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Database: UniProt
Entry: A0A0D1LRZ2_9MYCO
LinkDB: A0A0D1LRZ2_9MYCO
Original site: A0A0D1LRZ2_9MYCO 
ID   A0A0D1LRZ2_9MYCO        Unreviewed;      1209 AA.
AC   A0A0D1LRZ2;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 40.
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=TL10_01210 {ECO:0000313|EMBL:KIU18881.1};
OS   Mycolicibacterium llatzerense.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=280871 {ECO:0000313|EMBL:KIU18881.1, ECO:0000313|Proteomes:UP000032221};
RN   [1] {ECO:0000313|EMBL:KIU18881.1, ECO:0000313|Proteomes:UP000032221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLUC14 {ECO:0000313|EMBL:KIU18881.1,
RC   ECO:0000313|Proteomes:UP000032221};
RA   Greninger A.L., Langelier C., Cunningham G., Chiu C.Y., Miller S.;
RT   "Genome sequence of Mycobacterium llatzerense and Mycobacterium immunogenum
RT   recovered from brain abscess.";
RL   Submitted (JAN-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:KIU18881.1}.
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DR   EMBL; JXST01000001; KIU18881.1; -; Genomic_DNA.
DR   RefSeq; WP_043984072.1; NZ_JXST01000001.1.
DR   AlphaFoldDB; A0A0D1LRZ2; -.
DR   STRING; 280871.TL10_01210; -.
DR   PATRIC; fig|280871.6.peg.244; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000032221; 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   CDD; cd18810; SF2_C_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:UP000032221}.
FT   DOMAIN          656..817
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          835..992
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1209 AA;  129718 MW;  C8FD90F719BDD459 CRC64;
     MTSPGQQSIQ TPLAGLVQLA LTDPGLQELT RQAAEGIAEQ ALVGPVSARL PVAAALAAAG
     PVLVVTATGR EADDLTAELR AVHGDAVALF PSWETLPHER LSPGVDTVGA RLTVLRRLAR
     PDDTRLGPPL RVVVTTARSL LQPLAGGVTD AEPVTLTVGG EADFDDTVTR LVELAYNRVD
     MVGKRGEFAV RGGILDIFTP TAEHPVRIEF WGDEVTEMRM FSVADQRSIP EIAVETMIAV
     PCRELLLTPD VRERAAEIGA SLPSSDNQVT GSIADMMAKL AEGIPVDGME ALLPVLRPGD
     LALLTDRLPA GAPLLICDPE KVRTRAADLI KTGREFLEAS WSVAAVGGDA PIDVEQLGGS
     GFRDFVEIRE AAAAGGHPWW TLSQLANETA VEVDIRPAPS ARGQQSLEEI FAMLRAHIAT
     GGLAAVVTPG AGTAHRVVEQ LSESDVAATM LEPGAVPKAG VVGVLKGPLH DGLVLPGVNL
     VVITETDLTG NRAAATEGKR LAAKRRNVVD PLALTAGDLV VHDQHGIGKF IEMTERVVGG
     ARREYLVLEY GSSKRGGGSD RLYVPMDSLD QLSRYVGGTE PTLSRLGGSD WTNTKTKARK
     AVREIAGELV SLYAKRQSAP GHAFAPDTPW QNEMEDAFGF TETMDQLTAI TEVKADMEKP
     VPMDRVICGD VGYGKTEIAV RAAFKAVQDG KQVAVLVPTT LLADQHLQTF AARMAGFPVT
     VKGLSRFTDP AESRLVIEGL KDGSVDVVIG THRLLATGVT WKDLGLVIVD EEQRFGVEHK
     EHIKSMRTHV DVLTMSATPI PRTLEMSLAG IREMSTILTP PEERFPVLTY VGPHDDKQVA
     AALRRELLRD GQAFYIHNRV KSIDSAAARV RQLVPEARVV VAHGQMPEEL LEKTVEGFWN
     RDYDILVCTT IVETGLDISN ANTLIVERAD TFGLSQLHQL RGRVGRSRER GYAYFLYPPE
     VPLTETAHDR LATIAQNNDL GAGMAVAMKD LEIRGAGNVL GVEQSGHVAG VGFDLYVRLV
     GEAVEAYRAA VDGKTIAAVE EVKEVRVDLP IDAHLPPDYI GSDRLRLEAY RRLAAASDHA
     RVASVVEELV DRYGPLPEPA QRLVAVARLR LLCREYGVTE VTAISDSTIR LTPLTLMDSG
     QLRLKRMYPG ATYRATTSTV QIPIPRAGAG VGAPRIRDLE LARAVAGLLL ELDGKAPGEV
     DITDLGGSA
//
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