ID K9ECK1_9ACTO Unreviewed; 1204 AA.
AC K9ECK1;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 52.
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=HMPREF9233_01127 {ECO:0000313|EMBL:EKU94989.1};
OS Actinobaculum massiliense ACS-171-V-Col2.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinobaculum.
OX NCBI_TaxID=883066 {ECO:0000313|EMBL:EKU94989.1, ECO:0000313|Proteomes:UP000009888};
RN [1] {ECO:0000313|EMBL:EKU94989.1, ECO:0000313|Proteomes:UP000009888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-171-V-Col2 {ECO:0000313|Proteomes:UP000009888};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Saerens B., Vaneechoutte M.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Actinobaculum massiliae ACS-171-V-COL2.";
RL Submitted (SEP-2012) 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:EKU94989.1}.
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DR EMBL; AGWL01000006; EKU94989.1; -; Genomic_DNA.
DR RefSeq; WP_007001333.1; NZ_JH992955.1.
DR AlphaFoldDB; K9ECK1; -.
DR STRING; 202789.GCA_001457435_00988; -.
DR PATRIC; fig|883066.3.peg.1185; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_3_11; -.
DR Proteomes; UP000009888; 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:UP000009888}.
FT DOMAIN 664..825
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 843..1000
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1204 AA; 132376 MW; C0B3A733CF0B2A31 CRC64;
MNLRPVLPIV AENPDLAKLA DSAASSKNIP LPRGAVPAAV ALMLGGASPQ SPAPSDALHV
IVTATGREAE ELAGALRAYL PAEEMEVFPS WETLPHERLS PRSDTVAQRL LVQRRLAHPE
EFGPLRAVFM PVRALLQPIS AGLGEMEPVR LKVGDFTGLE DIENQLVAAA YSRVDMVEKR
GQFAVRGGIL DVFPPTEDHP LRVEFFGDEV DEIRSFSVSD QRSIEARGEM YAPPCREVLL
TDAVRARAKA LIPQLPGAVD MLDKLSEGIA VEGMESLAPA LVDKMIPVLE TVPEGARIVL
VEPERISQRA ESLIQTTEEF LTAAWSAAAA GAEVPIQASD ANFATVAETR RLARSRGQAW
WELGGISAQA PGVGVGSEAN AGSEANAAGA ANAPGKVRQP RKFLGKVDEA LRVIRDLTKR
RWRFVLVTQG PGLGRRLTEQ LGEVGAAASF VENLPQKLEP SVVYVTTAPI GEGFVMEEER
FAILSANDIT SRGGSSIREP RKLPKRRKAT VDPLALKPGD FVVHERHGVG KFVKMAKRSI
GSGAMRGDNQ REYLVLEYAS SKRGQPGDQL WVPTDQLDQI SRYSGGEAPR LNKMGGSDWA
KTKQKAKAAT RQMASELTRL YAERLATPGH AFGPDTPWQR ELEDAFEYVE TPDQLHTIEE
VKRDMERPVP MDRLISGDVG YGKTEIAVRA AFKAVMDNKQ VAVLVPTTLL VDQHRETFEE
RCSGFPVKVA SLSRFQSEKE SREVIEGLKD GSVDVVIGTH RLLTGNVRFK DLGLVVIDEE
QRFGVEHKET LKQMYPSVDV LSMSATPIPR TLEMAVTGVR EMSTLATPPE ERHPILTYVG
AREDKQLSAA IRRELLRDGQ VFFVHNRVQD LPKVAAMLAE LVPEARIAIA HGQMAERELE
QVIQSFWERE VDVLVCTTIV ETGLDIANAN TLIVDNADKM GLSQLHQLRG RVGRGRERAY
AYFLYEPHRM LTETALERLR TIASNTDLGA GMQVAMKDLE IRGAGNMLGG EQSGHIEGVG
FDLYVRMVSD AVAKIRGEHG EEEEDASDVR IELPVEAYLA EDYVPSERLR LEIYSKIANA
KNEEERQAVR EEMVDRYGEL PEEAERLFRI AALRERARAA GLEEITVAGR NLRFAPVDLP
DSKQARLKRL QPKALLKPAI RTLLVPMPSS GGKKLGQNHV LEGDELLAWV GDFIHAVFIA
SIGS
//
