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Conserved domains on  [gi|1841979023|ref|WP_170984573|]
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peptidylprolyl isomerase [Rhodoligotrophos defluvii]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 11433571)

peptidylprolyl isomerase (PPIase) accelerates the folding of proteins; it catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides

CATH:  3.10.50.40
EC:  5.2.1.8
Gene Ontology:  GO:0003755|GO:0006457
PubMed:  12871165
SCOP:  3000622

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 139-271 1.62e-49

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


:

Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 161.28  E-value: 1.62e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 139 AKVNSVERVHARHILV---------DTEEQARDALAKIEAGANFADLAKQISKD-GSAQYGGDLGFFSADEMVPEFSKAA 208
Cdd:COG0760     1 DQFDSPEEVRASHILVkvppsedraKAEAKAEELLAQLKAGADFAELAKEYSQDpGSAANGGDLGWFSRGQLVPEFEEAA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1841979023 209 FALQPGQVSQPVQTNYGWHIIKVEERKVGGAEPFDKVKNGLRMIVLRQKVQEKVAELRKSADV 271
Cdd:COG0760    81 FALKPGEISGPVKTQFGYHIIKVEDRRPAETPPFEEVKQQIRQELFQQALEAWLEELRKKAKI 143
 
Name Accession Description Interval E-value
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 139-271 1.62e-49

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 161.28  E-value: 1.62e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 139 AKVNSVERVHARHILV---------DTEEQARDALAKIEAGANFADLAKQISKD-GSAQYGGDLGFFSADEMVPEFSKAA 208
Cdd:COG0760     1 DQFDSPEEVRASHILVkvppsedraKAEAKAEELLAQLKAGADFAELAKEYSQDpGSAANGGDLGWFSRGQLVPEFEEAA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1841979023 209 FALQPGQVSQPVQTNYGWHIIKVEERKVGGAEPFDKVKNGLRMIVLRQKVQEKVAELRKSADV 271
Cdd:COG0760    81 FALKPGEISGPVKTQFGYHIIKVEDRRPAETPPFEEVKQQIRQELFQQALEAWLEELRKKAKI 143
prsA PRK00059
peptidylprolyl isomerase; Provisional
 125-279 7.51e-33

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 123.67  E-value: 7.51e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 125 VNEEDVRKLYDQEAAK-VNSVERVHARHILVDTEEQARDALAKIEAGANFADLAKQISKD-GSAQYGGDLGFFSADE--M 200
Cdd:PRK00059  174 VTDKDAQKYYNENKSKfTEKPNTMHLAHILVKTEDEAKKVKKRLDKGEDFAKVAKEVSQDpGSKDKGGDLGDVPYSDsgY 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 201 VPEFSKAAFALQPGQVSQPVQTNYGWHIIKVEERKVGGAEPFDKVKNGLRMIVLRQK----VQEKVAELRKSADVEMVDP 276
Cdd:PRK00059  254 DKEFMDGAKALKEGEISAPVKTQFGYHIIKAIKKKEYPVKPFDSVKEDIKKQLLQEKqsevFKKKIEEWKKALKVKKYEK 333


                  ...
gi 1841979023 277 DLQ 279
Cdd:PRK00059  334 NLL 336
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 131-235 1.12e-28

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: 106.30  E-value: 1.12e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 131 RKLYDQEAAKVNsverVHARHILVD-------TEEQAR----DALAKIEAGANFADLAKQISKD-GSAQYGGDLGFFSAD 198
Cdd:pfam13616   4 SKLVDKKSAPDS----VKASHILISysqavsrTEEEAKakadSLLAALKNGADFAALAKTYSDDpASKNNGGDLGWFTKG 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1841979023 199 EMVPEFSKAAFALQPGQVSQPVQTNYGWHIIKVEERK 235
Cdd:pfam13616  80 QMVKEFEDAVFSLKVGEISGVVKTQFGFHIIKVTDKK 116
 
Name Accession Description Interval E-value
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 139-271 1.62e-49

