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Conserved domains on  [gi|57526010|ref|NP_001003520|]
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peptidyl-prolyl cis-trans isomerase FKBP9 precursor [Danio rerio]

Protein Classification

FKBP-type peptidyl-prolyl cis-trans isomerase( domain architecture ID 10446695)

FKBP-type peptidyl-prolyl cis-trans isomerase, with EF-hand calcium binding motifs, acts as a PPIase that accelerates the folding of proteins; similar to Mus musculus peptidyl-prolyl cis-trans isomerase FKBP14

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;
264-356 3.13e-37

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 133.09  E-value: 3.13e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526010   264 CPRKSQVGDFMRYHYNGSLLDGTFFDSSYSRNHTYDTYIGKGYVIAGMDQGLLGVCVGERRRITIPPHLAYGEEG-TGTK 342
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPV 80

                          90
                  ....*....|....
gi 57526010   343 IPGSAVLVFDVHII 356
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
375-467 2.82e-34

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 125.00  E-value: 2.82e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526010   375 CTYNAKRGDFVKYHYNATLMDGTDIGSTHMYGKTYNVVLGSGQVVIGMEQGLTGMCIGEKRKLVIPPHLAYGERGVDG-E 453
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGpV 80

                          90
                  ....*....|....
gi 57526010   454 VPGSAVLVFEVEMV 467
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
40-132 3.00e-34

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 124.62  E-value: 3.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526010    40 CERAVKSGDYVRYHYIGMFPDGKKFDSSYDRGNTYNVFVGQKQLIAGMDKALVGMCVNERWMIKIPPQLAYGKDGY-GDI 118
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPV 80

                          90
                  ....*....|....
gi 57526010   119 IPPDSILHFDVLML 132
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
152-244 1.89e-32

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 119.61  E-value: 1.89e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526010   152 CERKVQVSDYIRYHYNGTLLDGTLFDSSHTRMRTYDTYVGIGWLIAGMDQGLLGMCVGEKRIITLPPFLGYGENG-DGSD 230
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPV 80

                          90
                  ....*....|....
gi 57526010   231 IPAQASLVFDVVLL 244
Cdd:pfam00254  81 IPPNATLVFEVELL 94
EFh super family cl08302
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 490-551 1.75e-04

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.


The actual alignment was detected with superfamily member cd00051:

Pssm-ID: 415501 [Multi-domain]  Cd Length: 63  Bit Score: 39.84  E-value: 1.75e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57526010 490 FSEMDKNKDAQVDKTEFSDyILQQVEEGKgrlapgfeSQRIIESMYDNQDRNKDGIITEDEF 551
Cdd:cd00051   6 FRLFDKDGDGTISADELKA-ALKSLGEGL--------SEEEIDEMIREVDKDGDGKIDFEEF 58
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
264-356 3.13e-37

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 133.09  E-value: 3.13e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526010   264 CPRKSQVGDFMRYHYNGSLLDGTFFDSSYSRNHTYDTYIGKGYVIAGMDQGLLGVCVGERRRITIPPHLAYGEEG-TGTK 342
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPV 80

                          90
                  ....*....|....
gi 57526010   343 IPGSAVLVFDVHII 356
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
375-467 2.82e-34

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 125.00  E-value: 2.82e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526010   375 CTYNAKRGDFVKYHYNATLMDGTDIGSTHMYGKTYNVVLGSGQVVIGMEQGLTGMCIGEKRKLVIPPHLAYGERGVDG-E 453
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGpV 80

                          90
                  ....*....|....
gi 57526010   454 VPGSAVLVFEVEMV 467
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
40-132 3.00e-34

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 124.62  E-value: 3.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526010    40 CERAVKSGDYVRYHYIGMFPDGKKFDSSYDRGNTYNVFVGQKQLIAGMDKALVGMCVNERWMIKIPPQLAYGKDGY-GDI 118
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPV 80

                          90
                  ....*....|....
gi 57526010   119 IPPDSILHFDVLML 132
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
152-244 1.89e-32

