ID   A0A1X2IMR2_9FUNG        Unreviewed;      1042 AA.
AC   A0A1X2IMR2;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   22-FEB-2023, entry version 19.
DE   SubName: Full=Cytoskeleton assembly control protein {ECO:0000313|EMBL:ORZ19052.1};
GN   ORFNames=BCR42DRAFT_490326 {ECO:0000313|EMBL:ORZ19052.1};
OS   Absidia repens.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX   NCBI_TaxID=90262 {ECO:0000313|EMBL:ORZ19052.1, ECO:0000313|Proteomes:UP000193560};
RN   [1] {ECO:0000313|EMBL:ORZ19052.1, ECO:0000313|Proteomes:UP000193560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 1336 {ECO:0000313|EMBL:ORZ19052.1,
RC   ECO:0000313|Proteomes:UP000193560};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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:ORZ19052.1}.
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DR   EMBL; MCGE01000008; ORZ19052.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X2IMR2; -.
DR   STRING; 90262.A0A1X2IMR2; -.
DR   OrthoDB; 7775at2759; -.
DR   Proteomes; UP000193560; 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:UP000193560}.
FT   DOMAIN          5..134
FT                   /note="ENTH"
FT                   /evidence="ECO:0000259|PROSITE:PS50942"
FT   DOMAIN          797..1039
FT                   /note="I/LWEQ"
FT                   /evidence="ECO:0000259|PROSITE:PS50945"
FT   REGION          265..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          955..986
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        306..321
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1042 AA;  119159 MW;  7B64CB757A6E0A75 CRC64;
     MSYLSAEKAE SELAQSIKKA TSIEETAPKQ KHVRKCIVYT WDHRTSAIIW NILKVQPVLS
     DEVQTFKSLI TVHKIIKDGH PNVIKDALRE TGWLETCARS VSGEGVRGYG TLIRQYVDLL
     LHKLQYHRGH PEFNGTFDYE EYISLKNIDD PNEGFETIND LMVLQDRIDR FQKVVFASFR
     MHSNNECRIA SLVPLVEESY GIYKFITSML RAMHKRTDAA DALQPLRQKF NTQHYNLLKF
     YYECSNLRYL TSLIKVPNLS PDPPSLIDAA TPTLPKRPEP ESVPVAQPSP EPVIDFWSEQ
     QAQQQREYED QQKRLAQQQA DEQERMRQQQ LQQQRDFEEQ QRLLAERERM QQEELLRQQM
     QNQQAGRIND LEMQLLNYRN QLERDQMLLE QYDRRVKALE QELQLINTNA QQRDASKDEL
     IRSLQNEIQM WKNKYEALAK LYSQLRKEHI DLLNKYKQLQ VKANSAQEAT EKLERMQADM
     RAKNTELADL IRERDRARNE LARLQGNQRD DMERLQRELD ESRSELQRIG KSKGDEVSTL
     LMKFNREKAD LEASLNEKQA LIDEFLRQLE DQQGDADHIR REKDEEIAVL QAGMDECLAQ
     LAALQQNDKQ ADLQEELELL ETQQTDKLNQ ILDSILSICI QKINDGVYEL ETPGQHGNEN
     ATPELTLSMI ERASITSVEF MSAFSKFLDG SNSGDHTSTI TRALNFADTI NDVLIHGKGI
     TRLVIDDEDI DEIIKLARQS AEACIQYFSS VMSTYLNMLP RAQRPEVVIQ GDMRVQEALM
     KLSTKTEDLI LTGATDINKL AEGEVGDLVE QEMSNAARAI EEATAKIQAL MRRPANPEFS
     ATDIQVNELI LNSVLALTNA IANLIKCATA SQQEIVAQGR GSSSKAAFYK KHNRWTEGLI
     SAAKAVAMAT NLLVEAADGV ISKTHSLEQL IVASNEVSAA TAQLVAASRV KSTFMSRTQE
     RLEIAAKAVK DAAAELVKQV KNLVAQKSEN LDIDFNKLSV HEFKRREMEQ QVKILKLDSE
     LVNARRILAE MRRSGYHTEE TD
//