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Conserved domains on  [gi|1281021737|ref|XP_022995118|]
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rhodanese-like/PpiC domain-containing protein 12, chloroplastic isoform X1 [Cucurbita maxima]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RHOD super family cl00125
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 183-286 8.28e-42

Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.


The actual alignment was detected with superfamily member cd01528:

Pssm-ID: 444705 [Multi-domain]  Cd Length: 101  Bit Score: 139.45  E-value: 8.28e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737 183 DIQPEELHLKMQDPNflNEAQLIDVREPEEVDQACLPAFQVLPLRQFGSWGPEVTTKfDPQKETYVMCHHGVRSLQVARY 262
Cdd:cd01528     1 QISVAELAEWLADER--EEPVLIDVREPEELEIAFLPGFLHLPMSEIPERSKELDSD-NPDKDIVVLCHHGGRSMQVAQW 77

                          90       100
                  ....*....|....*....|....
gi 1281021737 263 LQTQGFKKVYNVSGGIHAYSLKVD 286
Cdd:cd01528    78 LLRQGFENVYNLQGGIDAWSLEVD 101
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 84-181 1.04e-26

Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 101.96  E-value: 1.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737  84 GRELLVQHLLVK-------EDDIKLLSDLQQRIAGGDDLSDLAVEYSLCP-SKEEGGMLGWVKRGQMVPEFEEAAFNAPL 155
Cdd:COG0760     6 PEEVRASHILVKvppsedrAKAEAKAEELLAQLKAGADFAELAKEYSQDPgSAANGGDLGWFSRGQLVPEFEEAAFALKP 85

                          90       100
                  ....*....|....*....|....*..
gi 1281021737 156 NKVVK-CKTKFGWHLLQVLSERGESVL 181
Cdd:COG0760    86 GEISGpVKTQFGYHIIKVEDRRPAETP 112
 
Name Accession Description Interval E-value
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 183-286 8.28e-42

Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes uncharacterized putative rhodanese-related domains.


Pssm-ID: 238786 [Multi-domain]  Cd Length: 101  Bit Score: 139.45  E-value: 8.28e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737 183 DIQPEELHLKMQDPNflNEAQLIDVREPEEVDQACLPAFQVLPLRQFGSWGPEVTTKfDPQKETYVMCHHGVRSLQVARY 262
Cdd:cd01528     1 QISVAELAEWLADER--EEPVLIDVREPEELEIAFLPGFLHLPMSEIPERSKELDSD-NPDKDIVVLCHHGGRSMQVAQW 77

                          90       100
                  ....*....|....*....|....
gi 1281021737 263 LQTQGFKKVYNVSGGIHAYSLKVD 286
Cdd:cd01528    78 LLRQGFENVYNLQGGIDAWSLEVD 101
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 84-181 1.04e-26

Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 101.96  E-value: 1.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737  84 GRELLVQHLLVK-------EDDIKLLSDLQQRIAGGDDLSDLAVEYSLCP-SKEEGGMLGWVKRGQMVPEFEEAAFNAPL 155
Cdd:COG0760     6 PEEVRASHILVKvppsedrAKAEAKAEELLAQLKAGADFAELAKEYSQDPgSAANGGDLGWFSRGQLVPEFEEAAFALKP 85

                          90       100
                  ....*....|....*....|....*..
gi 1281021737 156 NKVVK-CKTKFGWHLLQVLSERGESVL 181
Cdd:COG0760    86 GEISGpVKTQFGYHIIKVEDRRPAETP 112
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 183-292 4.90e-25

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 96.19  E-value: 4.90e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737 183 DIQPEELHLKMQDPNflneAQLIDVREPEEVDQACLPAFQVLPLRQFGSWgpevTTKFDPQKETYVMCHHGVRSLQVARY 262
Cdd:COG0607     5 EISPAELAELLESED----AVLLDVREPEEFAAGHIPGAINIPLGELAER----LDELPKDKPIVVYCASGGRSAQAAAL 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 1281021737 263 LQTQGFKKVYNVSGGIHAYSLKVDSSIPTY 292
Cdd:COG0607    77 LRRAGYTNVYNLAGGIEAWKAAGLPVEKGK 106
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 95-172 1.52e-18

PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the interconversion of cis-proline and trans-proline.


