ID A0A134AH97_9FIRM Unreviewed; 1162 AA.
AC A0A134AH97;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=HMPREF1863_00770 {ECO:0000313|EMBL:KXB67044.1};
OS Peptoniphilus coxii.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=755172 {ECO:0000313|EMBL:KXB67044.1, ECO:0000313|Proteomes:UP000070442};
RN [1] {ECO:0000313|Proteomes:UP000070442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DNF00729 {ECO:0000313|Proteomes:UP000070442};
RA Mitreva M., Pepin K.H., Mihindukulasuriya K.A., Fulton R., Fronick C.,
RA O'Laughlin M., Miner T., Herter B., Rosa B.A., Cordes M., Tomlinson C.,
RA Wollam A., Palsikar V.B., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-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}.
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:KXB67044.1}.
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DR EMBL; LSDG01000023; KXB67044.1; -; Genomic_DNA.
DR RefSeq; WP_068367423.1; NZ_KQ960172.1.
DR AlphaFoldDB; A0A134AH97; -.
DR STRING; 755172.HMPREF1863_00770; -.
DR PATRIC; fig|755172.3.peg.739; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000070442; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000070442}.
FT DOMAIN 632..793
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 814..968
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1162 AA; 133069 MW; DE0B471CA5D4D828 CRC64;
MTSIYHELLK ANPSFRRVLN CLKDRETPIG VYGLPEQVIA PFAETVKEEC KRPVLLVTWD
LARATKLVED LSYFAEGGVY HLAARELFFF QRDAGSHELL ARRLQTLQAM LNGEGKIIVT
TPEALGGIFL KPHYLKNASF TLKVGKSMEI DDLMARLATA GYQRVDFVEG MGQFSVRGGI
VDIYPPGNLP CRIEFFDVEV DSIRLFDSKT QRSVEGVDSA DIFPVHDIIL DERLREIVSK
GIEKDLEKTD RLSLVSKERA MEKFKPLIEG LGTGERVSHT DLFLPYIPKE DRASVIDYFA
EEPIVFLDEP RRMDEIAQKQ ELSLVDTLTD LADAGEILKS HLKIQIDYDA VKRDLFRFDT
VLSSHIVRSK ESVDLKEVAN FHIKTVTSFG GRLRIFKEEI QRYIEEDYTI VLLGGSEEKT
ERLIKTLEDM GFATTPITGE LKPSVIQVDE GHVHGGFEFE HERFVLLNST EIFGDFKRQK
KRKKKRDVID LGTLHVGDYV VHETHGIGKF LGTTNLEVQN VQRDYISLMY KDGDKLFLPM
DQLSLIHRYI ASDDAPPKIN RLNTQTWRNT KAKAKRSVEE MAEDLIRLYS KREDVKGFAF
SADQPWQKEF EDSFQFEETD GQLLAAEEIK QDMEEDKPMD RLLCADVGYG KTEVALRAAF
KAVLDGKQVA FLVPTTILAQ QHYNTMRERF NDFALRTALL SRFRSAKEQK RDLEAIRNGS
VDIVVGTHRL LSKDVQFKDL GLLIIDEEQR FGVRHKEKLK LLKENVDTLT LTATPIPRTL
QMSLAGIRDM SVIEEPPQER FPVQTYVVEY NPMMVREAIL KELDRGGQVY FVYNRVQSME
KILADLRELV PEALFAMANG QMGERELENT MLQFVEHDID VLLCSTIIET GMDVANANTM
IVWEANRLGL SQLYQLRGRI GRSNRMAYAY FTYRRDASIS EVAEKRLAAI REFTEFGSGY
KIAMRDLEIR GSGNILGESQ HGHMNAIGYD LYIKFLRQAV SRAKGEEDVE TADTTMDVLI
DSYIPKHYIQ DESQRMEMYR KIAVIADDED ERDMIDELID RFSDPPKPVL QLIHLSKIRH
MASTLQVETV QQKKDDYILE FLEGYELPLA LMNEITSVFG KKVVFGFGER ATITLTAKEE
PLDALEKLLE LMKIHKTHTR KP
//