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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//