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Database: UniProt
Entry: A0A0J1ETV4_9MICC
LinkDB: A0A0J1ETV4_9MICC
Original site: A0A0J1ETV4_9MICC 
ID   A0A0J1ETV4_9MICC        Unreviewed;      1240 AA.
AC   A0A0J1ETV4;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, 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=ABL57_15330 {ECO:0000313|EMBL:KLU08884.1};
OS   Kocuria sp. SM24M-10.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Kocuria.
OX   NCBI_TaxID=1660349 {ECO:0000313|EMBL:KLU08884.1, ECO:0000313|Proteomes:UP000036489};
RN   [1] {ECO:0000313|EMBL:KLU08884.1, ECO:0000313|Proteomes:UP000036489}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM24M-10 {ECO:0000313|EMBL:KLU08884.1,
RC   ECO:0000313|Proteomes:UP000036489};
RA   Palermo B.R., Castro D.B., Cauz A.C., Magalhaes B.L., Carlos C.,
RA   Costa F.L., Scagion G.P., Higac J.H., Pereira L.B., Almeida L.D.,
RA   Neves M.S., Cordeiro M.A., Prado P.F., Silva T.M., Balsalobre T.W.,
RA   Paulino L.C., Vicentini R., Ferraz L.F., Ottoboni L.M.;
RT   "Draft genome sequence of Kocuria sp. SM24M-10 isolated from coral mucus.";
RL   Submitted (MAY-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:KLU08884.1}.
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DR   EMBL; LDNX01000129; KLU08884.1; -; Genomic_DNA.
DR   RefSeq; WP_047804345.1; NZ_LDNX01000129.1.
DR   AlphaFoldDB; A0A0J1ETV4; -.
DR   PATRIC; fig|1660349.3.peg.1088; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000036489; 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}.
FT   DOMAIN          701..862
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          887..1037
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1240 AA;  134365 MW;  E5013E3B905D7E48 CRC64;
     MTLSGLLAAL GAERSFANLR TQVAFPPGER SPETVISAPD GMRPVITAQL RGALDDASGG
     AADGRAPVLL AVTATGRESE DLAAALGAYL PTAGIAEFPA WETLPHERLS PRSDTVGRRL
     DVLRRLAGHD PERPLQVLTA PVRSVLQPVV EGLGEMTPVR FARGEELDFD AAVTALAQAA
     YARVDMVTRR GEFAVRGGII DVFSPVEDHP VRIEFFGDEV DELRWFAVAD QRTLTGTDHP
     DRLVAPPCRE VLITPSVMSR AAALRNALPG AESMLERIAG GIYVEGMESL APLLVDGMVP
     MLSLLPPGSL VVVMEPEKVR ARAHDLVATN EEFLLAAWDS ASDGLSAPID IGSAEHALPT
     GDDGGRTLSS GSFQTLAEAR STALGAGLGW WAVTALNVNA VAGQDVDADT AAEDIALLDS
     DADTLTVAAR DPLGFHGDVE AMLEFLSGRV ADGWRVVAVT EGPGPLARIA ELLHDAGIPA
     ARRESLEEPP QPGVVELTTA VAGKGFALDG PRIVLLTEAD LLGKASPYTT KDMRKLPVRR
     KRNAVDPLAL SPGDFVVHEQ HGVGQFVELI QRPIAGAMTK PGQPKPVREY LVLEYAASKR
     NGPKDRLFVP TDQLDQVTNY VGGETPSLSK MGGADWNKTK RAAKKAVKDI ANELIRLYSA
     RMASRGHAFG EDTPWQRELE EAFPYIETPD QLTTIDEVKA DMQREVPMDR LISGDVGYGK
     TEVAVRAAFK AVQDGKQVAV LVPTTLLAQQ HAETFTERFS GFPVHLAALS RFQTAKETKE
     TLAGLKDGSI DVVIGTHRLL SKEVQFKDLG LVVIDEEQRF GVEHKEKLKA MRTNVDVLAM
     SATPIPRTLE MSLTGIRETS TLATPPEERH PVLTYVGAYT DKQVSAAVRR ELMREGQVFY
     IHNRVSSIER KAKEIAELVP EARIAVAHGQ MSESRLEQII VDFWEKKFDV LVCTTIVETG
     LDIANANTLI VDGADRYGLS QLHQLRGRVG RGRERAYAYF LYQAEKPLSE TALERLKAVA
     AHNELGAGMQ LAVKDLEIRG AGNLLGGEQS GHIAGVGFDM YLRLVGEAVA EYRGEEDERP
     TEMKIELPVN AYLPHEYVPG EPLRLEAYRN LANAATEEAI QEVADELVDR YGEVPEPVQN
     LLEVARFRVT ARAAGLTDVA AQGNMVRFAP AELPESRQMR LTRLYPGAQV KTVPGTDTAQ
     VLIPKPKTAR IGGKDLVDRE ILEWARGVVE AVFAREPATA
//
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