GenomeNet

Database: UniProt
Entry: A0A136JI60_9PEZI
LinkDB: A0A136JI60_9PEZI
Original site: A0A136JI60_9PEZI 
ID   A0A136JI60_9PEZI        Unreviewed;      2043 AA.
AC   A0A136JI60;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=SH3 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=Micbo1qcDRAFT_129833 {ECO:0000313|EMBL:KXJ96831.1};
OS   Microdochium bolleyi.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Microdochiaceae; Microdochium.
OX   NCBI_TaxID=196109 {ECO:0000313|EMBL:KXJ96831.1, ECO:0000313|Proteomes:UP000070501};
RN   [1] {ECO:0000313|Proteomes:UP000070501}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J235TASD1 {ECO:0000313|Proteomes:UP000070501};
RG   DOE Joint Genome Institute;
RA   David A.S., May G., Haridas S., Lim J., Wang M., Labutti K., Lipzen A.,
RA   Barry K., Grigoriev I.V.;
RT   "Draft genome sequence of Microdochium bolleyi, a fungal endophyte of
RT   beachgrass.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00983}.
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DR   EMBL; KQ964245; KXJ96831.1; -; Genomic_DNA.
DR   STRING; 196109.A0A136JI60; -.
DR   InParanoid; A0A136JI60; -.
DR   OrthoDB; 8258at2759; -.
DR   Proteomes; UP000070501; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   CDD; cd08679; C2_DOCK180_related; 1.
DR   CDD; cd11684; DHR2_DOCK; 1.
DR   Gene3D; 1.25.40.410; -; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 1.20.1270.350; Dedicator of cytokinesis N-terminal subdomain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR027007; C2_DOCK-type_domain.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR026791; DOCK.
DR   InterPro; IPR043161; DOCK_C_lobe_A.
DR   InterPro; IPR032376; DOCK_N.
DR   InterPro; IPR042455; DOCK_N_sub1.
DR   InterPro; IPR027357; DOCKER_dom.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR45653; DEDICATOR OF CYTOKINESIS; 1.
DR   PANTHER; PTHR45653:SF10; MYOBLAST CITY, ISOFORM B; 1.
DR   Pfam; PF14429; DOCK-C2; 1.
DR   Pfam; PF16172; DOCK_N; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS51650; C2_DOCK; 1.
DR   PROSITE; PS51651; DOCKER; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070501};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          7..87
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          586..765
FT                   /note="C2 DOCK-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51650"
FT   DOMAIN          1414..1836
FT                   /note="DOCKER"
FT                   /evidence="ECO:0000259|PROSITE:PS51651"
FT   REGION          92..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          375..471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1748..1779
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1837..1866
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1896..2017
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..123
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..419
