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Conserved domains on  [gi|446662063|ref|WP_000739409|]
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peptidylprolyl isomerase CBF2 [Helicobacter pylori]

Protein Classification

SurA_N_3 and SurA domain-containing protein( domain architecture ID 11711307)

SurA_N_3 and SurA domain-containing protein

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, ...
 149-295 3.32e-35

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


:

Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 124.30  E-value: 3.32e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446662063 149 DQLFVKQEAHARHILV---------KTEDEAKRIISEIdkqpkaKKEAKFIELANRDTIDPNSknAQNGGDLGKFQKNQM 219
Cdd:COG0760    1 DQFDSPEEVRASHILVkvppsedraKAEAKAEELLAQL------KAGADFAELAKEYSQDPGS--AANGGDLGWFSRGQL 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446662063 220 APDFSKAAFALTPGDYTKtPVKTEFGYHIIYLISKDSPVTYTYEQAKPTIKgmlqEKLFQERMNQRIEELRKHAKI 295
Cdd:COG0760   73 VPEFEEAAFALKPGEISG-PVKTQFGYHIIKVEDRRPAETPPFEEVKQQIR----QELFQQALEAWLEELRKKAKI 143
SurA_N_3 super family cl21568
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
 41-105 5.64e-06

SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a helical domain of unknown function. The C-terminus of the SurA protein folds back and forms part of this domain also but is not included in the current alignment.


The actual alignment was detected with superfamily member pfam13624:

Pssm-ID: 473912 [Multi-domain]  Cd Length: 162  Bit Score: 45.64  E-value: 5.64e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446662063   41 SAGVLATVDGRPITKSDFDMIKQR---------NPNFDFDKLKEKE-KEALIDQAIRTALVENEAKAEKLNQTPE 105
Cdd:pfam13624  37 GGGAVAKVNGEKISRAEFQRAYRRqldqlrqqfGPNLDAELLDELGlRQQVLDQLIDRALLLQEAKKLGLAVSDE 111
 
Name Accession Description Interval E-value
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 149-295 3.32e-35

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 124.30  E-value: 3.32e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446662063 149 DQLFVKQEAHARHILV---------KTEDEAKRIISEIdkqpkaKKEAKFIELANRDTIDPNSknAQNGGDLGKFQKNQM 219
Cdd:COG0760    1 DQFDSPEEVRASHILVkvppsedraKAEAKAEELLAQL------KAGADFAELAKEYSQDPGS--AANGGDLGWFSRGQL 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446662063 220 APDFSKAAFALTPGDYTKtPVKTEFGYHIIYLISKDSPVTYTYEQAKPTIKgmlqEKLFQERMNQRIEELRKHAKI 295
Cdd:COG0760   73 VPEFEEAAFALKPGEISG-PVKTQFGYHIIKVEDRRPAETPPFEEVKQQIR----QELFQQALEAWLEELRKKAKI 143
prsA PRK00059
peptidylprolyl isomerase; Provisional
 44-298 7.38e-29

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 112.88  E-value: 7.38e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446662063  44 VLATVDGRPITKSDFDmikqRNPNFD--FDKLKEK----------EKEALIDQ--AIRTALVENEA---KAEKLNQTP-- 104
Cdd:PRK00059  37 TVATVNGEKITRGDLD----KDPKMQqvLEQLKQQygdnyekneqVKEQIKQQkeQILDSLITEKVllqKAKELKLIPse 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446662063 105 -----------------------EFKAMMEA-----------VKKQALVEfwaKKQAEEVKKVQIPEKEMQDFYNANKDQ 150
Cdd:PRK00059 113 eelnkevdkkineikkqfnndeeQFEEALKAtgfteetfkeyLKNQIIIE---KVINEVVKDVKVTDKDAQKYYNENKSK 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446662063 151 LFVK-QEAHARHILVKTEDEAKRIISEIDKQpkakkeAKFIELANRDTIDPNSKnaQNGGDLGKFQKN--QMAPDFSKAA 227
Cdd:PRK00059 190 FTEKpNTMHLAHILVKTEDEAKKVKKRLDKG------EDFAKVAKEVSQDPGSK--DKGGDLGDVPYSdsGYDKEFMDGA 261

