ID A0A0D0CZ24_9AGAR Unreviewed; 1135 AA.
AC A0A0D0CZ24;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Unplaced genomic scaffold GYMLUscaffold_22, whole genome shotgun sequence {ECO:0000313|EMBL:KIK61748.1};
GN ORFNames=GYMLUDRAFT_96594 {ECO:0000313|EMBL:KIK61748.1};
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:KIK61748.1, ECO:0000313|Proteomes:UP000053593};
RN [1] {ECO:0000313|EMBL:KIK61748.1, ECO:0000313|Proteomes:UP000053593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD-317 M1 {ECO:0000313|EMBL:KIK61748.1,
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; KN834770; KIK61748.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0CZ24; -.
DR HOGENOM; CLU_003080_0_0_1; -.
DR OrthoDB; 663280at2759; -.
DR Proteomes; UP000053593; Unassembled WGS sequence.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR CDD; cd13246; PH_Scd1; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR033511; Cdc24/Scd1_PH_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10579; CALCIUM-ACTIVATED CHLORIDE CHANNEL REGULATOR; 1.
DR PANTHER; PTHR10579:SF43; LOW QUALITY PROTEIN: EPITHELIAL CHLORIDE CHANNEL PROTEIN-LIKE ISOFORM X1-RELATED; 1.
DR Pfam; PF15411; PH_10; 1.
DR Pfam; PF13768; VWA_3; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS50234; VWFA; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000053593};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 100..161
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 614..819
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1135 AA; 124494 MW; C418E0CC92F2F3C6 CRC64;
MKEPVTAGGT WYSRRTDPHQ DTSSLYLNPR QAPVPTSKSS FRSLNSVFRQ PKSPKPPSIR
TVDSALSNPD SVASHPYAAM HIAPMPVVSS ADGLDDEEDC PVCLEPLSFS FRLPGEKPHI
VPECGHALHE ACFTAVYGPP PSQAKSAVPR KSNLGVCGVC RRPMKVGDGD GGKSNKLAAL
TGVGDHNSSS LYPGRDTPTN RRRPQPQNKP FDPSEDDPLD HNGSVKSDPT RDHSQYIVAP
SIQVRPEFSS LTRTHDANQP LTCIVVIELP GKRVLAPVPG PVPHEYNRRE NPSHHRQETG
HVSPQPRRQA ASESYSQDMQ YSSSSGHGHE SSSSQAALIQ EEDSPFNAIT EDLRNRIIDW
KGHPLSDLGP LQMYDLLSVR RDSLVREFYV YLFKEALICV VEEKKRSLGR LLSNASGLTD
ASSTMSSATQ SKGVLRLKGR IYVRHIKQVT ASSAAGEMSL TIDMEDELAS FILIFKDRSS
LEAWRNTIQT LVNMFQSQNL SYQQPQQEEP GLEMEEFGGN SKAMRMLSGS TSTTVSSGVD
SLLQNGSSRS TMSSSTSHGS MLQQSQRPQM QNKLSPLGEA DELDQYDSPT GLVTPYTSSG
PSNSLTPLPH PAMDLILVVS LPPPNASPST AQLKLRVIKA TLDFIVASLG PKDRLSLVTF
EVGQGGRVRK TPFLSVSKAQ SKGRLEKFVE NITVRPTSDP EGTGVGQNGQ DEFLVRVSKD
EKTDVVTAVN HGLDVVLQRK ARNSISGMIL VSDASDSTRR AQMDLVLARA EAANVPIHSF
GYGRSHDPAS LWLMSNHTSG TYTFVKDWYD LRDSVAGCVG GMMSIGLLNM KLHMKIVDGN
RFRIRKVSGG PSSILASDGQ NVDVEVGELR YGERKEMLIE LELDNSDLQR LVQAQGQRHR
DMRNMNATDR FVQSMGLDDL AIDDGTDFTA GMLNGMIDEV PVVEVDGSFF DPAAAKNVTR
LAHPVLLTVT LLPPSSNAPK PPSSVSDPVI VRRRMELLAS DMITRALVLV SRRNFPQAQK
IISETKRILH TVLQTISRSL PPPSSGATRN RKELLILGAV RAMQSILQDL QILSEALDDN
VDLFAHDQRN FGAQQAMILR DQKSWTGRSA TERLFWTTDN SIELVSRSTD WVARD
//
