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Database: UniProt
Entry: A0A395RZK1_FUSSP
LinkDB: A0A395RZK1_FUSSP
Original site: A0A395RZK1_FUSSP 
ID   A0A395RZK1_FUSSP        Unreviewed;      1054 AA.
AC   A0A395RZK1;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   22-FEB-2023, entry version 16.
DE   SubName: Full=Putative cytoskeleton assembly control sla2 {ECO:0000313|EMBL:RGP65484.1};
GN   ORFNames=FSPOR_7281 {ECO:0000313|EMBL:RGP65484.1};
OS   Fusarium sporotrichioides.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=5514 {ECO:0000313|EMBL:RGP65484.1, ECO:0000313|Proteomes:UP000266152};
RN   [1] {ECO:0000313|EMBL:RGP65484.1, ECO:0000313|Proteomes:UP000266152}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 3299 {ECO:0000313|EMBL:RGP65484.1,
RC   ECO:0000313|Proteomes:UP000266152};
RX   PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA   Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA   Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA   Busman M., Gutierrez S.;
RT   "Evolution of structural diversity of trichothecenes, a family of toxins
RT   produced by plant pathogenic and entomopathogenic fungi.";
RL   PLoS Pathog. 14:e1006946-e1006946(2018).
CC   -!- SIMILARITY: Belongs to the SLA2 family.
CC       {ECO:0000256|ARBA:ARBA00010135}.
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:RGP65484.1}.
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DR   EMBL; PXOF01000101; RGP65484.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395RZK1; -.
DR   STRING; 5514.A0A395RZK1; -.
DR   Proteomes; UP000266152; 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   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; SSF89009; GAT-like 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:UP000266152}.
FT   DOMAIN          9..140
FT                   /note="ENTH"
FT                   /evidence="ECO:0000259|PROSITE:PS50942"
FT   DOMAIN          812..1054
FT                   /note="I/LWEQ"
FT                   /evidence="ECO:0000259|PROSITE:PS50945"
FT   REGION          270..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          309..608
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1013..1040
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        280..307
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1054 AA;  118994 MW;  FD0F7309ABC8CE2E CRC64;
     MSAAVRGTEH TKSDQELAIN IKKATNAEEI SPKRKHVRAC IVYTWDHRSS AAFWSGIKVQ
     PILADEVQTF KALITIHKVL QEGHPSALKE AMANRAWIDS LNRGMGGGGE GMRGYAPLIR
     EYVYYLLAKL SFHHQHPEFN GTFEYEEYLS LKAINDPNEG YETISDLMVL QDKIEQFQKL
     IFSHFRNVGN NECRIAALVP LVQESYGIYK FITSMLRAMH STTGDDEALE PLRERYNAQH
     YRLVKFYYEC SNLRYLTSLI TIPKLPQDPP NLLAEDDDAP ALPARPKQEI ERKPSPLPEP
     KNDAPDEMNE FWKSELDRQN REYEEQQRIL EQQQQQALMA QQQAQMQAQR EFEQQQQQLM
     EQQQREQEAL MAQQAQWQTQ GRLAELEREN LNARAQYERD QLMLQQYDQR VKALEGELSH
     IQNSLGQQMN SKDDQIRALQ EQVNTWRTKY EALAKLYSQL RHEHLDLLQK FKAVQLKAAS
     AQEAIDRREK LEREIKTKNL ELADMIRERD RALHDKDRAS GSSKDEVEKL KRELRLAQDK
     ADNLERSKGN ELSTMLAKYN REMADLEEAL RNKSRQLEDA QMNVRDGSSD LEQLLRDKEE
     ELEVYKAGMD QTLIELNELK MNQGDTDNAL DGQIDALIMS NLDKINDIID SVLQAGVARV
     DDALYELDSN MQAGNQNASP SYVLSQIEKA SASAMEFATS FNNFIADGPN ATHSDLIKAI
     NVFSGAIADV CSNTKGLTRL ATDDKKTDSL MNGTRQPAIS AVQFLRGLQS FRLEGMDPLQ
     KTDVVINNNN DVQMNLQKLN KLVETFAPGF GQLANKKGDL GDLVDSELSK AADAIAAAAA
     RLAKLRNKPR DGYSTYELKV NDSILDAATA ITNAITQLIQ AATVTQQEIV QAGRGSTSRT
     AFYKKNNRWT EGLISAAKAV ASSTNTLIET ADGVISGRNS PEQLIVASND VAASTAQLVA
     ASRVKAGFMS KSQEKLEQAS KAVGAACRAL VRQVQSLIKE RSQEDDQVDY TKLGAHEFKV
     REMEQQVEIL QLENALASAR HRLGEMRKIS YQEE
//
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