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Conserved domains on  [gi|490273795|ref|WP_004169850|]
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fimbria/pilus chaperone family protein [Erwinia amylovora]

Protein Classification

PRK09918 family protein( domain architecture ID 11484522)

PRK09918 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK09918 PRK09918
putative fimbrial chaperone protein; Provisional
 1-232 1.66e-129

putative fimbrial chaperone protein; Provisional


:

Pssm-ID: 236632 [Multi-domain]  Cd Length: 230  Bit Score: 364.75  E-value: 1.66e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273795   1 MRFSTCCAAIAPVLWFFAPSLNATGILPETSVVIVEEEEGEGAINLKNTDAFPVLLLTNLQDIEPDTGRLLTITPPAARV 80
Cdd:PRK09918   1 NRFNLFFLFTALVLLSSSSAVHAAGMVPETSVVIVEESDGEGSINVKNTDSNPILLYTTLVDLPEDKSKLLLVTPPVARV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273795  81 EPGKTQRVRFILTSASSLKTEHLMRVAFEGVPPQEKGKNVVRMTVRQNLPVIIRPGGLKRDEAPWKHLVWTLKAGRLSVS 160
Cdd:PRK09918  81 EPGQSQQVRFILKSGSPLNTEHLLRVSFEGVPPKPGGKNKVVMPIRQDLPVLIQPAALPVVRDPWKLLVWSISGNNLVVS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490273795 161 NPSPYVVRLGQIVTTLPQGASWSLPNAWILPGQQLALSGedKKSEAKADRVRVFPATTWGFTVDSYDAPLAS 232
Cdd:PRK09918 161 NPSPYVVRLGQQVILLPSGKVVALPKPYILPGESLTVAI--TNSKATDTKVRFFPASRYGFVVPSYTAPLTP 230
 
Name Accession Description Interval E-value
PRK09918 PRK09918
putative fimbrial chaperone protein; Provisional
 1-232 1.66e-129

putative fimbrial chaperone protein; Provisional


Pssm-ID: 236632 [Multi-domain]  Cd Length: 230  Bit Score: 364.75  E-value: 1.66e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273795   1 MRFSTCCAAIAPVLWFFAPSLNATGILPETSVVIVEEEEGEGAINLKNTDAFPVLLLTNLQDIEPDTGRLLTITPPAARV 80
Cdd:PRK09918   1 NRFNLFFLFTALVLLSSSSAVHAAGMVPETSVVIVEESDGEGSINVKNTDSNPILLYTTLVDLPEDKSKLLLVTPPVARV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273795  81 EPGKTQRVRFILTSASSLKTEHLMRVAFEGVPPQEKGKNVVRMTVRQNLPVIIRPGGLKRDEAPWKHLVWTLKAGRLSVS 160
Cdd:PRK09918  81 EPGQSQQVRFILKSGSPLNTEHLLRVSFEGVPPKPGGKNKVVMPIRQDLPVLIQPAALPVVRDPWKLLVWSISGNNLVVS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490273795 161 NPSPYVVRLGQIVTTLPQGASWSLPNAWILPGQQLALSGedKKSEAKADRVRVFPATTWGFTVDSYDAPLAS 232
Cdd:PRK09918 161 NPSPYVVRLGQQVILLPSGKVVALPKPYILPGESLTVAI--TNSKATDTKVRFFPASRYGFVVPSYTAPLTP 230
FimC COG3121
P pilus assembly protein, chaperone PapD [Extracellular structures];
1-226 3.05e-41

P pilus assembly protein, chaperone PapD [Extracellular structures];


