ID F0UCU2_AJEC8 Unreviewed; 1382 AA.
AC F0UCU2;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Cell wall biogenesis protein phosphatase Ssd1 {ECO:0000313|EMBL:EGC43368.1};
GN ORFNames=HCEG_02583 {ECO:0000313|EMBL:EGC43368.1};
OS Ajellomyces capsulatus (strain H88) (Darling's disease fungus) (Histoplasma
OS capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544711 {ECO:0000313|Proteomes:UP000008142};
RN [1] {ECO:0000313|Proteomes:UP000008142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H88 {ECO:0000313|Proteomes:UP000008142};
RA Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Ajellomyces capsulatus strain H88.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; DS990637; EGC43368.1; -; Genomic_DNA.
DR STRING; 544711.F0UCU2; -.
DR VEuPathDB; FungiDB:I7I53_09941; -.
DR HOGENOM; CLU_002333_0_3_1; -.
DR OMA; QIQATHQ; -.
DR Proteomes; UP000008142; Unassembled WGS sequence.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0004540; F:RNA nuclease activity; IEA:InterPro.
DR Gene3D; 2.40.50.690; -; 1.
DR Gene3D; 2.40.50.700; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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 PANTHER; PTHR23355:SF9; DIS3-LIKE EXONUCLEASE 2; 1.
DR PANTHER; PTHR23355; RIBONUCLEASE; 1.
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; Nucleic acid-binding proteins; 3.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000008142}.
FT DOMAIN 756..1089
FT /note="Ribonuclease II/R"
FT /evidence="ECO:0000259|SMART:SM00955"
FT REGION 95..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1198..1320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1089..1116
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 141..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..647
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1223..1241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1252..1273
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1283..1317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1382 AA; 151940 MW; 3E52ABE0973F2997 CRC64;
MDQQGQSIPG PAGRRLHIAH RRSPSELTPL MMEQLALQQQ IELLQQQQQQ IAATHQQYVN
MGLLQPQQPL QHVAAYSPTM QAQAIPSVTH NNFQFPQSQQ QQPQHVSVPL NPQGPPSHRR
NQSALPNVGM GPPPAPSSGA AGSSYDYNQG QGQGHGQGHG SSNHNRENGQ QSRGRGAAPP
GGGHQRRHSL ALPEARKAAE LAQQKRTTSG FQFPIPGASG ASSTSNQGEG SPTEKPPPPA
SSSPQPPQGL GVQRAGNIRS GTHTRSQSLA VGSGRSGGTS GGRGAGGFQF PQSSEGSPAP
DSSSRRQSQP SHGRSGSRNF ESNWRQQNNN QGQGQDQQRT AMGSFGQQQG GANFQPGHRT
RGSVNQSVGS LGSFQYTGQP QLIQLPQGQV VMAPPQMFAG QHLNPIQIAQ LQAMQASGQL
ISKSSLCKPL LSMLPRSCLR SNNNSSSSSN SSNSVKHFLP LPSPGIIACS TERRSTGCRN
RALEGDLVAV ELLDVDEVWS QKREKEEKKK RKDITDTRSG STAGMDKNAR PDSITNGDPG
QIAPDGSIRR RGSLRQRPTQ KKNDDVEVEG QSLLLVEEDE ISDEQKPLYA GHVVAVIERV
AGQMFAGSLG LLRPSSQATK EKQEAERQAR DGGHSRHHHD RQQDKPKIVW FKPTDKRVPL
IAIPTEQAPR DFVEKHAEYA NNIFVACIKR WPITSLHPFG TLVEQLGAMG NLKVETDALL
RDNNFASDEF SDAVLKNVGF EKWSVKDEGE ALLENRRDFR GETTFTIDPN GYKELDDAIH
VKSLPDGKVE VGIHVADVAH FIKSNSLVDR EAKKRGTGVY LMNRVVNMIP PRLATEICSL
LPGEERLTVS VIFQVNSATG SVEGEPWIGK GVIKSSGKLT YDEVDAILNG NSDVELHGAT
ANDIKTLSDI ASKFKKARFG NRSSNIPSLR LLYQLDDENV PVEQNIFNST PAHELIEELS
HKANSFVAKK LLSAIPDKAF LRRQAPPNVR RLQTFVDRMT RLGYDIDPTS SGTLQTSLFK
IEDVDIRKGM ETLLLKAMQR AKYYVAGNMT EDQRQHYVLN LPVYTHFTNP SRRYADIIVH
RQLEAVLSNS ECTDDVENLT KTAEQCNNKK DSAQTAQEQS VHIESCRIMD KKRSEIGGDL
ISEGIVLCVY ESAFDVLIPE YGFEKRVHCD QLPLKKAEFR KEERVLELYW EKGVPSSAYI
PEDERPKAAQ STRAANAAAA AREAEAARER AREREEAQRK QTDTGTISTD DVDALFDDDE
EDDEDEDDDI SEATEMAAGV SLNSPVDRST QSMPPSPTRN GHLQQTPHRT RSDPKIASST
VEAPEAKLTN KEKYLKLFRL REEDGEYIQD VTEMTRVPII LKTDLSKSPP CLTIRSVNPY
AL
//
