ID A0A3N2PQ65_9PEZI Unreviewed; 1514 AA.
AC A0A3N2PQ65;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Helicase associated domain-containing protein {ECO:0000313|EMBL:ROT36516.1};
GN ORFNames=SODALDRAFT_315445 {ECO:0000313|EMBL:ROT36516.1};
OS Sodiomyces alkalinus F11.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Sodiomyces.
OX NCBI_TaxID=1314773 {ECO:0000313|EMBL:ROT36516.1, ECO:0000313|Proteomes:UP000272025};
RN [1] {ECO:0000313|EMBL:ROT36516.1, ECO:0000313|Proteomes:UP000272025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F11 {ECO:0000313|EMBL:ROT36516.1,
RC ECO:0000313|Proteomes:UP000272025};
RX PubMed=30368956; DOI=10.1111/mec.14912;
RA Grum-Grzhimaylo A.A., Falkoski D.L., van den Heuvel J.,
RA Valero-Jimenez C.A., Min B., Choi I.G., Lipzen A., Daum C.G., Aanen D.K.,
RA Tsang A., Henrissat B., Bilanenko E.N., de Vries R.P., van Kan J.A.L.,
RA Grigoriev I.V., Debets A.J.M.;
RT "The obligate alkalophilic soda-lake fungus Sodiomyces alkalinus has
RT shifted to a protein diet.";
RL Mol. Ecol. 27:4808-4819(2018).
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; ML119059; ROT36516.1; -; Genomic_DNA.
DR STRING; 1314773.A0A3N2PQ65; -.
DR OrthoDB; 1095660at2759; -.
DR Proteomes; UP000272025; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; 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; 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; IPR011709; DEAD-box_helicase_OB_fold.
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 Pfam; PF07717; OB_NTP_bind; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000272025}.
FT DOMAIN 716..887
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 966..1143
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1514 AA; 167814 MW; F63B1C45A250A4ED CRC64;
MAGAKKKKKP AANPARGFAT TSIASKARPE TVEGAENDAE SSSNTPVAAA KSAASSAAPP
AGGPFSTSSL TEGDTNGNGN GNGNAKALTG DEFARQLEES DLQLLVEKYG PKVRRDAARQ
RSRLETDRRL LRGQAESLNI RRWLPPELMS HILDLVQGEC RFSSSSISSE KSGNGRMLPE
EDIVIRLWTL KQTLDAAGFP SDRVQAVVRH ILDISPTIPT SVKDGLWGLD EAMDWLAIES
SLDELPKYET QSKPNPKPTD TPIDSPAPSG TVTPGNIEPT LRGQPGTRVS EQSPAPNKKP
AITYSSDIEP DDLIPTYLDA KEKLFKLDRS RQETKRQATE QDEERDDEEA AKLRAKLERI
EKDVLFDHPL AEHQWRAKRP ALEKELAVER RRRGKEKTAA TQKQTDSAEP LEQTEDPGDV
SGGDGGEVNE EAERIAAEIL AQGEEEDDGG GIAGLFNDLP TQEVDKETGA TSLVMNGSDG
VKITIRDFGK WAGISPVRAL EEACRSRDSS VKLRYTPISD TPFAVRHQLH ISWDKAQDLP
PSAVDPNVYT ALSPYSFNFS MESVAAPDKK QSEAYVATWA LFHIFGTSPK EEKVGMRLPP
VWRELWTELA DGRKSALDAE DRDVVRELRS LVRQRQDQEL EDGVILQSAF RGRGSARNLN
DTNRHGSQEA AAAARADGAH ELYRRIWSQK ASTQAYQAML PGRMQLPMWQ SRQQVMDTVD
REQVVIICGE TGCGKSTQVP SFLLEHQLSQ GKPCKIFCTE PRRISAISLA RRVSQELGEG
RNDLGTPRSL VGYSIRLESN TSKETRLVYA TTGVVMRMLE GSNDLQDITH VVLDEVHERS
IDSDFLLVVL KKLMLRRKDL KVVLMSATVD AERFSNYFGG APIITVPGRT FPVTVRYLED
AVELTGYSPG QTPREKIVDL DDDLEPESEG PSTTTSASGG GALAQYSAKT RNTLAQFDEY
RIDFDLIVQL IDKVASDPDY SPFSKAVLVF LPGIAEMRTL NDLLSGHPSF SQNWLIYLLH
SSIATEDQEA AFLVPPPGTR KLVLATNIAE TGITIPDVTC VIDTGKHREM RFDERRQLSR
LLDAFISRAN AKQRRGRAGR VQEGLCFHLF TKHRHDFLMN DQQTPEMLRL SLQDLAIRVK
TCKIGGIEET LGEALDPPSA KNIRRAVDAL IDVRALTSSE ELTPLGLQLA RLPLDVFLGK
LVLMGTVFKC LDAAITIAAI LSSKSPFSAP FGQRAQADLA RKAFRRGDSD LLTVYNAYLA
WKRVCQSANG SGGSEFQFCR KNFLSPPTLS NIEDLKGQLL VSVADSGFLS LTDEERRTLR
RMRYSSQSQR RHHFFDVPQR VNLHSENDAV TTAVISWSFY PKLLVRDAPG SRGLRNVGNN
QSISLHPSSV NKGHNDLKWL SYYHIMQAKT VYHAHETTAV DPFAVALLSG EARADMFAGV
LVLDGNKARF ALPDWKTMLV LKVLRTRLRE LLTRAFKQPG KLPTAQHERW LEVWQKVFSQ
ELNKENKPII VAKA
//