NCBI Conserved Domain Search
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RPS-BLAST 2.2.9 [May-01-2004] Query= local sequence: lcl|tmpseq_0 unnamed protein product (428 letters) Database: cdd.v2.00
gnl|CDD|25575 pfam00639, Rotamase, PPIC-type PPIASE domain. Rotamases increase the rate of protein folding by catalysing the interconversion of cis-proline and trans-proline gnl|CDD|10628 COG0760, SurA, Parvulin-like peptidyl-prolyl isomerase [Posttranslational modification, protein turnover, chaperones]
 Domain Relatives
    .. This CD alignment includes 3D structure. To display structure, download Cn3D!
  PSSMs producing significant alignments: Score
(bits)
E
value
 
gnl|CDD|25575 pfam00639, Rotamase, PPIC-type PPIASE domain. Rotamases increa... 38.8 0.001
  gnl|CDD|10628 COG0760, SurA, Parvulin-like peptidyl-prolyl isomerase [Posttr... 62.4 1e-10


gnl|CDD|25575, pfam00639, Rotamase, PPIC-type PPIASE domain. Rotamases increase the rate of protein folding by catalysing the interconversion of cis-proline and trans-proline.
             CD-Length = 90 residues,  88.9% aligned
             Score = 38.8 bits (90), Expect = 0.001
Query:  298  IRLADQASADKVYAELRNGLAFDEAVRRYSLADDRDRDPPGDLGLIRPQDGRLDLLRKTA  357
Sbjct:  9    DREAARQRAEQILKQLKKGADFADLAKEHS--IDPSAKNGGDLGWFSP--GTLPPAFEDA  64

Query:  358  LIQ-KADTVSQPMRIDGAFEIVRV  380
Sbjct:  65   AFKLKVGELSQPVKSEFGYHIIKV  88


gnl|CDD|10628, COG0760, SurA, Parvulin-like peptidyl-prolyl isomerase [Posttranslational modification, protein turnover, chaperones]
             CD-Length = 320 residues,  97.8% aligned
             Score = 62.4 bits (150), Expect = 1e-10
Query:  127  PRALSAERLREVLAPRSRGLVENSLLLDETQRREAAGVELIGWQFPGQPAQVLDLLSLYE  186
Sbjct:  1    AANSAIAKILLGLIALAFAAFGVSASLVAGVVNAGAVAKVGAQEISAKEKLNAQQKERNI  60

Query:  187  GDNVQGQVELQQGNLAYLARQVQTRIRRDYLWYRLARDGFGPAERQGVRTLVRDKLVRHR  246
Sbjct:  61   ALEQLGEQLLLLQAAAELGIKISQQVVAQLIAEIAVLDKLAKELLLGLSDEQGKQLIAEK  120

Query:  247  YLHQIGLYSDFHHESDALRELAGKVSDKDAEAYYRRNLERYRN--VAQVQAAHIRLADQA  304
Sbjct:  121  PAFQDVEGKFDARAYLKRLRIKGLTEEQEAEALRDKLQNKQQGKKVTEVQARHILVKAEA  180

Query:  305  SADKVYAELR-----NGLAFDEAVRRYSLADDRDRDPPGDLGLIRPQDGRLDLLRKTALI  359
Sbjct:  181  KAKEALALLKKGVREAKADFAELAKKQSEDPSSKNG--GGLLGWNKKGQLVPEFRKAAFI  238

Query:  360  QKADTVSQPMRIDGAFEIVRVRSREDRQLPLDD------RSVRFEVNQAVAREQLAAQFE  413
Sbjct:  239  LKVGEVSAPVKTSFGYHIIKVEKKRDAKLDFPEVKAVKEISLKQELLQKAALEKLLKGEQ  298

Query:  414  TRLRNLLAGARVEGL  428
Sbjct:  299  KSFDKLLKEAAIDIL  313

Citing CD-Search: Marchler-Bauer A, Anderson JB, DeWeese-Scott C, Fedorova ND, Geer LY, He S, Hurwitz DI, Jackson JD, Jacobs AR, Lanczycki CJ, Liebert CA, Liu C, Madej T, Marchler GH, Mazumder R, Nikolskaya AN, Panchenko AR, Rao BS, Shoemaker BA, Simonyan V, Song JS, Thiessen PA, Vasudevan S, Wang Y, Yamashita RA, Yin JJ, and Bryant SH (2003), "CDD: a curated Entrez database of conserved domain alignments", Nucleic Acids Res. 31:383-387.