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 161.28  E-value: 1.62e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 139 AKVNSVERVHARHILV---------DTEEQARDALAKIEAGANFADLAKQISKD-GSAQYGGDLGFFSADEMVPEFSKAA 208
Cdd:COG0760     1 DQFDSPEEVRASHILVkvppsedraKAEAKAEELLAQLKAGADFAELAKEYSQDpGSAANGGDLGWFSRGQLVPEFEEAA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1841979023 209 FALQPGQVSQPVQTNYGWHIIKVEERKVGGAEPFDKVKNGLRMIVLRQKVQEKVAELRKSADV 271
Cdd:COG0760    81 FALKPGEISGPVKTQFGYHIIKVEDRRPAETPPFEEVKQQIRQELFQQALEAWLEELRKKAKI 143
prsA PRK00059
peptidylprolyl isomerase; Provisional
 125-279 7.51e-33

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 123.67  E-value: 7.51e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 125 VNEEDVRKLYDQEAAK-VNSVERVHARHILVDTEEQARDALAKIEAGANFADLAKQISKD-GSAQYGGDLGFFSADE--M 200
Cdd:PRK00059  174 VTDKDAQKYYNENKSKfTEKPNTMHLAHILVKTEDEAKKVKKRLDKGEDFAKVAKEVSQDpGSKDKGGDLGDVPYSDsgY 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 201 VPEFSKAAFALQPGQVSQPVQTNYGWHIIKVEERKVGGAEPFDKVKNGLRMIVLRQK----VQEKVAELRKSADVEMVDP 276
Cdd:PRK00059  254 DKEFMDGAKALKEGEISAPVKTQFGYHIIKAIKKKEYPVKPFDSVKEDIKKQLLQEKqsevFKKKIEEWKKALKVKKYEK 333


                  ...
gi 1841979023 277 DLQ 279
Cdd:PRK00059  334 NLL 336
prsA PRK03002
peptidylprolyl isomerase PrsA;
118-279 3.82e-31

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 118.11  E-value: 3.82e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 118 HEKIQPTVNEEDVRKLYDQEaakvnsverVHARHILVDTEEQARDALAKIEAGANFADLAKQISKD-GSAQYGGDLGFFS 196
Cdd:PRK03002  117 NEAIKKSVTEKDVKDHYKPE---------IKASHILVSDENEAKEIKKKLDAGASFEELAKQESQDlLSKEKGGDLGYFN 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 197 ADEMVPEFSKAAFALQPGQVSQPVQTNYGWHIIKVEERKvgGAEPFDKVKNGLRMIVLRQKVQEKV-------AELRKsA 269
Cdd:PRK03002  188 SGRMAPEFETAAYKLKVGQISNPVKSPNGYHIIKLTDKK--DLKPYDEVKDSIRKNLEEERTADPIfgkkllqSELKK-A 264

                         170
                  ....*....|
gi 1841979023 270 DVEMVDPDLQ 279
Cdd:PRK03002  265 NIKINDSELE 274
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 117-279 5.41e-29

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 112.37  E-value: 5.41e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 117 FHEKIQPTVNEEDVRKLYDQEaakvnsverVHARHILVDTEEQARDALAKIEAGANFADLAKQISKD-GSAQYGGDLGFF 195
Cdd:PRK02998  114 FEKAIKATVTEKDVKDNYKPE---------MKVSHILVKDEKTAKEVKEKVNNGEDFAALAKQYSEDtGSKEQGGEISGF 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 196 SADEMVPEFSKAAFALQPGQVSQPVQTNYGWHIIKVEERKvgGAEPFDKVKNGLRMIVLRQKVQEK--------VAELRK 267
Cdd:PRK02998  185 APGQTVKEFEEAAYKLDAGQVSEPVKTTYGYHIIKVTDKK--ELKPFDEVKDSIRKDLEQQRLQDTtgkwkqqvVNDLLK 262

                         170
                  ....*....|..
gi 1841979023 268 SADVEMVDPDLQ 279
Cdd:PRK02998  263 DADIKVNDKEFK 274
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 131-235 1.12e-28

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: 106.30  E-value: 1.12e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 131 RKLYDQEAAKVNsverVHARHILVD-------TEEQAR----DALAKIEAGANFADLAKQISKD-GSAQYGGDLGFFSAD 198
Cdd:pfam13616   4 SKLVDKKSAPDS----VKASHILISysqavsrTEEEAKakadSLLAALKNGADFAALAKTYSDDpASKNNGGDLGWFTKG 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1841979023 199 EMVPEFSKAAFALQPGQVSQPVQTNYGWHIIKVEERK 235
Cdd:pfam13616  80 QMVKEFEDAVFSLKVGEISGVVKTQFGFHIIKVTDKK 116
prsA PRK03095
peptidylprolyl isomerase PrsA;
84-281 3.12e-28