Pssm-ID: 425792 [Multi-domain]  Cd Length: 96  Bit Score: 78.50  E-value: 1.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737  95 KEDDIKLLSDLQQRI-AGGDDLSDLAVEYSL-CPSKEEGGMLGWVKRGQMVPEFEEAAFNAPLNKVVK-CKTKFGWHLLQ 171
Cdd:pfam00639  14 RAEAKAKAEEILEQLkSGEDSFAELARKYSDdCPSAANGGDLGWFTRGQLPPEFEKAAFALKPGEISGpVETRFGFHIIK 93


                  .
gi 1281021737 172 V 172
Cdd:pfam00639  94 L 94
prsA PRK03095
peptidylprolyl isomerase PrsA;
86-211 1.30e-16

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 78.11  E-value: 1.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737  86 ELLVQHLLVKEDDIKllSDLQQRIAGGDDLSDLAVEYSLCP-SKEEGGMLGWVKRGQMVPEFEEAAFNAPLNKVVK-CKT 163
Cdd:PRK03095  132 EIKASHILVKDEATA--KKVKEELGQGKSFEELAKQYSEDTgSKEKGGDLGFFGAGKMVKEFEDAAYKLKKDEVSEpVKS 209

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1281021737 164 KFGWHLLQVLSERG-----ESVLLDIQPEELHLKMQDPNFLNEAQLIDVREPE 211
Cdd:PRK03095  210 QFGYHIIKVTDIKEpeksfEQSKADIKKELVQKKAQDGEFMNDLMMKEIKKAD 262
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 200-286 1.44e-13

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 65.56  E-value: 1.44e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737  200 NEAQLIDVREPEEVDQACLPAFQVLPLRQFGSWGPEVTT----------KFDPQKETYVMCHHGVRSLQVARYLQTQGFK 269
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDIlefeellkrlGLDKDKPVVVYCRSGNRSAKAAWLLRELGFK 82

                           90
                   ....*....|....*..
gi 1281021737  270 KVYNVSGGIHAYSLKVD 286
Cdd:smart00450  83 NVYLLDGGYKEWSAAGP 99
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 200-282 5.96e-11

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 57.88  E-value: 5.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737 200 NEAQLIDVREPEEVDQACLP-AFQVlPLRQFGSWG------PEVTTKFDPQKETYVMCHHGVRSLQVARYLQTQGFKKVY 272
Cdd:pfam00581   4 GKVVLIDVRPPEEYAKGHIPgAVNV-PLSSLSLPPlpllelLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKNVY 82

                          90
                  ....*....|
gi 1281021737 273 NVSGGIHAYS 282
Cdd:pfam00581  83 VLDGGFEAWK 92
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 172-292 1.29e-09

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 58.18  E-value: 1.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737 172 VLSERGESVLLD--IQPEELHlKMQDPNflNEAQLIDVREPEEVDQACLPAFQVLPLRQFGSwgPEVTTKFDPQKETYVM 249
Cdd:PRK07878  275 VVSDEAQQAAAGstITPRELK-EWLDSG--KKIALIDVREPVEWDIVHIPGAQLIPKSEILS--GEALAKLPQDRTIVLY 349

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1281021737 250 CHHGVRSLQVARYLQTQGFKKVYNVSGGIHAYSLKVDSSIPTY 292
Cdd:PRK07878  350 CKTGVRSAEALAALKKAGFSDAVHLQGGVVAWAKQVDPSLPMY 392
nifM_nitrog TIGR02933
nitrogen fixation protein NifM; Members of this protein family, found in a subset of ...
 88-170 1.75e-09

nitrogen fixation protein NifM; Members of this protein family, found in a subset of nitrogen-fixing bacteria, are the nitrogen fixation protein NifM. NifM, homologous to peptidyl-prolyl cis-trans isomerases, appears to be an accessory protein for NifH, the Fe protein, also called component II or dinitrogenase reductase, of nitrogenase. [Central intermediary metabolism, Nitrogen fixation]


