SSD1_CANAL
ID SSD1_CANAL Reviewed; 1274 AA.
AC Q5AK62; A0A1D8PP12; Q5AKM5;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Virulence protein SSD1;
GN Name=SSD1; OrderedLocusNames=CAALFM_C504730CA;
GN ORFNames=CaO19.11441, CaO19.3959;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP FUNCTION, AND INDUCTION.
RX PubMed=9846729; DOI=10.1099/00221287-144-11-2941;
RA Chen C.Y., Rosamond J.;
RT "Candida albicans SSD1 can suppress multiple mutations in Saccharomyces
RT cerevisiae.";
RL Microbiology 144:2941-2950(1998).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18515753; DOI=10.1128/ec.00402-07;
RA Gank K.D., Yeaman M.R., Kojima S., Yount N.Y., Park H., Edwards J.E. Jr.,
RA Filler S.G., Fu Y.;
RT "SSD1 is integral to host defense peptide resistance in Candida albicans.";
RL Eukaryot. Cell 7:1318-1327(2008).
RN [6]
RP FUNCTION.
RX PubMed=23314964; DOI=10.1128/ec.00285-12;
RA Jung S.I., Finkel J.S., Solis N.V., Chaili S., Mitchell A.P., Yeaman M.R.,
RA Filler S.G.;
RT "Bcr1 functions downstream of Ssd1 to mediate antimicrobial peptide
RT resistance in Candida albicans.";
RL Eukaryot. Cell 12:411-419(2013).
CC -!- FUNCTION: Plays a role in resistance to host antimicrobial peptides
CC such as protamine, RP-1, or human beta-defensin-2; allowing
CC colonization of human tissues. Required for resistance to membrane
CC permeabilization and maintenance of mitochondrial membrane potential
CC upon exposure to RP-1. {ECO:0000269|PubMed:18515753,
CC ECO:0000269|PubMed:23314964, ECO:0000269|PubMed:9846729}.
CC -!- INDUCTION: Constitutively expressed and not cell-cycle regulated like
CC its S.cerevisiae ortholog. {ECO:0000269|PubMed:9846729}.
CC -!- DISRUPTION PHENOTYPE: Decreases virulence in murine infection models.
CC {ECO:0000269|PubMed:18515753}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. {ECO:0000305}.
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DR EMBL; CP017627; AOW29879.1; -; Genomic_DNA.
DR RefSeq; XP_721868.2; XM_716775.2.
DR AlphaFoldDB; Q5AK62; -.
DR SMR; Q5AK62; -.
DR BioGRID; 1219452; 2.
DR STRING; 237561.Q5AK62; -.
DR PRIDE; Q5AK62; -.
DR GeneID; 3636520; -.
DR KEGG; cal:CAALFM_C504730CA; -.
DR CGD; CAL0000187484; SSD1.
DR VEuPathDB; FungiDB:C5_04730C_A; -.
DR eggNOG; KOG2102; Eukaryota.
DR HOGENOM; CLU_002333_0_3_1; -.
DR InParanoid; Q5AK62; -.
DR OMA; SLCKVQD; -.
DR OrthoDB; 1104619at2759; -.
DR PRO; PR:Q5AK62; -.
DR Proteomes; UP000000559; Chromosome 5.
DR GO; GO:0000178; C:exosome (RNase complex); IBA:GO_Central.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006402; P:mRNA catabolic process; IBA:GO_Central.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR041505; Dis3_CSD2.
DR InterPro; IPR041093; Dis3l2_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR001900; RNase_II/R.
DR Pfam; PF17877; Dis3l2_C_term; 1.
DR Pfam; PF17849; OB_Dis3; 1.
DR Pfam; PF00773; RNB; 1.
DR SMART; SM00955; RNB; 1.
DR SUPFAM; SSF50249; SSF50249; 2.
PE 2: Evidence at transcript level;
KW Reference proteome; Virulence.
FT CHAIN 1..1274
FT /note="Virulence protein SSD1"
FT /id="PRO_0000424599"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1174..1217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1274 AA; 141280 MW; 74146377AB95E932 CRC64;
MSSSQDYNNN SNNTPARVSS RKGKNLHVAH RRSPSELTNL MVEQYNLQRQ LEEVQAQQKL
LEEKQKQQQQ QFTYPSAQGS SELAPPPISS GYGGNRSSHS RSSSINTHRR TGSGSGGTAH
GHSRRHSLGL NEAIKAAANQ KQSNRNSLSP TIPNEAKTDS SDDIGSFKFP PSGGDQGDTS
GQSSSSHNRS RSLAYGQQSF KFPPTPDQSN DTRGNSLLPP NPNFSVTQSP DRGHNRRSSH
FRTGSRGSGS NTNTDGINSN WRAQQQSPQQ QQRQGGLLEP PQVGFTPGHK PRNSSYGGGS
SVSSLQQFLP NNGGSNNSGQ QGGHQGGGNN GRKTLFAPYL PQSSLPELIN EGRLVTGTLR
VNKKNRSDAY VSTDGLLDAD IFICGSKDRN RALEGDLVAV ELLIVDEVWE SKKEKEEKKR
RKDNTLHSRP LTDDIHNDAT SAPNTAEGSV TGTSKEDGAG SNEEETGGLA RRGSLKQRPT
MKKNDDVEVE GQSLLLVEEE EINDEIKPLY AGHVVAVVDR IPGQLFAGTL GLLRPAQAAQ
AARDKKNGKE STVQNPKAPK IVWFKPTDKK VPLIAIPTEQ APKDFVENHE KYADRLFVAS
IKRWPITSLH PFGTLVSNLG PIDSPETEID SILRDNNFLC DEYPDDDNDD IVSVNAYDLP
SIEPEFENTQ REEYLNDYII AFTQNGEFVD HALHVKRISN TKIELGFHVA DIAYFIKPGS
SLDRKSKKRS SSVFLPQKTV NLFPKQVNKI VSFKENEKNL AVSVVFEIDT SNFEVEDLYI
HESVIVPKQL VTYDAFDTIL SGQSVDSISS ATSDYVKTFS LIAKEFRRHR LSNRSLGITP
NLTLLDQLDD EKVRLDLNIF KDSLAFDVIS EISHKVNSAI AAKVHAGLGD QAILRRHPLP
TLQKMETFVR KATSLGFKID TTTSSTLQNS ILKIDDPVKR KCVETLLYKC MSRGRYYVAG
KQDTDSYAHY YFNLPLYTHF TAPLRRYADL IVHRQLKAVL NKQVEDKDLD SLKAITDYCN
FKKDCAANAQ EQAIHLLLSQ TINEMSETAG QLLCMGTVVQ VYESSFDVFI PEFGVEKRVH
GDQLPLVKAE FDKNERILEL WWEKGVDSAT YIPPDEKSSL SYRNSIKNKY RTSALQAAKI
QSKTALEKST TPADSVAEKL AKLNLEPPKL VVPSLKSNEL HEVEKDETKS MPSSPTQSEI
PKNVRTNSSS RISSSGNTFS LEPYLQNTIT RIEGDSYIQV IKELTQVPVL LRAEIGMALP
CLTVRVLNPF AEEQ
