ID A0A0G2FKQ1_9PEZI Unreviewed; 1084 AA.
AC A0A0G2FKQ1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Putative ef hand domain-containing protein {ECO:0000313|EMBL:KKY34641.1};
GN ORFNames=UCDDA912_g05393 {ECO:0000313|EMBL:KKY34641.1};
OS Diaporthe ampelina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY34641.1, ECO:0000313|Proteomes:UP000034680};
RN [1] {ECO:0000313|EMBL:KKY34641.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY34641.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY34641.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY34641.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the PAN1 actin cytoskeleton-regulatory complex
CC required for the internalization of endosomes during actin-coupled
CC endocytosis. The complex links the site of endocytosis to the cell
CC membrane-associated actin cytoskeleton. Mediates uptake of external
CC molecules and vacuolar degradation of plasma membrane proteins. Plays a
CC role in the proper organization of the cell membrane-associated actin
CC cytoskeleton and promotes its destabilization.
CC {ECO:0000256|ARBA:ARBA00025194}.
CC -!- SUBUNIT: Component of the PAN1 actin cytoskeleton-regulatory complex.
CC {ECO:0000256|ARBA:ARBA00011159}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004413};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm,
CC cytoskeleton, actin patch {ECO:0000256|ARBA:ARBA00004134}. Endosome
CC membrane {ECO:0000256|ARBA:ARBA00004125}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004125}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004125}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
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:KKY34641.1}.
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DR EMBL; LCUC01000194; KKY34641.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2FKQ1; -.
DR STRING; 1214573.A0A0G2FKQ1; -.
DR OrthoDB; 12127at2759; -.
DR Proteomes; UP000034680; Unassembled WGS sequence.
DR GO; GO:0030479; C:actin cortical patch; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd00052; EH; 3.
DR Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 1.10.238.10; EF-hand; 3.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000261; EH_dom.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR11216; EH DOMAIN; 1.
DR PANTHER; PTHR11216:SF161; EPIDERMAL GROWTH FACTOR RECEPTOR PATHWAY SUBSTRATE CLONE 15, ISOFORM A; 1.
DR Pfam; PF12763; EF-hand_4; 2.
DR Pfam; PF00627; UBA; 1.
DR SMART; SM00027; EH; 3.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF47473; EF-hand; 3.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50031; EH; 3.
DR PROSITE; PS50030; UBA; 1.
PE 4: Predicted;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Reference proteome {ECO:0000313|Proteomes:UP000034680}.
FT DOMAIN 20..106
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 148..239
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 302..337
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 303..393
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 1043..1083
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 238..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 392..489
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 241..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..956
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1084 AA; 113799 MW; 406C42A417FE548B CRC64;
MAESSSADAG APNLNLGPDE KRVYGQLFRQ ADTESVGVVT GEIAVKFFEK TRLDSRILGE
IWQLADQENR GFLTPAGFGI ALRLIGHAQA GREPSLQVAL QPGPIPRFDG FTPAPPPLAP
APTGSPQPIS AQGTGNAPIR IPPLTPDKVA QYAGLFERQQ LQPGNLLGGE QARQIFERSN
LPNETLGRIW QLADTEQRGA LVQTEFVIAM HLLTSMKSGA LRALPNILPA PLYEAATRRG
SSAGRPQSPS GPTAPISAIP RQLSGQAAHQ MPMRTASPLA GAHGRSPLAP QSTGDAWLIT
PGDKQRFDVI YDSLDKTKKG FITGEEAVPF LSQSNLPEAA LANIWDLADI RSEGRLNRDE
FAVAMYLIRQ QRMKQGDLPQ VLPANLIPPR QRNATQNELT QTSQQKKNFE QRLAQLRTLY
ENQAKEVREL QEKLNASRND TKKLQAESLA LDGTLHDLQT QYQTVATALQ ADQQENANLK
EKIRAVNAEV ASLKPQIEKL KSEARQQKGL VAINRKQLTT NEGERDKLKT EAEDLAKENS
ELARQLSQSP PPNPPPQVAS PALSNASGSN PFFRRTGSTD MMGAFASPGA SKTYNDKSFD
DVFGPAIPAF KPQTTGASAT STGSFATPTS NSPNVSRNPT FASEASAIAP APPEPRQVST
PAGEAATSAP LEAAATGGST SETQDLEVKP ADPGSFFDGA KSDPPAASGG DPFSAMDEAK
AKDDFESAFA SFKKNSSAAK SAPEDASATE QPKARSAFDS EFPPISELEK DDSSDTEDDQ
GGFDDDFAPA SPSANPTDKP ASPSLAKAVA PDAPAGGSDE TAQNEAEDMF GSAPPPGSFP
EPEQAPSTEA PAAAGSDGTT TGMSKQSSTF DDLDDDFADL EDAKEGSADD DFQTISRSGL
DDFNATFDSP PPAAKSDAAA GPPGSSHGPA APFSNESTFD FASIDNTASQ TSAAAPTEGA
PKGPAQPENH DWDAIFASLD DAPPAQSSGS PPPPGSAGSG TAPPAAAAAA AAPAEPSNES
GSNGLLTGPR PTGPGRALTE DGEHDDPILK NLTSMGYSRG DALNALEKYD YNLERAANYL
ASQS
//
