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Conserved domains on  [gi|511333615|gb|EPC06484|]
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hypothetical protein HMPREF0433_01796 [Gemella sanguinis M325]

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

 Zoom to residue level

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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, ...
 23-169 6.98e-46

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


:

Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 147.80  E-value: 6.98e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511333615  23 QYHLAHILISVksssnPNGLSDEEAKKKAEEVLKKIKDGGDFATLAKEYSNDTGNASNGGDLGWSSKEDnsYVSEFNNAA 102
Cdd:COG0760    8 EVRASHILVKV-----PPSEDRAKAEAKAEELLAQLKAGADFAELAKEYSQDPGSAANGGDLGWFSRGQ--LVPEFEEAA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511333615 103 YALNKDQVSDVVKTPFGYHIIKVLDTKDS---SYDELKTSLEEKAAEQAVKndstivsKALKKLFEEYNV 169
Cdd:COG0760   81 FALKPGEISGPVKTQFGYHIIKVEDRRPAetpPFEEVKQQIRQELFQQALE-------AWLEELRKKAKI 143
 
Name Accession Description Interval E-value
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 23-169 6.98e-46

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 147.80  E-value: 6.98e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511333615  23 QYHLAHILISVksssnPNGLSDEEAKKKAEEVLKKIKDGGDFATLAKEYSNDTGNASNGGDLGWSSKEDnsYVSEFNNAA 102
Cdd:COG0760    8 EVRASHILVKV-----PPSEDRAKAEAKAEELLAQLKAGADFAELAKEYSQDPGSAANGGDLGWFSRGQ--LVPEFEEAA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511333615 103 YALNKDQVSDVVKTPFGYHIIKVLDTKDS---SYDELKTSLEEKAAEQAVKndstivsKALKKLFEEYNV 169
Cdd:COG0760   81 FALKPGEISGPVKTQFGYHIIKVEDRRPAetpPFEEVKQQIRQELFQQALE-------AWLEELRKKAKI 143
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 25-129 3.18e-32

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: 112.08  E-value: 3.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511333615   25 HLAHILISvksSSNPNGLSDEEAKKKAEEVLKKIKDGGDFATLAKEYSNDTGNASNGGDLGWSSKEDNsyVSEFNNAAYA 104
Cdd:pfam13616  17 KASHILIS---YSQAVSRTEEEAKAKADSLLAALKNGADFAALAKTYSDDPASKNNGGDLGWFTKGQM--VKEFEDAVFS 91

                          90       100
                  ....*....|....*....|....*
gi 511333615  105 LNKDQVSDVVKTPFGYHIIKVLDTK 129
Cdd:pfam13616  92 LKVGEISGVVKTQFGFHIIKVTDKK 116
prsA PRK00059
peptidylprolyl isomerase; Provisional
 8-161 2.92e-23

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 94.39  E-value: 2.92e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511333615   8 ITEDKLKESYEKNKHQY-------HLAHILISvksssnpnglSDEEAKKkaeeVLKKIKDGGDFATLAKEYSNDTGNASN 80
Cdd:PRK00059 174 VTDKDAQKYYNENKSKFtekpntmHLAHILVK----------TEDEAKK----VKKRLDKGEDFAKVAKEVSQDPGSKDK 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511333615  81 GGDLGWSSKEDNSYVSEFNNAAYALNKDQVSDVVKTPFGYHIIKVLDTKDSSY-------DELKTSLEEKAAEQAVKNDS 153
Cdd:PRK00059 240 GGDLGDVPYSDSGYDKEFMDGAKALKEGEISAPVKTQFGYHIIKAIKKKEYPVkpfdsvkEDIKKQLLQEKQSEVFKKKI 319


                 ....*...
gi 511333615 154 TIVSKALK 161
Cdd:PRK00059 320 EEWKKALK 327
 
Name Accession Description Interval E-value
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 23-169 6.98e-46

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 147.80  E-value: 6.98e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511333615  23 QYHLAHILISVksssnPNGLSDEEAKKKAEEVLKKIKDGGDFATLAKEYSNDTGNASNGGDLGWSSKEDnsYVSEFNNAA 102
Cdd:COG0760    8 EVRASHILVKV-----PPSEDRAKAEAKAEELLAQLKAGADFAELAKEYSQDPGSAANGGDLGWFSRGQ--LVPEFEEAA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511333615 103 YALNKDQVSDVVKTPFGYHIIKVLDTKDS---SYDELKTSLEEKAAEQAVKndstivsKALKKLFEEYNV 169
Cdd:COG0760   81 FALKPGEISGPVKTQFGYHIIKVEDRRPAetpPFEEVKQQIRQELFQQALE-------AWLEELRKKAKI 143
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 25-129 3.18e-32

