ID A0A1S7UMG5_ROSNE Unreviewed; 2042 AA.
AC A0A1S7UMG5;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Putative sh3 domain-containing protein {ECO:0000313|EMBL:GAP83641.2};
GN ORFNames=SAMD00023353_0500230 {ECO:0000313|EMBL:GAP83641.2};
OS Rosellinia necatrix (White root-rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariaceae; Rosellinia.
OX NCBI_TaxID=77044 {ECO:0000313|EMBL:GAP83641.2};
RN [1] {ECO:0000313|EMBL:GAP83641.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W97 {ECO:0000313|EMBL:GAP83641.2};
RA Kanematsu S.;
RT "Draft genome sequence of Rosellinia necatrix.";
RL Submitted (MAR-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; DF977450; GAP83641.2; -; Genomic_DNA.
DR STRING; 77044.A0A1S7UMG5; -.
DR OMA; LWDNQAF; -.
DR OrthoDB; 8258at2759; -.
DR Proteomes; UP000054516; 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:UP000054516};
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 619..798
FT /note="C2 DOCK-type"
FT /evidence="ECO:0000259|PROSITE:PS51650"
FT DOMAIN 1447..1854
FT /note="DOCKER"
FT /evidence="ECO:0000259|PROSITE:PS51651"
FT REGION 88..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1915..1989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1925..1982
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2042 AA; 226193 MW; FF725F907447E435 CRC64;
MPWRPLPRIA FAVATYPFDT KAENELPLEI GDDLYIIEET PDGEWLRGYL LAPPSLLAGL
TSVKGQTLEA RVFSGIFPRN RVEIREVLGD GDGEGEGGED RDGNGSFHGS DEHASRRCSD
SGKSGIVSGD GKRDQGGNNW KIKSRGQLSS NHDSSQYAKP SGNANAGLPS GKPPAPVPML
RMGDETSTST NEPLIDEIAS CLREWHSTNF HELLLTRQYT KLEDMSHLIQ TIDLARRQLL
HSLLTDREAV ALREKTVWDL VRGNKLCGGE VIVRDPARRG KVLVGDDSVI ETTKLQSVMS
LLDDPPLPQV ESTSLHHLMV DVKSFAASSS ESATLDFYLA TRSAGGLLTL TETCAFEVPH
GGNMNSATKD AQMRTLFTDL TSADIGDGPS ADSELFLVVK VRAPQQIAAG KPPSRSGSFG
PSATSFSKEK SPAPSGSKAS RRSLMWGSTR SPFSRGATKL DALSEHPDER PQSGGNVPAR
DATVPPSTAG SVSGRTSVEG PQQIQIVTNR LVGVGVLNIK SIMKERGESE QVITIWSPSP
TAGPERPETT QGWDSLIRGI LDGEPNHHEK SRRAERLLVH LKSFDHLDAD VLIKSTPTLL
SAVNKTNKMG FSGAPTKPRS DIYITIDEAL LARQNLISRY GGSATSISSN MLGNNLVVSV
NVRRQTGERI ESCIFPSSNS HPITTWTSFA VQRGERWSKT LRLSLSPSDV TTSHVVLTIS
ELPNAPFAMS YLPLWDRQAF MSDGSHSLLL YRIDEHTQNA QPDSVGKGGY LSLPWSARTD
SSEVTGPLAV LRVESYLCST QFSQDRTILG LLKWKDGPKS EISTLLRQLI FVPEIEVVKL
LSDVLDSLFS ILVEHQGNDE FEDLVFTALV RVLGIVHDRR FNVSPLVDQY AEMRFNYPFA
TPCLVRSFTR LLTKPTESET ARKLRATLKV VRHILKFITH ARGQQKAKEA GIGITGSTPG
FTRHLQTIFK ALDSMMRSTA PVLVGSQTLA VQHFHTWLPE LTGLLTTEEI LHIAIDFMDS
CALVKGKLVL YKLILIINYS KLDLFAQPEQ RSALSANTVR WIAPHWGHTD EVTEQWRDQV
RLCCSVLASQ IGYLNSEIPD YIPKIVDSFL AIQSTERKPK DRFSLLFPTS YPFPTKPLPG
EPVVFDEPLI ELSALLAASS NSPSGMQLEL SVDDITIVLK NTLQVNLSIL QGEAFPSNWL
SVYTYHHKST MKILQYLAGI LLDSGLPDPD DAEDFDTELW RLFFMTLLKL VGSGCLALET
FPEQKRRAVW KIAGDVREHG AELLRQTWEA IGWETSTDER TRYGLSKMGG YQVQYVPTLV
GPIVQLCLSV HGGLRRVAVE VLQTMIVSEW TLSEDLSVIQ TEMIDCLDSF FKDQAMTESI
MQKLFIDELL DRFEYLSQIE DDPLYASLRE LIATVDTFLD LLVAVHSGDT TGEASNLMNR
LELMEFLRDM HKEDIFIRYV HQLAALQRDA GNHTEAGLAL RLHADLYDWD PAVIASALSD
PNYPEQSHFE RKEQIFFAMI KHFEDGEAWS SALAAYSELR TQYETNAFDF AKLARTERAV
ATIYETLAKG DKLMPKYFKV VFKGLGFPIT LRDKAYIYEG SYGERTNTFA DHMQEQYQSA
QILTNGDVDS EVEGQYLIVS AVSPHRDLQH QVFQRARVAH PIRDFLLSSN PQTFSVSSKR
NTTGQVAEHY SEKVIYTTSE AFPSILRRSE IIEVDHVKLN AKETALERIV RKTQEMTVVE
RQLAENEDNN ELAQLMVGAI SVSVLSESET GVASYRKLLP VIDLEDIDEI EPELSRQENS
IKIALVDHAI MIKRSLTNFS TSSNPILVKG YQDLYPHFMS TFAPEIAIFA PTRPQGDTSP
GASPAWQRFT PTRESGQLRG NIRTSLTNGT AVVEEASTVQ PIALRQRGAR LSFLGGKMKG
AQPSNRDSIG ATQGVGESSE SNSQYSRSKE TPSRVLRAQS IDTTSGSNSH RKNGSVDARV
STSIADRSRK SREIVDVVEG SFGRTVEGGV LRIGSVRKRL SMLKLGKKPS RYNGITGSVD
EE
//
