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Conserved domains on  [gi|767995519|ref|XP_011523402|]
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peptidyl-prolyl cis-trans isomerase FKBP10 isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
76-168 8.80e-39

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 136.56  E-value: 8.80e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995519   76 CPRMVQDGDFVRYHYNGTLLDGTSFDTSYSKGGTYDTYVGSGWLIKGMDQGLLGMCPGERRKIIIPPFLAYGEKGY-GTV 154
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPV 80

                          90
                  ....*....|....
gi 767995519  155 IPPQASLVFHVLLI 168
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
188-280 8.18e-36

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 128.47  E-value: 8.18e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995519  188 CVRRAGAGDFMRYHYNGSLMDGTLFDSSYSRNHTYNTYIGQGYIIPGMDQGLQGACMGERRRITIPPHLAYGENG-TGDK 266
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPV 80

                          90
                  ....*....|....
gi 767995519  267 IPGSAVLIFNVHVI 280
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
301-411 4.63e-28

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 107.28  E-value: 4.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995519  301 CNETTKLGDFVRYHYNCSLLDGTqLFTSGetdagshepsrphfrgqrHDYGAPQEATLGANKVIEGLDTGLQGMCVGERR 380
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGT-VFDSS------------------YDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKR 61

                          90       100       110
                  ....*....|....*....|....*....|...
gi 767995519  381 QLIVPPHLAHGESGARG--VPGSAVLLFEVELV 411
Cdd:pfam00254  62 KLTIPPELAYGEEGLAGpvIPPNATLVFEVELL 94
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
411-496 4.68e-08

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG5126:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 52.10  E-value: 4.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995519 411 VSREDgLPTGYLFVWHKdppanLFEDMDLNKDGEVPPEEFSTFIKAqvsegkgrlMPGQDPEKTIGDMFQNQDRNQDGKI 490
Cdd:COG5126   22 LERDD-FEALFRRLWAT-----LFSEADTDGDGRISREEFVAGMES---------LFEATVEPFARAAFDLLDTDGDGKI 86


                 ....*.
gi 767995519 491 TVDELK 496
Cdd:COG5126   87 SADEFR 92
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
76-168 8.80e-39

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 136.56  E-value: 8.80e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995519   76 CPRMVQDGDFVRYHYNGTLLDGTSFDTSYSKGGTYDTYVGSGWLIKGMDQGLLGMCPGERRKIIIPPFLAYGEKGY-GTV 154
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPV 80

                          90
                  ....*....|....
gi 767995519  155 IPPQASLVFHVLLI 168
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
188-280 8.18e-36

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 128.47  E-value: 8.18e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995519  188 CVRRAGAGDFMRYHYNGSLMDGTLFDSSYSRNHTYNTYIGQGYIIPGMDQGLQGACMGERRRITIPPHLAYGENG-TGDK 266
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPV 80

                          90
                  ....*....|....
gi 767995519  267 IPGSAVLIFNVHVI 280
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 80-170 3.80e-30

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 113.35  E-value: 3.80e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995519  80 VQDGDFVRYHYNGTLLDGTSFDTSYSKGGTYDTYVGSGWLIKGMDQGLLGMCPGERRKIIIPPFLAYGEKGYGTVIPPQA 159
Cdd:COG0545   14 PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPNS 93

                         90
                 ....*....|.
gi 767995519 160 SLVFHVLLIDV 170
Cdd:COG0545   94 TLVFEVELLDV 104
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 192-282 9.04e-30

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 112.20  E-value: 9.04e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995519 192 AGAGDFMRYHYNGSLMDGTLFDSSYSRNHTYNTYIGQGYIIPGMDQGLQGACMGERRRITIPPHLAYGENGTGDKIPGSA 271
Cdd:COG0545   14 PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPNS 93

                         90
                 ....*....|.
gi 767995519 272 VLIFNVHVIDF 282
Cdd:COG0545   94 TLVFEVELLDV 104
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
301-411 4.63e-28

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 107.28  E-value: 4.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995519  301 CNETTKLGDFVRYHYNCSLLDGTqLFTSGetdagshepsrphfrgqrHDYGAPQEATLGANKVIEGLDTGLQGMCVGERR 380
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGT-VFDSS------------------YDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKR 61

