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Database: UniProt
Entry: Q5KMI8_CRYNJ
LinkDB: Q5KMI8_CRYNJ
Original site: Q5KMI8_CRYNJ 
ID   Q5KMI8_CRYNJ            Unreviewed;       937 AA.
AC   Q5KMI8; Q55XE5;
DT   15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 2.
DT   27-MAR-2024, entry version 131.
DE   RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364117};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU364117};
GN   OrderedLocusNames=CNB01550 {ECO:0000313|EMBL:AAW41518.2};
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:AAW41518.2, ECO:0000313|Proteomes:UP000002149};
RN   [1] {ECO:0000313|EMBL:AAW41518.2, 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   -!- 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:ARBA00001665,
CC         ECO:0000256|RuleBase:RU364117};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU364117}.
CC   -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC       {ECO:0000256|ARBA:ARBA00005446, ECO:0000256|RuleBase:RU364117}.
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DR   EMBL; AE017342; AAW41518.2; -; Genomic_DNA.
DR   RefSeq; XP_568825.1; XM_568825.1.
DR   AlphaFoldDB; Q5KMI8; -.
DR   STRING; 214684.Q5KMI8; -.
DR   PaxDb; 214684-Q5KMI8; -.
DR   EnsemblFungi; AAW41518; AAW41518; CNB01550.
DR   VEuPathDB; FungiDB:CNB01550; -.
DR   eggNOG; KOG0351; Eukaryota.
DR   HOGENOM; CLU_001103_12_0_1; -.
DR   InParanoid; Q5KMI8; -.
DR   OrthoDB; 5474026at2759; -.
DR   Proteomes; UP000002149; Chromosome 2.
DR   GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; 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:0009378; F:four-way junction helicase activity; IBA:GO_Central.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR   CDD; cd17920; DEXHc_RecQ; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032284; RecQ_Zn-bd.
DR   NCBIfam; TIGR00614; recQ_fam; 1.
DR   PANTHER; PTHR13710:SF105; BLOOM SYNDROME PROTEIN; 1.
DR   PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF16124; RecQ_Zn_bind; 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:RU364117};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU364117};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364117};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU364117}; Nucleus {ECO:0000256|RuleBase:RU364117};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002149}.
FT   DOMAIN          69..244
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          282..444
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          519..562
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          578..629
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          657..697
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        536..562
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        587..626
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        669..686
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   937 AA;  106153 MW;  BB1A5B575A1B7A75 CRC64;
     MLAFPSSTPA ERPYTNLVNS TQFARNNFRP TKREWRRTMS PQETPSALQR NLKHHWGYND
     FRHPQLEICT DALRGCDLIV VAPTGLGKSL CFQLPAITIE HGVTIVVSPL KALMSDQVKD
     LTSRGIKAVQ LNEYTTLAEH NEVRRQMRMG HPEIRLLYVT PEMLLSDKHR STFDTAYAQK
     QVARLVVDEA HVITEWGTSF RGKYRELGKF RERYYDIPIT ALTASATKEV RHDIIQTLRI
     RKGYGQWVMP FNRRNLFYEI RYQGRGSIEK EEMEVQKNPL DDIVDFIEKY RPEAAKRNRE
     NGIFRICVTG IVYCRTTAAC EEVAGFLSNR RIKAMPYYKN LSQTVKDQAL AGWKDGSIEC
     IVATIAFGMG IDQANVRYVI HYQMPKTFEG YYQETGRAGR DGHISHCILY YSREDAKYLR
     WLLEQEDAKQ KRIARFKSGD ACAETSSQTL NSFKALQHYM ESLGRCRHVG ICSYFGEKID
     DKDPEIKAAY CQSMCDICKD NAKVRKAAMH LTDAIPVASA IAGREPTPIP DQDPKPEPLF
     DPREGDDTDT DEHHDEFLDL HGPDPDIFEE GLAGTAPPIF QIADPRSSGS HAGNHQNTPL
     VSSTNSHVQS SNTIPSSMSS KPPSVPLSRT PVLVRDLSSE RVAQPIRVRE IIHIETGGEP
     EPQSLANKRR RAGQGSMLSS SPTSSMEFEE IEKEREREME KVRLRKEKER QEAMARERER
     PIFSSNARLP DNVKFVQDSE EGTASELKLT REQRIKAERM LNSVKPVRGE GPYACYNAAP
     PAARFRKASS ASDKAFKPPI LKSPTKVRCD LLTKSARDNA VLEISNSLKD SLGHGDLART
     VLNSWGRLER GSKRVTVLQD VARAIERDFA AISREDPLGF ERRITEFRKA AKALRSSEVV
     DAIAQGDIDL FDDGSPEVGH LKSLEKYMRT WKPEPSE
//
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