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Database: UniProt
Entry: Q5KAW6_CRYNJ
LinkDB: Q5KAW6_CRYNJ
Original site: Q5KAW6_CRYNJ 
ID   Q5KAW6_CRYNJ            Unreviewed;       710 AA.
AC   Q5KAW6;
DT   15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE            EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN   OrderedLocusNames=CNJ00220 {ECO:0000313|EMBL:AAW45762.1};
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684 {ECO:0000313|EMBL:AAW45762.1, ECO:0000313|Proteomes:UP000002149};
RN   [1] {ECO:0000313|EMBL:AAW45762.1, ECO:0000313|Proteomes:UP000002149}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565 {ECO:0000313|Proteomes:UP000002149};
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J., Koo H.L., Krzywinski M.I., Kwon-Chung J.K.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
CC   -!- FUNCTION: RNA helicase. {ECO:0000256|RuleBase:RU365068}.
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         Evidence={ECO:0000256|RuleBase:RU365068};
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       {ECO:0000256|RuleBase:RU365068}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC       {ECO:0000256|RuleBase:RU365068}.
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DR   EMBL; AE017350; AAW45762.1; -; Genomic_DNA.
DR   RefSeq; XP_567279.1; XM_567279.1.
DR   AlphaFoldDB; Q5KAW6; -.
DR   STRING; 214684.Q5KAW6; -.
DR   PaxDb; 214684-Q5KAW6; -.
DR   EnsemblFungi; AAW45762; AAW45762; CNJ00220.
DR   GeneID; 3254163; -.
DR   KEGG; cne:CNJ00220; -.
DR   VEuPathDB; FungiDB:CNJ00220; -.
DR   eggNOG; KOG0342; Eukaryota.
DR   HOGENOM; CLU_003041_26_6_1; -.
DR   InParanoid; Q5KAW6; -.
DR   OMA; REAMTAC; -.
DR   OrthoDB; 276261at2759; -.
DR   Proteomes; UP000002149; Chromosome 10.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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   PANTHER; PTHR24031:SF384; DEAD-BOX ATP-DEPENDENT RNA HELICASE 31; 1.
DR   PANTHER; PTHR24031; RNA HELICASE; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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|RuleBase:RU365068};
KW   Helicase {ECO:0000256|RuleBase:RU365068, ECO:0000313|EMBL:AAW45762.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU365068};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU365068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002149};
KW   RNA-binding {ECO:0000256|RuleBase:RU365068}.
FT   DOMAIN          157..359
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          387..566
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          196..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          632..710
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   710 AA;  77345 MW;  2069E80B00B83E1D CRC64;
     MLPRQLSRAP RALGYVLPRF SPPSSVLRTV TPAFARSTQL SLRRILEKRG YAVSAVAEKD
     DDFFSGAELA PSSNTVVIPP QLDDPGHPAS EPLVDTVPFE SLKGRINHDT LKALTVKPFK
     FTAMSEVQKR VLGLLPHLSG GKLRSKAREE AEQEGEVEMK EEREDLLVKA KTGTGKTMAF
     LVPAIDARIN TLERLSKAPN PDGTIPDKHA QGRNHRAISR SHLGALIISP TRELATQIAV
     EAEKLCTWHK DLTVHSFVGG ESRLRQLKEF SRRSKDVVVA TPGRLRDLIS EPLVKDALAK
     TDMLVLDEAD TLLDMGFSED LKFIIDHLPK ERQTLFFSAT VSKEIAAIAR HSLRKGHKVI
     DCVPKNESNV HLHIPQYATV VPSSADAMPH IMRLIAQDQM ANPKSKIVLF LNTTKQTMLT
     ATLVRELVDT LPAQTAVYEI HSKLDQNKRT RSSDKFRREH RPAVLVTSDV SARGVDYPGV
     TRVIQLGVPS TTEQYIHRVG RTGRAGKEGR GDLVLFPFEA GFLDHLKGIP IQRISTSDLT
     SDVIAKAPSS YASVIDSLPS AVESLLPTLD PKAVEEVFMS MLGYYHSKQQ MLDASAQDIL
     KGLKAWSVEG GGLIEPPYVS EEFLKKVGFS EKRRNTRNGG GGSRGGFGRS SGGFGRGSGG
     FGKRDGGRRE DSGGFGGRGQ GGGGSGFGAR RDGGGGFAGK SRSGGFKRDY
//
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