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 110.08  E-value: 3.12e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023  84 LMAQEAVKEaiaETNEYKKRLAFYQAKAlrdayfhekIQPTVNEEDVRKLYDQEaakvnsverVHARHILVDTEEQARDA 163
Cdd:PRK03095   91 LLKQQGIKE---ETLKTGVRAQLAQEKA---------IEKTITDKELKDNYKPE---------IKASHILVKDEATAKKV 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 164 LAKIEAGANFADLAKQISKD-GSAQYGGDLGFFSADEMVPEFSKAAFALQPGQVSQPVQTNYGWHIIKVEERKvGGAEPF 242
Cdd:PRK03095  150 KEELGQGKSFEELAKQYSEDtGSKEKGGDLGFFGAGKMVKEFEDAAYKLKKDEVSEPVKSQFGYHIIKVTDIK-EPEKSF 228

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1841979023 243 DKVKNGLRMIVLRQKVQE-------KVAELRKsADVEMVDPDLQRL 281
Cdd:PRK03095  229 EQSKADIKKELVQKKAQDgefmndlMMKEIKK-ADVKVDDKDLKDL 273
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 151-233 1.33e-25

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: 97.76  E-value: 1.33e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 151 HILV-----------DTEEQARDALAKIEAGAN-FADLAKQISKD-GSAQYGGDLGFFSADEMVPEFSKAAFALQPGQVS 217
Cdd:pfam00639   1 HILIktpeaserdraEAKAKAEEILEQLKSGEDsFAELARKYSDDcPSAANGGDLGWFTRGQLPPEFEKAAFALKPGEIS 80

                          90
                  ....*....|....*.
gi 1841979023 218 QPVQTNYGWHIIKVEE 233
Cdd:pfam00639  81 GPVETRFGFHIIKLTD 96
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 145-230 1.29e-22

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 90.47  E-value: 1.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 145 ERVHARHILVD------------------TEEQARDALAK----IEAGAN-FADLAKQISKDGSAQYGGDLGFFSADEMV 201
Cdd:PTZ00356    4 DTVRAAHLLIKhtgsrnpvsrrtgkpvtrSKEEAIKELAKwreqIVSGEKtFEEIARQRSDCGSAAKGGDLGFFGRGQMQ 83

                          90       100
                  ....*....|....*....|....*....
gi 1841979023 202 PEFSKAAFALQPGQVSQPVQTNYGWHIIK 230
Cdd:PTZ00356   84 KPFEDAAFALKVGEISDIVHTDSGVHIIL 112
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 143-279 1.56e-22

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 96.73  E-value: 1.56e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 143 SVERVHARHIL-----VDTEEQARDALAKIEA-----GANFADLAKQISKD-GSAQYGGDLGFFSADEMVPEFSKAAFAL 211
Cdd:PRK10770  263 SVTEVHARHILlkpspIMTDEQARAKLEQIAAdiksgKTTFAAAAKEFSQDpGSANQGGDLGWATPDIFDPAFRDALMRL 342

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1841979023 212 QPGQVSQPVQTNYGWHIIKVEE-RKVGGAEPFDKvKNGLRMIVLR---QKVQEKVAELRKSADVEMVDPDLQ 279
Cdd:PRK10770  343 NKGQISAPVHSSFGWHLIELLDtRQVDKTDAAQK-DRAYRMLFNRkfsEEAQTWMQEQRASAYVKILSNSNA 413
Rotamase_2 pfam13145
PPIC-type PPIASE domain;
125-247 5.17e-19

PPIC-type PPIASE domain;


Pssm-ID: 432992 [Multi-domain]  Cd Length: 121  Bit Score: 80.95  E-value: 5.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 125 VNEEDVRKLYDQEAAKVNSVERVHARHILVDTEE--QARDALAKIEAGANFADLAKQISKDGsaqygGDLGFFSADEMVP 202
Cdd:pfam13145   1 VTEEELKAYYEENKDEFSTPEGRLLEILVFKDQVaaDAALALLKAGALEDFAALAKGEGIKA-----ATLDIVESAELLP 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1841979023 203 -EFSKAAFALQPGQVSQPVQTNYGWHIIKVEERKVGGAEPFDKVKN 247
Cdd:pfam13145  76 eELAKAAFALKPGEVSGPIKTGNGYYVVRVTEIKPAQPLPFEEAKD 121
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 149-235 6.05e-17

