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Database: UniProt
Entry: A0A134AH97_9FIRM
LinkDB: A0A134AH97_9FIRM
Original site: A0A134AH97_9FIRM 
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
//
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