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 119.61  E-value: 1.89e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526010   152 CERKVQVSDYIRYHYNGTLLDGTLFDSSHTRMRTYDTYVGIGWLIAGMDQGLLGMCVGEKRIITLPPFLGYGENG-DGSD 230
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPV 80

                          90
                  ....*....|....
gi 57526010   231 IPAQASLVFDVVLL 244
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 43-134 2.73e-31

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 116.82  E-value: 2.73e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526010  43 AVKSGDYVRYHYIGMFPDGKKFDSSYDRGNTYNVFVGQKQLIAGMDKALVGMCVNERWMIKIPPQLAYGKDGYGDIIPPD 122
Cdd:COG0545  13 KPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPN 92

                        90
                ....*....|..
gi 57526010 123 SILHFDVLMLDI 134
Cdd:COG0545  93 STLVFEVELLDV 104
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 269-358 8.36e-30

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 112.97  E-value: 8.36e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526010 269 QVGDFMRYHYNGSLLDGTFFDSSYSRNHTYDTYIGKGYVIAGMDQGLLGVCVGERRRITIPPHLAYGEEGTGTKIPGSAV 348
Cdd:COG0545  15 KAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPNST 94

                        90
                ....*....|
gi 57526010 349 LVFDVHIIDF 358
Cdd:COG0545  95 LVFEVELLDV 104
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 155-245 2.13e-28

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 108.73  E-value: 2.13e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526010 155 KVQVSDYIRYHYNGTLLDGTLFDSSHTRMRTYDTYVGIGWLIAGMDQGLLGMCVGEKRIITLPPFLGYGENGDGSDIPAQ 234
Cdd:COG0545  13 KPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPN 92

                        90
                ....*....|.
gi 57526010 235 ASLVFDVVLLD 245
Cdd:COG0545  93 STLVFEVELLD 103
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 379-469 7.06e-28

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 107.58  E-value: 7.06e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526010 379 AKRGDFVKYHYNATLMDGTDIGSTHMYGKTYNVVLGSGQVVIGMEQGLTGMCIGEKRKLVIPPHLAYGERGVDGEVPGSA 458
Cdd:COG0545  14 PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPNS 93

                        90
                ....*....|.
gi 57526010 459 VLVFEVEMVDV 469
Cdd:COG0545  94 TLVFEVELLDV 104
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 48-134 6.12e-16

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 76.76  E-value: 6.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526010   48 DYVRYHYIGMFPDGKKFDSSYDRGNTYNVFVGQkqLIAGMDKALVGMCVNERWMIKIPPQLAYGKDGYGDIIPPDSILHF 127
Cdd:PRK11570 121 DRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNG--VIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLVF 198


                 ....*..
gi 57526010  128 DVLMLDI 134
Cdd:PRK11570 199 EVELLEI 205
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 272-357 4.01e-15

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 74.45  E-value: 4.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526010  272 DFMRYHYNGSLLDGTFFDSSYSRNHTYDTYIGKgyVIAGMDQGLLGVCVGERRRITIPPHLAYGEEGTGTKIPGSAVLVF 351
Cdd:PRK11570 121 DRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNG--VIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLVF 198


                 ....*.
gi 57526010  352 DVHIID 357
Cdd:PRK11570 199 EVELLE 204
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 159-246 1.04e-14

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 73.29  E-value: 1.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526010  159 SDYIRYHYNGTLLDGTLFDSSHTRMRTYDTYVGigWLIAGMDQGLLGMCVGEKRIITLPPFLGYGENGDGSDIPAQASLV 238
Cdd:PRK11570 120 TDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVN--GVIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLV 197


                 ....*...
gi 57526010  239 FDVVLLDL 246
Cdd:PRK11570 198 FEVELLEI 205
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 381-469 2.02e-13

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 69.44  E-value: 2.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526010  381 RGDFVKYHYNATLMDGTDIGSTHMYGKTYNVVLgSGqVVIGMEQGLTGMCIGEKRKLVIPPHLAYGERGVDGEVPGSAVL 460
Cdd:PRK11570 119 RTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPV-NG-VIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTL 196


