ID A0A1J7JJG6_9PEZI Unreviewed; 2095 AA.
AC A0A1J7JJG6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=SH3 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CONLIGDRAFT_716207 {ECO:0000313|EMBL:OIW27794.1};
OS Coniochaeta ligniaria NRRL 30616.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX NCBI_TaxID=1408157 {ECO:0000313|EMBL:OIW27794.1, ECO:0000313|Proteomes:UP000182658};
RN [1] {ECO:0000313|EMBL:OIW27794.1, ECO:0000313|Proteomes:UP000182658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 30616 {ECO:0000313|EMBL:OIW27794.1,
RC ECO:0000313|Proteomes:UP000182658};
RG DOE Joint Genome Institute;
RA Jimenez D.J., Hector R.E., Riley R., Sun H., Grigoriev I.V.,
RA Van Elsas J.D., Nichols N.N.;
RT "Draft genome sequence of Coniochaeta ligniaria NRRL30616, a
RT lignocellulolytic fungus for bioabatement of inhibitors in plant biomass
RT hydrolysates.";
RL Submitted (OCT-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; KV875099; OIW27794.1; -; Genomic_DNA.
DR STRING; 1408157.A0A1J7JJG6; -.
DR InParanoid; A0A1J7JJG6; -.
DR OrthoDB; 8258at2759; -.
DR Proteomes; UP000182658; 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 Pfam; PF00018; SH3_1; 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:UP000182658};
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 626..808
FT /note="C2 DOCK-type"
FT /evidence="ECO:0000259|PROSITE:PS51650"
FT DOMAIN 1459..1874
FT /note="DOCKER"
FT /evidence="ECO:0000259|PROSITE:PS51651"
FT REGION 115..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1869..1926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1939..2095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1875..1891
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1892..1909
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1960..2003
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2034..2055
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2095 AA; 232793 MW; DE31C6EB83086007 CRC64;
MPWQPLPRIA FAVASYPFTP SSPADLPLEI GDELYIIEET PDGNWLRGYL VSPPSLLAGL
TSVKGQTLEA RVFSGIFPRS CVEIREVLGE SDGTEDNESE DGTFESLDIR HVGSDSAKSG
LASDRKTRRR DKLKGPEISI VGLGDSKAKK IKRESSVSNA PHGRLSVPVK REPGEPRPPA
PVPMLKVGDE TPTSASEPLI DEIASCLREW HSTNLHEMLL SRQYGKLDRL WQLITTLNMA
RQQFLHNVLT THEYEILREK TVWDLVHVNK LCGGEVIVRD PSARGRVLTG DDSVVEITKL
QSTMSLLDEP PTPIVELTAL HHLLVDVKGF AGASSESTTL VLYLASKQGG GNITPLSESY
IVEVPAGGQM GHLSRSTQMR TLFADLTAAD IGDGPSSSEI FLVIKVRAQQ QIVAAAPGSR
SGSITQNMTS FSKESSKPPL SSGNKSMRRS LMWAGKSTRQ AFSRGNPKLD SLEEHTEQRP
PTSGAPKTSE GYPPGTASSK GPRDSTDAQG GTMTAERTVG VGVLRLNSIM KHEEDVEHVV
SIWSPTSRLT SEKNENGDDW DPVLRDLVDS RTGQYEKSRR AERLQIHLRS FNNPDADLLI
KATPTVLSGI CKTNKIGFAG APTKPRSDIY VTIDEAILSR QTLLSRFGSS PGSLPSSLHG
NNLQVTLEVR KSTGERVDNC IFASSNTEAA SNWKTVAAER GEPWRQTIRL LIAPQDVHGS
HLVFQISDLP NHPFAVAYLP LWDEQAFIRD GPHGLLFYRI DENTATPQHN AQGRGGYLSL
PWTAKGKVEH QADVTGPLAM LRVETYLCST RFSQDRVVLG LLKWKESPRE EIPDLLKQFI
FVAEIEVVKL LNDVLDSLFG ILVEYQGNDE YEDLVFTALV RVLDIVHDRR FNLSPLVDQY
AENKFNYPYA TPCLVRSFTR LLSNPSEPET ARKLRATFKV VRHILKFITH SRGQQKVKEA
GIGITSSTAG AGFTRHLRSI FKALDAMMRN NSPVLVGSQT LAVQHFHTWL PELAGLLTTE
EILHIAIDFV DSCSNVKGKL ILYKLVLIIN YSKLEIFSHP EQRSALSANT VRWIAPHWGT
PEQVTEQWKE QVRLCCSILA SQVDHLGSEI PDHIPKIIES YLAIQAFPLK PRNRLSLLFP
TTYPFPTKST ANEVAFDEAL VELSAVLSAL SNSPTGMQLE LADDDISVIV ENTLRVQMSI
LEGEAFPASW LSVHIFHHKS TMRMLKYLAE TILLDSFLPH PDEAENFNTD LWKMFFSTLL
KLVGSPSLAL ETFPEQKRRA VWKIAGDVRE DGAELLRRTW EAIGWETSAD ERQRYGLSKM
GGYQVQYVPT LVGPIVELCL SVHEGLRRMA VEVLQTMIVS EWTLSEDLSV IQTEMIDCLD
VYFKSKPITE SILQKLFVNE LLGRFEPLAK IRDEPLYAAL RDLMGTVDEF LDLLVAVHSG
DGVGEATHLI HRLRLMEFLR DMQKEEIFVR YVHQLATLQT EARNHTEAGL ALRLHADLYD
WDPIKITPAL SDPVFPPQSH FDRKEKVYFE MIKHFEDGEA WTSALDAYKE LQLQYETNVY
DFAKLARTER AIATIYETLA KSDKLVPKYF KVIYKGLGFP TSLRDKEFVF EGSPAEKTSA
FTDRMQEQYP AAQIVTSEHI DDVEGQFLVI SAVSPHRNLG HHVFQRARVP LAMRDYVLST
HPQTFSVTRK RNTSGPVTGH YAEKTVYTTA EQFPTILRRS EIVSVNEVRL SAKQTALERI
IRKTAEMTAV EKRIADGEGN DEVTQVLVDA VRISVNPDSE NSVAIYRQLL PKARSPGEGE
DEDEDLQEVQ PVELDAQENA IKMALIDHAI MIKRCLASFS KINSPSLARH VEELQKYFES
TYAPEIAAFT PPQPVRSPNI TPSPTWPRSP PSTVNTPTLQ QQPLSGAKTN GTAAGEEVSV
VQPVQLRQGR GARLSFLGGR KKDQAAQQQH PPPPPIPQTN GDHQVNGDAE SATSGHSRGK
DNPNRLSFFR SNSSTQPVEV KLESPSNASK HHEWVVEQAL PGNKAPTAAP ARRKSSDISR
TLSSKENSNP SMTSAAADHA GGARKVGNVR KRLSMLKLGK KSSKGSGLMG SLDEE
//