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        431..446
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        448..471
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1758..1777
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1838..1866
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1922..1937
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1965..1980
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2043 AA;  226927 MW;  3122DF4A58485050 CRC64;
     MPWQPLPRIA FAVATYPFAP LGEHDLPLEI GDDLYIIEET PNGQWLRGYL LAPPSLTAGL
     TSVKGQTLEA RVFSGIFPRS CVEIRELLGE ADDISSSDDD EADSDERASS AGDHGEPRFG
     TTDDALRTKP APQRVPGEPK PAAPVPMLRI GDESPTSASE PLIDEIASCL REWHSTNFHE
     LLLSRQYGSL DKVSQIIQAL DLARRQFLHN VLTTHEYDAL REKTVWNLVR GNKLCGGEVI
     VRDPKQRGRV LTGEDSVVEI TKLQSVMSLL DEPPVVHAET TALHHLMVDI KSFAGSSNEP
     TTLLLSLVSR SIGGTVTTLS ESYVIEIPAG GLMGNNSRDG QLRTLFMDLT SGDIGDAPSA
     DSELFLVVKV RAPQQISTGK PSSRSGSFSQ PATPFSKEKP PPSSGTKASR RSLMWGSTRS
     AFSRAGGKLD ALSEQPEERP QTDRVESRDG QVPPSTAGSR GPRPSSDGTQ VTHMSVDKLV
     GMGVLKINSI MQQPDEVEHV VTIWSATSQS SFDTQHDEDC DILVKSLLDS KSGHYEKSRR
     AERLQVHLKP FNYPDPDALI KATPTLLSGI SKTPKMGFPG APTKPRSDIY ITLHQAHLGR
     QNLLSRFGGS ATALPSSMHG NNLTVTLEVR SQSGERIENC IYSASNAEAV STWRSFAAER
     SERWNQCLRL ALSPDEVMTS HVMVTMTDLP NQPFAVGYLP LWEQHAFVND GVHSLLLYKL
     DENTRTAQPG PTGQGGYLTV PWGPRIDSSE VTGPLATLRI ESYLCSTRFS QDRVILGLLK
     WKDVPKDEIP GLLRQVTFVP EIEIVKLLNE VLDALFGVLV DNQENDEYED LVFAALVRVL
     DIIHDRRFNL GPLVDHYAEN KFNYPFATAC LVRSLTRLLS KPTEPETARK LRATLKVVRY
     ILKFVTHARD QQKAKEAGIG IVNGNPGFTR HLQNIFKALD SMMRSTAPVL VGSQTLAVQH
     FHTWLPELTG LLTTEEILHI AIDFIDSCAL VKGKLILYKL VLIINYAKLA LFSQPEQRSA
     LCANTIRWIA PHWGQTLEVT EQWKDQVRLC CSIVASQADH LGPEVPDYIP KITDSFRAIQ
     AAGVQSKNKL SLLFPASYPF PAKNMGGDAV RFDESLIELS AVLSALSSSP AGLQLELTED
     DLASVLKNTL QVHMSILQGE AFPSSWLSVH IFHHKSTMKT LQYLASIMLE QFLPHPDDAE
     SFDTELWKMF FTTLLKLVGS ECLALETFPE QKRRAVWKIA GDVREHGAEL LRRTWEAIGW
     ETSSDERSRY GLSKMGGYQV QYVPSLVGPI VELCLSVHEG LRRMAVEVLQ TMIVSEWTLS
     DDLSVIQTEM IDCLDRFFKD KAMTESILQK LFVQELLDRF EPLSHIEDDA MYAGLRDLIA
     TVDEFLDLLV AVHSGEVTGQ ASNLINRLRL MEFLRDMQKE EIFIRYVHQL AHLQAEARNH
     TEAGLALKLH AELYEWDPTR NTRSLHDPDM PEQSHFERKE RIYFDMIKHF EDGEAWSSAL
     AAYKELQAQY ENNVFDFAKL ARAERAIATI YETLAKSERL VPKYFKVVYK GLGFPTTLRD
     KAFICEGSPN ERTTAFTDRM QGQYQAAQII TSGDVDSDTE GQFLVVSSVS PHRDLGHPVF
     QRARVQQPIR DYLLSAHPQM FSVSSKRNTT GPVATHHAEK TVYTTAESFP TILRRSEIVD
     IETVQLGAKE TGLERIVRKT QEMTAVEKRL DDGDEEVAQL FIDAIRISVT ADSDSSVVGY
     RELLPKPQHK SKELGNLDSD DDDSDDDGSD EGEVELDEQE NAIKMALVDH AIMLKRCLSS
     FARSSNPVLR KAYQDLHMHY ESTFAPEIAV FTPAAAPRDL QNTPSPTWQR SPRLTDSPPR
     GQLSSSVSKG IVEEAASVQP INLRQRGAAR LSFLGGKRKE SHSSAGGGDV SGSPQLNGDS
     DAGHGGDHHK TKDHGHRMSF FNTTSGENIH TPNHQHHREQ SNGFSHHRTS PSASTTQDRG
     LKSRDIIDVV EKGIDAQGNS HSSEGQHGEG GLMKKASIRK RFSTLKLGTK KSKNALMGDV
     REE
//
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