                          90       100       110
                  ....*....|....*....|....*....|...
gi 767995519  381 QLIVPPHLAHGESGARG--VPGSAVLLFEVELV 411
Cdd:pfam00254  62 KLTIPPELAYGEEGLAGpvIPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 303-412 7.22e-22

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 90.24  E-value: 7.22e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995519 303 ETTKLGDFVRYHYNCSLLDGTQLFTSGETdagshepsrphfrgqrhdyGAPQEATLGANKVIEGLDTGLQGMCVGERRQL 382
Cdd:COG0545   12 AKPKAGDTVTVHYTGTLLDGTVFDSSYDR-------------------GEPATFPLGVGQVIPGWDEGLQGMKVGGKRRL 72

                         90       100       110
                 ....*....|....*....|....*....|.
gi 767995519 383 IVPPHLAHGESGARGV-PGSAVLLFEVELVS 412
Cdd:COG0545   73 VIPPELAYGERGAGGViPPNSTLVFEVELLD 103
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 84-170 1.59e-14

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 72.52  E-value: 1.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995519  84 DFVRYHYNGTLLDGTSFDTSYSKGGTYDTYVGSgwLIKGMDQGLLGMCPGERRKIIIPPFLAYGEKGYGTVIPPQASLVF 163
Cdd:PRK11570 121 DRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNG--VIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLVF 198


                 ....*..
gi 767995519 164 HVLLIDV 170
Cdd:PRK11570 199 EVELLEI 205
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 189-281 2.58e-13

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 70.18  E-value: 2.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995519 189 VRRAGAG------DFMRYHYNGSLMDGTLFDSSYSRNHTYNtyIGQGYIIPGMDQGLQGACMGERRRITIPPHLAYGENG 262
Cdd:PRK10902 152 VEKEGTGeapkdsDTVVVNYKGTLIDGKEFDNSYTRGEPLS--FRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAG 229

                         90
                 ....*....|....*....
gi 767995519 263 TgDKIPGSAVLIFNVHVID 281
Cdd:PRK10902 230 V-PGIPANSTLVFDVELLD 247
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
411-496 4.68e-08

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 52.10  E-value: 4.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995519 411 VSREDgLPTGYLFVWHKdppanLFEDMDLNKDGEVPPEEFSTFIKAqvsegkgrlMPGQDPEKTIGDMFQNQDRNQDGKI 490
Cdd:COG5126   22 LERDD-FEALFRRLWAT-----LFSEADTDGDGRISREEFVAGMES---------LFEATVEPFARAAFDLLDTDGDGKI 86


                 ....*.
gi 767995519 491 TVDELK 496
Cdd:COG5126   87 SADEFR 92
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 309-411 9.97e-08

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 52.49  E-value: 9.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995519 309 DFVRYHYNCSLLDGTQLFTSGEtdagshepsrphfRGQrhdygaPQEatLGANKVIEGLDTGLQGMCVGERRQLIVPPHL 388
Cdd:PRK11570 121 DRVRVHYTGKLIDGTVFDSSVA-------------RGE------PAE--FPVNGVIPGWIEALTLMPVGSKWELTIPHEL 179

                         90       100
                 ....*....|....*....|....
gi 767995519 389 AHGESGA-RGVPGSAVLLFEVELV 411
Cdd:PRK11570 180 AYGERGAgASIPPFSTLVFEVELL 203
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 434-495 1.72e-06

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 45.23  E-value: 1.72e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767995519 434 FEDMDLNKDGEVPPEEFSTFIKAqvsegkgrLMPGQdPEKTIGDMFQNQDRNQDGKITVDEL 495
Cdd:cd00051    6 FRLFDKDGDGTISADELKAALKS--------LGEGL-SEEEIDEMIREVDKDGDGKIDFEEF 58
EF-hand_7 pfam13499
EF-hand domain pair;
433-496 1.76e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 36.85  E-value: 1.76e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767995519  433 LFEDMDLNKDGEVPPEEFSTFIKaqvsegkgRLMPGQDPEKT-IGDMFQNQDRNQDGKITVDELK 496
Cdd:pfam13499   7 AFKLLDSDGDGYLDVEELKKLLR--------KLEEGEPLSDEeVEELFKEFDLDKDGRISFEEFL 63
PLN02964 PLN02964
phosphatidylserine decarboxylase
 437-495 5.11e-03

phosphatidylserine decarboxylase


Pssm-ID: 215520 [Multi-domain]  Cd Length: 644  Bit Score: 39.46  E-value: 5.11e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767995519 437 MDLNKDGEVPPEEFSTFIKAqvsegKGRLMPGQDPEktigDMFQNQDRNQDGKITVDEL 495
Cdd:PLN02964 188 VDYDEDGQLSFSEFSDLIKA-----FGNLVAANKKE----ELFKAADLNGDGVVTIDEL 237
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
76-168 8.80e-39

