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Database: UniProt
Entry: A0A0Q8LYK7_9MICO
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Original site: A0A0Q8LYK7_9MICO 
ID   A0A0Q8LYK7_9MICO        Unreviewed;      1201 AA.
AC   A0A0Q8LYK7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
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=ASD93_03775 {ECO:0000313|EMBL:KRB39210.1};
OS   Microbacterium sp. Root180.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1736483 {ECO:0000313|EMBL:KRB39210.1, ECO:0000313|Proteomes:UP000050802};
RN   [1] {ECO:0000313|EMBL:KRB39210.1, ECO:0000313|Proteomes:UP000050802}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root180 {ECO:0000313|EMBL:KRB39210.1,
RC   ECO:0000313|Proteomes:UP000050802};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRB39210.1, ECO:0000313|Proteomes:UP000050802}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root180 {ECO:0000313|EMBL:KRB39210.1,
RC   ECO:0000313|Proteomes:UP000050802};
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:KRB39210.1}.
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DR   EMBL; LMHS01000001; KRB39210.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q8LYK7; -.
DR   STRING; 1736483.ASD93_03775; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000050802; 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:UP000050802}.
FT   DOMAIN          656..817
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          842..992
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1201 AA;  129897 MW;  FAFAB14A45FE0F37 CRC64;
     MRALEQASSF QDAAAAASVD GDFSLVEGLD APLLAALLER RRAAGRPPAI LLITPTGRRA
     ESIGPALGAL LPGAEVLHFP AWETLPHERL SPSPEIVGNR LEVLGRVGRW SGETPLVVTA
     SVRGAIQPLA AGLTDVAPID LAVGERGHEL GDVVLRLVEL AYHRVDMVSR RGEFAVRGGI
     LDIFPPTAAH PYRIEFFGDE VDQIRAFSVA DQRSLPGEVR EVSLIASREL LLTEAVRGRA
     RQLKDEFPSL AGMLERMSEG IPVEGMESLL PAVSDRLVTL VDYLPEGSAV ALVDPERAVA
     RAITLGETNR EFLEAAWSAA TAGASTPIDL GAGDFLTLPA LREAARARRQ VWWSLSAFDS
     GEADAAAEGL LDIDSALEAA AAIRVPGTAV PSFHGNVDGA TEHVGALLAD GWRVVVAASG
     TGLVERARDV LAERGIAARK VGDIHSAPEP GVAHLVTSVL ERGFEAADAK LAVLTETEFY
     GRTIGGDQRV VKKLASRRKN VVDPIQLKAG DHVVHVTHGI GRFVELQQRE VSSGGRNPVK
     SVREYLVIEY APSKRGFPGD KLLVPTDQLD LLSRYVGGEA PALSKMGGSD WAAAKGRARK
     AVRDIAVELV KLYSARMAAK GYAFGPDTPW QRELEEAFPF AETPDQLQTI DEVKADMEKP
     VPMDRLLSGD VGFGKTEVAV RASFKAIQEG KQVAMLVPTT LLVKQHIETF TERFAGFPVK
     VKALSRFQTD KQAREVVAGL ADGTVDMVIG THRILTEKVL FKDLGLMIID EEQRFGVEHK
     DTLKKLKTNV DILAMSATPI PRTLEMAVTG IREMSTLQTP PEDRHPILTF VGPRNDKQIA
     AAIRRELLRE GQIFYVHNRV QSIQRIATDL AELVPEARIA VAHGQMGEHQ LEQVVDDFWE
     RRADVLVSTT IIETGLDIAN ANTIIIDRAD KYGLSQLHQL RGRVGRARER AYAYFLYDEL
     KPLSETAADR LETIAVNNDL GSGIQVALKD LEIRGAGNLL GAEQAGHIAG VGFDLYLRMI
     GEAVSAFRGD DVEGPAELRL ELPVQARIPD SYIDSERLRL EAYQKLSAAA SVTAKDDALD
     LVVEELSDRY GEPPADVEGL LAVARLRRRA AQTGLTDVVA MGPNLRIAPA HLPDSMRVRL
     QRLYPKAKLL SGGDALVVPL PTAGGEALAD ADLIAWVRQL LDQLWPEKKA EAPAADGAPT
     P
//
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