Pssm-ID: 131979 [Multi-domain]  Cd Length: 256  Bit Score: 57.16  E-value: 1.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737  88 LVQHLL--VKEDD-----IKLLSDLQQRIAGGDDLSDLAVEYSLCPSKEEGGMLGWVKRGQMVPEFEEAAFN---APLNK 157
Cdd:TIGR02933 125 LTRHLLltVNEDDreavrTRILAILRRLRGKPAAFAEQAMRHSHCPTAMEGGLLGWVSRGLLYPQLDAALFQlaeGELSP 204

                          90
                  ....*....|...
gi 1281021737 158 VVkcKTKFGWHLL 170
Cdd:TIGR02933 205 PI--ESEIGWHLL 215
 
Name Accession Description Interval E-value
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 183-286 8.28e-42

Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes uncharacterized putative rhodanese-related domains.


Pssm-ID: 238786 [Multi-domain]  Cd Length: 101  Bit Score: 139.45  E-value: 8.28e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737 183 DIQPEELHLKMQDPNflNEAQLIDVREPEEVDQACLPAFQVLPLRQFGSWGPEVTTKfDPQKETYVMCHHGVRSLQVARY 262
Cdd:cd01528     1 QISVAELAEWLADER--EEPVLIDVREPEELEIAFLPGFLHLPMSEIPERSKELDSD-NPDKDIVVLCHHGGRSMQVAQW 77

                          90       100
                  ....*....|....*....|....
gi 1281021737 263 LQTQGFKKVYNVSGGIHAYSLKVD 286
Cdd:cd01528    78 LLRQGFENVYNLQGGIDAWSLEVD 101
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 84-181 1.04e-26

Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 101.96  E-value: 1.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737  84 GRELLVQHLLVK-------EDDIKLLSDLQQRIAGGDDLSDLAVEYSLCP-SKEEGGMLGWVKRGQMVPEFEEAAFNAPL 155
Cdd:COG0760     6 PEEVRASHILVKvppsedrAKAEAKAEELLAQLKAGADFAELAKEYSQDPgSAANGGDLGWFSRGQLVPEFEEAAFALKP 85

                          90       100
                  ....*....|....*....|....*..
gi 1281021737 156 NKVVK-CKTKFGWHLLQVLSERGESVL 181
Cdd:COG0760    86 GEISGpVKTQFGYHIIKVEDRRPAETP 112
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 183-292 4.90e-25

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 96.19  E-value: 4.90e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737 183 DIQPEELHLKMQDPNflneAQLIDVREPEEVDQACLPAFQVLPLRQFGSWgpevTTKFDPQKETYVMCHHGVRSLQVARY 262
Cdd:COG0607     5 EISPAELAELLESED----AVLLDVREPEEFAAGHIPGAINIPLGELAER----LDELPKDKPIVVYCASGGRSAQAAAL 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 1281021737 263 LQTQGFKKVYNVSGGIHAYSLKVDSSIPTY 292
Cdd:COG0607    77 LRRAGYTNVYNLAGGIEAWKAAGLPVEKGK 106
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 95-172 1.52e-18

PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the interconversion of cis-proline and trans-proline.


Pssm-ID: 425792 [Multi-domain]  Cd Length: 96  Bit Score: 78.50  E-value: 1.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737  95 KEDDIKLLSDLQQRI-AGGDDLSDLAVEYSL-CPSKEEGGMLGWVKRGQMVPEFEEAAFNAPLNKVVK-CKTKFGWHLLQ 171
Cdd:pfam00639  14 RAEAKAKAEEILEQLkSGEDSFAELARKYSDdCPSAANGGDLGWFTRGQLPPEFEKAAFALKPGEISGpVETRFGFHIIK 93


                  .
gi 1281021737 172 V 172
Cdd:pfam00639  94 L 94
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 89-173 7.22e-18

PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the interconversion of cis-proline and trans-proline.


