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Database: UniProt
Entry: A0A5B1QFB9_9AGAM
LinkDB: A0A5B1QFB9_9AGAM
Original site: A0A5B1QFB9_9AGAM 
ID   A0A5B1QFB9_9AGAM        Unreviewed;      1088 AA.
AC   A0A5B1QFB9;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   28-JUN-2023, entry version 11.
DE   SubName: Full=Cytoskeleton assembly control protein {ECO:0000313|EMBL:KAA1468016.1};
GN   ORFNames=DENSPDRAFT_793676 {ECO:0000313|EMBL:KAA1468016.1};
OS   Dentipellis sp. KUC8613.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Russulales; Hericiaceae; Dentipellis.
OX   NCBI_TaxID=1883078 {ECO:0000313|EMBL:KAA1468016.1, ECO:0000313|Proteomes:UP000322482};
RN   [1] {ECO:0000313|EMBL:KAA1468016.1, ECO:0000313|Proteomes:UP000322482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KUC8613 {ECO:0000313|EMBL:KAA1468016.1,
RC   ECO:0000313|Proteomes:UP000322482};
RX   PubMed=31482283; DOI=.1007/s00253-019-10089-6;
RA   Park H., Min B., Jang Y., Kim J., Lipzen A., Sharma A., Andreopoulos B.,
RA   Johnson J., Riley R., Spatafora J.W., Henrissat B., Kim K.H.,
RA   Grigoriev I.V., Kim J.J., Choi I.G.;
RT   "Comprehensive genomic and transcriptomic analysis of polycyclic aromatic
RT   hydrocarbon degradation by a mycoremediation fungus, Dentipellis sp.
RT   KUC8613.";
RL   Appl. Microbiol. Biotechnol. 103:8145-8155(2019).
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:KAA1468016.1}.
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DR   EMBL; NSJX01000003; KAA1468016.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5B1QFB9; -.
DR   InParanoid; A0A5B1QFB9; -.
DR   Proteomes; UP000322482; 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:UP000322482}.
FT   DOMAIN          27..156
FT                   /note="ENTH"
FT                   /evidence="ECO:0000259|PROSITE:PS50942"
FT   DOMAIN          842..1085
FT                   /note="I/LWEQ"
FT                   /evidence="ECO:0000259|PROSITE:PS50945"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          284..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          321..616
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        300..316
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1088 AA;  123134 MW;  6F60ADDC4D2BA9C2 CRC64;
     MFAGNRTRQT NYDIDGDEVH YPTRPVDKDK AEQELVVNIK KATSPEESAP KQKHVRKCIV
     YTWDYHSSIS FWSGLRVQPI LSDEVQTFKA LITVHKVLQE GHPVTIKEAQ SQTGWLETCA
     RTVGQDSGRG YGSLIRTYVQ FLLAKLRFHR LRPEFNGLFE YEEYVTLKGI DDPNEGYETI
     SDLMSLQDQI ESFQKMVFAH FRHSANNECR ISSLVPLVKE SWGIYRFITS MLRAMHRRAN
     DIEALEPLRQ RYNAQHYSLR KFYYECSNLK YLTGLINVPK LGQEPPNLMD SGGAPDLPAR
     PTTTAPPTPP PVAPTPDAAA VSEQARMLKQ YEDQQAALQA QREAEERRRL EQQQQQQLEF
     EQRQREQAER ERLAQEALVQ QQMQQQMQQY NNQAAQHLQD MEREMLAMRG QYERDQLLLE
     QYDRRVKALE GELSNVSLNV NSQMSSKDDL IKQLQDQVTL WRNKYEALAK LYSQLRTEHL
     DMLSKFKQMQ LKANSAQEAI DRMERMERDL KAKNLELADM IRERDRARFD VDRQKSSHKD
     ELDRLRRELN FANERAEDAS RSKSSEVSSV LAKYNRQMAE LEDSLRAKQI QIDDLLTKLD
     SSADDLERLR EEKDQEIMIL QAGMDSTIQR LSETQQNQGI AEEATNAQID TLILDNRKKL
     NQIIGTFSSA IAHISIDSIL QACVQKVDDA IYELESPTQA GNQNSTPEYT LSMIEKSLSN
     ATDFATIFNL YLDNQPGGDH VDVIKGANEF AQALADTLVN VKGITRLTND DDASDKLISI
     AKAAGDVGLR FFLNLQSYKL ELVDRKQRTA VAMRNNGEVR SALTKLSESV DAMVPKGAKS
     NALAKANGDI GDIVEQEMLG AAQAIEAATA RLQELMARPR DTGRYSAIDL QVHDSILQAA
     MAITSAIARL IKAATDSQQE IVAQGKGSSS TQQFYKRNNR WTEGLISAAR AVAFATNLLI
     ESADGVLSGT HSLEQLIVAS NEVAAATAQL VAASRVKANL MSKTQERLEL AAKAVTEACK
     ALVRQVRAIS AKQVQEEDVD YKNMATMEFK RREMEQQVEI LRLEKDLGAA RHRLGAMRRA
     GYHTDETD
//
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