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446662063 228 FALTPGDYTKtPVKTEFGYHIIYLISKDSPVTYTYEQAKPTIKGMLQEKLFQERMNQRIEELRKHAKIVIN 298
Cdd:PRK00059 262 KALKEGEISA-PVKTQFGYHIIKAIKKKEYPVKPFDSVKEDIKKQLLQEKQSEVFKKKIEEWKKALKVKKY 331
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 161-253 4.08e-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: 96.21  E-value: 4.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446662063  161 HILVKTED-------EAKRIISEIDKQPKaKKEAKFIELANRDTIDPNSKNaqNGGDLGKFQKNQMAPDFSKAAFALTPG 233
Cdd:pfam00639   1 HILIKTPEaserdraEAKAKAEEILEQLK-SGEDSFAELARKYSDDCPSAA--NGGDLGWFTRGQLPPEFEKAAFALKPG 77

                          90       100
                  ....*....|....*....|
gi 446662063  234 DYTKtPVKTEFGYHIIYLIS 253
Cdd:pfam00639  78 EISG-PVETRFGFHIIKLTD 96
SurA_N_3 pfam13624
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
 41-105 5.64e-06

SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a helical domain of unknown function. The C-terminus of the SurA protein folds back and forms part of this domain also but is not included in the current alignment.


Pssm-ID: 433358 [Multi-domain]  Cd Length: 162  Bit Score: 45.64  E-value: 5.64e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446662063   41 SAGVLATVDGRPITKSDFDMIKQR---------NPNFDFDKLKEKE-KEALIDQAIRTALVENEAKAEKLNQTPE 105
Cdd:pfam13624  37 GGGAVAKVNGEKISRAEFQRAYRRqldqlrqqfGPNLDAELLDELGlRQQVLDQLIDRALLLQEAKKLGLAVSDE 111
 
Name Accession Description Interval E-value
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 149-295 3.32e-35

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 124.30  E-value: 3.32e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446662063 149 DQLFVKQEAHARHILV---------KTEDEAKRIISEIdkqpkaKKEAKFIELANRDTIDPNSknAQNGGDLGKFQKNQM 219
Cdd:COG0760    1 DQFDSPEEVRASHILVkvppsedraKAEAKAEELLAQL------KAGADFAELAKEYSQDPGS--AANGGDLGWFSRGQL 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446662063 220 APDFSKAAFALTPGDYTKtPVKTEFGYHIIYLISKDSPVTYTYEQAKPTIKgmlqEKLFQERMNQRIEELRKHAKI 295
Cdd:COG0760   73 VPEFEEAAFALKPGEISG-PVKTQFGYHIIKVEDRRPAETPPFEEVKQQIR----QELFQQALEAWLEELRKKAKI 143
prsA PRK00059
peptidylprolyl isomerase; Provisional
 44-298 7.38e-29

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 112.88  E-value: 7.38e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446662063  44 VLATVDGRPITKSDFDmikqRNPNFD--FDKLKEK----------EKEALIDQ--AIRTALVENEA---KAEKLNQTP-- 104
Cdd:PRK00059  37 TVATVNGEKITRGDLD----KDPKMQqvLEQLKQQygdnyekneqVKEQIKQQkeQILDSLITEKVllqKAKELKLIPse 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446662063 105 -----------------------EFKAMMEA-----------VKKQALVEfwaKKQAEEVKKVQIPEKEMQDFYNANKDQ 150
Cdd:PRK00059 113 eelnkevdkkineikkqfnndeeQFEEALKAtgfteetfkeyLKNQIIIE---KVINEVVKDVKVTDKDAQKYYNENKSK 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446662063 151 LFVK-QEAHARHILVKTEDEAKRIISEIDKQpkakkeAKFIELANRDTIDPNSKnaQNGGDLGKFQKN--QMAPDFSKAA 227
Cdd:PRK00059 190 FTEKpNTMHLAHILVKTEDEAKKVKKRLDKG------EDFAKVAKEVSQDPGSK--DKGGDLGDVPYSdsGYDKEFMDGA 261

