SIS2_CANTR
ID SIS2_CANTR Reviewed; 531 AA.
AC Q12600;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Protein SIS2;
DE AltName: Full=Halotolerance protein HAL3;
GN Name=SIS2; Synonyms=HAL3;
OS Candida tropicalis (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5482;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NCYC 2512;
RX PubMed=8923737;
RX DOI=10.1002/(sici)1097-0061(199610)12:13<1321::aid-yea27>3.0.co;2-6;
RA Rodriguez P.L., Ali R., Serrano R.;
RT "CtCdc55p and CtHa13p: two putative regulatory proteins from Candida
RT tropicalis with long acidic domains.";
RL Yeast 12:1321-1329(1996).
CC -!- FUNCTION: May stimulate expression of certain genes that are
CC periodically expressed during late G1. Also modulates the expression of
CC the ENA1 ATPase (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HFCD (homooligomeric flavin containing Cys
CC decarboxylase) superfamily. {ECO:0000305}.
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DR EMBL; X88900; CAA61362.1; -; Genomic_DNA.
DR PIR; S57752; S57752.
DR AlphaFoldDB; Q12600; -.
DR SMR; Q12600; -.
DR VEuPathDB; FungiDB:CTMYA2_009710; -.
DR VEuPathDB; FungiDB:CTRG_05660; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR Gene3D; 3.40.50.1950; -; 1.
DR InterPro; IPR036551; Flavin_trans-like.
DR InterPro; IPR003382; Flavoprotein.
DR Pfam; PF02441; Flavoprotein; 1.
DR SUPFAM; SSF52507; SSF52507; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Nucleus.
FT CHAIN 1..531
FT /note="Protein SIS2"
FT /id="PRO_0000182036"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..516
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 531 AA; 58172 MW; D5FF196B8B957B14 CRC64;
MPSDKDIKSP AQPKKEEEIP KSILTRISSP PPILNQPDAN IIHHPQPQVP QSSLNIPGIK
LSPQISTSLE NREIVMAGGA YLKERMESPD SLNHKPTLLQ PDKSESIPSI DYTLNPPKES
QHHKSPSVHA HFYVEETLRP VRNRSRSGSN SNNNLTPITS PQHSEPSSIL NKDAIKSQES
LRATTNSISS AAASNQSTPR SIISGGGGGG GGANTATSSN STTSNTALAA QGTTTTTTTT
NSNSNTTTTK GEQNSNIDPR LPQDDGKFHV LIGVCGALSV GKVKLIVNKL LEIYTSDKIS
IQVILTKSSE NFLLPETLNV LENVKKVRVW TDIDEWTTWK TRLDPVLHIE LRRWADILLV
CPLTANTLAK ISLGICDNLL TNVIRAWNSS YPILLAPAMD SHSYSSSTTK RQLRLIADDM
PWIEVLKPLE KVFGSYGDIG MGGMTDWNEI VNRIVMKLGG YPEDEDEDEA DDSKDNIDES
AIIDDDDDDD DDDDDDDDDD DDDDDDDDDD EEDPPQQQST TDNSKDETTN L