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: 112.08  E-value: 3.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511333615   25 HLAHILISvksSSNPNGLSDEEAKKKAEEVLKKIKDGGDFATLAKEYSNDTGNASNGGDLGWSSKEDNsyVSEFNNAAYA 104
Cdd:pfam13616  17 KASHILIS---YSQAVSRTEEEAKAKADSLLAALKNGADFAALAKTYSDDPASKNNGGDLGWFTKGQM--VKEFEDAVFS 91

                          90       100
                  ....*....|....*....|....*
gi 511333615  105 LNKDQVSDVVKTPFGYHIIKVLDTK 129
Cdd:pfam13616  92 LKVGEISGVVKTQFGFHIIKVTDKK 116
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 28-127 3.46e-32

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: 111.24  E-value: 3.46e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511333615   28 HILISVKSSSnpnGLSDEEAKKKAEEVLKKIKDGGD-FATLAKEYSNDTGNASNGGDLGWSSKEDnsYVSEFNNAAYALN 106
Cdd:pfam00639   1 HILIKTPEAS---ERDRAEAKAKAEEILEQLKSGEDsFAELARKYSDDCPSAANGGDLGWFTRGQ--LPPEFEKAAFALK 75

                          90       100
                  ....*....|....*....|.
gi 511333615  107 KDQVSDVVKTPFGYHIIKVLD 127
Cdd:pfam00639  76 PGEISGPVETRFGFHIIKLTD 96
prsA PRK00059
peptidylprolyl isomerase; Provisional
 8-161 2.92e-23

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 94.39  E-value: 2.92e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511333615   8 ITEDKLKESYEKNKHQY-------HLAHILISvksssnpnglSDEEAKKkaeeVLKKIKDGGDFATLAKEYSNDTGNASN 80
Cdd:PRK00059 174 VTDKDAQKYYNENKSKFtekpntmHLAHILVK----------TEDEAKK----VKKRLDKGEDFAKVAKEVSQDPGSKDK 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511333615  81 GGDLGWSSKEDNSYVSEFNNAAYALNKDQVSDVVKTPFGYHIIKVLDTKDSSY-------DELKTSLEEKAAEQAVKNDS 153
Cdd:PRK00059 240 GGDLGDVPYSDSGYDKEFMDGAKALKEGEISAPVKTQFGYHIIKAIKKKEYPVkpfdsvkEDIKKQLLQEKQSEVFKKKI 319


                 ....*...
gi 511333615 154 TIVSKALK 161
Cdd:PRK00059 320 EEWKKALK 327
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 25-150 1.07e-20

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 88.26  E-value: 1.07e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511333615  25 HLAHILIsvKSSSNpngLSDEEAKKKAEEVLKKIKDGG-DFATLAKEYSNDTGNASNGGDLGWSSKEdnSYVSEFNNAAY 103
Cdd:PRK10770 268 HARHILL--KPSPI---MTDEQARAKLEQIAADIKSGKtTFAAAAKEFSQDPGSANQGGDLGWATPD--IFDPAFRDALM 340

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 511333615 104 ALNKDQVSDVVKTPFGYHIIKVLDT----------KDSSY---------DELKTSLEEKAAEQAVK 150
Cdd:PRK10770 341 RLNKGQISAPVHSSFGWHLIELLDTrqvdktdaaqKDRAYrmlfnrkfsEEAQTWMQEQRASAYVK 406
prsA PRK03095
peptidylprolyl isomerase PrsA;
8-177 4.19e-20

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 85.05  E-value: 4.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511333615   8 ITEDKLKESYeknKHQYHLAHILISvksssnpnglsDEEAKKKAEEVLKKikdGGDFATLAKEYSNDTGNASNGGDLGWS 87
Cdd:PRK03095 120 ITDKELKDNY---KPEIKASHILVK-----------DEATAKKVKEELGQ---GKSFEELAKQYSEDTGSKEKGGDLGFF 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511333615  88 SKedNSYVSEFNNAAYALNKDQVSDVVKTPFGYHIIKVLDTK--DSSYDELKTSLEEKAAEQAvKNDSTIVSKALKKLFE 165
Cdd:PRK03095 183 GA--GKMVKEFEDAAYKLKKDEVSEPVKSQFGYHIIKVTDIKepEKSFEQSKADIKKELVQKK-AQDGEFMNDLMMKEIK 259

