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Database: UniProt
Entry: A0A165I5E3_9BASI
LinkDB: A0A165I5E3_9BASI
Original site: A0A165I5E3_9BASI 
ID   A0A165I5E3_9BASI        Unreviewed;       945 AA.
AC   A0A165I5E3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Ankyrin {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CALCODRAFT_429802 {ECO:0000313|EMBL:KZT60153.1};
OS   Calocera cornea HHB12733.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC   Dacrymycetales; Dacrymycetaceae; Calocera.
OX   NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT60153.1, ECO:0000313|Proteomes:UP000076842};
RN   [1] {ECO:0000313|EMBL:KZT60153.1, ECO:0000313|Proteomes:UP000076842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12733 {ECO:0000313|EMBL:KZT60153.1,
RC   ECO:0000313|Proteomes:UP000076842};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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DR   EMBL; KV423933; KZT60153.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165I5E3; -.
DR   STRING; 1353952.A0A165I5E3; -.
DR   InParanoid; A0A165I5E3; -.
DR   OrthoDB; 38671at2759; -.
DR   Proteomes; UP000076842; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd16489; mRING-CH-C4HC2H_ZNRF; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR24171; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 39-RELATED; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF13857; Ank_5; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00248; ANK; 4.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00184; RING; 2.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 3.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
DR   PROSITE; PS50178; ZF_FYVE; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076842};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   REPEAT          116..138
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          150..173
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          186..218
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          232..265
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          733..805
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   DOMAIN          901..941
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          623..674
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          713..733
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..60
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        626..642
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        651..674
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   945 AA;  103424 MW;  BD8C4535A42D243D CRC64;
     MSTHLRPNSE EDEDSEEEFV YPGAADPGPP YAPEPPEEEE EDSDEEFVYP RPRDDEPAEA
     PGPSAKPSTA LLESLAAAAA SGDLTTLQQL CAAAYEAGGS EKFSAFALAN DAAPRTGLTA
     LHAAASRGRL EVVRWLIEEC GAMVDFEDKE GETALHKAAL NGHLPVVIYL ISNMKSPADV
     HAQDADGWTA MHNACSKGYL DIVRWLCEQG GAADVVSDDD SRVRRVDRKS KGGWTPLMNA
     ASKGHLPVVL YLVTKQAANP LIRNNWGETA YDAAAAVFEV WICEILQKAE AERWQGSSSP
     YDPIAVHTTI PLVIYENQRL DTRLKTLAVN GGRPKFSASG LGKKGRRAPF ELTVYPPEDG
     PERIAAWRSD VQLPLLDDPF NVKRVNAKGD AATPREGSER SFFWLSDWTL DLTPPKCDAT
     EGWQYARHLD DPDDQWSSEV PPQLERVLSG AGLMTSGLMG ASTSRTNGSP DATSGIWCRR
     RRWVRVMRRR LDIPPLPYLE PDGSLYLLQP DGSLTPYLSE YDETGGSEGG QEMGSMPQTF
     LSSAQDYLSR ARYLAGSQHA RKPAMPSAAD VRRSIGKLQR AVSELRTGLL NDEDPQRRAE
     ADALLTRYGR ELDRIRLQAG ADGLMTVGED EEEQDDDDDD SDDSFHYPVH RSSSPALTQS
     TARPPSVRSH STGVDYFNLR ASGSSSRTAA DLTPDLSQAP EFRVPTHDAP QKVVTPRWNA
     PQPHSLQPTW EPDSDAVECR NCHRRFGFLL RKHHCRRCGH IFCDRCSAHR VSLDPSEVIL
     DPSMSMPALP EAQHRVCQSC YEERAANASV PGQLRTGLNG IVIDSERLSV PGISRDSSSV
     VSDLTECPVC NQNLADLGSA ADQEAHVKNC LEGNTGGGVQ NSARYLVYRL PAESALIGSE
     CVICLEEFAK GSTVARLSCL CTFHNACLSA WLQRGRACPV HARDT
//
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