Pssm-ID: 404499 [Multi-domain]  Cd Length: 116  Bit Score: 77.41  E-value: 7.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737  89 VQHLLV--------KEDDIKLLSD-LQQRIAGGDDLSDLAVEYSLCP-SKEEGGMLGWVKRGQMVPEFEEAAFNAPLNKV 158
Cdd:pfam13616  18 ASHILIsysqavsrTEEEAKAKADsLLAALKNGADFAALAKTYSDDPaSKNNGGDLGWFTKGQMVKEFEDAVFSLKVGEI 97

                          90
                  ....*....|....*.
gi 1281021737 159 VKC-KTKFGWHLLQVL 173
Cdd:pfam13616  98 SGVvKTQFGFHIIKVT 113
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 188-281 5.52e-17

Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.


Pssm-ID: 238089 [Multi-domain]  Cd Length: 89  Bit Score: 74.26  E-value: 5.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737 188 ELHLKMQDPNflneAQLIDVREPEEVDQACLPAFQVLPLRQFGSWgpEVTTKFDPQKETYVMCHHGVRSLQVARYLQTQG 267
Cdd:cd00158     1 ELKELLDDED----AVLLDVREPEEYAAGHIPGAINIPLSELEER--AALLELDKDKPIVVYCRSGNRSARAAKLLRKAG 74

                          90
                  ....*....|....
gi 1281021737 268 FKKVYNVSGGIHAY 281
Cdd:cd00158    75 GTNVYNLEGGMLAW 88
prsA PRK03095
peptidylprolyl isomerase PrsA;
86-211 1.30e-16

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 78.11  E-value: 1.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737  86 ELLVQHLLVKEDDIKllSDLQQRIAGGDDLSDLAVEYSLCP-SKEEGGMLGWVKRGQMVPEFEEAAFNAPLNKVVK-CKT 163
Cdd:PRK03095  132 EIKASHILVKDEATA--KKVKEELGQGKSFEELAKQYSEDTgSKEKGGDLGFFGAGKMVKEFEDAAYKLKKDEVSEpVKS 209

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1281021737 164 KFGWHLLQVLSERG-----ESVLLDIQPEELHLKMQDPNFLNEAQLIDVREPE 211
Cdd:PRK03095  210 QFGYHIIKVTDIKEpeksfEQSKADIKKELVQKKAQDGEFMNDLMMKEIKKAD 262
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 91-173 1.60e-16

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 73.13  E-value: 1.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737  91 HLLVKEDdiKLLSDLQQRIAGGDDLSDLAVEYSLCPSKEEGGMLGWVKRGQMVPEFEEAAFNAP-LNKVVKCKTKFGWHL 169
Cdd:PRK15441    9 HILVKEE--KLALDLLEQIKNGADFGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCPvLEPTGPLHTQFGYHI 86


                  ....
gi 1281021737 170 LQVL 173
Cdd:PRK15441   87 IKVL 90
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 204-292 8.52e-14

Member of the Rhodanese Homology Domain superfamily. This CD includes several putative molybdopterin synthase sulfurylases including the molybdenum cofactor biosynthetic protein (CnxF) of Aspergillus nidulans and the molybdenum cofactor synthesis protein 3 (MOCS3) of Homo sapiens. These rhodanese-like domains are found C-terminal of the ThiF and MoeZ_MoeB domains.


Pssm-ID: 238784 [Multi-domain]  Cd Length: 122  Bit Score: 66.56  E-value: 8.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737 204 LIDVREPEEVDQACLPAFQVLPLRQFGSWGPEVTTKF------DPQKETYVMCHHGVRSLQVARYLQTQGFK-KVYNVSG 276
Cdd:cd01526    27 LLDVRPKVHFEICRLPEAINIPLSELLSKAAELKSLQelpldnDKDSPIYVVCRRGNDSQTAVRKLKELGLErFVRDIIG 106

                          90
                  ....*....|....*.
gi 1281021737 277 GIHAYSLKVDSSIPTY 292
Cdd:cd01526   107 GLKAWADKVDPTFPLY 122
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 200-286 1.44e-13

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 65.56  E-value: 1.44e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737  200 NEAQLIDVREPEEVDQACLPAFQVLPLRQFGSWGPEVTT----------KFDPQKETYVMCHHGVRSLQVARYLQTQGFK 269
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDIlefeellkrlGLDKDKPVVVYCRSGNRSAKAAWLLRELGFK 82

