ID A0A395I924_ASPHC Unreviewed; 655 AA.
AC A0A395I924;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=WD-repeat-containing protein slp1 {ECO:0000313|EMBL:RAL16667.1};
GN ORFNames=BO97DRAFT_402325 {ECO:0000313|EMBL:RAL16667.1};
OS Aspergillus homomorphus (strain CBS 101889).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450537 {ECO:0000313|EMBL:RAL16667.1, ECO:0000313|Proteomes:UP000248961};
RN [1] {ECO:0000313|EMBL:RAL16667.1, ECO:0000313|Proteomes:UP000248961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101889 {ECO:0000313|EMBL:RAL16667.1,
RC ECO:0000313|Proteomes:UP000248961};
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 (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the WD repeat CDC20/Fizzy family.
CC {ECO:0000256|ARBA:ARBA00006445}.
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; KZ824268; RAL16667.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395I924; -.
DR STRING; 1450537.A0A395I924; -.
DR VEuPathDB; FungiDB:BO97DRAFT_402325; -.
DR OrthoDB; 20041at2759; -.
DR Proteomes; UP000248961; Unassembled WGS sequence.
DR GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR GO; GO:0010997; F:anaphase-promoting complex binding; IEA:InterPro.
DR GO; GO:0097027; F:ubiquitin-protein transferase activator activity; IEA:InterPro.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR024977; Apc4-like_WD40_dom.
DR InterPro; IPR033010; Cdc20/Fizzy.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR19918; CELL DIVISION CYCLE 20 CDC20 FIZZY -RELATED; 1.
DR PANTHER; PTHR19918:SF68; FI02843P; 1.
DR Pfam; PF12894; ANAPC4_WD40; 1.
DR Pfam; PF00400; WD40; 3.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000248961};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT DOMAIN 377..434
FT /note="Anaphase-promoting complex subunit 4-like WD40"
FT /evidence="ECO:0000259|Pfam:PF12894"
FT REPEAT 385..419
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 461..496
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 592..625
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 655 AA; 71045 MW; C894BE8B9D7B94F6 CRC64;
MATPTVSTPV KTHHGIFSTK TAGGRMPLTP SPRRRDSVAS NHSSPFTPQC GAGESGKEFG
KSVYSGNLSS YFAKSVSKPT RKYCESPKSN LSTSRSYRES PKSNIARTRP RKSPKHLELG
VSEWALTGTG PSSSQTPSKE RLRKEVSRKE VSRKEVPREK VARKEEIRTT RTTRSGKTTV
RIAHNAGDRF IPNRTASEGL VTAGTAKPEE SQRPKSTSSE GSSVLASAAS AFDIGGRGSE
EDLTAALESL GIDDSEPSTS YTKPAPDAVA YESSLADACG VNLNTRILAF KPPPPESSKP
IDLRAQYNRP LKSAKSQSAQ FRRRVQTAPE RVLDAPGLLD DYYLNLLDWS SGNQVAIGLE
RNVYVWSADS GTVSCLLEAP TDTYVSSVKW SGDGAYVGVG LGTGEVQIWD VEEGTKLRSM
FGHDSRVGVM GWSKHTLSTG ARSGLVFNHD VRIAQHKVAE LVSHTSEVCG LEWRPDGAQL
ATGGNDNLVN IWDARSLSAP KFTKTNHRAA VKALSWCPWQ LNLLATGGGS YDRHIHFWNT
TTGARTNSID TGSQVTSLRW SNHYREIVSS SGFPDNSLSI WSYPTLVRNV EIPAHETRVL
HSCLSPDGQL LATAAADESL KFWKIFERKP GTSASASREG GVGSKAQMTK SMTIR
//
