ID   A0A1E3I068_9TREE        Unreviewed;      1411 AA.
AC   A0A1E3I068;
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=DEAH box polypeptide 36 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=L202_02313 {ECO:0000313|EMBL:ODN81982.1};
OS   Cryptococcus amylolentus CBS 6039.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus.
OX   NCBI_TaxID=1295533 {ECO:0000313|EMBL:ODN81982.1, ECO:0000313|Proteomes:UP000094065};
RN   [1] {ECO:0000313|EMBL:ODN81982.1, ECO:0000313|Proteomes:UP000094065}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 6039 {ECO:0000313|EMBL:ODN81982.1,
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   -!- 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:ODN81982.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AWGJ01000003; ODN81982.1; -; Genomic_DNA.
DR   RefSeq; XP_018996301.1; XM_019135898.1.
DR   STRING; 1295533.A0A1E3I068; -.
DR   GeneID; 30153622; -.
DR   OrthoDB; 1095660at2759; -.
DR   Proteomes; UP000094065; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   CDD; cd17917; DEXHc_RHA-like; 1.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF197; DEPENDENT RNA HELICASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G07950)-RELATED; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF21010; HA2_C; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094065}.
FT   DOMAIN          663..841
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          932..1115
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          294..314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          361..449
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          870..913
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..69
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        365..403
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1411 AA;  155704 MW;  3E47D50D0FA2D459 CRC64;
     MAKKKLSLKP VQRGFATTSA AKKPQSQQPP SPLSQHDATP EEPLGDQPRE KVEAESTDAK
     KEDWEDDDAT ERNALQGFVD RLHEKGEKEV VRVIKAIEFD QRLGASFPKV EINQSLRDQA
     LETALEEERA NLIDPSNPPT VTHPAANAPE TEKGLLRFFI AYHVLQRLGF RTARIEQCFL
     QGLQEGEGWE EALEWLWLHC TEDECLQKGE FAKQEERPLE EPEEALLPAL ESVIEEKVIQ
     DAPPLQTASV VTGPDPSTTA TSLFQAADSE SDSGSDLDDG NSVNEQWARL QLSLDTLRGP
     GSGKKGKKGK GSGVVLDTPE IRRLKEKIAA VEKEYMFSRK HADSILKTLK SQRNAESIAA
     KFKGLSTKPE EKAEEQVDKD VQPENERTGL PVQEEEEKPK ATDSSNILDA SASDDDDGGG
     LFGAMLDEPT KPKSGIQPDT VPSSSTSISV RSMPIPKQLS FAGTIPKNVL KAAFSKATKQ
     VVLSYVNLSG HSKAARAGLE CRWQSGSDKG RRIWRMDDIA CDDMAQAENY VSTLALSDLE
     AEKLISGVNW RTMPVAYREL WEELGIEKKE KEDASRREVW KTIKKLWDAK ATEVTMEKGI
     VDKSSGGKEK DGGQTKGVEM DKEDVFVKDL QDDYAKRRES APYQNMLKQR DTLPIASFRD
     EILATLEQNQ VMVFSGETGC GKSTQLPSYI LENQLSQGKP CKIVVTEPRR ISAISLAQRV
     SQELGDATGA VGSLSSLVGY SIRLESKTSA NTRLSFVTNG IALRMLESGS SGDSKGTAFD
     EITHIIVDEV HERSIESDFL LIVLKNLCQT RPDLKVVLMS ATVDAEKISN FFGRAPYMSV
     PGRTFPVTVN YLEDAVQLAG WSIDERSPYA VRGRRQKPQS QMLEWNEEGA KSDSDPSDDE
     EESTSVNPAK LSSARYSSQT VNTLNLLDSR QIPYDLIVAL LEKVCYGSLE HVTFSQATLV
     FMPGLAEIRK LNDMLLAHPQ FGSQEFVVWP LHSSISSEGQ GAVFQKPPKG VRKIVISTNI
     AETGVTIPDI TCVIDTGKQR EMRYDEKRQL SRFVESYVAR SNAKQRRGRA GRVQEGLAFH
     LFTKARHDTQ LAEHPIPEML RLSLQDLALR IKILKVPLGN TISSVLLQAL DPPSAINIQR
     AISSLVEVKA LTVNEDITPL GRLLSKLPMD VHLGKFLLVA AMYGCLDPAL TIAATLNSKS
     PFVTPFGFES QARAAKAGFA IGNSDFLTIA NVFASWRRAS DNPNFVRTFC KRNYVSHQNL
     QQIEELRQQL LAYLVDTAFV DTTPEQRRAI SQSRFSKGVR TRFVPVPAAV NVNGEDFKVL
     GAALVSGLYP KLLALDPSGG LKTITNQQPV VIVSTIHSIV HMSLIYSHST PAQSTSKFPT
     SLLGPTISHT SPSCTPRGCM HGKQGPWKIR R
//