ID A0A319CPW3_9EURO Unreviewed; 1043 AA.
AC A0A319CPW3;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Cytoskeleton assembly control protein Sla2 {ECO:0000313|EMBL:PYH80793.1};
GN ORFNames=BO82DRAFT_337681 {ECO:0000313|EMBL:PYH80793.1};
OS Aspergillus uvarum CBS 121591.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448315 {ECO:0000313|EMBL:PYH80793.1, ECO:0000313|Proteomes:UP000248340};
RN [1] {ECO:0000313|EMBL:PYH80793.1, ECO:0000313|Proteomes:UP000248340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121591 {ECO:0000313|EMBL:PYH80793.1,
RC ECO:0000313|Proteomes:UP000248340};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004287};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004287};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the SLA2 family.
CC {ECO:0000256|ARBA:ARBA00010135}.
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DR EMBL; KZ821707; PYH80793.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319CPW3; -.
DR STRING; 1448315.A0A319CPW3; -.
DR VEuPathDB; FungiDB:BO82DRAFT_337681; -.
DR OrthoDB; 7775at2759; -.
DR Proteomes; UP000248340; 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 Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000248340}.
FT DOMAIN 1..129
FT /note="ENTH"
FT /evidence="ECO:0000259|PROSITE:PS50942"
FT DOMAIN 800..1043
FT /note="I/LWEQ"
FT /evidence="ECO:0000259|PROSITE:PS50945"
FT REGION 255..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 298..572
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1002..1038
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 260..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1043 AA; 118657 MW; 4B360072C2119C63 CRC64;
MSRTEADLAI NIRKATSIEE TAPKRKHVRS CIVYTWDHKS SAAFWAGMKV QPVLADEVQT
FKALITIHKV LQEGHPIVIR EAQQHANWID SLMRGVGGEG IRGYGPLIRE YVYFLESKLA
FHRNHPEFNG LFEYEEYISL KTINDPNEGY ETISDLMTLQ DQIDAFQKLI FSHFQSGTNN
ECRISALVPL VQESYGIYKF ITSMLRAMHT TTGDHDALEP LRGRYDAQHY RLVRFYYECS
NLRYLTSLIT VPKLPQDPPN LLSEDDDRPA LPRRPAKEAE PEPTPPPKPV AADPEPINDF
WTTEAKRQQE EYEAEQRRLQ QQWEEQQRQQ LLAQQQAQQD FEEQQRLQAE QQRLAHEQLL
RDQYQTQTQG RLAELEQENL NARAQYERDQ LMLQQYDRRV KDLEEQMNQL TANLNLQNAS
KDDQIRSLQE QVNTWRSKYE ALAKLYSQLR QEHLDLLQTT KSLKLKAASA QEAIERREKL
ERELKTKNLE LADMIRERDR ALHDRDRLTG NNKEELEKLK RELRMALDRA ENAERSKGTE
ISTLLSKYNR EMADLEESLR KKTRALEEYS SRNSERDGDH ELVLREKDEE IEVYKSGMEQ
ALMELEELKL SQGDVDTALD TQIDQVLHGT VAKINDIIDS VLQTGVQRVD DALYEVDSTM
QAGNQNASPP YVLSQIEKAS ASATEFSTAF NNFIADGPNS THAEIIRTVS IFSGSIADVL
SNTKGLTRLA KDDKNADQLL NAARKSAQAT VRFFRGLQSF RLEGLEALQK TDVVINNNLE
VQRDLQALSK LVDVFAPKSA RITTNGDLGD LVDQELLKAA DAIDAAAQRL AKLKKKPRDG
YTTYELRIND VILEAAIAVT SAIAELIKAA TESQQEIVRE GRGSSSRTAF YKKNNRWTEG
LISAAKAVAN STNTLIETAD GVISGRNSPE QLIVASNDVA ASTAQLVAAS RVKASFMSKT
QDRLESASKA VGAACRALVR QVQSIIKEKN QEDNEAVDYS KLGSHEFKVR EMEQQVEILQ
LENSLARARQ RLGEMRKISY QEE
//