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 136.56  E-value: 8.80e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995519   76 CPRMVQDGDFVRYHYNGTLLDGTSFDTSYSKGGTYDTYVGSGWLIKGMDQGLLGMCPGERRKIIIPPFLAYGEKGY-GTV 154
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPV 80

                          90
                  ....*....|....
gi 767995519  155 IPPQASLVFHVLLI 168
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
188-280 8.18e-36

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 128.47  E-value: 8.18e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995519  188 CVRRAGAGDFMRYHYNGSLMDGTLFDSSYSRNHTYNTYIGQGYIIPGMDQGLQGACMGERRRITIPPHLAYGENG-TGDK 266
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPV 80

                          90
                  ....*....|....
gi 767995519  267 IPGSAVLIFNVHVI 280
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 80-170 3.80e-30

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 113.35  E-value: 3.80e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995519  80 VQDGDFVRYHYNGTLLDGTSFDTSYSKGGTYDTYVGSGWLIKGMDQGLLGMCPGERRKIIIPPFLAYGEKGYGTVIPPQA 159
Cdd:COG0545   14 PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPNS 93

                         90
                 ....*....|.
gi 767995519 160 SLVFHVLLIDV 170
Cdd:COG0545   94 TLVFEVELLDV 104
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 192-282 9.04e-30

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 112.20  E-value: 9.04e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995519 192 AGAGDFMRYHYNGSLMDGTLFDSSYSRNHTYNTYIGQGYIIPGMDQGLQGACMGERRRITIPPHLAYGENGTGDKIPGSA 271
Cdd:COG0545   14 PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPNS 93

                         90
                 ....*....|.
gi 767995519 272 VLIFNVHVIDF 282
Cdd:COG0545   94 TLVFEVELLDV 104
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
301-411 4.63e-28

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 107.28  E-value: 4.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995519  301 CNETTKLGDFVRYHYNCSLLDGTqLFTSGetdagshepsrphfrgqrHDYGAPQEATLGANKVIEGLDTGLQGMCVGERR 380
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGT-VFDSS------------------YDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKR 61

                          90       100       110
                  ....*....|....*....|....*....|...
gi 767995519  381 QLIVPPHLAHGESGARG--VPGSAVLLFEVELV 411
Cdd:pfam00254  62 KLTIPPELAYGEEGLAGpvIPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 303-412 7.22e-22

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 90.24  E-value: 7.22e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995519 303 ETTKLGDFVRYHYNCSLLDGTQLFTSGETdagshepsrphfrgqrhdyGAPQEATLGANKVIEGLDTGLQGMCVGERRQL 382
Cdd:COG0545   12 AKPKAGDTVTVHYTGTLLDGTVFDSSYDR-------------------GEPATFPLGVGQVIPGWDEGLQGMKVGGKRRL 72

                         90       100       110
                 ....*....|....*....|....*....|.
gi 767995519 383 IVPPHLAHGESGARGV-PGSAVLLFEVELVS 412
Cdd:COG0545   73 VIPPELAYGERGAGGViPPNSTLVFEVELLD 103
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 84-170 1.59e-14

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 72.52  E-value: 1.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995519  84 DFVRYHYNGTLLDGTSFDTSYSKGGTYDTYVGSgwLIKGMDQGLLGMCPGERRKIIIPPFLAYGEKGYGTVIPPQASLVF 163
Cdd:PRK11570 121 DRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNG--VIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLVF 198


                 ....*..
gi 767995519 164 HVLLIDV 170
Cdd:PRK11570 199 EVELLEI 205
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 80-187 1.89e-14

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 70.13  E-value: 1.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995519  80 VQDGDFVRYHYNGTLLDGTSFDTSYskGGTYDTY-VGSGWLIKGMDQGLLGMCPGERRKIIIPPflaygEKGYGtviPPQ 158
Cdd:COG1047    1 IEKGDVVTLHYTLKLEDGEVFDSTF--EGEPLEFlHGAGQLIPGLEEALEGMEVGDKKTVTLPP-----EEAYG---ERD 70

