ID A0A075AYI1_9FUNG Unreviewed; 1042 AA. AC A0A075AYI1; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 12-APR-2017, entry version 11. 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). CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KE560848; EPZ35342.1; -; Genomic_DNA. DR EnsemblFungi; EPZ35342; EPZ35342; O9G_000738. DR Proteomes; UP000030755; Unassembled WGS sequence. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0003993; F:acid phosphatase activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR Gene3D; 3.30.470.20; -; 1. DR Gene3D; 3.40.30.10; -; 1. DR Gene3D; 3.40.50.1240; -; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013651; ATP-grasp_RimK-type. DR InterPro; IPR013816; ATP_grasp_subdomain_2. 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 Complete proteome {ECO:0000313|Proteomes:UP000030755}; 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 //