                 ....*....
gi 57526010  461 VFEVEMVDV 469
Cdd:PRK11570 197 VFEVELLEI 205
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 490-551 1.75e-04

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: 39.84  E-value: 1.75e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57526010 490 FSEMDKNKDAQVDKTEFSDyILQQVEEGKgrlapgfeSQRIIESMYDNQDRNKDGIITEDEF 551
Cdd:cd00051   6 FRLFDKDGDGTISADELKA-ALKSLGEGL--------SEEEIDEMIREVDKDGDGKIDFEEF 58
EF-hand_7 pfam13499
EF-hand domain pair;
488-552 2.82e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.16  E-value: 2.82e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57526010   488 DLFSEMDKNKDAQVDKTEFSDYiLQQVEEGKGrlapgfESQRIIESMYDNQDRNKDGIITEDEFK 552
Cdd:pfam13499   6 EAFKLLDSDGDGYLDVEELKKL-LRKLEEGEP------LSDEEVEELFKEFDLDKDGRISFEEFL 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
488-552 1.22e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 39.39  E-value: 1.22e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57526010 488 DLFSEMDKNKDAQVDKTEFSDYIlqqveegKGRLAPGFESQRIIESMydnqDRNKDGIITEDEFK 552
Cdd:COG5126  73 AAFDLLDTDGDGKISADEFRRLL-------TALGVSEEEADELFARL----DTDGDGKISFEEFV 126
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
264-356 3.13e-37

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 133.09  E-value: 3.13e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526010   264 CPRKSQVGDFMRYHYNGSLLDGTFFDSSYSRNHTYDTYIGKGYVIAGMDQGLLGVCVGERRRITIPPHLAYGEEG-TGTK 342
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPV 80

                          90
                  ....*....|....
gi 57526010   343 IPGSAVLVFDVHII 356
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
375-467 2.82e-34

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 125.00  E-value: 2.82e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526010   375 CTYNAKRGDFVKYHYNATLMDGTDIGSTHMYGKTYNVVLGSGQVVIGMEQGLTGMCIGEKRKLVIPPHLAYGERGVDG-E 453
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGpV 80

                          90
                  ....*....|....
gi 57526010   454 VPGSAVLVFEVEMV 467
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
40-132 3.00e-34

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 124.62  E-value: 3.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526010    40 CERAVKSGDYVRYHYIGMFPDGKKFDSSYDRGNTYNVFVGQKQLIAGMDKALVGMCVNERWMIKIPPQLAYGKDGY-GDI 118
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPV 80

                          90
                  ....*....|....
gi 57526010   119 IPPDSILHFDVLML 132
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
152-244 1.89e-32

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 119.61  E-value: 1.89e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526010   152 CERKVQVSDYIRYHYNGTLLDGTLFDSSHTRMRTYDTYVGIGWLIAGMDQGLLGMCVGEKRIITLPPFLGYGENG-DGSD 230
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPV 80

                          90
                  ....*....|....
gi 57526010   231 IPAQASLVFDVVLL 244
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 43-134 2.73e-31

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 116.82  E-value: 2.73e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526010  43 AVKSGDYVRYHYIGMFPDGKKFDSSYDRGNTYNVFVGQKQLIAGMDKALVGMCVNERWMIKIPPQLAYGKDGYGDIIPPD 122
Cdd:COG0545  13 KPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPN 92

                        90
                ....*....|..
gi 57526010 123 SILHFDVLMLDI 134
Cdd:COG0545  93 STLVFEVELLDV 104
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 269-358 8.36e-30

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 112.97  E-value: 8.36e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526010 269 QVGDFMRYHYNGSLLDGTFFDSSYSRNHTYDTYIGKGYVIAGMDQGLLGVCVGERRRITIPPHLAYGEEGTGTKIPGSAV 348
Cdd:COG0545  15 KAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPNST 94

                        90
                ....*....|
gi 57526010 349 LVFDVHIIDF 358
Cdd:COG0545  95 LVFEVELLDV 104
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 155-245 2.13e-28

