ID C5M8E8_CANTT Unreviewed; 1043 AA.
AC C5M8E8;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=DNA repair and recombination protein RAD26 {ECO:0008006|Google:ProtNLM};
GN ORFNames=CTRG_02670 {ECO:0000313|EMBL:EER33852.1};
OS Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294747 {ECO:0000313|EMBL:EER33852.1, ECO:0000313|Proteomes:UP000002037};
RN [1] {ECO:0000313|EMBL:EER33852.1, ECO:0000313|Proteomes:UP000002037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; GG692397; EER33852.1; -; Genomic_DNA.
DR RefSeq; XP_002548373.1; XM_002548327.1.
DR AlphaFoldDB; C5M8E8; -.
DR STRING; 294747.C5M8E8; -.
DR EnsemblFungi; CTRG_02670-t43_1; CTRG_02670-t43_1-p1; CTRG_02670.
DR GeneID; 8302056; -.
DR KEGG; ctp:CTRG_02670; -.
DR VEuPathDB; FungiDB:CTRG_02670; -.
DR eggNOG; KOG0387; Eukaryota.
DR HOGENOM; CLU_000315_7_0_1; -.
DR OrthoDB; 5488252at2759; -.
DR Proteomes; UP000002037; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0061635; P:regulation of protein complex stability; IEA:EnsemblFungi.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IEA:EnsemblFungi.
DR CDD; cd18000; DEXHc_ERCC6; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.120.850; SWI2/SNF2 ATPases, N-terminal domain; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45629:SF7; DNA EXCISION REPAIR PROTEIN ERCC-6-RELATED; 1.
DR PANTHER; PTHR45629; SNF2/RAD54 FAMILY MEMBER; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000002037}.
FT DOMAIN 293..491
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 628..793
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 98..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 34..61
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 170..191
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..219
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1043 AA; 119862 MW; 2C0A56FFFF56974B CRC64;
MSELDQLDVK LVDQDELETS ITKKANKVLL SKDVELDEKR LEKATKLLER TKRQITALSN
QLSNPRTKIS ERKRLKDEIS YIEENDLAPQ LRDVDEIKKR LQENTKQIND KTPSQKNSSD
RLPDESERDY LIRTGKITAF GNENAFQSGE DHELEQTSHV FLREPGIDQD IESEPEEVGN
DDDEDYVYEE DKKHDDEEYV NDQDEVDVDT DEDDSRNIDD GDESLYQKRL QTWVRKRSSL
RPHSDDSENK DTPEWFLPHP TIADAKLNEN FRLPGDIYPS LFDYQKTCVQ WLWELYSQKT
GGILGDEMGL GKTIQIISFL AGLHYSGLLD KPVLIVVPAT VLNQWVNEFH RWWPPLRCVI
LHSIGSGMNG KNINEAKLEE FLENADPNSS KSSLSGVKSQ INAKEIIDRV MEKGHVLVTT
YVGLRIYSKY LLPREWGYVV LDEGHKIRNP DSDISLTCKM IKTVNRIILS GTPIQNNLIE
LWSLFDFVFP GRLGTLPVFQ QQFSIPINIG GYANSNNLQV KTAYKCAVVL RDLISPYMLR
RLKSDVAKDL PKKNEMVLFV KLTKPQQELY EKFLQSEDLD SILKGKRNML MGIDILRKIC
NHPDLVYRDA MMKKKSYGDP SRSGKMQVLK NLLQIWQSED HKTLLFCQTR QMLDILEKFV
ANLPLLNGGE FNYLRMDGST PISRRQMLVD KFNRDPNMHV FLLTTKVGGL GVNLTGADRV
IIYDPDWNPS TDIQARERAW RLGQKKDITI YRLMTTGSIE EKIYHRQIFK TFLTNKILKD
PKQRRFFKAN DLHDLFTLGD QDEEGTETEA MFNEKNNNNG SSLFTKKYKN DDDFYQVAKI
AGVSKLDKFE DGEDEDGNDK QSENKDDSRV MSSIFSTGGV HSTLAHDDIV NSQSKEDPTN
MLENEASKIA NAAAEALKES RKQARKNKIG VPTWTGKFGS VPKKRKINSS SSILANLKKK
NEIKDSKQKV ADVPLDRKQM IEKLVTYLNT VEDNFSTSNE IVKKVDLSMK SEEDMVLIRS
MLREVAVWDS ARKGWKLKDE FVD
//
