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Database: UniProt
Entry: A0A2M9R4I4_9FLAO
LinkDB: A0A2M9R4I4_9FLAO
Original site: A0A2M9R4I4_9FLAO 
ID   A0A2M9R4I4_9FLAO        Unreviewed;      1115 AA.
AC   A0A2M9R4I4;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
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   ECO:0000313|EMBL:PJR03769.1};
GN   ORFNames=CDL10_03950 {ECO:0000313|EMBL:PJR03769.1};
OS   Avrilella dinanensis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Avrilella.
OX   NCBI_TaxID=2008672 {ECO:0000313|EMBL:PJR03769.1, ECO:0000313|Proteomes:UP000231960};
RN   [1] {ECO:0000313|EMBL:PJR03769.1, ECO:0000313|Proteomes:UP000231960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UR159 {ECO:0000313|EMBL:PJR03769.1,
RC   ECO:0000313|Proteomes:UP000231960};
RA   Leyer C., Sassi M., Minet J., Kayal S., Cattoir V.;
RT   "Description of Avrilella dinanensis gen. nov. sp. nov.";
RL   Submitted (JUN-2017) 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:PJR03769.1}.
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DR   EMBL; NIPO01000001; PJR03769.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2M9R4I4; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000231960; 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; 3.40.50.300; 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; 3.
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:UP000231960}.
FT   DOMAIN          571..732
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          753..907
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1115 AA;  128207 MW;  CE726CF62D427516 CRC64;
     MNLSDIYANN SKTKQLLKSI LVKRNQILAK GFVGSSLSFV VQELFRQADN PFMLVFNDKE
     EAAYYLNDLE NLLNKKDVLF YPGSYRRPYE IETTDNANVL LRAEVLNRIN SRKKPAIIVT
     YADALLEKVV TKKQLEQNTL RLILNEEISL DKVNETLFEY DFKRVDFVTE PGEFSVRGGI
     LDVFSFSNDL PYRIEFFGDE IDSIRTFDIE TQLSVENLKK IDIIPNIANK STQEQRENFL
     SFIKNETIVF VQNTQFLKDR LQHLFEKAED AFARLDQTIK RLSPAEMFVS GKELTKQLFH
     FTSVCLNENP DFVPNEKIEF LFRPQPTFNK QFDLLIDNLN TNHQNGYVNY LYCTSEAQAT
     RFYDIFENFK ENGQKQVISY ETKVFPLYQG FIDDENQIAC YTDHQIFERY HRFSIKNSKN
     KKQNITLKEL TSLSVGDYVT HIDHGIGKFG GLQKIEVDGK KQEAIKLIYA DNDIVYVGIH
     ALHKIAKYNG KDGAEPKIYK LGSQAWKNLK KKTKARVKEI AFNLIKLYAK RRTERGFACA
     PDSYLQAELE SSFLYEDTPD QYKATNDVKA DMENERPMDR LVCGDVGFGK TEVAIRAAFK
     MVDNGKQVAV LVPTTVLAFQ HYQTFRERLK NLPIRVEYLN RFKTGKQKTQ TLEDLANGKI
     DIIIGTHQLV GKSIQFKDLG LLIVDEEQKF GVAVKDKLKT LGENIDTLTL TATPIPRTLQ
     FSLMAARDLS IISTPPPNRY PIETSVVGFN EETIRDAISM ELERGGQVFF INNRIENIRE
     IAGMIQRLVP DARVAVGHGQ MDGKQLERTL LDFIDGKYDV LVATTIIESG LDVPNANTIF
     INNANNFGLS DLHQMRGRVG RSNKKAFCYF ICPPYSLMTE EARKRLEALE QFSDLGSGFN
     IAMKDLEIRG AGDLLGGEQS GFINEIGFET YQKIMNEAIE ELKEDEFKEL YDENEPEKPK
     KYVRDFVLES DFEVLFPDDY VNNITERMNL YNELNAVKNE QELAKFEEKI TDIFGQIPPT
     ARNLLDSVKI KWKAVELGIE KLVLKQGKMI GYFVADQSSP FYQTDQFRKV LMFVQNNPTL
     CRLKEKETKK GLRLLLTFEQ VKSIDKALSL IYKIN
//
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