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Database: UniProt
Entry: A0A094AHZ1_9PEZI
LinkDB: A0A094AHZ1_9PEZI
Original site: A0A094AHZ1_9PEZI 
ID   A0A094AHZ1_9PEZI        Unreviewed;      2006 AA.
AC   A0A094AHZ1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=SH3 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=V493_03823 {ECO:0000313|EMBL:KFY26878.1};
OS   Pseudogymnoascus sp. VKM F-4281 (FW-2241).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420906 {ECO:0000313|EMBL:KFY26878.1, ECO:0000313|Proteomes:UP000029327};
RN   [1] {ECO:0000313|EMBL:KFY26878.1, ECO:0000313|Proteomes:UP000029327}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4281 (FW-2241) {ECO:0000313|Proteomes:UP000029327};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00983}.
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:KFY26878.1}.
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DR   EMBL; JPJV01001491; KFY26878.1; -; Genomic_DNA.
DR   STRING; 1420906.A0A094AHZ1; -.
DR   HOGENOM; CLU_000595_0_1_1; -.
DR   OrthoDB; 8258at2759; -.
DR   Proteomes; UP000029327; 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; 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; 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:UP000029327};
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          600..784
FT                   /note="C2 DOCK-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51650"
FT   DOMAIN          1435..1841
FT                   /note="DOCKER"
FT                   /evidence="ECO:0000259|PROSITE:PS51651"
FT   REGION          93..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          394..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1860..2006
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..135
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..459
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        472..486
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1866..1880
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1924..1948
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1949..1976
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1988..2006
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2006 AA;  223327 MW;  6FF73BAD0F4A799E CRC64;
     MPWQPLPRIA FAVATFPFQA QNAADLPLEL GDELYIIEQG GKNGDWFRGY LIAPPSLLAG
     LTSVKGQALE SRVFSGIFPR SCVEVREVLG ESSEEELVES SQLNGYHDES SSKSEGSANS
     LNNIAQKLTN GTKTTKKRNS LRDDLRNGTL PPVVRDTNAP KPAAPVPMLN IGDETPTSLS
     EPLVDEIASC LREWHSANLH EMLLSRQYPL LDKMTSLVQG LDKSRQQLLH NVLTTHEVEQ
     LREKTIWDLV KGNKLVSGEV IVRSPTERGR ILTGEDSAVE ITSLQSMMSC LEENPQHHVE
     LVALHHLLVD VKGFVGASTE TTTLVLYLAS RTQQAFPTTL SESFVLEIPP NGSLASLATA
     RDMRTLFMDL TSADIGDTNS ADTEVFLVAK VQQNQQPLHG KQPESRAGMV SRENLPSSTG
     EKTSLSGSVG KSARRSLMWG KSSQRSANSR NSPVSKMSSV SEKDVGLPPK TSESRTGRTP
     PRTATAKVVS RTVGVGALKL NSIMKQDADV EQVMTIWTPS ADFDPDSQTL GEGWDEVIRD
     LLESKTGCYE KSAKAERMHL NLRHFASEDG ESLIKATPTL LSNVSRTNKL GFSGAPTKPR
     SDIYVTIDKA TLPRGALLSR ATGSATALAT QMTCHNLQVT MEVRRATGDR IENCIYPSSN
     GEPVSSWEST VMERGEAWNQ TIRLAVPPQD VPGCHLAIFV SDAPNQPFAI SHLPLWHQQA
     FIRDGHHSLL MYKYDETTTH TKPDANGRGG YLGAPWNARG KDDVSKDEAI TGPLSKMRVQ
     TYLCSTRFSQ DKVLLGLLNW KDQSVGELSD LLKRLVFVPE IEIVKLLNDV LDSMFAVLVE
     HAGNDAFEDL VFNALVTVLG IVHDRRFNLG PLVDHYAETQ FNYPFATPCL VRSFVRLLSD
     PTDAESSKRL RATFKVTRHI LKFITHARGQ QIVKEADIGI SNGSPGFSRH LRGIFKALDA
     LMRNTSPILV GSQTLAVQHF QGWLPELTGL LTTEEILHIA IDFMDSCSAV KGKLVLYKLI
     LIINYAKLDL FSQPDQKAAL TTNTVRWIAP HWGKTAEVTS QWHDQVRLCC SVLSTQIEML
     GPEIPDHIPK IIDSYLAIQG APRRPSTRLS LLFPSSYPFP TKPIEGSKPE FDEALVELSA
     ILSATSSRPQ GMQLELAEDE MSTLLQDALR VHTSILECEA FPKSWLSIRI YHHRSTMKTL
     EYIAKILLES FLPDPEEEAG MDYNTDLWKA FFTTLLKLIG SDALALETFP EQKRRAVWKI
     AGDIREQGAE LLRRTWEAIG WETTPEEKQR YGLQKIGGYQ VQYVPGLVGP IVELCLSVHE
     GLRRVAVEVL QTMIASEWNL SEDLSTIQME MIDSLDLLFK SKPLTESILQ KFFVNELLDL
     FEPLSTMPGD NMYASLSDMI ATIDEFLDLL VAVYSADNAN EASGLIDRLR LMDFLRDMQK
     EEIFIRYVHQ LSVVQAESRN FTESGLALRL HADLYDWDPL KILPPLSDPD FPAQSAFERK
     ERIYFDMIKH FEDGEAWSSA LVAYKELQVQ YEENVFDFFK LARTQRAIGS VYESIAKSNK
     PMLKYFRVAY RGLGFPPGLR DKEFVFEGAP AEKTSAFTDH LQEQYPGAQI VSHLESDDVE
     GQFLKVSTLG PYRNLDHAVF QRAKVSNVTR DYLLSAHCQQ FATTVSRNTS GPVEEHFADK
     MVYITADQFP TISRRSEIIT AERIRLSPLQ TALERTVRKT QEMTSVERKA AEGDESVVPL
     LVEAVSISVS HSSESSIARY RALLPLPAFD EEGEEQVVVL SPLENALKMA LIDHAIMIKR
     ILTMFLRSMN PTVRYRQEEL TSREFVVPIF GISDILDFES TFGPELVTLA PVQPRQITPA
     PTWSVASPSV PSPPQPRPES PTQRRELGKL NFLNRKAGPP VSFKGGQGRK ESSDEGSSMH
     SGVSRGKENR RSFFGRGDNE DWQTDTDGSG LRRSESQGSE GLERPTTATS IGSKVGSVRK
     RLSKLTLGRK GSRKEFRAGV VIRETD
//
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