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 108.73  E-value: 2.13e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526010 155 KVQVSDYIRYHYNGTLLDGTLFDSSHTRMRTYDTYVGIGWLIAGMDQGLLGMCVGEKRIITLPPFLGYGENGDGSDIPAQ 234
Cdd:COG0545  13 KPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPN 92

                        90
                ....*....|.
gi 57526010 235 ASLVFDVVLLD 245
Cdd:COG0545  93 STLVFEVELLD 103
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 379-469 7.06e-28

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 107.58  E-value: 7.06e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526010 379 AKRGDFVKYHYNATLMDGTDIGSTHMYGKTYNVVLGSGQVVIGMEQGLTGMCIGEKRKLVIPPHLAYGERGVDGEVPGSA 458
Cdd:COG0545  14 PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPNS 93

                        90
                ....*....|.
gi 57526010 459 VLVFEVEMVDV 469
Cdd:COG0545  94 TLVFEVELLDV 104
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 48-134 6.12e-16

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 76.76  E-value: 6.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526010   48 DYVRYHYIGMFPDGKKFDSSYDRGNTYNVFVGQkqLIAGMDKALVGMCVNERWMIKIPPQLAYGKDGYGDIIPPDSILHF 127
Cdd:PRK11570 121 DRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNG--VIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLVF 198


                 ....*..
gi 57526010  128 DVLMLDI 134
Cdd:PRK11570 199 EVELLEI 205
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 272-357 4.01e-15

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 74.45  E-value: 4.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526010  272 DFMRYHYNGSLLDGTFFDSSYSRNHTYDTYIGKgyVIAGMDQGLLGVCVGERRRITIPPHLAYGEEGTGTKIPGSAVLVF 351
Cdd:PRK11570 121 DRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNG--VIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLVF 198


                 ....*.
gi 57526010  352 DVHIID 357
Cdd:PRK11570 199 EVELLE 204
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 159-246 1.04e-14

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 73.29  E-value: 1.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526010  159 SDYIRYHYNGTLLDGTLFDSSHTRMRTYDTYVGigWLIAGMDQGLLGMCVGEKRIITLPPFLGYGENGDGSDIPAQASLV 238
Cdd:PRK11570 120 TDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVN--GVIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLV 197


                 ....*...
gi 57526010  239 FDVVLLDL 246
Cdd:PRK11570 198 FEVELLEI 205
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 381-469 2.02e-13

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 69.44  E-value: 2.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526010  381 RGDFVKYHYNATLMDGTDIGSTHMYGKTYNVVLgSGqVVIGMEQGLTGMCIGEKRKLVIPPHLAYGERGVDGEVPGSAVL 460
Cdd:PRK11570 119 RTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPV-NG-VIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTL 196


                 ....*....
gi 57526010  461 VFEVEMVDV 469
Cdd:PRK11570 197 VFEVELLEI 205
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 380-470 5.99e-13

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 69.41  E-value: 5.99e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526010  380 KRGDFVKYHYNATLMDGTDIGSTHMYGKTYNVVLGSgqVVIGMEQGLTGMCIGEKRKLVIPPHLAYGERGVDGeVPGSAV 459
Cdd:PRK10902 162 KDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRLDG--VIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPG-IPANST 238

                         90
                 ....*....|.
gi 57526010  460 LVFEVEMVDVE 470
Cdd:PRK10902 239 LVFDVELLDVK 249
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 278-357 1.60e-12

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 67.87  E-value: 1.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526010  278 YNGSLLDGTFFDSSYSRNHTYDtyIGKGYVIAGMDQGLLGVCVGERRRITIPPHLAYGEEGTgTKIPGSAVLVFDVHIID 357
Cdd:PRK10902 171 YKGTLIDGKEFDNSYTRGEPLS--FRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGV-PGIPANSTLVFDVELLD 247
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 159-246 8.06e-12

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 65.94  E-value: 8.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526010  159 SDYIRYHYNGTLLDGTLFDSSHTRMRTYDtyVGIGWLIAGMDQGLLGMCVGEKRIITLPPFLGYGENGDgSDIPAQASLV 238
Cdd:PRK10902 164 SDTVVVNYKGTLIDGKEFDNSYTRGEPLS--FRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGV-PGIPANSTLV 240