Pssm-ID: 442355 [Multi-domain]  Cd Length: 237  Bit Score: 140.51  E-value: 3.05e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273795   1 MRfSTCCAAIAPVLWFFAPSLNATGILPETSVVIVEEEEGEGAINLKNTDAFPVLLLTNLQDIEPDTG-----RLLTITP 75
Cdd:COG3121    1 MK-RLLRLLLLALLLLLASAAAAAGISISPTRVIYPAGDKEASLTLTNTGDTPYLVQSWVDDWDQDAGpdkatAPFVVTP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273795  76 PAARVEPGKTQRVRFILTSAS-SLKTEHLMRVAFEGVPP---QEKGKNVVRMTVRQNLPVIIRPGGLKRD-EAPWKHLVW 150
Cdd:COG3121   80 PLFRLEPGKSQTVRIIRTGPPlPQDRESLFRLNVDEIPPkdaSEEGKNTLQIALRTRIKLFYRPAGLKGSpEDAAEKLTW 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490273795 151 TLKAGRLSVSNPSPYVVRLGQIvTTLPQGASWSLPNAWILPGQQLALSGEDKKSEAKADRVRVFPATTWGFTVDSY 226
Cdd:COG3121  160 SLVGNGLTVTNPGPYYVTLSDL-SLGAGGKKLKKGLGMVLPGSTRRWPLPAGASLAAGGKVTWATINDYGGAVPLE 234
PapD_N pfam00345
Pili and flagellar-assembly chaperone, PapD N-terminal domain; C2 domain-like beta-sandwich ...
 26-139 1.65e-16

Pili and flagellar-assembly chaperone, PapD N-terminal domain; C2 domain-like beta-sandwich fold. This domain is the n-terminal part of the PapD chaperone protein for pilus and flagellar assembly.


Pssm-ID: 425623  Cd Length: 123  Bit Score: 73.01  E-value: 1.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273795   26 ILPETSVVIVEEEEGEGAINLKNTDAFPVLLLT----NLQDIEPDTGRL-LTITPPAARVEPGKTQRVRFILTsASSLKT 100
Cdd:pfam00345   1 VVLGGTRVIYPAGEKEASVTVSNTGDNPYLVQSwvddGNEEGTDEKAKApFIVTPPLFRLEPGQEQVLRIYTT-GPPLPT 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 490273795  101 --EHLMRVAFEGVPP---QEKGKNVVRMTVRQNLPVIIRPGGLK 139
Cdd:pfam00345  80 drESLFWLNVLEIPPkdkPKGGQNGLQLALRSRIKLFYRPAGLA 123
CuRO_2_AAO_like_2 cd13873
The second cupredoxin domain of plant Ascorbate oxidase homologs; This family includes plant ...
 74-110 6.54e-03

The second cupredoxin domain of plant Ascorbate oxidase homologs; This family includes plant laccases similar to ascorbate oxidase. Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. Ascorbate oxidase belongs to multicopper oxidase (MCO) family which couples oxidation of substrates with reduction of dioxygen to water. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259941 [Multi-domain]  Cd Length: 161  Bit Score: 36.11  E-value: 6.54e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 490273795  74 TPPAARVEPGKTQRVRFILTSASSLKTehlmrVAFEG 110
Cdd:cd13873   59 HPPVIDVEPGKTYRFRFIGATALSFVS-----LGIEG 90
 
Name Accession Description Interval E-value
PRK09918 PRK09918
putative fimbrial chaperone protein; Provisional
 1-232 1.66e-129

putative fimbrial chaperone protein; Provisional


Pssm-ID: 236632 [Multi-domain]  Cd Length: 230  Bit Score: 364.75  E-value: 1.66e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273795   1 MRFSTCCAAIAPVLWFFAPSLNATGILPETSVVIVEEEEGEGAINLKNTDAFPVLLLTNLQDIEPDTGRLLTITPPAARV 80
Cdd:PRK09918   1 NRFNLFFLFTALVLLSSSSAVHAAGMVPETSVVIVEESDGEGSINVKNTDSNPILLYTTLVDLPEDKSKLLLVTPPVARV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273795  81 EPGKTQRVRFILTSASSLKTEHLMRVAFEGVPPQEKGKNVVRMTVRQNLPVIIRPGGLKRDEAPWKHLVWTLKAGRLSVS 160
Cdd:PRK09918  81 EPGQSQQVRFILKSGSPLNTEHLLRVSFEGVPPKPGGKNKVVMPIRQDLPVLIQPAALPVVRDPWKLLVWSISGNNLVVS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490273795 161 NPSPYVVRLGQIVTTLPQGASWSLPNAWILPGQQLALSGedKKSEAKADRVRVFPATTWGFTVDSYDAPLAS 232
Cdd:PRK09918 161 NPSPYVVRLGQQVILLPSGKVVALPKPYILPGESLTVAI--TNSKATDTKVRFFPASRYGFVVPSYTAPLTP 230
FimC COG3121
P pilus assembly protein, chaperone PapD [Extracellular structures];
1-226 3.05e-41