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 74.67  E-value: 6.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 149 ARHILVDTEEQARDALAKIEAGANFADLAKQISKDGSAQYGGDLGFFSADEMVPEFSKAAFALQPGQVSQPVQTNYGWHI 228
Cdd:PRK15441    7 ALHILVKEEKLALDLLEQIKNGADFGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTGPLHTQFGYHI 86


                  ....*..
gi 1841979023 229 IKVEERK 235
Cdd:PRK15441   87 IKVLYRN 93
PRK10788 PRK10788
periplasmic folding chaperone; Provisional
 124-264 1.73e-15

periplasmic folding chaperone; Provisional


Pssm-ID: 182731 [Multi-domain]  Cd Length: 623  Bit Score: 76.59  E-value: 1.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 124 TVNEEDVRKLYDQEAAKVNSVERVHARHILVDTEEQARDALAKIEAGANFADLAKQISKDG-SAQYGGDLGFFSADEMVP 202
Cdd:PRK10788  248 TVSDADIQAYYDQHQDQFTQPERKRYSIIQTKTEAEAKAVLDELKKGADFATLAKEKSTDIiSARNGGDLGWLEPATTPD 327

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1841979023 203 EFSKAAFAlQPGQVSQPVQTNYGWHIIKVEERKVGGAEPFDKVKNGLRMIVLRQK-------VQEKVAE 264
Cdd:PRK10788  328 ELKNAGLK-EKGQLSGVIKSSVGFLIVRLDDIQPAKVKPLSEVRDDIAAKVKQEKaldayyaLQQKVSD 395
prsA PRK04405
peptidylprolyl isomerase; Provisional
 91-284 3.86e-12

peptidylprolyl isomerase; Provisional


Pssm-ID: 235295 [Multi-domain]  Cd Length: 298  Bit Score: 65.57  E-value: 3.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023  91 KEAIAETNEYKKRL-----AFYQAKALRDAYFHEKIQPT-VNEEDVRKLYD----QEAAKVNSVE-RVHARHILVDTEEQ 159
Cdd:PRK04405   78 KKVDKQYNSYKKQYgssfdSVLSQNGMTTSSFKQNLRTNlLSEAALKKLKKvtnsQLKKAWKSYQpKVTVQHILVSKKST 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 160 ARDALAKIEAGANFADLAKQISKDGSAQY-GGDLGFF-SADEMV-PEFSKAAFALQPGQVSQ-PVQTNYGWHIIKV---- 231
Cdd:PRK04405  158 AETVIKKLKDGKDFAKLAKKYSTDTATKNkGGKLSAFdSTDTTLdSTFKTAAFKLKNGEYTTtPVKTTYGYEVIKMikhp 237

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1841979023 232 ------EERKVGGAEPFDKVKNGLRMIvlrQKVQEKVAelrKSADVEMVDPDLQRLQSQ 284
Cdd:PRK04405  238 akgtfsDHKKALTKQIYAKWASDSSVM---QRVISKVL---KKANVSIKDKDLKDALSS 290
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 124-266 9.70e-08

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 52.82  E-value: 9.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 124 TVNEEDVRKLYDQEAAKVNSVERVHARHILV------------DTEEQARDALAKIEAGANFADLAKQISKDGSAQYGGD 191
Cdd:PRK10770  133 TILPQEVDSLAKQIGNQNDASTELNLSHILIplpenptqdqvdEAESQARSIVDQARNGADFGKLAIAYSADQQALKGGQ 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 192 LGFFSADEMVPEFSKAAFALQPGQVSQPVQTNYGWHIIKVEERKvGGAEPFDKVKNGLRMIVL-----------RQKVQE 260
Cdd:PRK10770  213 MGWGRIQELPGLFAQALSTAKKGDIVGPIRSGVGFHILKVNDLR-GESQNISVTEVHARHILLkpspimtdeqaRAKLEQ 291


                  ....*.
gi 1841979023 261 KVAELR 266
Cdd:PRK10770  292 IAADIK 297
 
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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