                        170
                 ....*....|..
gi 511333615 166 EYNVKSDNSDVE 177
Cdd:PRK03095 260 KADVKVDDKDLK 271
prsA PRK03002
peptidylprolyl isomerase PrsA;
8-177 5.48e-18

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 79.21  E-value: 5.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511333615   8 ITEDKLKESYeknKHQYHLAHILISvksssnpnglsDEEakkKAEEVLKKIKDGGDFATLAKEYSNDTGNASNGGDLGWS 87
Cdd:PRK03002 124 VTEKDVKDHY---KPEIKASHILVS-----------DEN---EAKEIKKKLDAGASFEELAKQESQDLLSKEKGGDLGYF 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511333615  88 SKedNSYVSEFNNAAYALNKDQVSDVVKTPFGYHIIKVLDTKD-SSYDELKTSLEEKAAEQAVKnDSTIVSKALKKLFEE 166
Cdd:PRK03002 187 NS--GRMAPEFETAAYKLKVGQISNPVKSPNGYHIIKLTDKKDlKPYDEVKDSIRKNLEEERTA-DPIFGKKLLQSELKK 263

                        170
                 ....*....|.
gi 511333615 167 YNVKSDNSDVE 177
Cdd:PRK03002 264 ANIKINDSELE 274
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 6-151 6.95e-18

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 78.86  E-value: 6.95e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511333615   6 AGITEDKLKESYeknKHQYHLAHILISvksssnpnglsDEeakKKAEEVLKKIKDGGDFATLAKEYSNDTGNASNGGDLg 85
Cdd:PRK02998 120 ATVTEKDVKDNY---KPEMKVSHILVK-----------DE---KTAKEVKEKVNNGEDFAALAKQYSEDTGSKEQGGEI- 181

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 511333615  86 wSSKEDNSYVSEFNNAAYALNKDQVSDVVKTPFGYHIIKVLDTKD-SSYDELKTSLEEKAAEQAVKN 151
Cdd:PRK02998 182 -SGFAPGQTVKEFEEAAYKLDAGQVSEPVKTTYGYHIIKVTDKKElKPFDEVKDSIRKDLEQQRLQD 247
prsA PRK04405
peptidylprolyl isomerase; Provisional
 8-190 6.80e-17

peptidylprolyl isomerase; Provisional


Pssm-ID: 235295 [Multi-domain]  Cd Length: 298  Bit Score: 76.36  E-value: 6.80e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511333615   8 ITEDKLKESYEKNKHQYHLAHILISVKSSsnpnglsdeeakkkAEEVLKKIKDGGDFATLAKEYSNDTGNASNGGDLGWS 87
Cdd:PRK04405 129 VTNSQLKKAWKSYQPKVTVQHILVSKKST--------------AETVIKKLKDGKDFAKLAKKYSTDTATKNKGGKLSAF 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511333615  88 SKEDNSYVSEFNNAAYALNKDQVSDV-VKTPFGYHIIKVLDT-KDSSYDELKTSLeEKAAEQAVKNDSTIVSKALKKLFE 165
Cdd:PRK04405 195 DSTDTTLDSTFKTAAFKLKNGEYTTTpVKTTYGYEVIKMIKHpAKGTFSDHKKAL-TKQIYAKWASDSSVMQRVISKVLK 273

                        170       180
                 ....*....|....*....|....*
gi 511333615 166 EYNVKSDNSDVEAYIKSMLEGSSSN 190
Cdd:PRK04405 274 KANVSIKDKDLKDALSSYLSSSSSS 298
PRK10788 PRK10788
periplasmic folding chaperone; Provisional
 8-143 1.44e-16

periplasmic folding chaperone; Provisional


Pssm-ID: 182731 [Multi-domain]  Cd Length: 623  Bit Score: 76.59  E-value: 1.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511333615   8 ITEDKLKESYEKNKHQYHLA----HILISVKSssnpnglsDEEAKkkaeEVLKKIKDGGDFATLAKEYSNDTGNASNGGD 83
Cdd:PRK10788 249 VSDADIQAYYDQHQDQFTQPerkrYSIIQTKT--------EAEAK----AVLDELKKGADFATLAKEKSTDIISARNGGD 316

