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Database: UniProt
Entry: H1YFI3_9SPHI
LinkDB: H1YFI3_9SPHI
Original site: H1YFI3_9SPHI 
ID   H1YFI3_9SPHI            Unreviewed;      1119 AA.
AC   H1YFI3;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 54.
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=Mucpa_3187 {ECO:0000313|EMBL:EHQ27291.1};
OS   Mucilaginibacter paludis DSM 18603.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Mucilaginibacter.
OX   NCBI_TaxID=714943 {ECO:0000313|EMBL:EHQ27291.1, ECO:0000313|Proteomes:UP000002774};
RN   [1] {ECO:0000313|EMBL:EHQ27291.1, ECO:0000313|Proteomes:UP000002774}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18603 {ECO:0000313|EMBL:EHQ27291.1,
RC   ECO:0000313|Proteomes:UP000002774};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Held B.,
RA   Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The permanent draft genome of Mucilaginibacter paludis DSM 18603.";
RL   Submitted (SEP-2011) 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}.
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DR   EMBL; CM001403; EHQ27291.1; -; Genomic_DNA.
DR   RefSeq; WP_008507685.1; NZ_CM001403.1.
DR   AlphaFoldDB; H1YFI3; -.
DR   STRING; 714943.Mucpa_3187; -.
DR   eggNOG; COG1197; Bacteria.
DR   HOGENOM; CLU_005122_1_3_10; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000002774; 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; 3.40.50.300; 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}; Reference proteome {ECO:0000313|Proteomes:UP000002774}.
FT   DOMAIN          575..736
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          757..911
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1119 AA;  128177 MW;  E68D46FCA5E5B974 CRC64;
     MNIREILERY KTDERVQTLA KALNSVKHPR VQLRGLVGSS DAAMAVALYF LKHSHMLFIL
     PDREEAGYFQ SDLENLLDKE ILLFPSSYRK PFEFTQPDSS NVLARAEVLN ELNHTSEYGQ
     LIVTYPEALA EKVIDRASLE KNTLEIGVTN KLSLDFINEF LIEYAFERVD FVYSPGQFSI
     RGGIVDIFSF SHDLPYRVEF FGDFIESIRT FEIESQLSVE QVKTITIVPN VQSKFLTENN
     ISLLEYIDPS TQIWIKDVQF TLDIIQSGYK KATQLWKALS AEDKNANPDW IDPKFGFTDE
     KMIADQLHDF GLVEFGKQFF YTPTDSVQFD IRPQPSFNKD FSLLIHNFKN NEAEKIENCI
     FTDSTRQLER LYAIFEDLDK TIKFTPVNIS IREGFIDYAQ KIACYTDHQI FDRYYKYKLK
     KGYQRSQAIT LKDLRELKPG DYITHIDHGI GKYAGLEKVE VNGKMQEMIR LLYSDNDLLY
     VNINSLNRIS KYSGKEGTVP KMNKLGTDAW EKLKKTTKKK VKDIARDLIK LYAVRKAQDG
     NAFSPDSYLQ TELEASFIYE DTPDQEKATV DFKRDMESPH PMDRLICGDV GFGKTEIAIR
     AAFKAVADSK QVAVLVPTTI LAAQHYKTFT DRLKGFPCNI DYVNRFKTSK QIKDTLQRLA
     EGKLDIIIGT HRLVSKDVKF KDLGLMIIDE EQKFGVSTKE KLKAMRVNVD TLTLTATPIP
     RTLHFSLMGA RDLSIISTPP PNRQPVVTEL HVFNDKLIKE AVEYEIDRNG QVFFIHNRVA
     DLPQLGGMIK KLVPKARIGI AHGQLEGDDL EDVMLKFVSN EYDVLVATTI IEAGLDIPNA
     NTIIINYAHM FGLSDLHQMR GRVGRSNKKA FCYLLSPPLS TLTSEARKRL SAIEEFSDLG
     SGFNVAMRDL DIRGSGNLLG AEQSGFIAEI GFEMYHKILD EAIQELKDDE FKGLFKDEKP
     RPFISFTQID TDLEILIPDE YVTSIPERYN LYTELSKLEN ETELAAFAQQ LHDRFGPVPR
     QVNDLMNTMR LQWLGKSIGF EKLSLKKNVL RGYFIANQQS PYFETTQFRQ VLNFMQANPR
     RCNMKEVKNT LRISIDNVRT IDEAVAILEE MMEPVVGYS
//
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