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Conserved domains on  [gi|446760985|ref|WP_000838241|]
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MULTISPECIES: FKBP-type peptidyl-prolyl cis-trans isomerase [Vibrio]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10902 super family cl29493
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
1-257 2.64e-89

FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional


The actual alignment was detected with superfamily member PRK10902:

Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 265.47  E-value: 2.64e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446760985   1 MKSLFKVSLLAATVMLAVGCQKEEAPKTETTPAAQTAAAKtveFKSEDDKAAYAIGVSFANYLKTSIEKPSEIGIDLNKD 80
Cdd:PRK10902   1 MKSLFKVTLLATTMAVALNAPITFAADAAKPAATADSKAA---FKNDDQQSAYALGASLGRYMENSLKEQEKLGIKLDKD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446760985  81 LVLKGIEHVFAGNPEMSEEETRAALEALDKRVAETMQAKAAEKAAENKKKGDEFRAQFEKESGVVKTQSGLLYQVMTPAE 160
Cdd:PRK10902  78 QLIAGVQDAFADKSKLSDQEIEQTLQAFEARVKSAAQAKMEKDAADNEAKGKKYREKFAKEKGVKTTSTGLLYKVEKEGT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446760985 161 GDKPKDTDTVQVHYKGTLIDGSQFDSSYERGEPATFPLNRVIPGWTEGVQLMSVGSKFKLVIPPELAYGEQDTPTIPANS 240
Cdd:PRK10902 158 GEAPKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPGIPANS 237
                        250
                 ....*....|....*..
gi 446760985 241 TLVFEVELLKIENGKDA 257
Cdd:PRK10902 238 TLVFDVELLDVKPAPKA 254
 
Name Accession Description Interval E-value
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
1-257 2.64e-89

FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 265.47  E-value: 2.64e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446760985   1 MKSLFKVSLLAATVMLAVGCQKEEAPKTETTPAAQTAAAKtveFKSEDDKAAYAIGVSFANYLKTSIEKPSEIGIDLNKD 80
Cdd:PRK10902   1 MKSLFKVTLLATTMAVALNAPITFAADAAKPAATADSKAA---FKNDDQQSAYALGASLGRYMENSLKEQEKLGIKLDKD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446760985  81 LVLKGIEHVFAGNPEMSEEETRAALEALDKRVAETMQAKAAEKAAENKKKGDEFRAQFEKESGVVKTQSGLLYQVMTPAE 160
Cdd:PRK10902  78 QLIAGVQDAFADKSKLSDQEIEQTLQAFEARVKSAAQAKMEKDAADNEAKGKKYREKFAKEKGVKTTSTGLLYKVEKEGT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446760985 161 GDKPKDTDTVQVHYKGTLIDGSQFDSSYERGEPATFPLNRVIPGWTEGVQLMSVGSKFKLVIPPELAYGEQDTPTIPANS 240
Cdd:PRK10902 158 GEAPKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPGIPANS 237
                        250
                 ....*....|....*..
gi 446760985 241 TLVFEVELLKIENGKDA 257
Cdd:PRK10902 238 TLVFDVELLDVKPAPKA 254
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
151-251 6.34e-54

FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 169.59  E-value: 6.34e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446760985 151 LLYQVMTPAEGDKPKDTDTVQVHYKGTLIDGSQFDSSYERGEPATFPLN--RVIPGWTEGVQLMSVGSKFKLVIPPELAY 228
Cdd:COG0545    1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGvgQVIPGWDEGLQGMKVGGKRRLVIPPELAY 80
                         90       100
                 ....*....|....*....|....
gi 446760985 229 GEQ-DTPTIPANSTLVFEVELLKI 251
Cdd:COG0545   81 GERgAGGVIPPNSTLVFEVELLDV 104
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
163-249 3.23e-40

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 134.25  E-value: 3.23e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446760985  163 KPKDTDTVQVHYKGTLIDGSQFDSSYERGEPATFPL--NRVIPGWTEGVQLMSVGSKFKLVIPPELAYGEQDT--PTIPA 238
Cdd:pfam00254   4 KAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLgsGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLagPVIPP 83
                          90
                  ....*....|.
gi 446760985  239 NSTLVFEVELL 249
Cdd:pfam00254  84 NATLVFEVELL 94
 
Name Accession Description Interval E-value
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
1-257 2.64e-89

FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 265.47  E-value: 2.64e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446760985   1 MKSLFKVSLLAATVMLAVGCQKEEAPKTETTPAAQTAAAKtveFKSEDDKAAYAIGVSFANYLKTSIEKPSEIGIDLNKD 80
Cdd:PRK10902   1 MKSLFKVTLLATTMAVALNAPITFAADAAKPAATADSKAA---FKNDDQQSAYALGASLGRYMENSLKEQEKLGIKLDKD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446760985  81 LVLKGIEHVFAGNPEMSEEETRAALEALDKRVAETMQAKAAEKAAENKKKGDEFRAQFEKESGVVKTQSGLLYQVMTPAE 160
Cdd:PRK10902  78 QLIAGVQDAFADKSKLSDQEIEQTLQAFEARVKSAAQAKMEKDAADNEAKGKKYREKFAKEKGVKTTSTGLLYKVEKEGT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446760985 161 GDKPKDTDTVQVHYKGTLIDGSQFDSSYERGEPATFPLNRVIPGWTEGVQLMSVGSKFKLVIPPELAYGEQDTPTIPANS 240
Cdd:PRK10902 158 GEAPKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPGIPANS 237
                        250
                 ....*....|....*..
gi 446760985 241 TLVFEVELLKIENGKDA 257
Cdd:PRK10902 238 TLVFDVELLDVKPAPKA 254
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
151-251 6.34e-54

FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 169.59  E-value: 6.34e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446760985 151 LLYQVMTPAEGDKPKDTDTVQVHYKGTLIDGSQFDSSYERGEPATFPLN--RVIPGWTEGVQLMSVGSKFKLVIPPELAY 228
Cdd:COG0545    1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGvgQVIPGWDEGLQGMKVGGKRRLVIPPELAY 80
                         90       100
                 ....*....|....*....|....
gi 446760985 229 GEQ-DTPTIPANSTLVFEVELLKI 251
Cdd:COG0545   81 GERgAGGVIPPNSTLVFEVELLDV 104
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
44-251 1.40e-46

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 154.19  E-value: 1.40e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446760985  44 FKSEDDKAAYAIGVSFANYLktsiekpSEIGID-LNKDLVLKGIEHVFAGN-PEMSEEETRAALEALDKRVAETMQAKAA 121
Cdd:PRK11570   6 FDSIEAQASYGIGLQVGQQL-------SESGLEgLLPEALVAGLADALEGKhPAVPVDVVHRALREIHERADAVRRERQQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446760985 122 EKAAEnkkkGDEFRAQFEKESGVVKTQSGLLYQVMTPAEGDKPKDTDTVQVHYKGTLIDGSQFDSSYERGEPATFPLNRV 201
Cdd:PRK11570  79 AMAAE----GVKFLEENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGV 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446760985 202 IPGWTEGVQLMSVGSKFKLVIPPELAYGEQDT-PTIPANSTLVFEVELLKI 251
Cdd:PRK11570 155 IPGWIEALTLMPVGSKWELTIPHELAYGERGAgASIPPFSTLVFEVELLEI 205
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
163-249 3.23e-40

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 134.25  E-value: 3.23e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446760985  163 KPKDTDTVQVHYKGTLIDGSQFDSSYERGEPATFPL--NRVIPGWTEGVQLMSVGSKFKLVIPPELAYGEQDT--PTIPA 238
Cdd:pfam00254   4 KAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLgsGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLagPVIPP 83
                          90
                  ....*....|.
gi 446760985  239 NSTLVFEVELL 249
Cdd:pfam00254  84 NATLVFEVELL 94
FKBP_N pfam01346
Domain amino terminal to FKBP-type peptidyl-prolyl isomerase; This family is only found at the ...
48-155 4.30e-22

Domain amino terminal to FKBP-type peptidyl-prolyl isomerase; This family is only found at the amino terminus of pfam00254. This entry represents the N-terminal domain found in FKBP-type peptidylprolyl isomerases (PPIase). The N-terminal domain forms the dimer interface by the mutual exchange of two beta-strands between monomers.


Pssm-ID: 460169  Cd Length: 97  Bit Score: 87.55  E-value: 4.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446760985   48 DDKAAYAIGVSFANYLKTSiekpseiGIDLNKDLVLKGIEHVFAGNPEMSEEETRAALEALDKRvaetMQAKAAEKAAEN 127
Cdd:pfam01346   1 KDKVSYAIGLQIGQQLKQQ-------GIELDLDAFLAGLKDALAGKPLLTDEEAQEALQAFQEK----LQAKQEEQAEKN 69
                          90       100
                  ....*....|....*....|....*...
gi 446760985  128 KKKGDEFRAQFEKESGVVKTQSGLLYQV 155
Cdd:pfam01346  70 KAEGEAFLAENKKKEGVKTTESGLQYKV 97
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
165-232 7.33e-13

Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 63.97  E-value: 7.33e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446760985 165 KDTDTVQVHYKGTLIDGSQFDSSYERgEPATFPL--NRVIPGWTEGVQLMSVGSKFKLVIPPELAYGEQD 232
Cdd:COG1047    2 EKGDVVTLHYTLKLEDGEVFDSTFEG-EPLEFLHgaGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGERD 70
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
167-230 1.03e-03

FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 38.53  E-value: 1.03e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446760985 167 TDTVQ------VHYKGTLIDGSQFDSSYERGEPATFPL--NRVIPGWTEGVQLMSVGSKFKLVIPPELAYGE 230
Cdd:PRK15095   2 SESVQsnsavlVHFTLKLDDGSTAESTRNNGKPALFRLgdGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFGV 73
 
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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