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446662063 228 FALTPGDYTKtPVKTEFGYHIIYLISKDSPVTYTYEQAKPTIKGMLQEKLFQERMNQRIEELRKHAKIVIN 298
Cdd:PRK00059 262 KALKEGEISA-PVKTQFGYHIIKAIKKKEYPVKPFDSVKEDIKKQLLQEKQSEVFKKKIEEWKKALKVKKY 331
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 161-253 4.08e-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: 96.21  E-value: 4.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446662063  161 HILVKTED-------EAKRIISEIDKQPKaKKEAKFIELANRDTIDPNSKNaqNGGDLGKFQKNQMAPDFSKAAFALTPG 233
Cdd:pfam00639   1 HILIKTPEaserdraEAKAKAEEILEQLK-SGEDSFAELARKYSDDCPSAA--NGGDLGWFTRGQLPPEFEKAAFALKPG 77

                          90       100
                  ....*....|....*....|
gi 446662063  234 DYTKtPVKTEFGYHIIYLIS 253
Cdd:pfam00639  78 EISG-PVETRFGFHIIKLTD 96
prsA PRK03002
peptidylprolyl isomerase PrsA;
41-298 1.77e-19

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 86.14  E-value: 1.77e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446662063  41 SAGVLATVDGRPITKSDFDmiKQRNPNFDFDKLKEKEKEALIDQAIRTA--LVENEAKAEKLNQTPEFKAMMEAVKKQAL 118
Cdd:PRK03002  26 SSATVATATDSTITKSDFE--KQLKDRYGKDMLYEMMAQDVITKKYKVSddDVDKEVQKAKSQYGDQFKNVLKNNGLKDE 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446662063 119 VEFWA----KKQAEEVKKVQIPEKEMQDFYnankdqlfvKQEAHARHILVKTEDEAKRIISEIDKQpkakkeAKFIELAN 194
Cdd:PRK03002 104 ADFKNqikfKLAMNEAIKKSVTEKDVKDHY---------KPEIKASHILVSDENEAKEIKKKLDAG------ASFEELAK 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446662063 195 RDTIDPNSKnaQNGGDLGKFQKNQMAPDFSKAAFALTPGDYTKtPVKTEFGYHIIYLISKDSpvTYTYEQAKPTI-KGML 273
Cdd:PRK03002 169 QESQDLLSK--EKGGDLGYFNSGRMAPEFETAAYKLKVGQISN-PVKSPNGYHIIKLTDKKD--LKPYDEVKDSIrKNLE 243

                        250       260
                 ....*....|....*....|....*..
gi 446662063 274 QEKLFQERMNQRI--EELRKhAKIVIN 298
Cdd:PRK03002 244 EERTADPIFGKKLlqSELKK-ANIKIN 269
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 153-249 1.86e-16

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: 73.94  E-value: 1.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446662063  153 VKQEAHARHILV-------KTEDEAKRIISEIDKQpkAKKEAKFIELANRDTIDPNSKNaqNGGDLGKFQKNQMAPDFSK 225
Cdd:pfam13616  12 APDSVKASHILIsysqavsRTEEEAKAKADSLLAA--LKNGADFAALAKTYSDDPASKN--NGGDLGWFTKGQMVKEFED 87

                          90       100
                  ....*....|....*....|....
gi 446662063  226 AAFALTPGDYTKtPVKTEFGYHII 249
Cdd:pfam13616  88 AVFSLKVGEISG-VVKTQFGFHII 110
prsA PRK04405
peptidylprolyl isomerase; Provisional
 161-261 6.21e-14

peptidylprolyl isomerase; Provisional


Pssm-ID: 235295 [Multi-domain]  Cd Length: 298  Bit Score: 70.58  E-value: 6.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446662063 161 HILVKTEDEAKRIISEIdkqpkaKKEAKFIELANRDTIDPNSKNaqNGGDLGKF--QKNQMAPDFSKAAFALTPGDYTKT 238
Cdd:PRK04405 149 HILVSKKSTAETVIKKL------KDGKDFAKLAKKYSTDTATKN--KGGKLSAFdsTDTTLDSTFKTAAFKLKNGEYTTT 220

                         90       100
                 ....*....|....*....|...
gi 446662063 239 PVKTEFGYHIIYLISKDSPVTYT 261
Cdd:PRK04405 221 PVKTTYGYEVIKMIKHPAKGTFS 243
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 155-252 1.05e-12

