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ROK1_CANAL
ID   ROK1_CANAL              Reviewed;         578 AA.
AC   Q9Y7C4; A0A1D8PFI1; Q59M31;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2017, sequence version 2.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=ATP-dependent RNA helicase CHR1;
DE            EC=3.6.4.13;
GN   Name=CHR1; Synonyms=ROK1; OrderedLocusNames=CAALFM_C112600CA;
GN   ORFNames=CaO19.11240, CaO19.3756;
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 [GENOMIC DNA].
RC   STRAIN=SC5314 / CAI4 / ATCC MYA-682;
RX   PubMed=10705369;
RX   DOI=10.1002/(sici)1097-0061(20000330)16:5<401::aid-yea531>3.0.co;2-r;
RA   Kim W.I., Lee W.B., Song K., Kim J.;
RT   "Identification of a putative DEAD-box RNA helicase and a zinc-finger
RT   protein in Candida albicans by functional complementation of the S.
RT   cerevisiae rok1 mutation.";
RL   Yeast 16:401-409(2000).
RN   [2]
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   [3]
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   [4]
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).
CC   -!- FUNCTION: ATP-dependent RNA helicase involved in 40S ribosomal subunit
CC       biogenesis. Required for the processing and cleavage of 35S pre-rRNA at
CC       sites A0, A1, and A2, leading to mature 18S rRNA.
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   -!- SUBUNIT: Interacts with the U3 snoRNA and is associated with the 90S
CC       and 40S pre-ribosomes. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC       family of RNA helicases and controls ATP binding and hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX52/ROK1
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AOW26875.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF140505; AAD26468.1; -; Genomic_DNA.
DR   EMBL; CP017623; AOW26875.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_710786.2; XM_705694.2.
DR   AlphaFoldDB; Q9Y7C4; -.
DR   SMR; Q9Y7C4; -.
DR   STRING; 237561.Q9Y7C4; -.
DR   PRIDE; Q9Y7C4; -.
DR   GeneID; 3647601; -.
DR   KEGG; cal:CAALFM_C112600CA; -.
DR   CGD; CAL0000178978; CHR1.
DR   eggNOG; KOG0344; Eukaryota.
DR   HOGENOM; CLU_003041_1_4_1; -.
DR   InParanoid; Q9Y7C4; -.
DR   OrthoDB; 400908at2759; -.
DR   PRO; PR:Q9Y7C4; -.
DR   Proteomes; UP000000559; Chromosome 1.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030490; P:maturation of SSU-rRNA; IBA:GO_Central.
DR   CDD; cd17957; DEADc_DDX52; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR044764; DDX52/Rok1_DEADc.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT   CHAIN           1..578
FT                   /note="ATP-dependent RNA helicase CHR1"
FT                   /id="PRO_0000232300"
FT   DOMAIN          162..339
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          350..514
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          517..578
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           131..159
FT                   /note="Q motif"
FT   MOTIF           286..289
FT                   /note="DEAD box"
FT   COMPBIAS        29..55
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..81
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        517..535
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        543..578
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         175..182
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   CONFLICT        65
FT                   /note="S -> N (in Ref. 1; AAD26468)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        152
FT                   /note="V -> I (in Ref. 1; AAD26468)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        310
FT                   /note="P -> L (in Ref. 1; AAD26468)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        565
FT                   /note="E -> K (in Ref. 1; AAD26468)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   578 AA;  65427 MW;  B9C3831905A4F699 CRC64;
     MDIFRILSRG ASLNKKKGIT TDYALPSEKQ TQKQKHKQES LLNEVERETD FFHTRKHNSN
     STTTSGKGDK LTNGANSNKE EQMETNETKA KEEEIPPPEL TTEEDAQTFR NLHKSKVTGD
     DIPIPIGSFQ DMIGRFHINK KVLSNLIDNE FVEPTPIQCE SIPITLNNRD LIACAPTGSG
     KTLAFLIPLV QQILSKNVSK NHGIRGLIIS PTNELAVQIF QELEIITRGC KQINVAILSK
     QLASKLNNNI IKSSKYDIIV STPLRLIDVV KQGNMDLSKI EQLIIDEADK LFDHGFAEQT
     DEILTHCTNP KIRKSIFSAT IPSSVEEMAH SIMKDPLRII IGHKEAASNT IDQKLVFTGN
     EQGKLLAIRQ MIQQGEFKPP IIIFLQSITR AKALFHELLY DRLNVDVIHA ERTPKQREEV
     IKRFKNGDIW VLITTDVLAR GVDFKGVNLV INYDVPQSAQ AYVHRIGRTG RGGKAGKAVT
     FFTKEDDKAI KPILNVMKQS GCNDGYSQWM EDMGKLSKKE KKQIKTHEIQ RKKISTVPKV
     IKQKRKQRQD MIAASKRRKQ ESKQESKQES HSNDEREE
 
 
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