ID A0A165YT37_9AGAM Unreviewed; 2186 AA.
AC A0A165YT37;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Cytoplasmic protein {ECO:0000313|EMBL:KZV61768.1};
GN ORFNames=PENSPDRAFT_759207 {ECO:0000313|EMBL:KZV61768.1};
OS Peniophora sp. CONT.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Peniophoraceae; Peniophora.
OX NCBI_TaxID=1314672 {ECO:0000313|EMBL:KZV61768.1, ECO:0000313|Proteomes:UP000077086};
RN [1] {ECO:0000313|EMBL:KZV61768.1, ECO:0000313|Proteomes:UP000077086}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CONT {ECO:0000313|EMBL:KZV61768.1,
RC ECO:0000313|Proteomes:UP000077086};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000256|PROSITE-
CC ProRule:PRU00983}.
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DR EMBL; KV424758; KZV61768.1; -; Genomic_DNA.
DR STRING; 1314672.A0A165YT37; -.
DR InParanoid; A0A165YT37; -.
DR OrthoDB; 8258at2759; -.
DR Proteomes; UP000077086; 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; 1.20.58.740; -; 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 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; IPR043162; DOCK_C_lobe_C.
DR InterPro; IPR032376; DOCK_N.
DR InterPro; IPR042455; DOCK_N_sub1.
DR InterPro; IPR027357; DOCKER_dom.
DR InterPro; IPR046769; DOCKER_Lobe_A.
DR InterPro; IPR046773; DOCKER_Lobe_C.
DR InterPro; IPR006594; LisH.
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; PF20421; DHR-2_Lobe_C; 1.
DR Pfam; PF14429; DOCK-C2; 1.
DR Pfam; PF16172; DOCK_N; 1.
DR SMART; SM00667; LisH; 2.
DR PROSITE; PS51650; C2_DOCK; 1.
DR PROSITE; PS51651; DOCKER; 1.
DR PROSITE; PS50896; LISH; 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:UP000077086}.
FT DOMAIN 659..856
FT /note="C2 DOCK-type"
FT /evidence="ECO:0000259|PROSITE:PS51650"
FT DOMAIN 1584..1995
FT /note="DOCKER"
FT /evidence="ECO:0000259|PROSITE:PS51651"
FT REGION 152..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1994..2019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2118..2137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2186 AA; 240854 MW; A2CD6CE29908D9C3 CRC64;
MVLSPSRPTT PGRSGVWEPL PAFVYGYAVH PLSPSHRDTR ISHRPRLSTV TESSVGESSF
LHRDVVSLEV GDEVYAFERY TGREGEWYRG YVVCTTRRPA VVWNAVDAGP KLEEAQQVFI
GIFPASHIHR RDELPDAEGR LAVVAHEFAQ GKRPPPSIID DRESRKSFKL GPPPDQAGSS
RAGLSVYPAS VRSASPESHL GKPLPPRPTL KPGDETESGA LQPIVDEIAS ALREWHMLMF
QYLARRDYNK FNIVKDHIDA LHLSRRQLLA NTLSVEETAA VRAECVTRLV AGNLVQGLDV
IVRHPQGGGL VTVDVEGELD PRNWMSTVRM FALQAGLAYM SPDSPKPALP SPTPLRTQTS
FENLSSAPLP TPALSAFPEF AARSPVPKSA TTPRTFGPST PLESPTSPPD AVKFFHVFFE
MRAFVASPCA PGETAELFFS LYNKHDARFV TEEFCAVLNH NGVMARDPTS RVRTLFAELA
PSDIEHPLFL VCRIVRNGAL RMGNAVSSSE LARRTSGSVY NEKDGHEGIT SPRLGGAKEL
NGNGSDNAPF RRPFGCAVLE LTQVGRMSAD QDASATREFT MPIFSPVNEA IFSMLHQDII
GGNNKEFEKT SRADSMAVSI KVFHGNAERI TRENTTLLQD TPRTLRLGFP DVVFPGDTRN
ELYIKLWSGE FPSARDKSVR GSVSPFVPRS SSSSGANNIQ VSLEVRDGDG RLVPDALSPG
AGQPPIPIFH SLVFARNSQP TFGELIKVAL PQRALPRWHL FFTFRQRRPG STTLDRPFAF
AFLPLSSRGA HTFLEDGGHT LILYRADRMG QLTPDVYLEA PAALPPDGRE PPAIPPEMAR
VAPALRDVLV IRSSLCSARH TQNTVLLSLL HWQALAQDPA LLKDALSKFT FVNPVEIVKF
LRDVFDALFG IMTSPANASM NGEMDAPAFD ALVTVLGIVQ DRRFSNFRPV LDVYIREHFH
HYSAGLHLLN SLNRLLMNPT SNETASQLRA ALKVWPHIFA LIARARELQK ERDAGVGAAA
TADHLEHQFR RELKTHLGEV GRMMGTSSPP SIIGTQTLAL RAFPRVLPAL GSAFNPLELV
GIAVQFANAL PSHLEKGKMA VEKLVLYLRL VKSSLFADAA ARAALVETVV LWLKPHCGAF
DTHFRTLGLD EEEAPEGSPR RDAARVGWLE RIRLCVGIVA VMLDSLQSKL VDPLVSSDRR
ALRQEQDNVE FLLSLLPRLL ESYAEFTDGR NAGALERVRG AATAPASVPV IFPESYPFSL
VALLPGSSHG LFSPAQSETA VVLLALILSS PKKHLVNFFE SILEIEGRLH FSRLLRALFD
AGKNMLDNAA WPRNWLNVNI LAHKVLVRAM DAAAVLLTRS FVPGQNPDED IFPFDKELWS
EGLQMLLKLL SSDQLLIEEL TSQKRRAVWR LAGDIRGDGA AILLTLWDAL GWPEDVCESH
GVVTRFGGFQ TELAGLVGPV VDLCVSHHDQ LRNNAVQMLY SMIVSQWHAH GHFSSIENEL
VSKLDGLFMS GAKGDDVSRA FFITQLRQLF ESSAVDKQLQ LRVSEFMDSV DQFLELLLSV
RALPEGEEYA DDRVIATLRL MNFIRRIGRN EMYIKYVHQL VNMHLQAQNY VEAALTLKLH
ADLHEWDLNS FAEPMEDLGL PQQSQFHRKE TLHLLILDYL GKGKAWESAI EMCKELAFQH
QEVTFNYGRL AEIMRHQASL LELIVTEQRY YPDYFRVAFF GNFPTAIRNK QFIYRGFDWE
KFGAFCERML GKHPGARLLR SASDPPVDIR FGGDQYIQCS PVVPEPDQTL AIFTNPDVPI
AVRTYYEHSA IRLFSSSRQV TRLDREGNEE TWVEKTYFTT EEIFPTVLRR SEIITAEMIE
ISPVETALHD VEARNKELGA LNTRYAALAR TGQIVSTNPL SMTLNSVVDA PASGGIISYR
EVFLSPDYLE HYPERVEHVE KLRDAIDTQV RIIDNCLRLH GQLCPPEMLA FHDTLEKFFR
KNFSEEIHRL TFDGPAEQHP AVAGTRSRKP SEASPYAAAN ARMQSDAISI APSVATTHRG
GGGAPAFPVP PLPSRASVIS SPSSLGTIDA GTYGTAMSSI SYGVGTGSGS GSLAAGSKQT
PLQRGLARLT RHGINSVVGS VTNDGSDGMS VAESPSDSFV NVSQSTGNIA SQGAIGSSAS
IVGSISGSIK GRFSRLGALS FGRGGA
//
