ID H8XAE2_CANO9 Unreviewed; 894 AA.
AC H8XAE2;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Sap185 protein {ECO:0000313|EMBL:CCG25119.1};
GN ORFNames=CORT_0G04420 {ECO:0000313|EMBL:CCG25119.1};
OS Candida orthopsilosis (strain 90-125) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=1136231 {ECO:0000313|EMBL:CCG25119.1, ECO:0000313|Proteomes:UP000005018};
RN [1] {ECO:0000313|EMBL:CCG25119.1, ECO:0000313|Proteomes:UP000005018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=90-125 {ECO:0000313|Proteomes:UP000005018};
RX PubMed=22563396; DOI=10.1371/journal.pone.0035750;
RA Riccombeni A., Vidanes G., Proux-Wera E., Wolfe K.H., Butler G.;
RT "Sequence and analysis of the genome of the pathogenic yeast Candida
RT orthopsilosis.";
RL PLoS ONE 7:e35750-e35750(2012).
CC -!- SIMILARITY: Belongs to the SAPS family.
CC {ECO:0000256|ARBA:ARBA00006180}.
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; HE681725; CCG25119.1; -; Genomic_DNA.
DR RefSeq; XP_003871244.1; XM_003871195.1.
DR AlphaFoldDB; H8XAE2; -.
DR GeneID; 14541871; -.
DR KEGG; cot:CORT_0G04420; -.
DR eggNOG; KOG2073; Eukaryota.
DR HOGENOM; CLU_003676_2_0_1; -.
DR OrthoDB; 5491840at2759; -.
DR Proteomes; UP000005018; Chromosome 7.
DR GO; GO:0019903; F:protein phosphatase binding; IEA:InterPro.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR007587; SAPS.
DR PANTHER; PTHR12634:SF8; FIERY MOUNTAIN, ISOFORM D; 1.
DR PANTHER; PTHR12634; SIT4 YEAST -ASSOCIATING PROTEIN-RELATED; 1.
DR Pfam; PF04499; SAPS; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
PE 3: Inferred from homology;
FT REGION 92..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..159
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..724
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..744
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..759
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..776
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..806
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..869
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 894 AA; 101280 MW; D0E56269F1F48F38 CRC64;
MSGSFWKFSN GFTSLSNITT LLENYNSNQE QNDSSSVNTN KVEEEQRDVL IKLLDENDLL
QELLSNNPML LEFLRDEHVL SMLVDIVISN DSETETSEDK KGAKGKDTVT TPKDASKPSD
SKEEETHEES SSGDKRDEEE PTHQDSGDSD DQDDEAEDES PEDRFRRRAT LASEVLSADV
WSLTDTVMES TENLNKLWSV LDSKDALDIH VSTHFMKIME HLLDMKCDEM ITYLIDNQPN
LVEKFINHLS NPPLMDFLLK LISTDKPDNS TGIIEFLQNQ DLISHLINAL DVSDVPESDT
EKGSKSHELL LIEQSSAADF LKALITISAN STADNSTIGP NELTRELVSK QQMTRLCDIM
LKGGYALANG VGIIIEIIRK NNSDYDILPV LYITLESHPP TGRDPIYLGH LLRVFGERIS
DFNELLIKEH TDSKLRTPFG VIQPLGFERF KICELIAELL HCSNMALLND NKGFDVVKER
DELRTKMKEY DPISFKYNEA ITLPHEDEEN EEINDADETG NSIRDDTIDE FNKQEDTIDE
DEPHANSNLT EEQIRANPVV GDFLKIALFD TQIISNILSM FFRFPWNNFL HNVVFDVVQQ
VLNGSMDIGF NKFLAIDLFH SADITNKIIE GQRLCTDYET SHNGLRLGFM GHLTLIAEEV
VKFVQLFPSN TLSEYINEKI ESDVWEDYVS NVLYDTREKY NAILGGNEDE DDRDEEDNTT
FDEGLGEIIE EVKTGLVFHD DEEREVEEAH DEDTGNGDDE EKSDESKAKD KKDLLDSDES
ESDEDDHFSN YMSQQLANTS NNANQEREES SSEEDEDDKH ITNEGDADDY IDPNDDGMSY
KKSNPLYDSK GELKNAHPEF DKDADDDSDS SSNSSSDEEL DADAPKLTRS ASKN
//