P pilus assembly protein, chaperone PapD [Extracellular structures];


Pssm-ID: 442355 [Multi-domain]  Cd Length: 237  Bit Score: 140.51  E-value: 3.05e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273795   1 MRfSTCCAAIAPVLWFFAPSLNATGILPETSVVIVEEEEGEGAINLKNTDAFPVLLLTNLQDIEPDTG-----RLLTITP 75
Cdd:COG3121    1 MK-RLLRLLLLALLLLLASAAAAAGISISPTRVIYPAGDKEASLTLTNTGDTPYLVQSWVDDWDQDAGpdkatAPFVVTP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273795  76 PAARVEPGKTQRVRFILTSAS-SLKTEHLMRVAFEGVPP---QEKGKNVVRMTVRQNLPVIIRPGGLKRD-EAPWKHLVW 150
Cdd:COG3121   80 PLFRLEPGKSQTVRIIRTGPPlPQDRESLFRLNVDEIPPkdaSEEGKNTLQIALRTRIKLFYRPAGLKGSpEDAAEKLTW 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490273795 151 TLKAGRLSVSNPSPYVVRLGQIvTTLPQGASWSLPNAWILPGQQLALSGEDKKSEAKADRVRVFPATTWGFTVDSY 226
Cdd:COG3121  160 SLVGNGLTVTNPGPYYVTLSDL-SLGAGGKKLKKGLGMVLPGSTRRWPLPAGASLAAGGKVTWATINDYGGAVPLE 234
PapD_N pfam00345
Pili and flagellar-assembly chaperone, PapD N-terminal domain; C2 domain-like beta-sandwich ...
 26-139 1.65e-16

Pili and flagellar-assembly chaperone, PapD N-terminal domain; C2 domain-like beta-sandwich fold. This domain is the n-terminal part of the PapD chaperone protein for pilus and flagellar assembly.


Pssm-ID: 425623  Cd Length: 123  Bit Score: 73.01  E-value: 1.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273795   26 ILPETSVVIVEEEEGEGAINLKNTDAFPVLLLT----NLQDIEPDTGRL-LTITPPAARVEPGKTQRVRFILTsASSLKT 100
Cdd:pfam00345   1 VVLGGTRVIYPAGEKEASVTVSNTGDNPYLVQSwvddGNEEGTDEKAKApFIVTPPLFRLEPGQEQVLRIYTT-GPPLPT 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 490273795  101 --EHLMRVAFEGVPP---QEKGKNVVRMTVRQNLPVIIRPGGLK 139
Cdd:pfam00345  80 drESLFWLNVLEIPPkdkPKGGQNGLQLALRSRIKLFYRPAGLA 123
PRK09926 PRK09926
fimbrial chaperone;
44-169 5.81e-10

fimbrial chaperone;


Pssm-ID: 236634 [Multi-domain]  Cd Length: 246  Bit Score: 57.42  E-value: 5.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273795  44 INLKNTDAFPVLLLTNLQD----IEPDTGRL-LTITPPAARVEPGKTQRVRFILTSASSLKT--EHLMRVAFEGVPP--- 113
Cdd:PRK09926  45 VRLENKGNNPLLVQSWLDTgddnAEPGSIKVpFTATPPVSRIDPKRGQTIKLMYTASTALPKdrESVFWFNVLEVPPkpd 124

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490273795 114 --QEKGKNVVRMTVRQNLPVIIRPGGLKRD--EAPwKHLVWTLKAGR----LSVSNPSPYVVRL 169
Cdd:PRK09926 125 aeKVANQSLLQLAFRTRIKLFYRPDGLKGNpsEAP-LALKWSWAGSEgkasLRVTNPTPYYVSF 187
PRK15254 PRK15254
fimbrial chaperone protein StdC; Provisional
 33-167 4.70e-09

fimbrial chaperone protein StdC; Provisional


Pssm-ID: 185166 [Multi-domain]  Cd Length: 239  Bit Score: 54.78  E-value: 4.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273795  33 VIVEEEEGEGAINLKNTD-AFPVLLLTNLQDIEPDTGRLLTITPPAARVEPGKTQRVRFI----LTSASSLKTEHLMRVA 107
Cdd:PRK15254  25 IIMDAPQKTVAITLNNDDkTTPFLAQSWVTDADGVRTDALMALPPLQRIDAGQKSQVRITqvrgLTDKLPQDRETLFWFN 104