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 63.51  E-value: 1.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446662063 155 QEAHARHILVK------------------TEDEAKRIISEIdKQPKAKKEAKFIELAnrdTIDPNSKNAQNGGDLGKFQK 216
Cdd:PTZ00356   4 DTVRAAHLLIKhtgsrnpvsrrtgkpvtrSKEEAIKELAKW-REQIVSGEKTFEEIA---RQRSDCGSAAKGGDLGFFGR 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446662063 217 NQMAPDFSKAAFALTPGDYTKtPVKTEFGYHIIYLI 252
Cdd:PTZ00356  80 GQMQKPFEDAAFALKVGEISD-IVHTDSGVHIILRL 114
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 155-255 1.31e-12

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 62.73  E-value: 1.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446662063 155 QEAHARHILVKTEDEAKRIISEIdkqpkaKKEAKFIELANRDTIDPNSKNaqnGGDLGKFQKNQMAPDFSKAAFAlTPGD 234
Cdd:PRK15441   3 KTAAALHILVKEEKLALDLLEQI------KNGADFGKLAKKHSICPSGKR---GGDLGEFRQGQMVPAFDKVVFS-CPVL 72

                         90       100
                 ....*....|....*....|.
gi 446662063 235 YTKTPVKTEFGYHIIYLISKD 255
Cdd:PRK15441  73 EPTGPLHTQFGYHIIKVLYRN 93
prsA PRK03095
peptidylprolyl isomerase PrsA;
135-280 4.46e-12

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 65.02  E-value: 4.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446662063 135 IPEKEMQDFYnankdqlfvKQEAHARHILVKTEDEAKRIISEIdKQPKAkkeakFIELANRDTIDPNSKnaQNGGDLGKF 214
Cdd:PRK03095 120 ITDKELKDNY---------KPEIKASHILVKDEATAKKVKEEL-GQGKS-----FEELAKQYSEDTGSK--EKGGDLGFF 182

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446662063 215 QKNQMAPDFSKAAFALTPgDYTKTPVKTEFGYHIIYLISKDSPVTyTYEQAKPTIKGMLQEKLFQE 280
Cdd:PRK03095 183 GAGKMVKEFEDAAYKLKK-DEVSEPVKSQFGYHIIKVTDIKEPEK-SFEQSKADIKKELVQKKAQD 246
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 128-298 6.28e-12

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 64.61  E-value: 6.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446662063 128 EEVKKVQIPEKEMQDFYnankdqlfvKQEAHARHILVKTEDEAKRIiseidkQPKAKKEAKFIELANRDTIDPNSKnaQN 207
Cdd:PRK02998 115 EKAIKATVTEKDVKDNY---------KPEMKVSHILVKDEKTAKEV------KEKVNNGEDFAALAKQYSEDTGSK--EQ 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446662063 208 GGDLGKFQKNQMAPDFSKAAFALTPGDYTKtPVKTEFGYHIIYLISKDSpvTYTYEQAKPTIKGMLQEKLFQERM----N 283
Cdd:PRK02998 178 GGEISGFAPGQTVKEFEEAAYKLDAGQVSE-PVKTTYGYHIIKVTDKKE--LKPFDEVKDSIRKDLEQQRLQDTTgkwkQ 254

                        170
                 ....*....|....*
gi 446662063 284 QRIEELRKHAKIVIN 298
Cdd:PRK02998 255 QVVNDLLKDADIKVN 269
Rotamase_2 pfam13145
PPIC-type PPIASE domain;
135-267 2.42e-11

PPIC-type PPIASE domain;


Pssm-ID: 432992 [Multi-domain]  Cd Length: 121  Bit Score: 59.76  E-value: 2.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446662063  135 IPEKEMQDFYNANKDQLFVKQEAHARHILVKTEDEAKRIiseiDKQPKAKKEAKFIELAnrdtidpnSKNAQNGGDLGKF 214
Cdd:pfam13145   1 VTEEELKAYYEENKDEFSTPEGRLLEILVFKDQVAADAA----LALLKAGALEDFAALA--------KGEGIKAATLDIV 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446662063  215 QKNQMAP-DFSKAAFALTPGDYTKtPVKTEFGYHIIYLISKDSPVTYTYEQAKP 267
Cdd:pfam13145  69 ESAELLPeELAKAAFALKPGEVSG-PIKTGNGYYVVRVTEIKPAQPLPFEEAKD 121
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 156-297 1.94e-08

