ID   A0A075AYI1_9FUNG        Unreviewed;      1042 AA.
AC   A0A075AYI1;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   10-MAY-2017, entry version 12.
DE   SubName: Full=Thioredoxin-like fold domain-containing protein {ECO:0000313|EMBL:EPZ35342.1};
GN   ORFNames=O9G_000738 {ECO:0000313|EMBL:EPZ35342.1};
OS   Rozella allomycis CSF55.
OC   Eukaryota; Fungi; Cryptomycota; Rozella.
OX   NCBI_TaxID=988480 {ECO:0000313|EMBL:EPZ35342.1, ECO:0000313|Proteomes:UP000030755};
RN   [1] {ECO:0000313|EMBL:EPZ35342.1, ECO:0000313|Proteomes:UP000030755}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CSF55 {ECO:0000313|EMBL:EPZ35342.1,
RC   ECO:0000313|Proteomes:UP000030755};
RX   PubMed=23932404; DOI=10.1016/j.cub.2013.06.057;
RA   James T.Y., Pelin A., Bonen L., Ahrendt S., Sain D., Corradi N.,
RA   Stajich J.E.;
RT   "Shared signatures of parasitism and phylogenomics unite Cryptomycota
RT   and microsporidia.";
RL   Curr. Biol. 23:1548-1553(2013).
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DR   EMBL; KE560848; EPZ35342.1; -; Genomic_DNA.
DR   EnsemblFungi; EPZ35342; EPZ35342; O9G_000738.
DR   Proteomes; UP000030755; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:EnsemblFungi.
DR   GO; GO:0003993; F:acid phosphatase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0033857; F:diphosphoinositol-pentakisphosphate kinase activity; IEA:EnsemblFungi.
DR   GO; GO:0101012; F:inositol 1,5-bisdiphosphate 2,3,4,6-tetrakisphosphate 1-diphosphatase activity; IEA:EnsemblFungi.
DR   GO; GO:0101011; F:inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate 1-diphosphatase activity; IEA:EnsemblFungi.
DR   GO; GO:0000829; F:inositol heptakisphosphate kinase activity; IEA:EnsemblFungi.
DR   GO; GO:0052723; F:inositol hexakisphosphate 1-kinase activity; IEA:EnsemblFungi.
DR   GO; GO:0052724; F:inositol hexakisphosphate 3-kinase activity; IEA:EnsemblFungi.
DR   GO; GO:0000830; F:inositol hexakisphosphate 4-kinase activity; IEA:EnsemblFungi.
DR   GO; GO:0000831; F:inositol hexakisphosphate 6-kinase activity; IEA:EnsemblFungi.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0006020; P:inositol metabolic process; IEA:EnsemblFungi.
DR   GO; GO:0032958; P:inositol phosphate biosynthetic process; IEA:EnsemblFungi.
DR   GO; GO:0051516; P:regulation of bipolar cell growth; IEA:EnsemblFungi.
DR   GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IEA:EnsemblFungi.
DR   Gene3D; 3.40.50.1240; -; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013651; ATP-grasp_RimK-type.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   Pfam; PF08443; RimK; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   SUPFAM; SSF53254; SSF53254; 3.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Complete proteome {ECO:0000313|Proteomes:UP000030755};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030755}.
FT   DOMAIN      340    549       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   1042 AA;  120389 MW;  DDE1933D5B800656 CRC64;
     MNGMPDMYAQ ALEESILQAA SVVEAQIDEK IRELENADEN SLESIRRQRI QQMKNAALQK
     AHWRSLGHGS YSELLSEKAF FEEGKKSKDL VCHFYRTSTF RCKILDRHLE ALSKAHLEAK
     FVKIDAEKSP FLCERLGVRV LPTLVIVKDR KPVDQIVGFA EIGNNDDFET IALARRIAKS
     GVIRFEENED YSEYGVMMNK NNFYGCVFRS SSLRKLIIGV CAMDTKARSK PMRNILDRIT
     ATSDFEVVIF GDKTILDDPI EEWPQCQFLI SFFSKGFPLQ KAIEYVALRR PFCINDLPLQ
     QLLWDRRWVL SVLDAIDVPT PKRIIVNRDE GPKYYKGVIE ELNKNLGIDL GNMTNFSREN
     VIQIDKDTIM VGKQRLEKPF VEKPVDGEDH NIYIYYPESM GGGVRKLFRK VGNKSSEFFP
     DEWEIRKEGS FIYETFIDVE KAEDIKVYTI GPYYAHAETR KSPVVDGIVR RNTDGKEVRH
     LTDLSEEEQE LARRVSMAFG QTICGFDLVR CGSKSMVIDV NGWSFVKGND NYYDMCAKIM
     SQTFLKIARK RRTTILKEPL NENQWKLKSF ISIFRHADRT PKQKMKFNVS SAPFLDLIVK
     GKEETMIRNP DGLERIEKAA EASLSLGIEE KSKLLQLMEI LSKKKKSPGT KVQIKPSYSK
     SREIEKAQLI VKWGGEFTHA GRHHSKDFGE NLRKDLLLMN RKMIDDVKVY TSSERRVMAT
     ADIFSKALMF VAELPDDFLS IKKEMLDDNF DAKEKLDKIP ENVQFLNVHP EFKNPRVTLD
     EVFITLKDLR QVMRSNFDTL DVDSLSHRWC CAESSILFKE RWEKLFKDFC DVEINNFDPS
     KVSELYDSLK YDALHHREFF ERIFVKNQNC PNEKAALADL IRKAKILFDF IAPQEFGLFP
     EEKVEIGKII ANRLLAQILD DLNEAKIHAT DPCTRLYFTK ESHVHALLNI VRFGGLECSI
     GNWDELDYLT QITFEVYERF KSNTSGFEYS IRIGFSPGAH DSNILDVQID QKHALSVAPR
     RWITEHIPLD HAISIIEKML NK
//