ID A0A0D0D1T9_9AGAR Unreviewed; 2229 AA.
AC A0A0D0D1T9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Sec63-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=GYMLUDRAFT_242222 {ECO:0000313|EMBL:KIK63168.1};
OS Collybiopsis luxurians FD-317 M1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Collybiopsis;
OC Collybiopsis luxurians.
OX NCBI_TaxID=944289 {ECO:0000313|EMBL:KIK63168.1, ECO:0000313|Proteomes:UP000053593};
RN [1] {ECO:0000313|EMBL:KIK63168.1, ECO:0000313|Proteomes:UP000053593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD-317 M1 {ECO:0000313|EMBL:KIK63168.1,
RC ECO:0000313|Proteomes:UP000053593};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN834765; KIK63168.1; -; Genomic_DNA.
DR HOGENOM; CLU_000335_1_0_1; -.
DR OrthoDB; 57056at2759; -.
DR Proteomes; UP000053593; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase 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; cd18021; DEXHc_Brr2_2; 1.
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; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
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; 2.
DR InterPro; IPR003593; AAA+_ATPase.
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 InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR47961; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1.
DR PANTHER; PTHR47961:SF4; U5 SMALL NUCLEAR RIBONUCLEOPROTEIN HELICASE; 1.
DR Pfam; PF21188; BRR2_plug; 1.
DR Pfam; PF00270; DEAD; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF18149; Helicase_PWI; 1.
DR Pfam; PF02889; Sec63; 2.
DR PIRSF; PIRSF039073; BRR2; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00487; DEXDc; 2.
DR SMART; SM00490; HELICc; 2.
DR SMART; SM00973; Sec63; 2.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR SUPFAM; SSF158702; Sec63 N-terminal domain-like; 2.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR PROSITE; PS51194; HELICASE_CTER; 2.
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:UP000053593}.
FT DOMAIN 527..716
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 760..988
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1414..1590
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1620..1834
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 26..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2207..2229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..258
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2209..2229
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2229 AA; 249701 MW; 6820EA9B8A7E1D1E CRC64;
MSQKPAKQDL SQYNYGAISS LVLTADRSAL PRRDKEPDGA PTSLAGRIDV KEMGSRAFRE
GPKDLEKRKK KAEKDAGKGE EKQAKRKAEL GGGGAGFGYT DILAATQDVE GLLYRPRTAE
TRQVYELILS IVYNSLGGQA QDIVRSAADM VLETLKKEGV KDFDKKKEID EVLGGVSSEE
FTQLINLGKK ITDWGEEDEE MRDPDDVDGG KKEGEIDDEV GVAVVFDEEE EEDEDEEGYE
VRGSDESDEE DEEGGEGKDK NDEDIPTEEV PSDELVIGSE SGKKGSSSTS ADSDLVTPHQ
VDAFWVQREI STIYPDPVTA QSLAASVLSI LSSESSLRDC ENQLMELFEY QSFHITTKFL
KNRDVVVWCT KLQRSSAEER VNVEVAMREK GVGWILRELA GDRTAKRPSA PQTAAGTDTA
AMDVDEQAKP TLPSGAPAPS RTLDLSTLAF SQGGHLMSNK NVKLPEGSFK RARKGFEEIH
VPAPKSRYST KTMNDDGEMV LIESLPVWTR KAFSVKNLNR VQSKVFPIAF GTDEPILLCA
PTGAGKTNVA LLTILNEMSK YMTSDPSSAD PTFDLDSFKI IYVAPMKALV QEMVGNFTSR
LTSAYGVKVA ELTGDSQLTK AQIAETQIIV TTPEKWDVIT RKATDSSYTN LVRLLIVDEI
HLLHDDRGPV LESVISRTRR HASATGNPVR LVGLSATLPN YVDVARFLGI DTSGSTAANP
STKGLFYFDS SYRPCALQTQ FIGITEKKAI KRYQVTNQVC YEKTLETLKS GNQVLVFVHS
RKETGKTARY LRDTALGETT SADGTTASSG ASTDDITHFV RSSDSGATRE ILNEEAGNVR
DSILKDLLPF GIGIHHAGMS KEDRGLVEEL FADGALKVLV CTATLAWGVN LPAHTVIIKG
TQIYDPTKGR WTELSPQDVL QMLGRAGRPQ YDTYGEGIII TSHSELQYYL SLLHSQLPIE
SQLISRMVDS LNAEIVLGTI RNREEGVDWL GWTYLYIRML KSPSLYSVSS DYLSPSDPTL
LQKRSDLIHS AAVLLEKAQL VKYNRTTGAL VSTELGKIAS HYYVTYNSML TYNRHLRPTM
GMLELCRVFA LSEEFRLIPV RQEEKLELAK LLERVPIPVK ESVEEPAAKI NVLLQAYISQ
LKLDGFVLLA DMVFVQQSAG RIIRAMFEIC LKRGWAVPAK AALDLCKMVE KRMWGSMTPL
RQFKGVPAEV IRKAEGKQFP WYRYFDLSPP EIGELINLQN AGRLVHRLVH SFPKLQLTAQ
VQPITRSLLR IELSITPDFR WDEKIHSSSE SFHILVEDVD GEVILYHDTF LLLQRYAEDE
HTVTFSVPMF DSPVPPNYYI SVISDRWLHA ETRLPISFKH LILPEKFPSP TPLLDLQPLP
LSALHNKEFE RIYEDEESGY RIETFNKIQT QVFQALYTSD ENVFIGAPTG SGKTICAEFA
LLRLWSKRTR GRAVCIEPFQ EMVDMRVQEW KAKFGSVQGG KEIVALTGET TADLRLLEKG
DVIICTPSQW DVLSRRWRQR KNVQTVALLI ADEVHLVGGE VGPTYEVILS RTRYVSAQTE
LKTRIVALGV SLANARDLGE WIGVPSHAIF NFSPSARPLD MDIHLQSFSI THFPSLMLAM
SKPAYLAISE YAPSKPVIIF VPSRKQCQLT VDDLLVHAAA EEKADRFLHV DVEDLEVHLE
RLADEGLKET LRHGVGYFHE ALSKQDKRIV QRLFESGAVQ VLVASKDTAW SLPVSCYMTI
IMGVQYYEGK EHRYIDYPVM DVLQMIGRAC RPREDERSRC VLMCQQTKKD FYKKFLAEGL
PIESHLTAML HDYFLAEIAV KTIENKQDAM DILTWTYFYR RMTQNPNYYN LHNVSHQHLS
EHLSELVETT LTDLTNSKCI AIEDESDEVS PLNLGMIAAY YNISYVTVEV YTLSLKERTK
LRGLLEVVSS SAEFEIVPIR RHEDVLLRRL YDRLPVKLDA SSVNYESPHF KTFLLLQAHF
SRIQLPADLV ADQRLILEKV LNLLSACVDV LSSNAWLNAL SAMDLAQMCV QALWDRDSPL
KQIPHFESEV IKRCTDAGVD SVYDVMDMED DKRTALLQMT NAQMQDVAAF VNSYPSLDVS
HELVKGDYTA GAPILLQVTL SRDVDEDDDA DDQTVVAPYY PTKKMVNWWL VVGEPSTRQL
LVIKRVTVNK TLVNKLEFTL PKGKHSLKLY VICDSYVGAD HDIGLGELDV AEGEDEDDSD
ESDSDAMEE
//
