ID A0A364LE55_9EURO Unreviewed; 2125 AA.
AC A0A364LE55;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=SH3 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BHQ10_010085 {ECO:0000313|EMBL:RAO74073.1};
OS Talaromyces amestolkiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1196081 {ECO:0000313|EMBL:RAO74073.1, ECO:0000313|Proteomes:UP000249363};
RN [1] {ECO:0000313|EMBL:RAO74073.1, ECO:0000313|Proteomes:UP000249363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIB {ECO:0000313|EMBL:RAO74073.1,
RC ECO:0000313|Proteomes:UP000249363};
RX PubMed=28649280; DOI=10.1186/s13068-017-0844-7;
RA de Eugenio L.I., Mendez-Liter J.A., Nieto-Dominguez M., Alonso L.,
RA Gil-Munoz J., Barriuso J., Prieto A., Martinez M.J.;
RT "Differential ?-glucosidase expression as a function of carbon source
RT availability in Talaromyces amestolkiae: a genomic and proteomic
RT approach.";
RL Biotechnol. Biofuels 10:161-161(2017).
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:RAO74073.1}.
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DR EMBL; MIKG01000029; RAO74073.1; -; Genomic_DNA.
DR STRING; 1196081.A0A364LE55; -.
DR OrthoDB; 8258at2759; -.
DR Proteomes; UP000249363; 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:UP000249363};
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 590..772
FT /note="C2 DOCK-type"
FT /evidence="ECO:0000259|PROSITE:PS51650"
FT DOMAIN 1415..1832
FT /note="DOCKER"
FT /evidence="ECO:0000259|PROSITE:PS51651"
FT REGION 121..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1750..1771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1824..2087
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1752..1769
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1827..1846
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1895..1929
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1930..1960
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1981..2014
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2015..2087
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2125 AA; 237507 MW; 4FEA5D24915409F5 CRC64;
MPWRPLPRIA FAVAIYPFQP SSPADLPLEL GDELYIIEQG GANGSWFRGY LVAPPSLLAG
LTSVKGQTLE ARVFSGIFPR NCVEIREYLG DAEGRKALDN GDTLLANGIN GHQEEVVKHR
QDTADSLEDV GHNPRSGSAA TYRSGSVPLT PSSFVARNPN GSKPAAPVPM LKIGDETPTS
YEEPLVDEIA SSLREWHSTN LHELLLTRQY GSVETMYNVV LDLDLARRQL LHDVLTSKEK
SAVRQTTVWN LVRGNKMLTG EVIVRDPKQN GRLLTGDDSA IELTKLQSEM SMFDSDPRQQ
VDASTLRHLL LEIKTIAGSH AGPVTLSLYL STKTDSGALK PLSETYVLEI QSADSFMALA
HTSKLKTLFT ELCAADVGDG AGNEAHLYLV VIIQSAELPR PSLPYATRTS SSRDGGLNRS
PSTMHSVKGS VKGRRSMVWT AKSPRPGQPE TIKETPPRSS DSTNSQGQGE NTTLKDATVI
RTVGAGILDV AHIVRQNSEA EHVINIWSPL GEDVEEGGND LEGFDELIRN VLPSSSGRYF
KCYQASQLHL HFYPFIDSDA DALVRSNPTL MHNVTQTRRM GFAAAPSQPR SDIYLNISRA
KFPWPALLCH PQSGQVPVPV NTGFRNLQLT LEVRNGSGAR LERCIFASSN STGHTAWRTT
VTDRNASWNQ TIRLNIPTEQ VPGAHVIMSI ADAPEFPFAL CWLPLWNQQA FIHDGPHSLL
LHAYDKVTSS VDEEGRGAYL SLPWSSLHKN SSVPDESVTG PLSTVHVETN LCSTEYSQDQ
IILGLISWKK QTGNEVLELL RRVLFVPQIE IVKQLRDVFD ALFGILVENA GSEEYEDLIF
NALVTVLGIT HDRRYNLGPL VDHYTENQFN FPFATPCLIR SYLRLLQSHD TPQQSRNLRA
AFKVGRHLLK FIINAREQQK LKEEGIGVTN VQPTFNRDLH SIFKSLETLM RNPSPVLVGT
KTLVVQHFHS WLPELTNVLP KDEIIMIALS FMDSCKDVKG MLILYKLILI QNYTKLDVFA
SGEDRDTLIS CCSSWLDPYW GNTGEVSDQY RDQVRLCASI VAEFSKQPQP QLYMFMHKIT
SSYCAVVLEG VDDTDYLSML YSKSFPFQVK ASDRKQKFDE ALVELAGLMA AISNIQDPKL
PILKLDDMAL FIFNSLEAHR SIISCEAYPE DWLSLHIYNH RAAVKNFENL SSMLIHSFLP
PPDEADTFDM KLWELFFTTL LKVVSSEALA LETFPEQKRR AVWKIGGDVR EQGAALLRQT
WEAIGWETSE DERAKYALDR LGGYQVQYVP SLVPGIIELC LSVHEGLRRV AVEVLQTMII
SEWDLNQDLS IIEMEIVTSL DVLFQTKHMN ESITQKLFIT ELLDLFEKIE DSDEALATDV
KGLIGTIDEL LELLVACNSG GITESLHTLR LMEFMKDMDR EDIFIRYVHE LAQTQATEHN
YTQAGLALQF HADLYTWEPT RMVPALTNPA YPEQSAFDRK EALYFKIIQH FEDGKAWTHA
LACYKELIEQ YEHIVMDFTK LSRAQGSMAK IYESISKEEK AFPRYFRVSY RGLGFQATLR
DKHFIFEALP NERMASFTDR MQKLHPAAQI TSSHEIEDIE GQFLQISAVS PHREIMHPVY
QRSKVPHSVR EHLLISVPLQ FSYTSKRHTS GLNVKEQWVE KTIFTTAEPF PNILRRSEIV
ATEVVELTPL QTAIERTWRK TQELHLLEQH AISGDDSTLS GLTEALVQLL DLGAPHSSCV
AIYRPFLASE KEDDNEQEEG EEEDEIEQKP IDPLENALAV ALIDHALSIK RCLSLFSRPS
HQATQIELLA RFEDAFGPEI ASLAAHAQTL SPPQSANHSS NRSXPHANGH GADLAGRSFS
PEQELIRTSR SNSQRKHSAK PSLSHRISIA NPFKRATHHA SSSVATAKDT HQSPDLRQLA
DAQSSRQSIN LQDRDDDAVT VHSRATAKSE KRRSWFGGDV KPKHKATPSV TGYAGEQQVD
EQSRNRSRAR SATNKSTKSH DESNQPRTRQ SRLESKKSTP VMASGGWDTA QTALPRTSQS
DNRPNTSERF GYPDKSLTST VTISAGGSTS QSNGNTQNNN VSAVSTGGVR DSVKKRFSLL
KGINKKTSRM NVREGGVLAE SLREE
//