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 511333615  84 LGWssKEDNSYVSEFNNAAYAlNKDQVSDVVKTPFGYHIIKVLDTKDS---SYDELKTSLEEK 143
Cdd:PRK10788 317 LGW--LEPATTPDELKNAGLK-EKGQLSGVIKSSVGFLIVRLDDIQPAkvkPLSEVRDDIAAK 376
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 25-127 3.79e-13

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 62.74  E-value: 3.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511333615  25 HLAHILISVKSSSNPNG--------LSDEEAKKKAEEVLKKIKDG-GDFATLAKEYSnDTGNASNGGDLGWSSKedNSYV 95
Cdd:PTZ00356   7 RAAHLLIKHTGSRNPVSrrtgkpvtRSKEEAIKELAKWREQIVSGeKTFEEIARQRS-DCGSAAKGGDLGFFGR--GQMQ 83

                         90       100       110
                 ....*....|....*....|....*....|..
gi 511333615  96 SEFNNAAYALNKDQVSDVVKTPFGYHIIKVLD 127
Cdd:PTZ00356  84 KPFEDAAFALKVGEISDIVHTDSGVHIILRLA 115
Rotamase_2 pfam13145
PPIC-type PPIASE domain;
8-131 1.30e-11

PPIC-type PPIASE domain;


Pssm-ID: 432992 [Multi-domain]  Cd Length: 121  Bit Score: 58.99  E-value: 1.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511333615    8 ITEDKLKESYEKNKHQYHLAHI---LISVKSSSNPNGLSDEEAKKKAEEvlkkikdggDFATLAKEYSNdtgnasNGGDL 84
Cdd:pfam13145   1 VTEEELKAYYEENKDEFSTPEGrllEILVFKDQVAADAALALLKAGALE---------DFAALAKGEGI------KAATL 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 511333615   85 GWSSKEDNsYVSEFNNAAYALNKDQVSDVVKTPFGYHIIKVLDTKDS 131
Cdd:pfam13145  66 DIVESAEL-LPEELAKAAFALKPGEVSGPIKTGNGYYVVRVTEIKPA 111
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 26-166 6.11e-11

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 60.14  E-value: 6.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511333615  26 LAHILISVksSSNPNGLSDEEAKKKAEEVLKKIKDGGDFATLAKEYSNDTgNASNGGDLGWSSKEDnsYVSEFNNAAYAL 105
Cdd:PRK10770 158 LSHILIPL--PENPTQDQVDEAESQARSIVDQARNGADFGKLAIAYSADQ-QALKGGQMGWGRIQE--LPGLFAQALSTA 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511333615 106 NKDQVSDVVKTPFGYHIIKVLDTKDS----SYDE-------LKTS-----------LEEKAAEqaVKNDSTIVSKALKKL 163
Cdd:PRK10770 233 KKGDIVGPIRSGVGFHILKVNDLRGEsqniSVTEvharhilLKPSpimtdeqarakLEQIAAD--IKSGKTTFAAAAKEF 310


                 ...
gi 511333615 164 FEE 166
Cdd:PRK10770 311 SQD 313
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 48-126 6.35e-08

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 48.48  E-value: 6.35e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 511333615  48 KKKAEEVLKKIKDGGDFATLAKEYSNdTGNASNGGDLGwsSKEDNSYVSEFNNAAYALNKDQVSDVVKTPFGYHIIKVL 126
Cdd:PRK15441  15 EKLALDLLEQIKNGADFGKLAKKHSI-CPSGKRGGDLG--EFRQGQMVPAFDKVVFSCPVLEPTGPLHTQFGYHIIKVL 90
prsA PRK01326
foldase protein PrsA; Reviewed
 46-170 1.20e-06

foldase protein PrsA; Reviewed


Pssm-ID: 179281 [Multi-domain]  Cd Length: 310  Bit Score: 47.50  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511333615  46 EAKKKAEEVLKKIK-DGGDFATLAKEYSNDTGNasnGGDLGWSSKEDNsYVSEFNNAAYALNKDQVSDVVKTP------F 118
Cdd:PRK01326 154 DNEDKAKSVLEEAKaEGADFAQIAKENTTTKEK---KGEYKFDSGSTN-VPEQVKKAAFALDEDGVSDVISVLdptayqS 229

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 511333615 119 GYHIIKVLDT--KDSSYDELKTSLEEKAAEQAvKNDSTIVSKALKKLFEEYNVK 170
Cdd:PRK01326 230 KYYIVKVTKKteKKSDWKDYKKRLKAIILAQK-QNDSNFQNKVIAKALDKANVK 282
 
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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