SUV3_CANAL
ID SUV3_CANAL Reviewed; 720 AA.
AC Q59TB2; A0A1D8PH29;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=ATP-dependent RNA helicase SUV3, mitochondrial;
DE EC=3.6.4.13;
DE Flags: Precursor;
GN Name=SUV3; OrderedLocusNames=CAALFM_C204350CA;
GN ORFNames=CaO19.11994, CaO19.4519;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP FUNCTION.
RX PubMed=14663094; DOI=10.1099/mic.0.26640-0;
RA Nobile C.J., Bruno V.M., Richard M.L., Davis D.A., Mitchell A.P.;
RT "Genetic control of chlamydospore formation in Candida albicans.";
RL Microbiology 149:3629-3637(2003).
RN [5]
RP FUNCTION.
RX PubMed=16087754; DOI=10.1128/ec.4.8.1493-1502.2005;
RA Richard M.L., Nobile C.J., Bruno V.M., Mitchell A.P.;
RT "Candida albicans biofilm-defective mutants.";
RL Eukaryot. Cell 4:1493-1502(2005).
RN [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=20223293; DOI=10.1016/j.micinf.2010.03.001;
RA Fuchs B.B., Eby J., Nobile C.J., El Khoury J.B., Mitchell A.P.,
RA Mylonakis E.;
RT "Role of filamentation in Galleria mellonella killing by Candida
RT albicans.";
RL Microbes Infect. 12:488-496(2010).
CC -!- FUNCTION: Required for intron-independent turnover and processing of
CC mitochondrial RNA. It is a key control element in nuclear-mitochondrial
CC interactions (By similarity). Required for embedded hyphal growth, for
CC wild-type respiratory growth, and biofilm development. Required for
CC chlamydospore formation, distinctive morphological feature of the
CC fungal pathogen C.albicans that can be induced to form in oxygen-
CC limited environments and has been reported in clinical specimens. Plays
CC am important role in virulence. {ECO:0000250,
CC ECO:0000269|PubMed:14663094, ECO:0000269|PubMed:16087754,
CC ECO:0000269|PubMed:20223293}.
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=3.6.4.13;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Leads to completely attenuated virulence in a
CC mouse keratitis model. {ECO:0000269|PubMed:20223293}.
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DR EMBL; CP017624; AOW27461.1; -; Genomic_DNA.
DR RefSeq; XP_712944.2; XM_707851.2.
DR AlphaFoldDB; Q59TB2; -.
DR SMR; Q59TB2; -.
DR STRING; 237561.Q59TB2; -.
DR GeneID; 3645451; -.
DR KEGG; cal:CAALFM_C204350CA; -.
DR CGD; CAL0000176369; SUV3.
DR VEuPathDB; FungiDB:C2_04350C_A; -.
DR eggNOG; KOG0953; Eukaryota.
DR HOGENOM; CLU_010647_2_2_1; -.
DR InParanoid; Q59TB2; -.
DR OrthoDB; 1106167at2759; -.
DR PRO; PR:Q59TB2; -.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0000262; C:mitochondrial chromosome; IEA:EnsemblFungi.
DR GO; GO:0045025; C:mitochondrial degradosome; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008859; F:exoribonuclease II activity; IEA:EnsemblFungi.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0009060; P:aerobic respiration; IMP:CGD.
DR GO; GO:0036187; P:cell growth mode switching, budding to filamentous; IMP:CGD.
DR GO; GO:0071467; P:cellular response to pH; IMP:CGD.
DR GO; GO:0001410; P:chlamydospore formation; IMP:CGD.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IMP:CGD.
DR GO; GO:0036180; P:filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR GO; GO:0036177; P:filamentous growth of a population of unicellular organisms in response to pH; IMP:CGD.
DR GO; GO:0000372; P:Group I intron splicing; IEA:EnsemblFungi.
DR GO; GO:0006264; P:mitochondrial DNA replication; IEA:EnsemblFungi.
DR GO; GO:0000965; P:mitochondrial RNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0000957; P:mitochondrial RNA catabolic process; IEA:EnsemblFungi.
DR GO; GO:0006390; P:mitochondrial transcription; IMP:CGD.
DR GO; GO:0006401; P:RNA catabolic process; IBA:GO_Central.
DR GO; GO:0044011; P:single-species biofilm formation on inanimate substrate; IMP:CGD.
DR CDD; cd17913; DEXQc_Suv3; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022192; SUV3_C.
DR InterPro; IPR044774; Suv3_DEXQc.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF12513; SUV3_C; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Helicase; Hydrolase; Mitochondrion; Nucleotide-binding;
KW Reference proteome; Transit peptide; Virulence.
FT TRANSIT 1..40
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 41..720
FT /note="ATP-dependent RNA helicase SUV3, mitochondrial"
FT /id="PRO_0000422108"
FT DOMAIN 208..349
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 359..523
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT BINDING 221..228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 720 AA; 81824 MW; B71A4E8FAB19754B CRC64;
MLLCQKPTYR LLRYSVKRYV ASLYSLRGVS TRVNLIHRTY ATTVAKDNID HNDSSPVFNN
NEVRFENINA SIHPILLDLK NKLIKGKFDS PYTILNDQPS DVKTEIFQSF EQQLSKALSS
KSTPENKITL VDYLNPTLDN ISSLLHLISN NTYPNNFLEF SNLSSNNDLI MQLFTQLLHK
IFLQYRIENA SFEKPKVDFS NPAEWFPEAR KMKRKIIMHV GPTNSGKTYN SLIKLSKSKT
GYYAGPLRLL AREIYEKFNS QGIGCNLITG EEVVPSIDKY GKVSGIASGT IEMIPLHKKM
DLCVIDEIQM IADPLRGSVW TNAVLGVLAH EIHLCGEESA VPFIQKMVEI TGDELEIKKF
NRLGKLTVEK SNTSLQQLKK GDCLVVFSKK KILKFKCDIE RNTRLKVGVI YGALPPEIRS
QEASKFNNGE YDVLVASDAI GMGLNLKINR IVFSGVNKFN GSTVEKLSVS QVKQIAGRAG
RFSAQHGSKE GFVTALHRSS LVYIDQCLKT PVSEISKACI WPTSNIWRQY MANDPHKSSL
SSVYENFLTN VLKFQSDNFF ISELDQKVQL LNLVAKNRLL STMIIDDQLT ISETPINFRT
SVNPKLLKNT VIKFYETIVK RDCKSILDFD FLDLELLSQN SFVGTDVMVP LQKVDKLEDM
HRLVLLFLWL SQRFPTLFID KDSAMEVKAL VEKRINQELV NVERANSFFS DRSNGYEPRR
