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Database: UniProt
Entry: A0A165IMA7_9BASI
LinkDB: A0A165IMA7_9BASI
Original site: A0A165IMA7_9BASI 
ID   A0A165IMA7_9BASI        Unreviewed;       198 AA.
AC   A0A165IMA7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   25-OCT-2017, entry version 7.
DE   RecName: Full=Translation machinery-associated protein 22 {ECO:0000256|RuleBase:RU361273};
GN   ORFNames=CALCODRAFT_480426 {ECO:0000313|EMBL:KZT60761.1};
OS   Calocera cornea HHB12733.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Dacrymycetes; Dacrymycetales; Dacrymycetaceae; Calocera.
OX   NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT60761.1, ECO:0000313|Proteomes:UP000076842};
RN   [1] {ECO:0000313|EMBL:KZT60761.1, ECO:0000313|Proteomes:UP000076842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12733 {ECO:0000313|EMBL:KZT60761.1,
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.,
RA   Labutti K., Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T.,
RA   Yoshinaga Y., Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi
RT   Provides Insights into the Origins of Lignocellulose Decay
RT   Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- SUBUNIT: Interacts with the 40S ribosomal subunit.
CC       {ECO:0000256|RuleBase:RU361273}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU361273}.
CC   -!- DOMAIN: The SUI1 domain may be involved in RNA binding.
CC       {ECO:0000256|RuleBase:RU361273}.
CC   -!- SIMILARITY: Belongs to the DENR family.
CC       {ECO:0000256|RuleBase:RU361273}.
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DR   EMBL; KV423928; KZT60761.1; -; Genomic_DNA.
DR   EnsemblFungi; KZT60761; KZT60761; CALCODRAFT_480426.
DR   Proteomes; UP000076842; Unassembled WGS sequence.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:InterPro.
DR   Gene3D; 3.30.780.10; -; 1.
DR   InterPro; IPR005873; Drp1.
DR   InterPro; IPR001950; SUI1.
DR   InterPro; IPR005872; SUI1_arc_bac.
DR   InterPro; IPR036877; SUI1_dom_sf.
DR   PANTHER; PTHR12789; PTHR12789; 1.
DR   Pfam; PF01253; SUI1; 1.
DR   SUPFAM; SSF55159; SSF55159; 2.
DR   TIGRFAMs; TIGR01159; DRP1; 1.
DR   PROSITE; PS50296; SUI1; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000076842};
KW   Cytoplasm {ECO:0000256|RuleBase:RU361273};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076842};
KW   Ribonucleoprotein {ECO:0000256|RuleBase:RU361273};
KW   Ribosomal protein {ECO:0000256|RuleBase:RU361273}.
FT   DOMAIN      102    173       SUI1. {ECO:0000259|PROSITE:PS50296}.
FT   COILED       81    110       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   198 AA;  22005 MW;  E951D1AE52368AC2 CRC64;
     MADTAGPSVP PILPLYVLYC EVCTFPPEYC EFGSSVSKCK SWLAEEHPEL YDKYWSDEAL
     VKKIGTLSLE NQKKLDDDSA KKEAKAEAKA SLAEKKRKES KITIKRVERN KRKHVTSVQG
     LEAFGVDLKK ASKLFAQKFA TGSSVSKNLQ GLEEIVVQGD VTEEIVDMII DQVGVLKGVP
     EKNVVRVEEK KKKGGDDE
//
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