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Database: UniProt
Entry: B8MSF5_TALSN
LinkDB: B8MSF5_TALSN
Original site: B8MSF5_TALSN 
ID   B8MSF5_TALSN            Unreviewed;      1180 AA.
AC   B8MSF5;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=Ankyrin repeat-containing protein, putative {ECO:0000313|EMBL:EED11950.1};
GN   ORFNames=TSTA_000280 {ECO:0000313|EMBL:EED11950.1};
OS   Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS   1006) (Penicillium stipitatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441959 {ECO:0000313|EMBL:EED11950.1, ECO:0000313|Proteomes:UP000001745};
RN   [1] {ECO:0000313|Proteomes:UP000001745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC   {ECO:0000313|Proteomes:UP000001745};
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
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DR   EMBL; EQ962660; EED11950.1; -; Genomic_DNA.
DR   RefSeq; XP_002487604.1; XM_002487559.1.
DR   AlphaFoldDB; B8MSF5; -.
DR   STRING; 441959.B8MSF5; -.
DR   GeneID; 8107456; -.
DR   VEuPathDB; FungiDB:TSTA_000280; -.
DR   eggNOG; KOG0502; Eukaryota.
DR   HOGENOM; CLU_000288_34_2_1; -.
DR   InParanoid; B8MSF5; -.
DR   OMA; ACYRGHD; -.
DR   OrthoDB; 2166716at2759; -.
DR   PhylomeDB; B8MSF5; -.
DR   Proteomes; UP000001745; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 4.
DR   Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR46082:SF11; AAA+ ATPASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR46082; ATP/GTP-BINDING PROTEIN-RELATED; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 4.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 10.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 7.
DR   PROSITE; PS50088; ANK_REPEAT; 8.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001745}.
FT   REPEAT          872..904
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          905..937
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          938..970
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          971..1003
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1004..1036
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1037..1069
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1102..1134
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1135..1167
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
SQ   SEQUENCE   1180 AA;  132232 MW;  6DD2BA2F7C5FFAC9 CRC64;
     MAGQQYAHED YTVGWICALP KTELVAAAAM LDEEYLILPA TDPQDANTYL LGRIGDHNVV
     IACLPAEMTG KVSAATVATD MIRSFPSIRF GLMVGIGGGA PRRAYPEQGT GGGLVEDDFD
     ESEDEMEEIP DIRLGDVVVC LHTKSAEAVV QYDFGKSLQE KEFVHTGGKL NKPPRIVLNA
     VGRLQANHIR GHRKIPELLS KMLTENSDMI HFQHPGLEKD RLFRPDVVHV EGRKSCRDCC
     GLNNANIVKR DSRSDTVPKI HYGTIGSADQ VMKDAILRDQ WALKENILCF EMEAAGLMDS
     FPCLVIRGIC DYADSHKNKV WQPYAAATAA AYAKELLLVI PGQGLMKLSP IKQLLHLSEQ
     IEAVNSTLEK TFEQRENHHH DQIMRYATED QRRCHQVFKT STYEKFKNIN PNRVEGTCEW
     VLKSPEYLRW WNATHNDLLW ISADPGCGKS VLAKSLIDEV FALSDLNVLI VYFFFKDNDE
     QNNLATALCA VLHQLFSLQP QLLRHALPFW ERSKEKIQYE VDDMWRIFMA TMSDGTFGNT
     ICVFDALDEC RDHDQKQLIE RLHDFHNRRP ASQENWLKFL VTSRPYDDIQ DRFRPLTECF
     PQIHLRGEEE NDQIHEEINL VVKVKLTELG KDLGLRANTQ ERLERELYEM KHRTYLWLYL
     AIDDIKRTLK NSLRPDRETI PPLPKNVSKA YERILDRVPS DQKTKVETIL RIIIGARRPL
     TVQEMAMALG TAREFLISKH GRSPNVHWHL EQRKTEIQMT EICVKYLVMN DLVSNDGESI
     RSLLDYSAEN WADHFRDVLS PEAELVDWVW KLYDVMTKRF RLWFPKFWTV AMRHRQDPKM
     KALHLAAFNG HPDILCRVDV NKTDAVDQFD RSGTTALQWA CERGHLEIAQ LLLEKGADVN
     AQGGYYGNAL NAAAEGGYLE IVQLLLEKEA DVNTQRVEHS NALQAAARGG YLEIVQLLLE
     KGADVNAQGG YYGNALNAAA RGGYLEIFQL LLEKGADVNT HGIEHGDALQ AAARGGYLEI
     VQLLLEKGAD VNAQGGYHGN ALNAAAKGGY LKIVQLLLAK GADVNIQGGN YGNALYAAAQ
     KGHLEIIQLL LEGADVNAQG GYYGNALNAA AGRGYLETFQ LLLEKGADIN AQGGYYGNAL
     NAAARGGYLE IVQLLLEKGA DAKTHGGEYG NALQAAARGG
//
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