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Database: UniProt
Entry: C5MD77_CANTT
LinkDB: C5MD77_CANTT
Original site: C5MD77_CANTT 
ID   C5MD77_CANTT            Unreviewed;       705 AA.
AC   C5MD77;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   ORFNames=CTRG_04178 {ECO:0000313|EMBL:EER32507.1};
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:EER32507.1, ECO:0000313|Proteomes:UP000002037};
RN   [1] {ECO:0000313|EMBL:EER32507.1, 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00000600};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC         Evidence={ECO:0000256|ARBA:ARBA00000600};
CC   -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family.
CC       {ECO:0000256|ARBA:ARBA00007913}.
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DR   EMBL; GG692399; EER32507.1; -; Genomic_DNA.
DR   RefSeq; XP_002549881.1; XM_002549835.1.
DR   AlphaFoldDB; C5MD77; -.
DR   STRING; 294747.C5MD77; -.
DR   EnsemblFungi; CTRG_04178-t43_1; CTRG_04178-t43_1-p1; CTRG_04178.
DR   GeneID; 8299442; -.
DR   KEGG; ctp:CTRG_04178; -.
DR   VEuPathDB; FungiDB:CTRG_04178; -.
DR   eggNOG; KOG1803; Eukaryota.
DR   HOGENOM; CLU_001666_8_2_1; -.
DR   OrthoDB; 170190at2759; -.
DR   Proteomes; UP000002037; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   CDD; cd18808; SF1_C_Upf1; 1.
DR   Gene3D; 2.40.30.270; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041679; DNA2/NAM7-like_C.
DR   InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR047187; SF1_C_Upf1.
DR   InterPro; IPR004483; SMUBP-2/Hcs1-like.
DR   InterPro; IPR048761; SMUBP-2_HCS1_1B.
DR   NCBIfam; TIGR00376; IGHMBP2 family helicase; 1.
DR   PANTHER; PTHR43788:SF19; DNA-BINDING PROTEIN SMUBP-2; 1.
DR   PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF13086; AAA_11; 1.
DR   Pfam; PF13087; AAA_12; 1.
DR   Pfam; PF21138; SMUBP-2_HCS1_1B; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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          234..491
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|SMART:SM00487"
FT   DOMAIN          252..457
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   COILED          362..389
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   705 AA;  80026 MW;  CA146E900DB54E7F CRC64;
     MRSNYNKIAL ISRNKVQTFF FFYRSTNTYI KTMRLYDKFK TAIIEEQQED VEQTTTYINT
     FTPKKLAQLG LGIINLQIAN IRTGLGGKTI LELQLDPGFS ATDEINTSTL RTGDIVRLSR
     MSSSKPDKKS KKDGEESTSD GIDAVVLKVT TQAISISVDE ANDDSKVLQY YNNTNDQNSR
     MWLVKLANSI TYKRMLMSMD KVNALEDKND IHRILLGESK YIPKPTSNLK LEFINDRLND
     SQKEAIDFAI NKSNITIIHG PPGTGKTYTL IELIQQLTNN LGEKVLVCGP SNISVDTILE
     RLHDKYKKPE KLIRMGHPAR LLPGNLAHSL EILSKSYGHD VIKDIEKDIQ STLSQIKKCK
     RYAERKALYQ ELKLLRKELK QREKKIVAEL LQQSQVVIST LHGAGSFDLK GVSFDTIIID
     EVSQSLEPQC WIPLLLTSNF KRLVIAGDNM QLPPTIKCKK NESFLGTTLF DRLVKQCDGD
     SFRKLLNVQY RMNQSIMEFP SMQLYDNKLL CDSSVKDISL LDLPGVEDNE TTSAKCIWYD
     TQGGEFPEQI NESIEGGDSK YNEMEILVVQ GHLQKLLDSG VRPQDIGIIS PYAAQVQLLK
     KKVVPEVEVH TVDGFQGREK EVIILSLVRS NDDREIGFLS EQRRLNVAIT RPKRHLCIVG
     DLELLNQGGQ GSNSFLRKWC KYVEDGEGEE PYEIEYPNLT DYLEN
//
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