                 ....*...
gi 57526010  239 FDVVLLDL 246
Cdd:PRK10902 241 FDVELLDV 248
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 379-448 1.11e-11

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 62.43  E-value: 1.11e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526010 379 AKRGDFVKYHYNATLMDGTDIGSTHmYGKTYNVVLGSGQVVIGMEQGLTGMCIGEKRKLVIPPHLAYGER 448
Cdd:COG1047   1 IEKGDVVTLHYTLKLEDGEVFDSTF-EGEPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGER 69
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 44-111 1.40e-11

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 62.04  E-value: 1.40e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57526010  44 VKSGDYVRYHYIGMFPDGKKFDSSYDRGnTYNVFVGQKQLIAGMDKALVGMCVNERWMIKIPPQLAYG 111
Cdd:COG1047   1 IEKGDVVTLHYTLKLEDGEVFDSTFEGE-PLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYG 67
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 160-224 1.98e-10

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 58.96  E-value: 1.98e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57526010 160 DYIRYHYNGTLLDGTLFDSSHTRM-RTYdtYVGIGWLIAGMDQGLLGMCVGEKRIITLPPFLGYGE 224
Cdd:COG1047   5 DVVTLHYTLKLEDGEVFDSTFEGEpLEF--LHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGE 68
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 43-134 3.25e-10

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 60.93  E-value: 3.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526010   43 AVKSGDYVRYHYIGMFPDGKKFDSSYDRGNTYNvfVGQKQLIAGMDKALVGmcVNERWMIK--IPPQLAYGKDGYGDiIP 120
Cdd:PRK10902 160 APKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLS--FRLDGVIPGWTEGLKN--IKKGGKIKlvIPPELAYGKAGVPG-IP 234

                         90
                 ....*....|....
gi 57526010  121 PDSILHFDVLMLDI 134
Cdd:PRK10902 235 ANSTLVFDVELLDV 248
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 271-336 2.58e-09

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 55.49  E-value: 2.58e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57526010 271 GDFMRYHYNGSLLDGTFFDSSYSRN-HTYdtYIGKGYVIAGMDQGLLGVCVGERRRITIPPHLAYGE 336
Cdd:COG1047   4 GDVVTLHYTLKLEDGEVFDSTFEGEpLEF--LHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGE 68
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 388-451 2.41e-05

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


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 44.70  E-value: 2.41e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57526010  388 HYNATLMDGTDIGSTHMYGKTYNVVLGSGQVVIGMEQGLTGMCIGEKRKLVIPPHLAYGERGVD 451
Cdd:PRK15095  14 HFTLKLDDGSTAESTRNNGKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFGVPSPD 77
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 490-551 1.75e-04

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: 39.84  E-value: 1.75e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57526010 490 FSEMDKNKDAQVDKTEFSDyILQQVEEGKgrlapgfeSQRIIESMYDNQDRNKDGIITEDEF 551
Cdd:cd00051   6 FRLFDKDGDGTISADELKA-ALKSLGEGL--------SEEEIDEMIREVDKDGDGKIDFEEF 58
Tig COG0544
FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, ...
 41-98 2.10e-04

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


Pssm-ID: 440310 [Multi-domain]  Cd Length: 424  Bit Score: 43.96  E-value: 2.10e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 57526010  41 ERAVKSGDYVRYHYIGmFPDGKKFDSSydRGNTYNVFVGQKQLIAGMDKALVGMCVNE 98
Cdd:COG0544 155 ERAAEEGDRVTIDFEG-TIDGEEFEGG--KAEDYSLELGSGSFIPGFEEQLVGMKAGE 209
EF-hand_7 pfam13499
EF-hand domain pair;
488-552 2.82e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.16  E-value: 2.82e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57526010   488 DLFSEMDKNKDAQVDKTEFSDYiLQQVEEGKGrlapgfESQRIIESMYDNQDRNKDGIITEDEFK 552
Cdd:pfam13499   6 EAFKLLDSDGDGYLDVEELKKL-LRKLEEGEP------LSDEEVEELFKEFDLDKDGRISFEEFL 63
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 156-224 2.95e-04