                         90       100
                 ....*....|....*....|....*....
gi 767995519 159 ASLVFHVllidvhnPKDAVQlETLELPPG 187
Cdd:COG1047   71 PELVQTV-------PREQFP-EDEELEVG 91
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 189-281 2.58e-13

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 70.18  E-value: 2.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995519 189 VRRAGAG------DFMRYHYNGSLMDGTLFDSSYSRNHTYNtyIGQGYIIPGMDQGLQGACMGERRRITIPPHLAYGENG 262
Cdd:PRK10902 152 VEKEGTGeapkdsDTVVVNYKGTLIDGKEFDNSYTRGEPLS--FRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAG 229

                         90
                 ....*....|....*....
gi 767995519 263 TgDKIPGSAVLIFNVHVID 281
Cdd:PRK10902 230 V-PGIPANSTLVFDVELLD 247
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 196-281 3.81e-13

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 68.29  E-value: 3.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995519 196 DFMRYHYNGSLMDGTLFDSSYSRNHTYNTYIGQgyIIPGMDQGLQGACMGERRRITIPPHLAYGENGTGDKIPGSAVLIF 275
Cdd:PRK11570 121 DRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNG--VIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLVF 198


                 ....*.
gi 767995519 276 NVHVID 281
Cdd:PRK11570 199 EVELLE 204
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 82-176 1.84e-12

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 67.48  E-value: 1.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995519  82 DGDFVRYHYNGTLLDGTSFDTSYSKGGTYDTYVGSgwLIKGMDQGLLGMCPGERRKIIIPPFLAYGEKGYGTvIPPQASL 161
Cdd:PRK10902 163 DSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRLDG--VIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPG-IPANSTL 239

                         90
                 ....*....|....*
gi 767995519 162 VFHVLLIDVHNPKDA 176
Cdd:PRK10902 240 VFDVELLDVKPAPKA 254
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 194-260 8.04e-11

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 59.73  E-value: 8.04e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767995519 194 AGDFMRYHYNGSLMDGTLFDSSYSRN-HTYNtyIGQGYIIPGMDQGLQGACMGERRRITIPPHLAYGE 260
Cdd:COG1047    3 KGDVVTLHYTLKLEDGEVFDSTFEGEpLEFL--HGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGE 68
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
411-496 4.68e-08

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 52.10  E-value: 4.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995519 411 VSREDgLPTGYLFVWHKdppanLFEDMDLNKDGEVPPEEFSTFIKAqvsegkgrlMPGQDPEKTIGDMFQNQDRNQDGKI 490
Cdd:COG5126   22 LERDD-FEALFRRLWAT-----LFSEADTDGDGRISREEFVAGMES---------LFEATVEPFARAAFDLLDTDGDGKI 86


                 ....*.
gi 767995519 491 TVDELK 496
Cdd:COG5126   87 SADEFR 92
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 309-411 9.97e-08

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 52.49  E-value: 9.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995519 309 DFVRYHYNCSLLDGTQLFTSGEtdagshepsrphfRGQrhdygaPQEatLGANKVIEGLDTGLQGMCVGERRQLIVPPHL 388
Cdd:PRK11570 121 DRVRVHYTGKLIDGTVFDSSVA-------------RGE------PAE--FPVNGVIPGWIEALTLMPVGSKWELTIPHEL 179

                         90       100
                 ....*....|....*....|....
gi 767995519 389 AHGESGA-RGVPGSAVLLFEVELV 411
Cdd:PRK11570 180 AYGERGAgASIPPFSTLVFEVELL 203
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 303-412 1.01e-06

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 50.15  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995519 303 ETTKLGDFVRYHYNCSLLDGTQLFTSgetdagshepsrphfrgqrHDYGAPqeATLGANKVIEGLDTGLQGMCVGERRQL 382
Cdd:PRK10902 159 EAPKDSDTVVVNYKGTLIDGKEFDNS-------------------YTRGEP--LSFRLDGVIPGWTEGLKNIKKGGKIKL 217

                         90       100       110
                 ....*....|....*....|....*....|
gi 767995519 383 IVPPHLAHGESGARGVPGSAVLLFEVELVS 412
Cdd:PRK10902 218 VIPPELAYGKAGVPGIPANSTLVFDVELLD 247
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
433-496 1.59e-06