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 54.75  E-value: 1.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446662063 156 EAHARHILVK-----TEDEAKRIISEIDKQPKAKKeAKFIELANRDTIDPNSknAQNGGDLGKFQKNQMAPDFSKAAFAL 230
Cdd:PRK10770 266 EVHARHILLKpspimTDEQARAKLEQIAADIKSGK-TTFAAAAKEFSQDPGS--ANQGGDLGWATPDIFDPAFRDALMRL 342

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446662063 231 TPGDyTKTPVKTEFGYHIIYLISKDSpVTYTYEQAKPTIKGMLQEKLFQERMNQRIEELRKHAKIVI 297
Cdd:PRK10770 343 NKGQ-ISAPVHSSFGWHLIELLDTRQ-VDKTDAAQKDRAYRMLFNRKFSEEAQTWMQEQRASAYVKI 407
PRK10788 PRK10788
periplasmic folding chaperone; Provisional
 80-251 2.09e-08

periplasmic folding chaperone; Provisional


Pssm-ID: 182731 [Multi-domain]  Cd Length: 623  Bit Score: 55.02  E-value: 2.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446662063  80 ALIDQAIRTALVENEAKAEKLNQT-PEFKAMMEAVKK------QALVEFWAKKQAEEVKKVQIPEKEMQDFYNANKDQLF 152
Cdd:PRK10788 187 VAQQRVVREATIDVNALAAKQTVTdEEIKSYYDQNKNnfmapeQFKVSYIKLDAATMQQKITVSDADIQAYYDQHQDQFT 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446662063 153 VKQEAHARHILVKTEDEAKRIISEIdkqpkaKKEAKFIELANRDTIDPNSknAQNGGDLGKFQKNQMAPDFSKAafALTP 232
Cdd:PRK10788 267 QPERKRYSIIQTKTEAEAKAVLDEL------KKGADFATLAKEKSTDIIS--ARNGGDLGWLEPATTPDELKNA--GLKE 336

                        170
                 ....*....|....*....
gi 446662063 233 GDYTKTPVKTEFGYHIIYL 251
Cdd:PRK10788 337 KGQLSGVIKSSVGFLIVRL 355
SurA_N_3 pfam13624
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
 41-105 5.64e-06

SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a helical domain of unknown function. The C-terminus of the SurA protein folds back and forms part of this domain also but is not included in the current alignment.


Pssm-ID: 433358 [Multi-domain]  Cd Length: 162  Bit Score: 45.64  E-value: 5.64e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446662063   41 SAGVLATVDGRPITKSDFDMIKQR---------NPNFDFDKLKEKE-KEALIDQAIRTALVENEAKAEKLNQTPE 105
Cdd:pfam13624  37 GGGAVAKVNGEKISRAEFQRAYRRqldqlrqqfGPNLDAELLDELGlRQQVLDQLIDRALLLQEAKKLGLAVSDE 111
PTZ00491 PTZ00491
major vault protein; Provisional
 77-198 4.83e-03

major vault protein; Provisional


Pssm-ID: 240439 [Multi-domain]  Cd Length: 850  Bit Score: 38.46  E-value: 4.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446662063  77 EKEALIDQA----IRTALVENEAKAEKLNQTPEFKAMMEAVKKQALVEfwakKQAeEVKKVQIPEKEMQDFYNANKDQLF 152
Cdd:PTZ00491 684 ERQKMHDKAkaeeQRTKLLELQAESAAVESSGQSRAEALAEAEARLIE----AEA-EVEQAELRAKALRIEAEAELEKLR 758

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446662063 153 VKQEAHARHILVKTEDEAKRI--ISEIDkqpkAKKEAKFIELANRDTI 198
Cdd:PTZ00491 759 KRQELELEYEQAQNELEIAKAkeLADIE----ATKFERIVEALGRETL 802
 
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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