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Database: UniProt
Entry: A0A1Y1W3I3_9FUNG
LinkDB: A0A1Y1W3I3_9FUNG
Original site: A0A1Y1W3I3_9FUNG 
ID   A0A1Y1W3I3_9FUNG        Unreviewed;      1698 AA.
AC   A0A1Y1W3I3;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Sec63-domain-containing protein {ECO:0000313|EMBL:ORX68028.1};
GN   ORFNames=DL89DRAFT_269171 {ECO:0000313|EMBL:ORX68028.1};
OS   Linderina pennispora.
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC   Kickxellomycetes; Kickxellales; Kickxellaceae; Linderina.
OX   NCBI_TaxID=61395 {ECO:0000313|EMBL:ORX68028.1, ECO:0000313|Proteomes:UP000193922};
RN   [1] {ECO:0000313|EMBL:ORX68028.1, ECO:0000313|Proteomes:UP000193922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12442 {ECO:0000313|EMBL:ORX68028.1,
RC   ECO:0000313|Proteomes:UP000193922};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-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:ORX68028.1}.
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DR   EMBL; MCFD01000011; ORX68028.1; -; Genomic_DNA.
DR   STRING; 61395.A0A1Y1W3I3; -.
DR   OrthoDB; 57056at2759; -.
DR   Proteomes; UP000193922; 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   GO; GO:0006397; P:mRNA processing; IEA:UniProt.
DR   CDD; cd18795; SF2_C_Ski2; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 5.
DR   Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 2.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR041094; Brr2_helicase_PWI.
DR   InterPro; IPR048863; BRR2_plug.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004179; Sec63-dom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR47961; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1.
DR   PANTHER; PTHR47961:SF6; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1.
DR   Pfam; PF21188; BRR2_plug; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF18149; Helicase_PWI; 1.
DR   Pfam; PF02889; Sec63; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00973; Sec63; 2.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF158702; Sec63 N-terminal domain-like; 2.
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:UP000193922}.
FT   DOMAIN          445..605
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          628..796
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          51..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          195..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          346..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..221
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..257
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..367
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1698 AA;  189453 MW;  29B401A750D0F7E2 CRC64;
     MGEELTKEQQ KLYQYAGNSN LVLQSDRSGL ARRGERGKEV ESLYGKIDAR DMGANVRHEA
     PPKAPTQGKT RREQRALRTN YGYTNILAAT EDIEGVAYRP RSRETRRVWE MILAQARKYL
     GDQAPEVLMS ATDEALAVLK NDNVREREKK KQTEFSVFIQ LARQITDYED EPMEVDAGRP
     DAQSGMAVAG QFVVDGESSG SDSEDDEDRK APEDHGSDVG SVQGDDEAGG YRTVIHGFGK
     DAADDGSDTE MVDAPDRLPP RSIDAFWLQR EIGKHFPDHM AALRLLANRR LAAGELENEL
     AELFDYDHFE TVQVLVQNRE LIAEDDSQQK TGIEEEMREN GLGWIAQQQP PQQPPQQRQS
     ASSQDVVMEE AKANEPRDFE PRQTIDLAEL AFTQGGHLMT NEKWVPPKGA EKEIRVPAPE
     RPPPAGDDEP IWSRTAFPGA KELNRVQSRA DDNMLICAPT GAGKTNCAAL TMMRTIGQFR
     DSATGEINVD QFKMALVAEV AGSFSKRLAP LGISLTKQQI AATQLIVTTP EKWDVITRKG
     GEGSYTQLVR LVIIDEIHLL HDDRGPVLEA LEQTQQRVRL VGLSATLPNY EDVATFLRVP
     RDRALFHFDA RFRPCPLQQE FHIKRLERMD QVCYDKVKKH AQGSQVLVFT ESQTGLAILE
     DAAESTRDQA LKELLPFGFG CHHAGMSKAD RGQMEDLFAN GRLKVLVSTA TLAWGVNLPA
     HAVIIKGTQL SPQDVLQMLG RAGRPQYDTF GEGLRYYLSL LNQQLPIESQ LMSRLADALN
     AEVALGTIRS RNDAVDWLGY TYLPSVYGVP GGEIDEDPAL VGRPAVELAR SAMVQLAHRD
     IDILRFRLIP VRAEERRVPA KINVLLQAHI ASLGLTGFAL VSDMVYVTQS AGRIFRALFE
     LCLPHRVLGW CKQFGRACPT DLVRSVERKP FPWARYLGEL VGSPKAGRLL HGLVHLVPRL
     EVSAHLRLTP DFRWQDAFWI WRMLHSELFV LKKLYVGQEH PLPPQYFVCT RLAVSFNCMT
     LSSSAFTRLP SRQCSAPRRA PARRWLGSWR CCGFSSTRRC GRELTRWRGH EHMSGSSGLH
     RCRAERLWRF CQATWPGDLK RIENAHIIWR ARQHHAVREI GLVIADELHC GSDYGAGADL
     VGDQLAATYE VVVSRIERPI RIIALSVPLA NARDVAAWIG APPSAVFNFS PAVRPTSTIP
     HFASRMAALA APTYRAVCGD PSREPAIVFV PSRRQCRVVA GELLTLAAAD GASIIESAIG
     RFLAYGVGYY HEALTDADRQ TVTGFRETCW ALDSVHAQTV HRYVDYSIPD VLQMMGRASR
     PGIDTKGLCR ELYKKFLYEP LPLDEIQEAV DYLTWTLMYR RLGTTHPASI RLPCVTLDDD
     EVGVSATNLG IISAFYQIRY LTVEMFALSL AAKTKLRGVL DIVSAADEFE ALPIRHREAH
     VLNKIARRCP LALPSTSNDS DDGRWNSPRV RTHLLLQAHF SRLALPADLA ADQAWVLARV
     MPLLQALVDA PALASMELSQ MCVQAMQVPH LGGSERLQMC ESMQVDSVFA VMDMEDEDRA
     NQVAEVAAYV NRYPNIEVEF EVAGEVHANG IVSLVLSLDR EWDEEEEGDI PGPVIAPFFP
     YARAEGWWVV IADGQTLVNV RKISVGKELQ RTIKFAAPEV AGQRNLKMFL MCDGYLGCDQ
     ELDVELDVLP PEEESDSE
//
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