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490273795 108 FEGVPPQEKGKNVVRMTVRQNLPVIIRPGGLKRDEA--PWKHLVWTLKAGRLSVSNPSPYVV 167
Cdd:PRK15254 105 VRGVPPKPEDDNVLQLAMQSQLKLFYRPKAIIRSSSdqPERKLTAERNAGHLTLRNPTPYYI 166
PRK15274 PRK15274
putative periplasmic fimbrial chaperone protein SteC; Provisional
 8-165 3.40e-08

putative periplasmic fimbrial chaperone protein SteC; Provisional


Pssm-ID: 185177 [Multi-domain]  Cd Length: 257  Bit Score: 52.47  E-value: 3.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273795   8 AAIAPVLwFFAPSLNATGILPETSVVIVEEEEGEGAINLKNTDA-FPVLLLTNLQD--IEPDTgRLLTITPPAARVEPGK 84
Cdd:PRK15274  11 ALIASVL-LAAPLVSHSAIVPDRTRVIFNGNENSITVTLKNGNAtLPYLAQAWLEDdkFAKDT-RYFTALPPLQRIEPKS 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273795  85 TQRVRF-ILTSASSLKT--EHLMRVAFEGVPPQEKGKNVVRMTVRQNLPVIIRPGGLKRD---EAPWK-HLVWTLKAGRL 157
Cdd:PRK15274  89 DGQVKVqPLPAAASLPQdrESLFYFNVREIPPKSDKPNTLQLALQTRIKFFYRPVAVARQvdkTHPWQtKLTLTYQGDGV 168


                 ....*...
gi 490273795 158 SVSNPSPY 165
Cdd:PRK15274 169 IFDNPTPF 176
PRK15246 PRK15246
fimbrial assembly chaperone;
43-169 4.95e-08

fimbrial assembly chaperone;


Pssm-ID: 185158 [Multi-domain]  Cd Length: 233  Bit Score: 51.88  E-value: 4.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273795  43 AINLKNTDAFPVLL--LTNLQDIE--PDTGRL-LTITPPAARVEPGKTQRVRFILTSASSLKT--EHLMRVAFEGVPP-Q 114
Cdd:PRK15246  29 SLTLSNDNTTPMLLqvWTDAGNIDasPDNSKTpLVALPPVFKMQPGELRTLRLLLSSRQQLATdrESLFWLNIYQIPPvT 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490273795 115 EKGKNVVRMTV---RQNLPVIIRPGGLKR-DEAPWKHLVWTLKAGRLSVSNPSPYVVRL 169
Cdd:PRK15246 109 QDIKNHPRKLVlplRLRLKILIRPTGLKApTEAEEKKLRFIAKENTIRIVNPTSWYMSL 167
PRK15299 PRK15299
fimbrial chaperone protein StiB; Provisional
 22-186 1.82e-07

fimbrial chaperone protein StiB; Provisional


Pssm-ID: 185199 [Multi-domain]  Cd Length: 227  Bit Score: 50.16  E-value: 1.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273795  22 NATGILPETSVVIVEEEEGEGAINLKNTDAFPVLLLTNLQDIEpDTGRL----LTITPPAARVEPGKTQRVRFILTSAS- 96
Cdd:PRK15299  20 HAAGINIGTTRVIFHGDAKDASISISNSDNVPYLIQSWAQSIS-ETGASgdapFMVTPPLFRLNGGQKNVLRIIRTGGNl 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273795  97 SLKTEHLMRVAFEGVP---PQEKgKNVVRMTVRQNLPVIIRPGGL-KRDEAPWKHLVWTLKAGRLSVSNPSP-------- 164
Cdd:PRK15299  99 PEDRESLYWLDIKSIPssnPDNK-HNTLMLAVKAEFKLIYRPKALtQKPEEVADRLTWSRQGRTLTVKNPTPyymnfatl 177

