Fungal Genome Collection
University of Nebraska Lincoln
School of Biological Sciences and Center for Plant Science Innovation
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UniProt_SwissProt BLAST: Single locus
Species:
Saccharomyces cerevisiae S288C
Locus:
YOR020C
Length:
106
Number of sequences:
5887
Description:
YOR020C HSP10 SGDID:S000005546, Chr XV from 370844-370524, Genome Release 64-1-1, reverse complement, Verified ORF, "Mitochondrial matrix co-chaperonin that inhibits the ATPase activity of Hsp60p, a mitochondrial chaperonin; involved in protein folding and sorting in the mitochondria; 10 kD heat shock protein with similarity to E. coli groES"
rec.SubjectHit LengthDescriptionAlign.LenE valueBit score% ident.  % pos.GO associations
271P37283    94   CH10_LACLA 10 kDa chaperonin OS=lactis). GN=g...890.00000000000009     66.2     38     66GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0005524; F:ATP binding; IEA:InterPro.
GO:0006457; P:protein folding; IEA:InterPro.
272Q3K7L5    97   CH10_PSEPF 10 kDa chaperonin OS=Pseudomonas f...920.0000000000001     66.2     41     62GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0005524; F:ATP binding; IEA:InterPro.
GO:0006457; P:protein folding; IEA:InterPro.
273Q0AVV0    96   CH10_SYNWW 10 kDa chaperonin OS=Syntrophomona...940.0000000000001     66.2     40     65GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0006457; P:protein folding; IEA:InterPro.
274B1L1K1    95   CH10_CLOBM 10 kDa chaperonin OS=Clostridium b...920.0000000000001     66.2     41     66GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0005524; F:ATP binding; IEA:InterPro.
GO:0006457; P:protein folding; IEA:InterPro.
275A7GIN4    95   CH10_CLOBL 10 kDa chaperonin OS=Clostridium b...920.0000000000001     66.2     41     66GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0005524; F:ATP binding; IEA:InterPro.
GO:0006457; P:protein folding; IEA:InterPro.
276B1IFD5    95   CH10_CLOBK 10 kDa chaperonin OS=Clostridium b...920.0000000000001     66.2     41     66GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0005524; F:ATP binding; IEA:InterPro.
GO:0006457; P:protein folding; IEA:InterPro.
277C1FLV6    95   CH10_CLOBJ 10 kDa chaperonin OS=Clostridium b...920.0000000000001     66.2     41     66GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0005524; F:ATP binding; IEA:InterPro.
GO:0006457; P:protein folding; IEA:InterPro.
278A5I724    95   CH10_CLOBH 10 kDa chaperonin OS=Clostridium b...920.0000000000001     66.2     41     66GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0005524; F:ATP binding; IEA:InterPro.
GO:0006457; P:protein folding; IEA:InterPro.
279C3KUC9    95   CH10_CLOB6 10 kDa chaperonin OS=Clostridium b...920.0000000000001     66.2     41     66GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0005524; F:ATP binding; IEA:InterPro.
GO:0006457; P:protein folding; IEA:InterPro.
280A7FYP4    95   CH10_CLOB1 10 kDa chaperonin OS=Clostridium b...920.0000000000001     66.2     41     66GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0005524; F:ATP binding; IEA:InterPro.
GO:0006457; P:protein folding; IEA:InterPro.
281Q39ZP6    95   CH10_GEOMG 10 kDa chaperonin OS=Geobacter met...920.0000000000001     66.2     42     67GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0005524; F:ATP binding; IEA:InterPro.
GO:0006457; P:protein folding; IEA:InterPro.
282P35474    104   CH105_RHIME 10 kDa chaperonin 5 OS=meliloti)....910.0000000000001     66.2     35     65GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0005524; F:ATP binding; IEA:InterPro.
GO:0006457; P:protein folding; IEA:InterPro.::GO:0006950; P:response to stress; IEA:UniProtKB-KW.
283Q820G1    102   CH10_STRAW 10 kDa chaperonin OS=Streptomyces ...1040.0000000000001     66.2     40     61GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0005524; F:ATP binding; IEA:InterPro.
GO:0006457; P:protein folding; IEA:InterPro.
284B2TIX6    94   CH10_CLOBB 10 kDa chaperonin OS=Clostridium b...910.0000000000001     66.2     43     69GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0005524; F:ATP binding; IEA:InterPro.
GO:0006457; P:protein folding; IEA:InterPro.