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 47.48  E-value: 1.59e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767995519 433 LFEDMDLNKDGEVPPEEFSTFIKAqvsegkgrlmpGQDPEKTIGDMFQNQDRNQDGKITVDELK 496
Cdd:COG5126   74 AFDLLDTDGDGKISADEFRRLLTA-----------LGVSEEEADELFARLDTDGDGKISFEEFV 126
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 434-495 1.72e-06

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 45.23  E-value: 1.72e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767995519 434 FEDMDLNKDGEVPPEEFSTFIKAqvsegkgrLMPGQdPEKTIGDMFQNQDRNQDGKITVDEL 495
Cdd:cd00051    6 FRLFDKDGDGTISADELKAALKS--------LGEGL-SEEEIDEMIREVDKDGDGKIDFEEF 58
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 308-392 1.86e-05

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 44.32  E-value: 1.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995519 308 GDFVRYHYNCSLLDGTQLFTSGEtdagshepsrphfrgqrhdyGAPQEATLGANKVIEGLDTGLQGMCVGERRQLIVPPH 387
Cdd:COG1047    4 GDVVTLHYTLKLEDGEVFDSTFE--------------------GEPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPE 63


                 ....*
gi 767995519 388 LAHGE 392
Cdd:COG1047   64 EAYGE 68
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 431-504 5.21e-04

EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This family corresponds to a group of uncharacterized RCN2-like proteins, which are mainly found in protostomes. Although their biological function remains unclear, they show high sequence similarity with RCN2 (also known as E6BP or TCBP-49), which is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. Members in this family contain six copies of the EF-hand Ca2+-binding motif, but may lack a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER).


Pssm-ID: 320025 [Multi-domain]  Cd Length: 263  Bit Score: 41.92  E-value: 5.21e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767995519 431 ANLFEDMDLNKDGEVPPEEFSTFIKaqvsegkgRLMPGQDPEKTIgDMFQNQDRNQDGKITVDELKLKS--DEDEE 504
Cdd:cd16227   39 AVLAKKMDLNDDGFIDRKELKAWIL--------RSFKMLDEEEAN-ERFEEADEDGDGKVTWEEYLADSfgYDDED 105
EF-hand_7 pfam13499
EF-hand domain pair;
433-496 1.76e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 36.85  E-value: 1.76e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767995519  433 LFEDMDLNKDGEVPPEEFSTFIKaqvsegkgRLMPGQDPEKT-IGDMFQNQDRNQDGKITVDELK 496
Cdd:pfam13499   7 AFKLLDSDGDGYLDVEELKKLLR--------KLEEGEPLSDEeVEELFKEFDLDKDGRISFEEFL 63
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 80-148 4.07e-03

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


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 38.15  E-value: 4.07e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767995519  80 VQDGDFVRYHYNGTLLDGTSFDTSYSKGGTYDTYVGSGWLIKGMDQGLLGMCPGERRKIIIPPFLAYGE 148
Cdd:PRK15095   5 VQSNSAVLVHFTLKLDDGSTAESTRNNGKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFGV 73
Tig COG0544
FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, ...
 78-138 4.08e-03

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


Pssm-ID: 440310 [Multi-domain]  Cd Length: 424  Bit Score: 39.73  E-value: 4.08e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767995519  78 RMVQDGDFVRYHYNGTLlDGTSFDtsyskGGTYDTY---VGSGWLIKGMDQGLLGMCPGERRKI 138
Cdd:COG0544  156 RAAEEGDRVTIDFEGTI-DGEEFE-----GGKAEDYsleLGSGSFIPGFEEQLVGMKAGEEKTF 213
PLN02964 PLN02964
phosphatidylserine decarboxylase
 437-495 5.11e-03

phosphatidylserine decarboxylase


Pssm-ID: 215520 [Multi-domain]  Cd Length: 644  Bit Score: 39.46  E-value: 5.11e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767995519 437 MDLNKDGEVPPEEFSTFIKAqvsegKGRLMPGQDPEktigDMFQNQDRNQDGKITVDEL 495
Cdd:PLN02964 188 VDYDEDGQLSFSEFSDLIKA-----FGNLVAANKKE----ELFKAADLNGDGVVTIDEL 237
 
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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