                           90
                   ....*....|....*..
gi 1281021737  270 KVYNVSGGIHAYSLKVD 286
Cdd:smart00450  83 NVYLLDGGYKEWSAAGP 99
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 86-196 1.82e-13

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 69.23  E-value: 1.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737  86 ELLVQHLLVKedDIKLLSDLQQRIAGGDDLSDLAVEYSLCP-SKEEGGMLGWVKRGQMVPEFEEAAFNAPLNKVVK-CKT 163
Cdd:PRK02998  134 EMKVSHILVK--DEKTAKEVKEKVNNGEDFAALAKQYSEDTgSKEQGGEISGFAPGQTVKEFEEAAYKLDAGQVSEpVKT 211

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1281021737 164 KFGWHLLQVLSERG----ESVLLDIQPEELHLKMQDP 196
Cdd:PRK02998  212 TYGYHIIKVTDKKElkpfDEVKDSIRKDLEQQRLQDT 248
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 184-280 1.17e-12

GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain superfamily. Unlike other rhodanese sulfurtransferases, GlpE is a single domain protein but indications are that it functions as a dimer. The active site contains a catalytically active cysteine.


Pssm-ID: 238721 [Multi-domain]  Cd Length: 96  Bit Score: 62.66  E-value: 1.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737 184 IQPEELHLKMQDPNflnEAQLIDVREPEEVDQAC--LPAFQVLPLRQFGSWGPEvttkFDPQKETYVMCHHGVRSLQVAR 261
Cdd:cd01444     2 ISVDELAELLAAGE---APVLLDVRDPASYAALPdhIPGAIHLDEDSLDDWLGD----LDRDRPVVVYCYHGNSSAQLAQ 74

                          90
                  ....*....|....*....
gi 1281021737 262 YLQTQGFKKVYNVSGGIHA 280
Cdd:cd01444    75 ALREAGFTDVRSLAGGFEA 93
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 184-283 1.38e-11

Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus lactis NADH oxidase, Bacillus cereus NADH dehydrogenase, and Bacteroides thetaiotaomicron pyridine nucleotide-disulphide oxidoreductase, and similar rhodanese-like domains found C-terminal of the pyridine nucleotide-disulphide oxidoreductase (Pyr-redox) domain and the Pyr-redox dimerization domain.


Pssm-ID: 238782 [Multi-domain]  Cd Length: 90  Bit Score: 59.59  E-value: 1.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737 184 IQPEEL-HLKMqdpnflNEAQLIDVREPEEVDQACLPAFQVLPLRQFgswgPEVTTKFDPQKETYVMCHHGVRSLQVARY 262
Cdd:cd01524     1 VQWHELdNYRA------DGVTLIDVRTPQEFEKGHIKGAINIPLDEL----RDRLNELPKDKEIIVYCAVGLRGYIAARI 70

                          90       100
                  ....*....|....*....|.
gi 1281021737 263 LQTQGFkKVYNVSGGIHAYSL 283
Cdd:cd01524    71 LTQNGF-KVKNLDGGYKTYST 90
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 200-282 5.96e-11

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 57.88  E-value: 5.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737 200 NEAQLIDVREPEEVDQACLP-AFQVlPLRQFGSWG------PEVTTKFDPQKETYVMCHHGVRSLQVARYLQTQGFKKVY 272
Cdd:pfam00581   4 GKVVLIDVRPPEEYAKGHIPgAVNV-PLSSLSLPPlpllelLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKNVY 82

                          90
                  ....*....|
gi 1281021737 273 NVSGGIHAYS 282
Cdd:pfam00581  83 VLDGGFEAWK 92
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 95-171 7.19e-10

peptidyl-prolyl cis-trans isomerase (PPIase); Provisional


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 55.42  E-value: 7.19e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1281021737  95 KEDDIKLLSDLQQRIAGGDDL-SDLAVEYSLCPSKEEGGMLGWVKRGQMVPEFEEAAFNAPLNKVVK-CKTKFGWHLLQ 171
Cdd:PTZ00356   34 KEEAIKELAKWREQIVSGEKTfEEIARQRSDCGSAAKGGDLGFFGRGQMQKPFEDAAFALKVGEISDiVHTDSGVHIIL 112
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 172-292 1.29e-09