285B4SEN0    95   CH10_PELPB 10 kDa chaperonin OS=Pelodictyon p...890.0000000000001     66.2     42     62GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0005524; F:ATP binding; IEA:InterPro.
GO:0006457; P:protein folding; IEA:InterPro.
286Q930X9    105   CH103_RHIME 10 kDa chaperonin 3 OS=meliloti)....920.0000000000001     66.2     32     65GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0005524; F:ATP binding; IEA:InterPro.
GO:0006457; P:protein folding; IEA:InterPro.::GO:0006950; P:response to stress; IEA:UniProtKB-KW.
287P28599    94   CH10_BACSU 10 kDa chaperonin OS=Bacillus subt...920.0000000000001     66.2     35     64GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0005524; F:ATP binding; IEA:InterPro.
GO:0006457; P:protein folding; IEA:InterPro.::GO:0006950; P:response to stress; IEA:UniProtKB-KW.
288A7Z206    94   CH10_BACA2 10 kDa chaperonin OS=Bacillus amyl...920.0000000000001     66.2     35     64GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0005524; F:ATP binding; IEA:InterPro.
GO:0006457; P:protein folding; IEA:InterPro.
289Q67KB7    97   CH10_SYMTH 10 kDa chaperonin OS=Symbiobacteri...920.0000000000001     66.2     37     65GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0006457; P:protein folding; IEA:InterPro.
290P26822    94   CH10_CLOPE 10 kDa chaperonin OS=Clostridium p...920.0000000000001     65.9     40     65GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0005524; F:ATP binding; IEA:InterPro.
GO:0006457; P:protein folding; IEA:InterPro.
291Q0TN26    94   CH10_CLOP1 10 kDa chaperonin OS=Clostridium p...920.0000000000001     65.9     40     65GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0005524; F:ATP binding; IEA:InterPro.
GO:0006457; P:protein folding; IEA:InterPro.
292B1W3U3    102   CH10_STRGG 10 kDa chaperonin OS=Streptomyces ...1050.0000000000001     66.2     40     61GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0005524; F:ATP binding; IEA:InterPro.
GO:0006457; P:protein folding; IEA:InterPro.
293B0U417    95   CH10_XYLFM 10 kDa chaperonin OS=Xylella fasti...950.0000000000001     65.9     41     59GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0005524; F:ATP binding; IEA:InterPro.
GO:0006457; P:protein folding; IEA:InterPro.
294A1WZJ1    96   CH10_HALHL 10 kDa chaperonin OS=halophila (st...920.0000000000001     65.9     37     64GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0005524; F:ATP binding; IEA:InterPro.
GO:0006457; P:protein folding; IEA:InterPro.
295B0KFQ3    97   CH10_PSEPG 10 kDa chaperonin OS=Pseudomonas p...920.0000000000002     65.9     43     63GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0005524; F:ATP binding; IEA:InterPro.
GO:0006457; P:protein folding; IEA:InterPro.
296B9E8A0    94   CH10_MACCJ 10 kDa chaperonin OS=Macrococcus c...890.0000000000002     65.5     39     62GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0006457; P:protein folding; IEA:InterPro.
297B8GL18    96   CH10_THISH 10 kDa chaperonin OS=Thioalkalivib...920.0000000000002     65.5     38     63GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0005524; F:ATP binding; IEA:InterPro.
GO:0006457; P:protein folding; IEA:InterPro.
298Q0SQQ6    94   CH10_CLOPS 10 kDa chaperonin OS=Clostridium p...920.0000000000002     65.5     40     65GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0005524; F:ATP binding; IEA:InterPro.
GO:0006457; P:protein folding; IEA:InterPro.
299Q6NJ38    98   CH10_CORDI 10 kDa chaperonin OS=gravis). GN=g...960.0000000000002     65.5     42     61GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0005524; F:ATP binding; IEA:InterPro.
GO:0006457; P:protein folding; IEA:InterPro.
300C5BP09    96   CH10_TERTT 10 kDa chaperonin OS=Teredinibacte...950.0000000000002     65.5     43     63GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0005524; F:ATP binding; IEA:InterPro.
GO:0006457; P:protein folding; IEA:InterPro.
301A8FAG2    94   CH10_BACP2 10 kDa chaperonin OS=Bacillus pumi...920.0000000000002     65.5     34     63GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0005524; F:ATP binding; IEA:InterPro.
GO:0006457; P:protein folding; IEA:InterPro.
records
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