYGNEWPYRI EMFDEEVESI RTFNPTTQLS INNIEQVSII PNINSNFSQE
QKISIFEVFD HNTCVWIKEP DLLIEKLQIC FEQVEQFAAK VENRSEEDLK ELFAERAFIY
PGQIISEVSN FDILALAKSP HIHTDKTLDF NGTAQPSFNK NFDLLIANLN ENTDRGYTNF
IFTDSIKQIE RFYAIFEDKG AHVQFHPLHK SIHAGFIDHD NKVACYTDHQ IFDRFHRYKL
RQGFTEDMAI SLKMLRELQP GDYVTHIDHG IGKYSGLETI EINGHKQETV RLIYQNNDVL
YVGINSLHKI SRYVGKDGTE PKLSKIGSEA WKALKRKTKA KVKDIAKELI KLYAKRKASK
GYAFPPDGYL QTELEASFIY EDTPDQLTAT QDVKNDMQRE YPMDRLICGD VGFGKTEVAI
RGAFKAVAAG KQVAVLVPTT ILALQHYKTF SDRLKEFGIK VEYVNRFRST KEKNEIFKKT
EDGTVEILIG THAILNKGLK FKDLGLLIID EEQKFGVAAK ERLRSIQVNV DTLTLTATPI
PRTLQFSLMA ARDLTVIRTP PPNRQPIYTE RRVFSEELIK DAIYYEVQRG GQVFFVHNRV
KTLYEMADLI KRLCPDVEVA AAHGQMESKD LENTLIDFID GTYDVLVCTN IIETGLDIPN
ANTMIINNAH QFGMSDLHQL RGRVGRSNKR AFCYLFAPPL SVLTSDAKKR IQTLEEFSEL
GSGFQIAMKD MDIRGAGNLL GAEQSGFIAD IGYETYQKIL EEAVSELKET DFKDLFEEEN
AAKKAFVRDV EIDTDIEMLI PAEYVSNTQE RMLLYTELNK LESENDIERF SAKITDRFGK
IPPQVSELFE GIRLRLMAKE MGFERIVLKN RKMNCYFVSN PQSAYYETPI FDSIMKFISK
DGYLRGFSMK QSKTHLIMTK ENVRTLREAM SLLLLVQKAV EE
//
