ID C1GL73_PARBD Unreviewed; 2195 AA.
AC C1GL73;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=SH3 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PADG_07859 {ECO:0000313|EMBL:EEH43039.1};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH43039.1, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:EEH43039.1, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:EEH43039.1,
RC ECO:0000313|Proteomes:UP000001628};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
CC -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000256|PROSITE-
CC ProRule:PRU00983}.
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DR EMBL; KN275969; EEH43039.1; -; Genomic_DNA.
DR RefSeq; XP_010763315.1; XM_010765013.1.
DR STRING; 502780.C1GL73; -.
DR GeneID; 22586273; -.
DR KEGG; pbn:PADG_07859; -.
DR VEuPathDB; FungiDB:PADG_07859; -.
DR eggNOG; KOG1998; Eukaryota.
DR HOGENOM; CLU_000595_0_1_1; -.
DR InParanoid; C1GL73; -.
DR OMA; LWDNQAF; -.
DR OrthoDB; 8258at2759; -.
DR Proteomes; UP000001628; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
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; 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; IPR046769; DOCKER_Lobe_A.
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; PF06920; DHR-2_Lobe_A; 1.
DR Pfam; PF14429; DOCK-C2; 1.
DR Pfam; PF16172; DOCK_N; 1.
DR SMART; SM00326; SH3; 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 Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001628};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 7..88
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 613..794
FT /note="C2 DOCK-type"
FT /evidence="ECO:0000259|PROSITE:PS51650"
FT DOMAIN 1438..1855
FT /note="DOCKER"
FT /evidence="ECO:0000259|PROSITE:PS51651"
FT REGION 90..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1848..1880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1893..2054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2076..2127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2143..2195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1897..1911
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1912..1966
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2000..2022
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2040..2054
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2076..2101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2110..2127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2177..2195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2195 AA; 243263 MW; 80BD12DD3B78195C CRC64;
MPWRPLPRIA FAVAIYPFQP SSPADLPLEL GDELYIIEQG GINGSWYRGY LVAPPSLLAG
LTSVKGRTLE ARVFSGIFPK NCVEVREVLG DSDGSKDGRL STEPVPRRYA GSTTSAGSLE
DSFSAVDSKT LHNGEGDLKA SQKKMSQITI IKLEEDGTRR RSVSPSLPLT PISLGPRDPN
TTKPPAPVPM LKIGDETPTS VSEPLVDEIA SCLREWHSTN IHQLLLARQY TTLESLSNIV
LELDLARRQL LHNILTAQEL ATLREETVWN LVRGNKMLSG EVVVRDPKQR GRLLTGDDSA
TELTKLQSEM SMLDSGLTPQ VDNISLHHVL FEVNAVSGTD ANSVILGISL WLKQANGDTR
QLSETYTLDL PAVETFSNLV DNTKMKTLFT ELSASDIGEG SNSDSKLYLV IKAMGPESPR
IDAPPKTRSS SSRDGSFSNK VSSSLNSAGK GSLKGRRSMM WGHKSRGSGL EVGKEPSRSL
SQSSDSVTAK PNKPDTPGKE PTVIRTVGVG ALEIGSLLKQ NKEVEQVINF WSPVGENDEE
GNYSEGFDEV IQSLLYSPTG QYVRSHRISR VHSHLHPFTS NDAETLVRNN PTSLHNVAQT
KRIGFTGAPT KPRSDIYITI NRATISQDAL LSHPINGQLP VPQMTGLRNL QLTVEVRNAA
GVRLEHCIYP SSNGPGQTAW RTTVTQRGSP WNQSIRLNIP ADEVPGSHLI MSVADAPEFP
FALSWMPLWD QQAFIRDGPH SLLLYAYDKS TSSIENGRGA YLSLPWSALG KNESAKDEAV
TGPLATLSIE TDLCSTEYSQ DQVILGLIGW RERSATEVLA LLKRIVFVPE IEIVKQLRDV
FDALFGIIVE NAGNEEYEDL VFNDLVTVLG IVHDRRFNLG PLVDHYAEKQ FNFPFATSCL
IRSYCRLLQA TPDSQQSRNL RAAFKVGRHL LKFIINAREQ QKVKEEGIGI TKVQSTFNRD
LHFIFQSVES LMQNPSPILV GSKTLVVQHF HTWLPELSNA LTKEEIMNIA LSFMDACKDV
KSMLILYKLV LILNYIQLPL FESVKDRQTL YTCCIGWLAP YWGRTSDAND QYRDQVRLCS
SIVAEQLKHP SPELYAYMPK AVASYCALVG DGVEETNWLS MLFSKSFPFQ LKQSKIKQKF
EESLVELAAI IASLAKIPNP TPLLLKDEDL ALFLTQSLQT HKSILSCEAY PSTWLSVHIY
HHRSTMKSLE YLSTMLISSF LPPPDDADNF DMELWKLFFD TLLKLVSSDA LALETFPEQK
RRAVWKIAGD VREHGADLLQ RTWESIGWDT TADEQERYGL KKLGGYQVQY VPTLVSPIIE
LCLSIHEGLR HVAVRILQTM IVSEWQLNED LSIVEAEIIS SLDLLFKTKN ISESGTQKLF
ISELLDLFET STSNPDAELL VALKELVATV DELLDLLVAS HNGNITESLN TLKLMEFMKD
MDKEDIFIRY VHELARGQVA ARNYTEAGLA LQLHADLYDW DLSKLVPTLT NPAFPEQTSF
ERKEALYFEI IQHFEDGKAW AHALSCYRKL AHYYEHMTLD FSKLSRTKAS MAKIYDQIVK
DTNPPQRYFR VTFKGLGFPT SLRDKQYIFE GSPTDRMATF TDRMQKEYPA AQIISSDEPE
DVEGQFLQIS AVSVHRDMNH TVYQRSKVPH SVREHLLTSL PSQFSVTSKR HTSGDNVKEQ
WVAKTIYTTA EPFPNILRRS EIVSTDEIVL TPLQTAIERT WRKTNELLLL ERRASSENDL
NLTGLTDVLT NLLDLESSHS GCVALYRQFL LDESQAAMNL HDGEDDEGQI AHPIDPLNNA
LAVALIDHAL AIKRCLALYS RPAYQATQAE LTRRFEFAFA PEVASLTPVC NTPETEEPPN
LPGDHSEPLI SSRPQPITNA RSISPEQDLI RAARQQDNPS HTKHNHEKSI STHRISLNPF
KRSNHTANNS TSTITATAND ARQQSESKLN GTHTSRPSTA KTDGADAVSV TPSRAASRRS
RTRGGDTPSK RRSWFGGGGG NDTHKNSSPI SAPATSTEDI RTTQQRIMKR ARSSRSHKGR
NENNVSSPYN TEKSTGGVVI SSISNAAAKM SQITRTVSGG THGNNGNNNV TSASNAHPVT
SERLGAKTAM GGTATSSQNN HGKNHIYEDN SVINSSSITA SRAPVDGSAN ANTGGGGGGV
RDSVMKRLSM LKAGRKATRL NVRDGGRTGG TLKEE
//
