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Database: UniProt
Entry: E3QL14_COLGM
LinkDB: E3QL14_COLGM
Original site: E3QL14_COLGM 
ID   E3QL14_COLGM            Unreviewed;      2063 AA.
AC   E3QL14;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=SH3 domain-containing protein {ECO:0000313|EMBL:EFQ31552.1};
GN   ORFNames=GLRG_06841 {ECO:0000313|EMBL:EFQ31552.1};
OS   Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS   anthracnose fungus) (Glomerella graminicola).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN   [1] {ECO:0000313|Proteomes:UP000008782}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
RX   PubMed=22885923; DOI=10.1038/ng.2372;
RA   O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA   Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA   Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA   Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA   Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA   Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA   Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA   Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA   Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA   Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA   van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA   Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA   Ma L.-J., Vaillancourt L.J.;
RT   "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT   by genome and transcriptome analyses.";
RL   Nat. Genet. 44:1060-1065(2012).
CC   -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00983}.
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DR   EMBL; GG697356; EFQ31552.1; -; Genomic_DNA.
DR   RefSeq; XP_008095572.1; XM_008097381.1.
DR   STRING; 645133.E3QL14; -.
DR   EnsemblFungi; EFQ31552; EFQ31552; GLRG_06841.
DR   GeneID; 24412206; -.
DR   VEuPathDB; FungiDB:GLRG_06841; -.
DR   eggNOG; KOG1998; Eukaryota.
DR   HOGENOM; CLU_000595_0_1_1; -.
DR   OrthoDB; 8258at2759; -.
DR   Proteomes; UP000008782; 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:UP000008782};
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          629..811
FT                   /note="C2 DOCK-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51650"
FT   DOMAIN          1461..1871
FT                   /note="DOCKER"
FT                   /evidence="ECO:0000259|PROSITE:PS51651"
FT   REGION          90..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          131..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          416..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1792..1816
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1866..1904
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1930..2016
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        416..449
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        456..473
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        481..501
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1796..1810
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1870..1904
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1934..1956
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1963..2010
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2063 AA;  228820 MW;  D15E85C0DFD97D38 CRC64;
     MPWQPLPRIA FAVATYPFAA SGPADLPLEL GDELYIIEET PDGNWLRGYL VAPPSLLAGL
     TSVKGQTLEA RVFSGIFPRS CVEVREVLGE ADDTDDADDA ASDDATADTH FGSDSAKSGL
     TRTAIDIPKA IQRHKSFGNA KGPRGNRTGT KGRTPLQELP NGTHGRLSIP VKRDPDAPRP
     AAPVPMLKIG DETPTSAAEP LIDEIASCLR EWHSTNLHGL LLSRQYSRLE KLSQLIHTLN
     LSRQQFLHNV LTRHEYQRLR EKTVWDLVRV NKLCGGEVVV RDPADRGRVL TGDDSVVDIT
     KLQSVMSVLD EPPQPTVEPT ALHHLLFDVK GFAGASAEET SLAAYLVAKP VGGKVTTLTE
     CFIIEIPPGG TIGSLAKSGQ TRTVFADLSS QDIGDGASAD TELYLVVKVR SSEQIIASRK
     PDSRSGAKSQ GTGYSKDPTK PTSAGNGKPS RRSLMWGSKS GRSAFSRGNA TPKLDSLTEY
     PEARPSTQDD GQGSAPPPST DGSRPRGSFD AGAGFLMAER TVGVGVLKLN SIMKQDDDVE
     QVVSIWSASL TPPAEKQSLN DEWDGLIRDL MDSKSGHYEK SRRTERVQVH LRSFNHPDVD
     ELVKTTPTLL AGIRKTNKLG FSGAPTKARS DIYVTLDSAA LSKHNLLSRY AGSPTTLASS
     VQGNHLQVML EVRRSDGEKI PNCIFSSSNT EGITTWKSVA VERGDHWSQT VRLAISPEDV
     FTSHLVMFLS DMPNPPFAVA HMPLWNQEAF VRDGTHALLL YKADEFTSTA QAGPSGRGGY
     LSLQWSARGN EEHSADVTGP QAILRVDTYL CSTRFSQDRV VLGLLKWKEA AKDDIPTLLK
     HLIFVPEIEV VKLLSDVLDA LFGVLVEYSG NDELEDLVFT ALVRVLGIVH DRRFNLGPLV
     DHYAENRFNY PFATACLVRS FTRLLEKPAE PTTSRKLRST FKVVRHILKF ITHARGQQQA
     KEAGIGITHS HSAPGFTREL RNIFKALDAM MRSHAPVLVG SQTLAVQHFH TWLPELTGLL
     STEEILHIAI DFLDSCADVK GKLVLYKLVL IINYSKLDIF SHPDQKSALT ANTVRWIAPH
     WGHTEAVTDS WKEQVRLCCS VLAGQIDNLG PEIPDYLPKI IDSYMSIVAV PTKPRNRLSL
     LFPTSYPFPC KPVTEKCTFD EALVELSAIL SAVSNSPSGM QLELIEGDLT LLLENTLRVH
     MSILMGEAFP PDWLSVHIYH HKSTMKTLQY LSSILLESYL PHPDDAENFN TELWKMFFTT
     MLKLVGSPSL ALETFPEQKR RAVWKIAGDV REHGAELLRR TWEAIGWETS ADERDRYKLS
     KMGGYQVQYV PTLVGPIVEL CLSVHQGLRR MAVEVLQTMI VSEWTLSEDL SVIQTEIIDS
     LDQYFKSKPL TESILQKLFI GEVLERFAPL ATGPDEALHA AICELMGTVN EFLDLLVAVH
     SSDNTSEASH LINRLRLMEF LRDMQKEEIF IRYVHQLAAL QAEARNHCEA GLALRLHADL
     YDWDPTKQVP ALSEPEFPVQ TSFERKERIY FDMIKHFEDG EAWSSALAAY RELRTQYESN
     VFDFAKLART ERAIATVYET ISRSDRLIPK YFKVVYKGLG FPSSLRDKEF VYEGSPTERA
     SAFTDRMQEL YPSAQIVTGG DVDDVEGQFL VVSAITPHRD LTHQVFQRAR VPQVIRDYLL
     SANPQSFSVS SKRDTSGPVK EHHAEKIVFT TADPFPTILR RSEIVYTEDI KLGARETGLE
     RIVRKTQEMT VIEKRVAEGD EENAQLLVDA VSVSVNPGSD NSVACYRQLL PAASSDDDNG
     DDDDEEQETR LDPQDNAIKM ALVDHAIMIK RCLATFAKSS NEVLNRRHEE LRQYFESTFA
     PEIALFAPQQ PTRDFTNIQP WRRSSPSTEQ GSPQPQSTTG ATDNVVVAEE VSTVQPIAIR
     QGRGTRLSFL GGRKRQSPVQ QQTNSNSSAS GDADDTLSQH SRSRSRAQDT SSRLSFFRAP
     STDGGRMNGS NDAASEWVTD SGGRQSSDTG FNLTEKEREY RDESLADDPI VIKRSSVRKR
     LSMLKLGKKS HKHGGVMGSV HEE
//
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