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 58.18  E-value: 1.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737 172 VLSERGESVLLD--IQPEELHlKMQDPNflNEAQLIDVREPEEVDQACLPAFQVLPLRQFGSwgPEVTTKFDPQKETYVM 249
Cdd:PRK07878  275 VVSDEAQQAAAGstITPRELK-EWLDSG--KKIALIDVREPVEWDIVHIPGAQLIPKSEILS--GEALAKLPQDRTIVLY 349

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1281021737 250 CHHGVRSLQVARYLQTQGFKKVYNVSGGIHAYSLKVDSSIPTY 292
Cdd:PRK07878  350 CKTGVRSAEALAALKKAGFSDAVHLQGGVVAWAKQVDPSLPMY 392
prsA PRK00059
peptidylprolyl isomerase; Provisional
 82-174 1.56e-09

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 57.80  E-value: 1.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737  82 EDGRELLVQHLLVK-EDDIKllsDLQQRIAGGDDLSDLAVEYSLCP-SKEEGGMLGWV--KRGQMVPEFEEAAFNAPLNK 157
Cdd:PRK00059  192 EKPNTMHLAHILVKtEDEAK---KVKKRLDKGEDFAKVAKEVSQDPgSKDKGGDLGDVpySDSGYDKEFMDGAKALKEGE 268

                          90
                  ....*....|....*...
gi 1281021737 158 VVK-CKTKFGWHLLQVLS 174
Cdd:PRK00059  269 ISApVKTQFGYHIIKAIK 286
nifM_nitrog TIGR02933
nitrogen fixation protein NifM; Members of this protein family, found in a subset of ...
 88-170 1.75e-09

nitrogen fixation protein NifM; Members of this protein family, found in a subset of nitrogen-fixing bacteria, are the nitrogen fixation protein NifM. NifM, homologous to peptidyl-prolyl cis-trans isomerases, appears to be an accessory protein for NifH, the Fe protein, also called component II or dinitrogenase reductase, of nitrogenase. [Central intermediary metabolism, Nitrogen fixation]


Pssm-ID: 131979 [Multi-domain]  Cd Length: 256  Bit Score: 57.16  E-value: 1.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737  88 LVQHLL--VKEDD-----IKLLSDLQQRIAGGDDLSDLAVEYSLCPSKEEGGMLGWVKRGQMVPEFEEAAFN---APLNK 157
Cdd:TIGR02933 125 LTRHLLltVNEDDreavrTRILAILRRLRGKPAAFAEQAMRHSHCPTAMEGGLLGWVSRGLLYPQLDAALFQlaeGELSP 204

                          90
                  ....*....|...
gi 1281021737 158 VVkcKTKFGWHLL 170
Cdd:TIGR02933 205 PI--ESEIGWHLL 215
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 202-282 2.03e-09

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 57.57  E-value: 2.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737 202 AQLIDVREPEEVDQACLPAFQVLPLRQFgsWGPEVTTKFDPQKETYVMCHHGVRSLQVARYLQTQGFKKVYNVSGGIHAY 281
Cdd:PRK05597  275 VTLIDVREPSEFAAYSIPGAHNVPLSAI--REGANPPSVSAGDEVVVYCAAGVRSAQAVAILERAGYTGMSSLDGGIEGW 352


                  .
gi 1281021737 282 S 282
Cdd:PRK05597  353 L 353
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
184-281 6.35e-09

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 52.72  E-value: 6.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737 184 IQPEELHLKMQDpnflNEAQLIDVREPE-----------EVDQACLPAFqvlpLRQfgswgpevtTKFDpqKETYVMCHH 252
Cdd:PRK00162    7 INVEQAHQKLQE----GGAVLVDIRDPQsfamghapgafHLTNDSLGAF----MRQ---------ADFD--TPVMVMCYH 67