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 490273795 165 -----------YVVRLGQIVTTLPQGAS----WSLPN 186
Cdd:PRK15299 178 svgsqkvkaprYVAPFGNAQYTLPAAASgpiaWSIIN 214
PRK15208 PRK15208
molecular chaperone LpfB;
73-172 2.08e-07

molecular chaperone LpfB;


Pssm-ID: 237925 [Multi-domain]  Cd Length: 228  Bit Score: 49.91  E-value: 2.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273795  73 ITPPAARVEPGKTQRVRFILTSASSLKT-EHLMRVAFEGVPPQE---KGKNVVRMTVRQNLPVIIRPGGLKRD-EAPWKH 147
Cdd:PRK15208  71 ITPPLFKLDPTKNNVLRIVNITNTLPQDrESVYWINVKAIPAKSedaENKNVLQIAVRTRLKLFYRPAGLKGNsMDAWNK 150

                         90       100
                 ....*....|....*....|....*
gi 490273795 148 LVWTLKAGRLSVSNPSPYVVRLGQI 172
Cdd:PRK15208 151 LRFTRAGNQIKVENPSAFNLTFNQF 175
PRK15192 PRK15192
pili/flagellar-assembly chaperone;
71-169 7.48e-07

pili/flagellar-assembly chaperone;


Pssm-ID: 185114 [Multi-domain]  Cd Length: 234  Bit Score: 48.54  E-value: 7.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273795  71 LTITPPAARVEPGKTQRVRFILTSAS-SLKTEHLMRVAFEGVPPQEKGKNVVRMTVRQNLPVIIRPGGLKRD-EAPWKHL 148
Cdd:PRK15192  76 FVVTPPLFMLSARQENSMRVVYTGAPlPADRESLFTLSIAAIPSGKPEANRVQMAFRSALKLLYRPEGLAGNpQQAYRHL 155

                         90       100
                 ....*....|....*....|.
gi 490273795 149 VWTLKAGRLSVSNPSPYVVRL 169
Cdd:PRK15192 156 IWSLTPDGATVRNPTPYYVTL 176
PRK15249 PRK15249
fimbrial chaperone;
44-213 1.08e-06

fimbrial chaperone;


Pssm-ID: 237930 [Multi-domain]  Cd Length: 253  Bit Score: 48.26  E-value: 1.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273795  44 INLKNTDAFPVLLLTNLQD----IEPDTGRLL--TITPPAARVEPGKTQRVRFILTSASSL--KTEHLMRVAFEGVPP-- 113
Cdd:PRK15249  48 VQLKNNDAIPYIVQTWFDDgdmnTSPENSSAMpfIATPPVFRIQPKAGQVVRVIYNNTKKLpqDRESVFWFNVLQVPPtn 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273795 114 --QEKGKNVVRMTVRQNLPVIIRPGGLKRDEAPWKHL-VWTLKAGR----LSVSNPSPYVVRLGQIVTTLpQGASWSLPN 186
Cdd:PRK15249 128 igSDSGQNKMLVMLRSRIKLFYRPDGLGKPDNLAKKLqIKTVNKGSgksgIVIVNPQPWFASLSNLNVKV-NGASYNLDA 206

                        170       180
                 ....*....|....*....|....*....
gi 490273795 187 AWILP--GQQLALSGeDKKSEAKADRVRV 213
Cdd:PRK15249 207 DMIAPfsSQTWWLPG-KRSLKSFSGTVTV 234
PRK15285 PRK15285
fimbrial chaperone StfD;
25-200 1.35e-06

fimbrial chaperone StfD;


Pssm-ID: 185185 [Multi-domain]  Cd Length: 250  Bit Score: 47.85  E-value: 1.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273795  25 GILPETSVVIVEEEEGEGAINLKNTDA-FPVLLLTNLQDIEP-DTGRLLTITPPAARVEPGKTQRVRFI-LTSASSLKT- 100
Cdd:PRK15285  26 AIAPDRTRLVFRGEDKSISVDLKNANSkLPYLAQSWVEDEKGvKITSPLIVVPPVQRIEPSAIGQVKIQgMPALASLPQd 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273795 101 -EHLMRVAFEGVPPQEKGKNVVRMTVRQNLPVIIRPGGLKRDEA--PWKHLVWTLKAGR-LSVSNPSPYVVRLGQIVTTL 176
Cdd:PRK15285 106 rETLFYYNVREIPPQSDKPNTLQIALQTRIKVFYRPQALSKIDMqhPWQYKITLQRQGNgYQVSNPTGYYVVLSNASNRM 185

