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Database: UniProt
Entry: A0A194UZA1_9PEZI
LinkDB: A0A194UZA1_9PEZI
Original site: A0A194UZA1_9PEZI 
ID   A0A194UZA1_9PEZI        Unreviewed;      1036 AA.
AC   A0A194UZA1;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   03-MAY-2023, entry version 24.
DE   SubName: Full=Endocytosis protein end4 {ECO:0000313|EMBL:KUI57020.1};
GN   ORFNames=VP1G_04340 {ECO:0000313|EMBL:KUI57020.1};
OS   Valsa mali var. pyri (nom. inval.).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX   NCBI_TaxID=694573 {ECO:0000313|EMBL:KUI57020.1, ECO:0000313|Proteomes:UP000078576};
RN   [1] {ECO:0000313|Proteomes:UP000078576}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SXYL134 {ECO:0000313|Proteomes:UP000078576};
RA   Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA   Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT   "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT   Colonization on Woody Bark.";
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the SLA2 family.
CC       {ECO:0000256|ARBA:ARBA00010135}.
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DR   EMBL; KN714695; KUI57020.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A194UZA1; -.
DR   STRING; 694573.A0A194UZA1; -.
DR   OrthoDB; 7775at2759; -.
DR   Proteomes; UP000078576; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0030276; F:clathrin binding; IEA:InterPro.
DR   GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR   GO; GO:0006897; P:endocytosis; IEA:InterPro.
DR   CDD; cd17007; ANTH_N_Sla2p; 1.
DR   Gene3D; 1.25.40.90; -; 1.
DR   Gene3D; 1.20.1410.10; I/LWEQ domain; 1.
DR   InterPro; IPR011417; ANTH_dom.
DR   InterPro; IPR013809; ENTH.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR035964; I/LWEQ_dom_sf.
DR   InterPro; IPR002558; ILWEQ_dom.
DR   InterPro; IPR030224; Sla2_fam.
DR   PANTHER; PTHR10407; HUNTINGTIN INTERACTING PROTEIN 1; 1.
DR   PANTHER; PTHR10407:SF15; HUNTINGTIN INTERACTING PROTEIN 1; 1.
DR   Pfam; PF07651; ANTH; 1.
DR   Pfam; PF01608; I_LWEQ; 1.
DR   SMART; SM00273; ENTH; 1.
DR   SMART; SM00307; ILWEQ; 1.
DR   SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR   SUPFAM; SSF109885; I/LWEQ domain; 1.
DR   PROSITE; PS50942; ENTH; 1.
DR   PROSITE; PS50945; I_LWEQ; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078576}.
FT   DOMAIN          3..132
FT                   /note="ENTH"
FT                   /evidence="ECO:0000259|PROSITE:PS50942"
FT   DOMAIN          803..1036
FT                   /note="I/LWEQ"
FT                   /evidence="ECO:0000259|PROSITE:PS50945"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          262..300
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          301..614
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..300
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1036 AA;  117116 MW;  20B8B66FC6605F32 CRC64;
     MASHTKSETD LSINIRKATN PDETAPKRKH VRSCIVYTWD HKSGHSFWAA LKVQPILADE
     VQTFKALIMV HKVLQEGHPN VIREALANRG WIESLNRGMA GEGMRGYGAL IQEYVYFLLA
     KLSFHSQHPE FNGTFEYEEY LSLKAINDPN EGYETITDLM TLQDKIDQFQ KLIFSHFRNV
     GSNECRISAL VPLVAESYGI YKFITSMLRA MHSMTGDTEA LEPLRTRYDA QHHRLVKFYY
     ECSNLRYLTS LITIPKLPQD PPNLLAEDEN APKLPARPKQ EIERAPTPPR QPKTEEPDEI
     SEFWKNELER QNREYEEQQR VLEAQQLAQQ QAQQQAALQA QREFEEQQRQ LAEQQRMQHE
     ALMAQQAQSF TQGRLAELEQ ENLNARAQYE RDQLMLQQYD QRVRALEGEL QQLQANYGQQ
     IGSKDDQIRA LQEQVNTWRT KYEALAKLYS QLRHEHLDLL QKFKSVQLKA ASAQEAIDRR
     EKLEREIKTK NLELADMIRE RDRALHDKDR LTGSNKDELE KLKRELRMAH DRADNLERSK
     GNELSTMLAK YNREMADLEE ALRNKNRALE EAQAKVRDGS SDLEQLLRDK EEELEVYKAG
     MDQALVELNE LKQNQGDTDQ VIDGQIDALI MANLDKINEI IDSVLQSGVA RVDDAIYELD
     STMQAGNQNA SPSYVLSQIE KASSSAMEFA TAFNNFIADG PNAAYGELIK AINVYSSSMA
     DVCNNTKGLT RLATDEKKGE QLMNGARLSA QATVKFFRGL QSFRLEGMDP IQKTDVVINN
     NNEAQMNLQK LNKLVETFAP GFGKLANKGD LGDLVESELS KAADAIAAAA ARLAKLRNKP
     RDGYSTYELK VHDSILDAAL AITDAIARLI KAATATQEEI VQAGRGSSSR QAFYKKNNRW
     TEGLISAAKA VATSTNTLIE TADGVLSGRN SPEQLIVASN DVAASTAQLV AASRVKAGFM
     SNKAVGAACR SLVRQVQAMI KDRQGEEDQV DYSKLGAHEF KVREMEQQVE ILQLENALSA
     ARHRLGEMRK ISYQEE
//
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