                          90       100
                  ....*....|....*....|....*....
gi 1281021737 253 GVRSLQVARYLQTQGFKKVYNVSGGIHAY 281
Cdd:PRK00162   68 GNSSQGAAQYLLQQGFDVVYSIDGGFEAW 96
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
183-282 2.61e-08

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 54.25  E-value: 2.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737 183 DIQPEELHlKMQDpnflNEAQLIDVREPEEVDQACLPAFQVLPlRQFGSWGPEvTTKFDPQKETYVMCHHGVRSLQVARY 262
Cdd:PRK08762    4 EISPAEAR-ARAA----QGAVLIDVREAHERASGQAEGALRIP-RGFLELRIE-THLPDRDREIVLICASGTRSAHAAAT 76

                          90       100
                  ....*....|....*....|
gi 1281021737 263 LQTQGFKKVYNVSGGIHAYS 282
Cdd:PRK08762   77 LRELGYTRVASVAGGFSAWK 96
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
204-292 2.66e-08

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 54.36  E-value: 2.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737 204 LIDVREPEEVDQACLPAFQVLPLRQFGSwGPEVTT--KFDPQKETYVMCHHGVRSLQVARYLQTQGFKKVyNVSGGIHAY 281
Cdd:PRK07411  302 LIDVRNPNEYEIARIPGSVLVPLPDIEN-GPGVEKvkELLNGHRLIAHCKMGGRSAKALGILKEAGIEGT-NVKGGITAW 379

                          90
                  ....*....|.
gi 1281021737 282 SLKVDSSIPTY 292
Cdd:PRK07411  380 SREVDPSVPQY 390
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
 183-281 3.09e-08

Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, Bacillus subtilis YbfQ, and similar uncharacterized proteins.


Pssm-ID: 238776 [Multi-domain]  Cd Length: 101  Bit Score: 50.66  E-value: 3.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737 183 DIQPEELHLKMQDPNFLneaqLIDVREPEEVD-----QACLPafQVLPLRQFGSWgpeVTTKFDPQKETYVM--CHHGVR 255
Cdd:cd01518     3 YLSPAEWNELLEDPEVV----LLDVRNDYEYDighfkGAVNP--DVDTFREFPFW---LDENLDLLKGKKVLmyCTGGIR 73

                          90       100
                  ....*....|....*....|....*.
gi 1281021737 256 SLQVARYLQTQGFKKVYNVSGGIHAY 281
Cdd:cd01518    74 CEKASAYLKERGFKNVYQLKGGILKY 99
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 184-281 7.29e-08

Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as a polysulfide binding and transferase domain in anaerobic gram-negative bacteria, functioning in oxidative phosphorylation with polysulfide-sulfur as a terminal electron acceptor. The active site contains the same conserved cysteine that is the catalytic residue in other Rhodanese Homology Domain proteins.


Pssm-ID: 238724 [Multi-domain]  Cd Length: 103  Bit Score: 49.73  E-value: 7.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737 184 IQPEELHLKMQDPnflnEAQLIDVREPEEVDQ-ACLPAFQVLPLRQFGSW----GPEVTTKFDPQKETYVMCHHGVRSLQ 258
Cdd:cd01447     1 LSPEDARALLGSP----GVLLVDVRDPRELERtGMIPGAFHAPRGMLEFWadpdSPYHKPAFAEDKPFVFYCASGWRSAL 76

                          90       100
                  ....*....|....*....|...
gi 1281021737 259 VARYLQTQGFKKVYNVSGGIHAY 281
Cdd:cd01447    77 AGKTLQDMGLKPVYNIEGGFKDW 99
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 204-277 5.66e-07

Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein 67B2 of Drosophila melanogaster and other similar proteins, many of which are uncharacterized.


Pssm-ID: 238777 [Multi-domain]  Cd Length: 106  Bit Score: 47.26  E-value: 5.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737 204 LIDVREPEEVDQACLPAFQVLPLRQF-GSW---GPEVTTKF-----DPQKETYVMCHHGVRSLQVARYLQTQGFKKVYNV 274
Cdd:cd01519    18 LIDVREPEELKTGKIPGAINIPLSSLpDALalsEEEFEKKYgfpkpSKDKELIFYCKAGVRSKAAAELARSLGYENVGNY 97


                  ...
gi 1281021737 275 SGG 277
Cdd:cd01519    98 PGS 100
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
 184-277 8.91e-07

Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative rhodanese-related sulfurtransferases of several uncharacterized proteins.