                        170       180
                 ....*....|....*....|....
gi 490273795 177 PQGASWSLPNAWILPGQQLALSGE 200
Cdd:PRK15285 186 DGTPARGFSPLVIAPKSNVTLGGD 209
PRK11385 PRK11385
fimbrial chaperone;
71-191 1.20e-05

fimbrial chaperone;


Pssm-ID: 183112 [Multi-domain]  Cd Length: 236  Bit Score: 45.12  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273795  71 LTITPPAARVEPGKTQRVRFILTSASSLKT--EHLMRVAFEGVPPQEKGKNVVRMTVRQNLPVIIRPGGLKRDE-APWKH 147
Cdd:PRK11385  80 LLAAPPLILLKPGTTGTLRLLRTESDILPVdrETLFELSIASVPSGKVENQSVKVAMRSVFKLFWRPEGLPGDPlEAYQQ 159

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 490273795 148 LVWTLKAGRLSVSNPSPYVVRLGQIVTTlpqgaSWSLPNAWILP 191
Cdd:PRK11385 160 LRWTRNSQGVQLTNPTPYYINLIQVSVN-----GKALSNAGVVP 198
PRK15224 PRK15224
pili assembly chaperone PapD;
33-172 6.72e-05

pili assembly chaperone PapD;


Pssm-ID: 185146 [Multi-domain]  Cd Length: 237  Bit Score: 42.81  E-value: 6.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273795  33 VIVEEEEGEGAINLKNTDAFPVLLLTNLQDIEPDTGRLLTITPPAARVEPGKTQRVRFILTSAS-SLKTEHLMRVAFEGV 111
Cdd:PRK15224  37 VIYHAGTAGATLSVSNPQNYPILVQSSVKAADKSSPAPFLVMPPLFRLEANQQSQLRIVRTGGDmPTDRETLQWVCIKAV 116

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273795 112 PP-------QEKGKNV-VRMTVRQNLPVIIRPGGLK-RDEAPWKHLVWTLKAGRLSVSNPSPYVVRLGQI 172
Cdd:PRK15224 117 PPenepsdtQAKGATLdLNLSINVCDKLIFRPDAVKgTPEDVAGNLRWVETGNKLKVENPTPFYMNLASV 186
PRK15233 PRK15233
fimbrial chaperone SefB;
30-199 2.84e-04

fimbrial chaperone SefB;


Pssm-ID: 185149 [Multi-domain]  Cd Length: 246  Bit Score: 40.86  E-value: 2.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273795  30 TSVVIVEEEEGEGAINLKNTDAFPVLLLTNLQDIEPDTGRLLTITPPAARVEPGKTQRVRFILTSASSLKTEH-LMRVAF 108
Cdd:PRK15233  46 TTRVIYKEDAPSTSFWIMNEKEYPILVQTQVYNDDKSSKAPFIVTPPILKVESNARTRLKVIPTSNLFNKNEEsLYWLCV 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273795 109 EGVPP----QEKGKNVVRMTVRQN------LPVIIRPGGLKRDEAP-WKHLVWTLKAGRLSVSNPSPYVVRLGQIVTTlp 177
Cdd:PRK15233 126 KGVPPlndnESNNKNNITTNLNVNvvtnscIKLIYRPKTIDLTTMEiADKLKLERKGNSIVIKNPTSSYVNIANIKSG-- 203

                        170       180
                 ....*....|....*....|..
gi 490273795 178 qGASWSLPNAWILPGQQLALSG 199
Cdd:PRK15233 204 -NLSFNIPNGYIEPFGYAQLPG 224
PRK15188 PRK15188
fimbrial chaperone protein BcfB; Provisional
 73-197 3.99e-04

fimbrial chaperone protein BcfB; Provisional


Pssm-ID: 185110 [Multi-domain]  Cd Length: 228  Bit Score: 40.52  E-value: 3.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273795  73 ITPPAARVEPGKTQRVRfILTSASSLKT--EHLMRVAFEGVPPQEKGK---NVVRMTVRQNLPVIIRPGGLKrdEAPwKH 147
Cdd:PRK15188  77 ITPPLFVIQPKKENILR-IMYVGPSLPTdrESVFYLNSKAIPSVDKNKltgNSLQIATQSVIKLFIRPKNLA--EAP-AH 152

