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Database: UniProt
Entry: A0A0Q5VIK5_9ACTN
LinkDB: A0A0Q5VIK5_9ACTN
Original site: A0A0Q5VIK5_9ACTN 
ID   A0A0Q5VIK5_9ACTN        Unreviewed;      1180 AA.
AC   A0A0Q5VIK5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=ASG36_05085 {ECO:0000313|EMBL:KQS61076.1};
OS   Geodermatophilus sp. Leaf369.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Geodermatophilus.
OX   NCBI_TaxID=1736354 {ECO:0000313|EMBL:KQS61076.1, ECO:0000313|Proteomes:UP000051830};
RN   [1] {ECO:0000313|EMBL:KQS61076.1, ECO:0000313|Proteomes:UP000051830}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf369 {ECO:0000313|EMBL:KQS61076.1,
RC   ECO:0000313|Proteomes:UP000051830};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQS61076.1, ECO:0000313|Proteomes:UP000051830}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf369 {ECO:0000313|EMBL:KQS61076.1,
RC   ECO:0000313|Proteomes:UP000051830};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQS61076.1}.
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DR   EMBL; LMQA01000001; KQS61076.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q5VIK5; -.
DR   STRING; 1736354.ASG36_05085; -.
DR   Proteomes; UP000051830; 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:UP000051830}.
FT   DOMAIN          640..801
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          819..976
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1180 AA;  128879 MW;  F56454D8B5BFDFFA CRC64;
     MRGVLDVVLS DPGLARVVEQ AGAADLTVTA PPSVQPLVAA ALAAPSPGAG VPVLVVTAGE
     RDADRTADLL RCFLPDRRVE VFPAWETLPH ERLSPRPDTV GRRLAVLRDL THPEAATGRI
     DVVVAPVRSL LQPLAPGLGD LVPVELAAGD SAELGEISKR LADAAYTRVE LVEKRGEFAV
     RGGLLDVFPP TEPHPVRVEF WGDEVDELRY FSAADQRSLD ERPDRLWAPP CRELLLTPTV
     RERARALTLE HPELAEVTDS LAEGIAVEGM EALTPALIGG EHMELLTDLV PRDTHVLVCD
     PERVRSRAAD LVRTAEEFLA ASWQTAAEAG QAPIDLGASS FRDLEDVADD ARGRGLPWWT
     TGAFTLQTED DDTHVTLTAT PVERFHGDQD AALGQLRDWG RDDWRVVLTF AGPGPAQRAA
     DQLTEADLGV RLLPDLAAAP ESGLTHVTQA NLEAGFAFPG IKLALLTEHD LTGQRGTSMR
     DAQKMPARRR NAVDLVQLQP GDVVVHEQHG VGRYVEMVSR TVHGGQRDYL IVEYAPGKKN
     QPPDRLFVPT DALDQLTRYV GGDAPALSKL GGADWAKTKG QARKAVKQIA AELIRLYSAR
     MASKGHAFGP DTVWQRELED AFPFQETPDQ LAAIDEVKAD MAQPVPMDRI ICGDVGYGKT
     EIAIRAAFKA VQDGKQVGVL VPTTLLANQH FKTFSERMAQ FPVTVAVLSR FQSKTESDET
     LRKLADGEVD ILVGTHRLLQ PTTRFKDLGL VIVDEEQRFG VEHKEYLKTM RTAVDVLSMS
     ATPIPRTLEM SLTGIREMST ILTPPEERHP VLTYVGAWED KQMAAAIRRE LLRDGQVFVI
     HNRVQSIDKA AATIRRLVPE ARVAVGHGQM KEHELEKIMV GFWEKEYDVL IATTIVESGL
     DIPNANTLIV DRADTFGLSQ LHQIRGRVGR GRERAYAYFT YDPNRPLTET SVDRLTTIAN
     NTDLGAGMAV AMKDLEIRGS GNLLGGEQSG HIAGVGFDLY VRLVGEAVSD YRAQATGESP
     AVEPADVRVD LPVDAHLPHD YVPGERLRME AYRKVASVQD DDQAQAVLDE LTDRYGPAPA
     PVLNLLAVAR FRAAMRQLGV TEVSMAGRNV RISPVDLRES QQMKLTRLAE GVSYKGTVNT
     VSLKVPVGPD RRTPLRDVAL LEKLHALMTS VLEQPAGAAT
//
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