ID N6X5T8_9ACTO Unreviewed; 1196 AA.
AC N6X5T8;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-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 ECO:0000313|EMBL:ENO18717.1};
GN ORFNames=HMPREF9004_0387 {ECO:0000313|EMBL:ENO18717.1};
OS Schaalia cardiffensis F0333.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Schaalia.
OX NCBI_TaxID=888050 {ECO:0000313|EMBL:ENO18717.1, ECO:0000313|Proteomes:UP000013015};
RN [1] {ECO:0000313|EMBL:ENO18717.1, ECO:0000313|Proteomes:UP000013015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0333 {ECO:0000313|EMBL:ENO18717.1,
RC ECO:0000313|Proteomes:UP000013015};
RA Aqrawi P., Ayvaz T., Bess C., Blankenburg K., Coyle M., Deng J., Forbes L.,
RA Fowler G., Francisco L., Fu Q., Gibbs R., Gross S., Gubbala S., Hale W.,
RA Hemphill L., Highlander S., Hirani K., Jackson L., Jakkamsetti A.,
RA Javaid M., Jayaseelan J.C., Jiang H., Joshi V., Korchina V., Kovar C.,
RA Lara F., Lee S., Liu Y., Mata R., Mathew T., Munidasa M., Muzny D.,
RA Nazareth L., Ngo R., Nguyen L., Nguyen N., Okwuonu G., Ongeri F.,
RA Palculict T., Patil S., Petrosino J., Pham C., Pham P., Pu L.-L., Qin X.,
RA Qu J., Reid J., Ross M., Ruth R., Saada N., San Lucas F., Santibanez J.,
RA Shang Y., Simmons D., Song X.-Z., Tang L.-Y., Thornton R., Warren J.,
RA Weissenberger G., Wilczek-Boney K., Worley K., Youmans B., Zhang J.,
RA Zhang L., Zhao Z., Zhou C., Zhu D., Zhu Y.;
RT "Reference genome for the Human Microbiome Project.";
RL Submitted (MAR-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:ENO18717.1}.
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DR EMBL; AQHZ01000007; ENO18717.1; -; Genomic_DNA.
DR RefSeq; WP_005962118.1; NZ_KB822674.1.
DR AlphaFoldDB; N6X5T8; -.
DR STRING; 888050.HMPREF9004_0387; -.
DR PATRIC; fig|888050.3.peg.375; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_3_11; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000013015; 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:UP000013015}.
FT DOMAIN 663..824
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 849..999
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1196 AA; 130173 MW; 8D6E35A5C9867A67 CRC64;
MKLTGLAPLI GTDEALDRAT GSLASKRNAT LVAPLGVRPP ALAALAQASS DLPLVVLTAT
GREAERLTAA LRSWSDAVEM LPAWETLPHE RLSPQVDTMA RRIAVLRRLA HPVEGDPHAG
PLSILVIPIR AFLQPVIRGL AEREPVRVHV GDRVDLPDLA RRLGELGYQR VDMVEGRGQL
SIRGGILDVF PPQEAHPVRV ELWDDEVDEI RAFSVQDQRT LGALDDGLWA TACRELLLTR
AVRARARELA AELPGAAEML ALASEGIPAP GIESLAPVLS SGMERLLDLL PAGSPIICSD
PERVRARAAD LLATTEEFLA AAWSVAAEGA QTPLEASQAS FLNFEELWAS DSRPWWELSA
LPPAELAEAL GESEEDESGA QKDTRALVVS SSLMAMGARE VRPYRGDFAA ACTDLGGLAK
NGWTIVVTTE GPGPARRIRT ILSEAEVPAT LVDDILDAPQ PGTVVVTTAQ AGSGFVAPEL
KLAILSESDL TGRVGASTRD MRRMPSRRKK GVDPLSLTPG DYIVHDQHGI GRFIELVSRT
TGRGEAAVRR DYLVLEYAPS KRGQPGDRLY VPSDCLDQIS KYTGSDQPSL TKMGGADWAK
TKAKAKKAVN EIAKELIRLY AARQATKGHA FAPDTPWQRE LEDAFPYVET PDQLVTIDEV
KADMEKPIPM DRLLTGDVGY GKTEIAVRAA FKAIQDGKQA AVLVPTTLLV QQHIETFTER
YAGFPVTIAA LSRFSTPKEA EEVKAGLASG KIDLVIGTHS LLTGAISFKA LGLVIIDEEQ
RFGVEHKETL KAIRTDVDVL SMSATPIPRT LEMAVSGIRE MSILQTPPEE RQPVLTFVGA
YTDAQVSAAI RRELLRDGQV FFVHNRVDSI ASVAAHIQEL VPEARVRVAH GKLSEHQLEE
VIVDFWNHEF DVLVCTTIVE TGLDISNANT LIVDRADVFG LSQLHQLRGR VGRGRERAYA
YFFYPADKTL TETAHERLKT IAANTDLGAG LAVAQKDLEI RGAGNLLGGA QSGHVEGVGF
DLYVRMVADA VAAYRGQARE EKSDLRLDIA VDAHIPEEYV PGERLRLEVY AKIAAITSPE
QEADVREELI DRYGPLPREV ELLFLISRLR RLVRSTGIEE IVTQGKYVRV GPVELRDSQV
LRLKRLHPGS VIKAAVRQVL VPLPLTQRIG GTPLVDEALL QWVETLVTKV LTPFSS
//
