ID A0A0D0B2S1_9AGAM Unreviewed; 1278 AA.
AC A0A0D0B2S1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Unplaced genomic scaffold CY34scaffold_272, whole genome shotgun sequence {ECO:0000313|EMBL:KIK38243.1};
GN ORFNames=CY34DRAFT_402958 {ECO:0000313|EMBL:KIK38243.1};
OS Suillus luteus UH-Slu-Lm8-n1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Suillineae; Suillaceae; Suillus.
OX NCBI_TaxID=930992 {ECO:0000313|EMBL:KIK38243.1, ECO:0000313|Proteomes:UP000054485};
RN [1] {ECO:0000313|EMBL:KIK38243.1, ECO:0000313|Proteomes:UP000054485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UH-Slu-Lm8-n1 {ECO:0000313|EMBL:KIK38243.1,
RC ECO:0000313|Proteomes:UP000054485};
RG DOE Joint Genome Institute;
RA Kuo A., Ruytinx J., Rineau F., Colpaert J., Kohler A., Nagy L.G.,
RA Floudas D., Copeland A., Barry K.W., Cichocki N., Veneault-Fourrey C.,
RA LaButti K., Lindquist E.A., Lipzen A., Lundell T., Morin E., Murat C.,
RA Sun H., Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.,
RA Nordberg H.P., Cantor M.N., Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UH-Slu-Lm8-n1 {ECO:0000313|Proteomes:UP000054485};
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 (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN835403; KIK38243.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0B2S1; -.
DR STRING; 930992.A0A0D0B2S1; -.
DR HOGENOM; CLU_001592_2_1_1; -.
DR InParanoid; A0A0D0B2S1; -.
DR OrthoDB; 8175at2759; -.
DR Proteomes; UP000054485; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45865:SF1; E3 UBIQUITIN-PROTEIN LIGASE SHPRH; 1.
DR PANTHER; PTHR45865; E3 UBIQUITIN-PROTEIN LIGASE SHPRH FAMILY MEMBER; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054485};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 54..296
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 937..977
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 150..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1278 AA; 144387 MW; 9EA9824226115534 CRC64;
MLLREGKTMN QEGDVVPHTF SQSQFPMPLF WDEISLGGQE HFFNTLVGVV NPSPVEGNTA
LGGILAEEPG LGKTIECISL ILLNPAPDRN PTNTRWDAEA KLEVKEIKTT LIVTPPALAP
QWADEIAVHA PGLKVLIYDG WSKVAVPITQ DDVEDERERR RSEAGKKGSK VQKTRKGKTI
YNEDDDILDW CSYVNTFDVC ITTYNVLRQD LTVARAPPKR PRRAQVEYSN LDRPRSPLVM
CEWYRVIMDE VQMMGTGKSE EMVSLVPRLS SFAVSGTPAR TQVSDLIRVL RFLRVDDVVG
PTRMWNRLMK HTFKKQFADL FQRYAIRTLK SAVKDELTIP QQRRYLVSIE LGRVERHVYD
HHLEAALVEL GLDMRGVAVN EGWQIDATLL RNVLRKLRGI CTHPQVGQLQ RPGDKLAKPG
ALKSIGDVLE AMRDQNWRNF MDDRKAKVQT LVRFAQLQQH NEQNLDRYKR ALDSLLMAEQ
EANEIIDDIK TTTAEHQVKG EALKNEARAL REFRQQDLSD LSKTDKGKGK RAMSPLADAD
EDIDDIEDVE DRGLPKTPAG EEHSIKRRAL QQRLRECLIV LHRVKFLQGD VYHVLGASQS
DKEDASYAAA ETLRKNLLKS TEESANKVMN LLRVDSTGRG VTEESLQIPL PFLDGGGIKS
THLFDEANEI IELALNEQTA LLWEWRTRIY ALLTQKLAAN SDQADGEEYS RTLETQGEAE
IYMQAYAALL ADRREAISSE RTLLAAHDAR EHKTRRTKAA ARAAAQAMSE DFEIPEDVEV
QPQHEVLHRD LTEQRKDLHD QFSGRALRSI MVDLSAVAAR IASEKDPEKV IAKDGANSLR
TLIAQQVTLM DKLDADLSQL RKIFNERILY FRQLQEISDT VTEAIWEGTV VLAMEECTVE
RMELEGKINT SRARQRYLNH LAKNKEEGIT DEDDEACILC RCDFKRGFIT QCAHVFCEGC
MKAWVTRREG RACPVCRVII NLDQLQRFTV EADKPAPAKP VMANKEPAPV SRRKIQYNMI
NPTIFEEIQS TESNGSYGSK IQALVRHLLY IQFTDPGAKS IVFSAWADSL QIIEHAFNCN
GIPYLRLDHA KGRGKDSGAK KFRTDPTLQV LLLHGERDNA GLNVTCASRV FLVESVVNHG
FEVQAIARID RMGQTKPTEV FCYYAEDTVE KNILDLAARQ GLSLYTKDNS AGTLNLTPFA
MDAGKKTVES SGKKKQAQKG DFIFKVNDML AILFPHMFEE IQYLLPPEEP SDEIAMEVEP
TGRREQLNAE AGPSRLPF
//