ID A0A165Z6Z9_9AGAM Unreviewed; 474 AA.
AC A0A165Z6Z9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=WH1-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=FIBSPDRAFT_938133 {ECO:0000313|EMBL:KZP10284.1};
OS Fibularhizoctonia sp. CBS 109695.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Atheliales; Atheliaceae; Fibularhizoctonia.
OX NCBI_TaxID=436010 {ECO:0000313|EMBL:KZP10284.1, ECO:0000313|Proteomes:UP000076532};
RN [1] {ECO:0000313|EMBL:KZP10284.1, ECO:0000313|Proteomes:UP000076532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 109695 {ECO:0000313|EMBL:KZP10284.1,
RC ECO:0000313|Proteomes:UP000076532};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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DR EMBL; KV417683; KZP10284.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165Z6Z9; -.
DR STRING; 436010.A0A165Z6Z9; -.
DR OrthoDB; 3837860at2759; -.
DR Proteomes; UP000076532; Unassembled WGS sequence.
DR CDD; cd00132; CRIB; 1.
DR CDD; cd01205; EVH1_WASP-like; 1.
DR Gene3D; 3.90.810.10; CRIB domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR036936; CRIB_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR033927; WASPfam_EVH1.
DR InterPro; IPR000697; WH1/EVH1_dom.
DR Pfam; PF00786; PBD; 1.
DR Pfam; PF00568; WH1; 1.
DR PRINTS; PR01217; PRICHEXTENSN.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00461; WH1; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS50229; WH1; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022527};
KW Reference proteome {ECO:0000313|Proteomes:UP000076532};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT DOMAIN 19..130
FT /note="WH1"
FT /evidence="ECO:0000259|PROSITE:PS50229"
FT DOMAIN 154..169
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT REGION 130..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..395
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 474 AA; 49111 MW; A49BB79223A142CE CRC64;
MPSQTTLNSD DKAKVKSALI TPTTKILTAV LARIYYAYPQ PGQWSYAGLQ GALALVNDKQ
KGCFSLKMVD LAGTRGVIWE HEFYEGFDYF QDRPFFHSFA GDECMIGVVF AEESEARTFH
KKVAGRKAEK AKSAAAAPVK KKASKNGKID KSMISGPTTG SFKHVAHMGY DQDNGFTSTN
VDPSWSAFLG QLESQGVDPG MIADNMDFIK DFVRDSQKSP PKKSRPPPPA PRSRGHNQTD
SVGSIQRDTP TPPPAPPVRS SPPPAAPAPP PPRQAPPPAA PPPPPMRAPS SQSPPTPPPA
RVPPPPARPT SAAPMAPPPP ARPSAPPPAP PAPPSRQAAA PPAPPPPPPP PPPGGSGAPP
PPPPPPPPPP GGGPPPPPPP PPPPGAPPGA PPAPAAALPS NLLASIQGMS VANLRKSNPN
AQPARSSPAP PPIEETPSGS TGGGDLTSAL AAALLERNKK LGDSDDEEEE DDWD
//
