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Database: UniProt
Entry: A0A010YXL8_9ACTN
LinkDB: A0A010YXL8_9ACTN
Original site: A0A010YXL8_9ACTN 
ID   A0A010YXL8_9ACTN        Unreviewed;      1210 AA.
AC   A0A010YXL8;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 45.
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=CryarDRAFT_0996 {ECO:0000313|EMBL:EXG79943.1};
OS   Cryptosporangium arvum DSM 44712.
OC   Bacteria; Actinomycetota; Actinomycetes; Cryptosporangiales;
OC   Cryptosporangiaceae; Cryptosporangium.
OX   NCBI_TaxID=927661 {ECO:0000313|EMBL:EXG79943.1, ECO:0000313|Proteomes:UP000021053};
RN   [1] {ECO:0000313|EMBL:EXG79943.1, ECO:0000313|Proteomes:UP000021053}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44712 {ECO:0000313|EMBL:EXG79943.1,
RC   ECO:0000313|Proteomes:UP000021053};
RG   DOE Joint Genome Institute;
RA   Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (JUL-2013) 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:EXG79943.1}.
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DR   EMBL; JFBT01000001; EXG79943.1; -; Genomic_DNA.
DR   RefSeq; WP_035848712.1; NZ_KK073874.1.
DR   AlphaFoldDB; A0A010YXL8; -.
DR   PATRIC; fig|927661.3.peg.979; -.
DR   HOGENOM; CLU_005122_2_2_11; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000021053; 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:UP000021053}.
FT   DOMAIN          675..836
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          861..1011
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1210 AA;  131113 MW;  A98BB75474A294A8 CRC64;
     MSLSGLLDAS LADPALGQIA RRAAGDAAGE LDLTAPEALR PFVVAALAAA RAKAGSAAPV
     LAVTATGREA DDLAAALTCL LPPDRIAVYP AWETLPHEKL SPRADTIGRR LAVLRRLAHP
     STDDPTTGPL DVVIAPVRSV LQPQLAGLGE LEPVGLQAGD TAPLDAVVER LVSIAYARVD
     LVEKRGEFAV RGGILDVFPP TEEHPVRVEF WGDEVEEVRY FAVADQRSLE IAAHGLWAPP
     CRELLLTPEV RERAAQLAKD HPALAEMLDK VADGIPVEGM ESLTPALLEG SGQLELLVEA
     VPAGTHVLLC DPERIRARAR DLVATSAEFL EASWAAAAGG GEAPIDLGAA AFRSLADVRS
     TGTGRGLPWW TVAPFGVSAA GSASAADFDD DAIDVAIPAV ADPGVPRDSL TVEAKSVDGF
     RGDTGRAVEE LRQRVAEGWR AALVFEGPGS AQRAAEMLRE ADLGAQLVVD VPTAPEARSV
     LVTTGQLAGG FLLESAQLVV FTESDLTGAR SGSGRERGRM PSRRRNAVDP LQLQPGDYVV
     HEQHGVGKYI EMIKRTINGG EREYLVLEYA PSKRGHPGDR LFVPTDSLEQ LTRYVGGESP
     ALHKMGGADW QKAKGRARKA VKEIAGELIR LYAARTSTKG FTFSADTPWQ RELEDAFPYI
     ETPDQLVAIN EVKADMEKPY PMDRVICGDV GYGKTEIAVR AAFKAVQDGK QVAVLVPTTI
     LAKQHFLTFS ERMAQFPVKI AQLSRFQTDG EAAETVAKLA TGEVDIVVGT HRLLQASTRF
     KDLGLVIVDE EQRFGVEHKE QLKQMRTAVD VLTMSATPIP RTLEMSLTGI REMSTILTPP
     EERHPVLTFV GPYEERQIGA AIRRELLREG QVFYLHNRVE SIERAAARLR SMVPEARIAV
     AHGQMNEDAL ERVMLGFDEK EYDVLVSTTI VESGLDIPNA NTLIVERADV LGLSQLHQIR
     GRVGRGRERA YAYFLYPPER PLTETAHDRL ATIAQNSDLG AGMAVAMKDL EIRGSGNLLG
     GEQSGHIANV GFDLYVRLVG EAVAEYKGER TEIESEVKVD LPVDAHLPHD YIPGERLRLE
     AYRKLAGVTT SEELAQVREE IRDRYGNPPE PVENLFAVAA FRVKARAATI TEVSLQGRQV
     RFAPLRLPES KVMRLQRLYP GAMYKQAVDV VLVPRPSTAR VGGQPLRDTA LLDWAAGFLD
     AMAPEPARAP
//
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