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Database: UniProt
Entry: A0A1Y2GSS8_9FUNG
LinkDB: A0A1Y2GSS8_9FUNG
Original site: A0A1Y2GSS8_9FUNG 
ID   A0A1Y2GSS8_9FUNG        Unreviewed;      1121 AA.
AC   A0A1Y2GSS8;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=PH domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BCR41DRAFT_321096 {ECO:0000313|EMBL:ORZ20038.1};
OS   Lobosporangium transversale.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC   Mortierellomycetes; Mortierellales; Mortierellaceae; Lobosporangium.
OX   NCBI_TaxID=64571 {ECO:0000313|EMBL:ORZ20038.1, ECO:0000313|Proteomes:UP000193648};
RN   [1] {ECO:0000313|EMBL:ORZ20038.1, ECO:0000313|Proteomes:UP000193648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 3116 {ECO:0000313|EMBL:ORZ20038.1,
RC   ECO:0000313|Proteomes:UP000193648};
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:ORZ20038.1}.
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DR   EMBL; MCFF01000013; ORZ20038.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2GSS8; -.
DR   STRING; 64571.A0A1Y2GSS8; -.
DR   InParanoid; A0A1Y2GSS8; -.
DR   OrthoDB; 1367385at2759; -.
DR   Proteomes; UP000193648; Unassembled WGS sequence.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR   CDD; cd00174; SH3; 1.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR12844; CONNECTOR ENCHANCER OF KINASE SUPPRESSOR OF RAS; 1.
DR   PANTHER; PTHR12844:SF42; CONNECTOR ENHANCER OF KSR PROTEIN CNK; 1.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF07647; SAM_2; 1.
DR   Pfam; PF14604; SH3_9; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00033; CH; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00454; SAM; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50021; CH; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   4: Predicted;
KW   Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193648};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          1..63
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          218..281
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   DOMAIN          581..677
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          899..1004
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   REGION          51..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          306..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          438..571
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          700..721
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          745..802
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          815..894
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1003..1093
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..139
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..355
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..471
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        483..510
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        745..767
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        768..782
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        849..867
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1007..1052
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1075..1093
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1121 AA;  124301 MW;  D99F348FB846AF29 CRC64;
     MPETVWAIHN FEAEAEDEIS FQIGEPIIVL HRDELYQDGW WEGTNVRGET GLFPQNYTTQ
     NPPEKPLPEA PSSDSNAYGS NTNSGVGSND YNGNGNSRNN NQNYASNITN NSSSMGHTTD
     NLNNNHNNSN IRTHESQTNS NVRMLAQQSQ SNYNNTPSNG NNMYIQQNPV IASPSVDSTR
     GGSLSGGSIN GAPTSKIIAQ NVEESLSDPQ LAGHPSTWSI DQVAHWLRCC GFGTVVSSFI
     DNEISGAILL ELNLNNLKEL DITSFGKRFN IINAITSLKQ LTKSNLDSKN SYGGLSNMSS
     MYSVGSPGGP NIPPRMTSAP INVPANGVNL PEPRASYDSR GDYLRDSRHK DLSDPRNAPL
     PPGPSHNARL YQQIHAQNLA SSSQQPLQTL PQQQQFSDYD IQAGQPQNRS AANLARSDTL
     GSVMSGASIG DYGSPTLVDA PSLNGQRQSA TSAFSSNPNL HRSNNPWDRH ASRAPQPQMP
     SPVASQPRGA LSTDFDNMGY GQQQSPQPQL PMDHYPRPME VSRNAPGSPE VLRPDPYSNS
     MMYEQPTPKP RKFHNPDTTN RPQNGKADPS DKVVPLELIG RPDYAGWLKK RGDTYRTWKS
     RWFMLKGVTL YYMNSPKDSA SKDYINLVGY KIIQDENIYA GKYCFKAVHE DLRNFYFYTD
     SESDMKGWLK ALMKVTIGRD PTAPVISSSN IPTIPLHVAR KLAPRPPSPS RRVNRNLGAN
     GQPIHSQQLQ KLQYDQGFQQ QKQLLQQQMQ QLQQSSQPQP RSSHQQQQLL DYDDHDSDGE
     GYHPNDYSNN HPGNIPQKNG DEKRIAEHPE SPVLQSLSVD QQRHSFVHSD QRDGDDDPWR
     DEDGEGFGHQ QKQQQQQQQQ QQQELKYLRP DSELDSFRQP KDVSQPKIQE QEPLPINTRW
     TQEQYVEWIN RHLPSTVEPV SDMTQSLRSG VVLVRLIEQL SGETVDKRVP NATYTLQMLE
     NLLTAFKFMD RVGVSTDGYT VKDVFNGNEE KIAFMFEAIR ARFPENTPSG PNPTGTNSNA
     SASSVSTLHQ QQQQLSASSS LSTLNASVAP ASSLPPLPNG PSKGSPVPKM NGRASPAVMN
     NNSGRSPLIG NANTPRMQIQ HIGDESEYEA LYDEAARSTI S
//
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