Pssm-ID: 238780 [Multi-domain]  Cd Length: 117  Bit Score: 46.94  E-value: 8.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737 184 IQPEELHLKMQDpnfLNEAQLIDVREPEEVD-QACLPAFQVLPLRQFGSWGP------EVTTKFDPQKETYVMCHHGVRS 256
Cdd:cd01522     1 LTPAEAWALLQA---DPQAVLVDVRTEAEWKfVGGVPDAVHVAWQVYPDMEInpnflaELEEKVGKDRPVLLLCRSGNRS 77

                          90       100
                  ....*....|....*....|.
gi 1281021737 257 LQVARYLQTQGFKKVYNVSGG 277
Cdd:cd01522    78 IAAAEAAAQAGFTNVYNVLEG 98
prsA PRK03002
peptidylprolyl isomerase PrsA;
86-198 1.01e-06

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 49.16  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737  86 ELLVQHLLVK-EDDIKllsDLQQRIAGGDDLSDLAVEYSLCP-SKEEGGMLGWVKRGQMVPEFEEAAFNAPLNKVVK-CK 162
Cdd:PRK03002  136 EIKASHILVSdENEAK---EIKKKLDAGASFEELAKQESQDLlSKEKGGDLGYFNSGRMAPEFETAAYKLKVGQISNpVK 212

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1281021737 163 TKFGWHL--------LQVLSERGESVLLDIQPEelhlKMQDPNF 198
Cdd:PRK03002  213 SPNGYHIikltdkkdLKPYDEVKDSIRKNLEEE----RTADPIF 252
PRK00142 PRK00142
rhodanese-related sulfurtransferase;
184-285 1.49e-06

rhodanese-related sulfurtransferase;


Pssm-ID: 234663 [Multi-domain]  Cd Length: 314  Bit Score: 48.69  E-value: 1.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737 184 IQPEELHLKMQDPNFLneaqLIDVREPEEVD-----QACLP---AFQVLPlrqfgswgPEVTTKFDPQKETYVM--CHHG 253
Cdd:PRK00142  114 LKPKEVNELLDDPDVV----FIDMRNDYEYEighfeNAIEPdieTFREFP--------PWVEENLDPLKDKKVVmyCTGG 181

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1281021737 254 VRSLQVARYLQTQGFKKVYNVSGGIHAYSLKV 285
Cdd:PRK00142  182 IRCEKASAWMKHEGFKEVYQLEGGIITYGEDP 213
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 86-176 3.59e-04

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 41.65  E-value: 3.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737  86 ELLVQHLLVKEDDIklLSDLQQR-----IA-----GGDDLSDLAVEYSLCP-SKEEGGMLGWVkrgqmVPEFEEAAFNAP 154
Cdd:PRK10770  266 EVHARHILLKPSPI--MTDEQARakleqIAadiksGKTTFAAAAKEFSQDPgSANQGGDLGWA-----TPDIFDPAFRDA 338

                          90       100
                  ....*....|....*....|....*...
gi 1281021737 155 LNKVVK------CKTKFGWHLLQVLSER 176
Cdd:PRK10770  339 LMRLNKgqisapVHSSFGWHLIELLDTR 366
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 84-179 5.05e-03

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 38.18  E-value: 5.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281021737  84 GRELLVQHLLVK----------EDDIKLLSDLQQRIAGGDDLSDLAVEYSLCPSKEEGGMLGWVKRGQMVPEFEEAAFNA 153
Cdd:PRK10770  153 STELNLSHILIPlpenptqdqvDEAESQARSIVDQARNGADFGKLAIAYSADQQALKGGQMGWGRIQELPGLFAQALSTA 232

                          90       100
                  ....*....|....*....|....*..
gi 1281021737 154 PLNKVV-KCKTKFGWHLLQVLSERGES 179
Cdd:PRK10770  233 KKGDIVgPIRSGVGFHILKVNDLRGES 259
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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