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490273795 148 LVWTLKA----GRLSVSNPSPYVVRLGQIvttlpQGASWSLPNAWILPGQQLAL 197
Cdd:PRK15188 153 APSTLRCrnerGQLTITNPSPYYVSMVEL-----YSAGKKLPNTMVPPKGAITL 201
PRK15195 PRK15195
molecular chaperone FimC;
63-191 2.23e-03

molecular chaperone FimC;


Pssm-ID: 185117 [Multi-domain]  Cd Length: 229  Bit Score: 38.30  E-value: 2.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273795  63 IEPDTG---RLLTITPPAARVEPGKTQRVRFILTS-ASSLKTEHLMRVAFEGVPPQEK----GKNVVRMTVRQNLPVIIR 134
Cdd:PRK15195  62 IENSSGvkeKSFIVTPPLFVSEPKSENTLRIIYAGpPLAADRESLFWMNVKAIPSVDKnaleGRNVLQLAILSRIKLFVR 141

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490273795 135 PGGLKR--DEAPwKHLVWTLKAGRLSVSNPSPYVVRLGQIvttlpQGASWSLPNAWILP 191
Cdd:PRK15195 142 PINLQElpEEAP-DTLKFSRSGNHLKVHNPSPYYVTLVNL-----QVGSQKLGNAMIAP 194
PRK15218 PRK15218
fimbrial assembly chaperone;
73-173 2.67e-03

fimbrial assembly chaperone;


Pssm-ID: 185140 [Multi-domain]  Cd Length: 226  Bit Score: 38.04  E-value: 2.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490273795  73 ITPPAARVEPGKTQRVRfILTSASSL--KTEHLMRVAFEGVPP---QEKGKNVVRMTVRQNLPVIIRPGGL-KRDEAPWK 146
Cdd:PRK15218  72 MTPPVIRVAANSGQQLK-IKKLANNLpgDRESLFYLNVLDIPPnsdENKDKNIIKFALQNRIKLIYRPPGVqKVDKATFS 150

                         90       100
                 ....*....|....*....|....*..
gi 490273795 147 HLVWTLKAGRLSVSNPSPYVVRLGQIV 173
Cdd:PRK15218 151 RLQLLRAPGSISVKNNSANWITIPEIK 177
CuRO_2_AAO_like_2 cd13873
The second cupredoxin domain of plant Ascorbate oxidase homologs; This family includes plant ...
 74-110 6.54e-03

The second cupredoxin domain of plant Ascorbate oxidase homologs; This family includes plant laccases similar to ascorbate oxidase. Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. Ascorbate oxidase belongs to multicopper oxidase (MCO) family which couples oxidation of substrates with reduction of dioxygen to water. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259941 [Multi-domain]  Cd Length: 161  Bit Score: 36.11  E-value: 6.54e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 490273795  74 TPPAARVEPGKTQRVRFILTSASSLKTehlmrVAFEG 110
Cdd:cd13873   59 HPPVIDVEPGKTYRFRFIGATALSFVS-----LGIEG 90
PapD_C pfam02753
Pili assembly chaperone PapD, C-terminal domain; Ig-like beta-sandwich fold. This domain is ...
 159-213 7.09e-03

Pili assembly chaperone PapD, C-terminal domain; Ig-like beta-sandwich fold. This domain is the C-terminal part of the pilus and flagellar-assembly chaperone protein PapD.


Pssm-ID: 426960 [Multi-domain]  Cd Length: 63  Bit Score: 34.16  E-value: 7.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 490273795  159 VSNPSPYVVRLGQIvTTLPQGASWSLPNAWILPGQQLALSGedKKSEAKADRVRV 213
Cdd:pfam02753   1 VKNPTPYYVTFSSL-SLGGGGKELALDPGMVAPFSSQTFAG--LPAPAAGGTVSY 52
 
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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