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Database: UniProt
Entry: A0A0G2GJN2_9EURO
LinkDB: A0A0G2GJN2_9EURO
Original site: A0A0G2GJN2_9EURO 
ID   A0A0G2GJN2_9EURO        Unreviewed;      1275 AA.
AC   A0A0G2GJN2;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Putative 20s cyclosome subunit (Cut9 cdc16) {ECO:0000313|EMBL:KKY23713.1};
GN   ORFNames=UCRPC4_g02811 {ECO:0000313|EMBL:KKY23713.1};
OS   Phaeomoniella chlamydospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Phaeomoniellales; Phaeomoniellaceae; Phaeomoniella.
OX   NCBI_TaxID=158046 {ECO:0000313|EMBL:KKY23713.1, ECO:0000313|Proteomes:UP000053317};
RN   [1] {ECO:0000313|EMBL:KKY23713.1, ECO:0000313|Proteomes:UP000053317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY23713.1};
RA   Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT   "Distinctive expansion of gene families associated with plant cell wall
RT   degradation and secondary metabolism in the genomes of grapevine trunk
RT   pathogens.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY23713.1, ECO:0000313|Proteomes:UP000053317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY23713.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKY23713.1}.
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DR   EMBL; LCWF01000065; KKY23713.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2GJN2; -.
DR   OrthoDB; 1215698at2759; -.
DR   Proteomes; UP000053317; Unassembled WGS sequence.
DR   GO; GO:0005680; C:anaphase-promoting complex; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR12558; CELL DIVISION CYCLE 16,23,27; 1.
DR   PANTHER; PTHR12558:SF9; CELL DIVISION CYCLE PROTEIN 16 HOMOLOG; 1.
DR   Pfam; PF12895; ANAPC3; 1.
DR   Pfam; PF13374; TPR_10; 1.
DR   Pfam; PF13432; TPR_16; 1.
DR   Pfam; PF13181; TPR_8; 1.
DR   SMART; SM00028; TPR; 7.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF48452; TPR-like; 2.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS50005; TPR; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000053317};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT   DOMAIN          1..197
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REPEAT          467..500
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REGION          895..945
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1053..1080
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        898..931
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1062..1080
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1275 AA;  141144 MW;  EDED85EFF19C1DDE CRC64;
     MISAKDIATF QQWAERENTE PSARKIDGDH IIYLSQRFRR SRDISAIGVP ILSDFGEARV
     GDVQDGIIQP NLYRAPEVLL GMKWTSKVDI WNVGTLCTRG NAERISEYLK YPGFTMASIQ
     NFMRKWRQDA LDKSQYESAI YIGDKVYALT NDPSDAFWLA QVHFSSENYT RALALLLGTD
     LIDRSPACRY LAGHCYIKQN KYEQALSTLG EHNPTHLISS SHNSRRKLQH VNGNTTRHVT
     LRNGKVAQRS DRYDRSEERD QFDASMLKYE ATMCYLRGLC YAKRNAFDRA RDCYKDAVRI
     DVQCFEAFDQ LMKNSLMSPA EELDFLETLD FDSINVSDDP SASQEAAHFT KLLYTTRLSK
     YASPTALSHA TETLSTHYNL ANNPDLLLSR AETLFTQCRF PEALAITTSI FNSQNDSALS
     SSSSIATHIG HNPTLYPLHL ACLYETNSIN TLFLLSHTLA DNAPDEPYTY LAIGVYYLSI
     GKIAEARRFF SKSSLMDPHS AAAWIGFAHT FAAEGEHDQA IAAYSTAARL FQGSHLPQLF
     LGMQHLALNN MSLAHEYLSA AHAMSSGSLR SNLPFDAAKD SLGGDPLVLN ELGVILYHQS
     NLPAAIKLFQ QSLVLATQLA CSPIAWIATR ANLAHALRRL GRYDESLTEF DECLRIASGG
     STISHFAGGH GPFFGMGPTA TGGGNSAVSG YEDRNLTGSI HTSKGLVLLS LGRPREAVVT
     LHEAVRLLGG DASGGGIAGT LLNRAVEMWA LDERSDREHD TYQSFRQPEG ANMDVDADEG
     LTREAAMDAA ADNMLAKVLG RRGIKAKRNP TMARGLEERE ETPIADESGI QQWDMGAALS
     SPPEAPPNDS SLMEGSEASM AGRLIEGFLE MGEFLDAEED LSDSPKDYRP AIEIDYASSS
     GHSESVSLRR STSDHSASIP QNGNGQVSPL TQRGKARRLG QKTKAKTKQF LGLTLPSFKD
     ESSPTKLATR MVEQDPAFNP DQTLSNSPPN VKRTSIANVK DLAKDTVAAT MHPVSTTRSA
     LKGKAAKKIA RAQRPFLTSE DDRELLQAHD DLATSTSHSV DDRSSLEAET NSLKEKRDRV
     EAIESHRESL RTAWAVGRHV DRVLEKRAYL QQMEVDHTIS KKAGAWGRIE ERSSAANPLS
     TDGHVESLDP AASDLVQEVF KFRVWDEGKP SNLLISRKSV SLRRMRTVAW VVHYQRLVEL
     RKEEEKAATT SQAMTMGHAR YSLCLECSSE DGGVTQRRFD VSHDQRDEIF NVIIGWSGLH
     WKSFRAANRY KGAKI
//
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