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Database: UniProt
Entry: J3EQ34_9LACO
LinkDB: J3EQ34_9LACO
Original site: J3EQ34_9LACO 
ID   J3EQ34_9LACO            Unreviewed;      1173 AA.
AC   J3EQ34;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 53.
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=A11Y_119167 {ECO:0000313|EMBL:EJN55385.1};
OS   Loigolactobacillus coryniformis subsp. coryniformis CECT 5711.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Loigolactobacillus.
OX   NCBI_TaxID=1185325 {ECO:0000313|EMBL:EJN55385.1, ECO:0000313|Proteomes:UP000007271};
RN   [1] {ECO:0000313|EMBL:EJN55385.1, ECO:0000313|Proteomes:UP000007271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT5711 {ECO:0000313|Proteomes:UP000007271};
RA   Rodriguez J.M.;
RT   "Complete Genome Sequence of Lactobacillus coryniformis CECT5711.";
RL   Submitted (MAY-2012) 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:EJN55385.1}.
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DR   EMBL; AKFP01000055; EJN55385.1; -; Genomic_DNA.
DR   RefSeq; WP_003679464.1; NZ_AKFP01000055.1.
DR   AlphaFoldDB; J3EQ34; -.
DR   STRING; 1185325.A11Y_119167; -.
DR   GeneID; 65916208; -.
DR   PATRIC; fig|1185325.3.peg.2002; -.
DR   Proteomes; UP000007271; 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; 3.40.50.11140; -; 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; IPR048635; MFD_D3.
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; PF21132; MFD_D3; 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:UP000007271}.
FT   DOMAIN          635..796
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          821..971
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1173 AA;  132048 MW;  A45CD56B0ADAEF10 CRC64;
     MDLTELLLQA PKIKDWLGQV TPHSRQLVTG LQDSARSLLL SAILRAKKQP MLVVTNSLFN
     ASQLVDDLTN LLPETQVKLF PVDEVMAAQV AVSSPEYRSE RVQALTFLAQ QQPGIVVASL
     AGIRQLLPTP EMWRASALTI KPGGELDPLQ LRQQLVGMGY TREQLVGRPG EFAMRGDIID
     IYPLTAANPV RIDLFDTEVD SLRYFEASTQ RSIENLSEFT LLPATDFLVT PELLQQAAPT
     VKKAYQTELA TLKEASERTA LTDHLTPVIA ALEKGEVVPE LVRYRDLIYA PAANLTDYLP
     DDGLVILDDY PRMQESETEL AADAAQWLSE ELANQRMLHS QSVSTELKTL LRKNKHTHLY
     LTLFQKGMGN LRLDQILDLQ NRDMQQFFGQ MPLLKAEIDR WQVQQQTVVV MVGDDERRER
     VGRILRDFKM QATLAKPDTL QLQQVQIVAA TLQNGFELPD ANLVVITEKE LFNQPIKKRV
     RRQTLANAER IKSYNELNPG DYVVHVNHGI GKYVGMQTLE VDGAHQDYIT ILYQDNAKLF
     IPVSQLNLVQ KYVASEGKTP RVNKLGGSEW AKTKRKVSSK IEDIADDLIE LYAQREAEKG
     YAFSPDNEYQ REFEDAFPYT ETDDQLRSVA EIKHDMERPK PMDRLLVGDV GFGKTEVALR
     AIFKAIQDGK QAAFLVPTTI LAQQHFDTMM QRFADFPVQV ELLSRFRTAK QIKASLAAIK
     SGQADVVIGT HRILSKDVEF RDLGLLVVDE EQRFGVKAKE RLKTLRSNVD VLTMTATPIP
     RTLNMSMVGV RDLSVIETPP ANRYPVQTYV MEQNAGALRS GIERELARGG QVFYLHNRVE
     DIERTVANIE ALVPEATVTY AHGQMTEAQL ENTLYEFVHG QYDVIVTTTI IENGVNMPNV
     NTLFVEDADH MGLAQLYQLR GRVGRSSRVG YAYFMYRQDK VLTEISEKRL AAIRDFTELG
     SGFKIAMRDL SIRGAGNLLG KQQHGFIDSV GYDLYSQMLA DAVAQKQGKA VQAKSDAELD
     LGIEAYLPSE YITDQRQKIE LYKRVRELSS PADLEELQAD LFDRFGDYPD PVAHLLAIGL
     LKVYADQALV ERIRHVDQQL RVKLSAKGTR QIAPEDVFKA LSKTKLKATV KMDGDKLVIT
     LIIQPKMRQP DWLEELTQFL TGLAAIVQQA TPA
//
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