ID A0A1E3H914_9TREE Unreviewed; 1598 AA.
AC A0A1E3H914;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=L202_08260 {ECO:0000313|EMBL:ODN72827.1};
OS Cryptococcus amylolentus CBS 6039.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus.
OX NCBI_TaxID=1295533 {ECO:0000313|EMBL:ODN72827.1, ECO:0000313|Proteomes:UP000094065};
RN [1] {ECO:0000313|EMBL:ODN72827.1, ECO:0000313|Proteomes:UP000094065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 6039 {ECO:0000313|EMBL:ODN72827.1,
RC ECO:0000313|Proteomes:UP000094065};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ODN72827.1}.
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DR EMBL; AWGJ01000014; ODN72827.1; -; Genomic_DNA.
DR RefSeq; XP_018988768.1; XM_019143105.1.
DR STRING; 1295533.A0A1E3H914; -.
DR GeneID; 30159569; -.
DR OrthoDB; 57056at2759; -.
DR Proteomes; UP000094065; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
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; IPR004179; Sec63-dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR47835; HFM1, ATP DEPENDENT DNA HELICASE HOMOLOG; 1.
DR PANTHER; PTHR47835:SF2; SEC63 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF02889; Sec63; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00973; Sec63; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF158702; Sec63 N-terminal domain-like; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000094065}.
FT DOMAIN 215..396
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 462..651
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1060..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1157..1223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1281..1502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1519..1583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..68
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1164..1199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1299..1316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1335..1360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1361..1376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1402..1428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1441..1475
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1552..1574
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1598 AA; 178939 MW; 5DAC4A80FF524CCF CRC64;
MDFTDDQPLW GTGSDDDGKD EYLQFGAGMR NMNQSPVVLA LPSYHPPFQP PPARPFHPAS
PAFQRPTPPF PRSQKTTELP NTARHQRAYL SDRQDAPEYN SRSREMSFAS AKTLQRAKSG
VTAQKSEDFG DEIWDDDDFV QAANQSLQYE ADAVYDDDEQ PVATADVVKN RESMKKDVAP
NKRGKPLVPI SRLPMDERKL FKFPAFNDVQ SYVFDDTYSS DENLVVSAPT GSGKTTIFEL
AFLHCLSYKT PDDSVKPLAI YIAPTKALCN EKAKDWQERM GVALPDVTCV EITGDYGNAS
TIYNSIRGAD LIVTTPEKFD SMTRRSRNMD NMAHRLRLIM IDEVHILRES RGATLEVVIS
RMKGLGKGIR FVALSATVPN IHDIARWLGP ARYEYGQLSR GVIIGKDLDK KKTQGETNVD
DMSMAKVYKF GEEFRPVPLS RETYGIDSGG NDWALANRMD KELFPILLKH TAGQPVLVFC
PTRKSCQATA DLIFSTYEES RAKGLKLPWQ HPPGARLDLQ DKRISELSTC GIAVHHAGLD
YGDRRAIEDG FRDGKLHMIA STSTLAVGVN LPAHTVVIKG VMAWQGPATG FKEYSDIDIQ
QMMGRAGRPQ YDNSGVVVVM CERSKVRKYE TMLRSQTVLE SCLHENLTEY INSEIGLGTI
TSVYSAQECS FFHIRIQQNP RYYALSNAKD KPADDSWEEW LDRFVEEALL NLERDGFIER
SEDDGLTPTE TGKIMSGSMI SYGTMCSIKE MSPMSTLQDL LEILAGATEF ADLRIRQGES
SFLNKLRDNQ EIRFPLGEKV QNYADKVFLM LQVTFGNIIL DDIVKKTEIS PPIQTLMAIY
NHAPRIAKAI VQFALNREYG TAARSALELH RTISGKAWED SPTIFRQIPS IGPKSICVLG
QNGISTFEEL LDVGTEKIQL WLNRNSEFAR GIHDQARRMP RFHVSIEEEG MDYDGASNVL
NLRINIRPKS KVLSTESKGK RGGFITLYNL SALFLRQDGS FIGYRRMELR RLDNKDTSFV
LRVTLDRRCE KVVAVVAVDE VAGCCTVEEY ETHLDSSVYP EDMEEQNEAL AQSPQRTVVE
PSPDPEERLP NGNVPCHHNC KDKQSCQHNC CKVGVPSRKK NKATVKGAGN GNVKTATDRM
KETQETIDAL QIDSRPTAVA KAVQRVQQDR SMSRSPSPIV SSQKASQTAQ PTPRNRAQSI
SGLGKPKDVS NAPNKQALKP STAISRVRES RIVRRWESVD EQGSKVKSTA PLDSEIEDTL
ESKGMYFNHA RHHQEPLFMA HSDDETPDTY NLDDLAPSDE ETGPVKSRLF DKSKSGKSSK
SKKRTAPPAR VRDSHLLASQ QNSQVSLKNP TRSQSPAPPI SSKKRKHDED MRELMPTRGI
FSDGYETLTD SPDFGPKPLK ESTVPMQSTV KAQTKTPLTL SSSPHPVQDF NVDDLLQKYE
EDEEESHHPT RKQSPFRQSR TDGDWDLDIR KMSIELHSKP CTPVTMGDDS RDGGLPRDEM
PVSQPTTIVQ PVKRLAPLNI GGFGRPAAKR SRMMEPSDQH KTQPNLYEEV SMETVDTDKR
GSAVRKENEV DQRAVPGLEV DVPVDEDDQF EKWCTGGI
//