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


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 41.62  E-value: 2.95e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57526010  156 VQVSDYIRYHYNGTLLDGTLFDSSHTRMRTYDTYVGIGWLIAGMDQGLLGMCVGEKRIITLPPFLGYGE 224
Cdd:PRK15095   5 VQSNSAVLVHFTLKLDDGSTAESTRNNGKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFGV 73
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 488-563 5.25e-04

EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also termed stromal cell-derived factor 4 (SDF-4), is a soluble, lumenal Golgi resident low-affinity Ca2+-binding protein that contains six copies of the EF-hand Ca2+-binding motif. It is required for secretory pathway calcium ATPase1 (SPCA1)-dependent Ca2+ import into the trans-Golgi network (TGN) and plays an essential role in Ca2+-dependent secretory cargo sorting at the TGN.


Pssm-ID: 320023 [Multi-domain]  Cd Length: 278  Bit Score: 42.29  E-value: 5.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526010 488 DLFSEMDKNKDAQVDKTEFSDYILQQVEEgkgrlapGFEsqriiESMYDNQ------DRNKDGIITEDEFKLK------- 554
Cdd:cd16225  38 EIFKKVDVNTDGFLSAEELEDWIMEKTQE-------HFQ-----EAVEENEqifkavDTDKDGNVSWEEYRVHfllskgy 105

                        90
                ....*....|
gi 57526010 555 -ADEAAAHDE 563
Cdd:cd16225 106 sEEEAEEKIK 115
Tig COG0544
FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, ...
 379-475 1.02e-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: 41.65  E-value: 1.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526010 379 AKRGDFVKYHYNATLmDGTDI--GSthmyGKTYNVVLGSGQVVIGMEQGLTGMCIGEKRKLVIpphlAYGERGVDGEVPG 456
Cdd:COG0544 158 AEEGDRVTIDFEGTI-DGEEFegGK----AEDYSLELGSGSFIPGFEEQLVGMKAGEEKTFEV----TFPEDYHAEELAG 228

                        90       100
                ....*....|....*....|
gi 57526010 457 SAVlVFEVEMVDVEE-GLPE 475
Cdd:COG0544 229 KTA-TFKVTVKEVKEkELPE 247
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
488-552 1.22e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 39.39  E-value: 1.22e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57526010 488 DLFSEMDKNKDAQVDKTEFSDYIlqqveegKGRLAPGFESQRIIESMydnqDRNKDGIITEDEFK 552
Cdd:COG5126  73 AAFDLLDTDGDGKISADEFRRLL-------TALGVSEEEADELFARL----DTDGDGKISFEEFV 126
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 277-337 2.07e-03

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


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 38.92  E-value: 2.07e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57526010  277 HYNGSLLDGTFFDSSYSRNHTYDTYIGKGYVIAGMDQGLLGVCVGERRRITIPPHLAYGEE 337
Cdd:PRK15095  14 HFTLKLDDGSTAESTRNNGKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFGVP 74
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
473-552 2.26e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 38.62  E-value: 2.26e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526010 473 LPEGYMFVWNnnvtpDLFSEMDKNKDAQVDKTEFSDYILQQVEEGKGRLApgfesqriiESMYDNQDRNKDGIITEDEFK 552
Cdd:COG5126  27 FEALFRRLWA-----TLFSEADTDGDGRISREEFVAGMESLFEATVEPFA---------RAAFDLLDTDGDGKISADEFR 92
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 489-555 4.65e-03

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: 39.22  E-value: 4.65e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57526010 489 LFSEMDKNKDAQVDKTEFSDYILQQV-----EEGKGRLapgfesqriiesmyDNQDRNKDGIITEDEFKLKA 555
Cdd:cd16227  41 LAKKMDLNDDGFIDRKELKAWILRSFkmldeEEANERF--------------EEADEDGDGKVTWEEYLADS 98
 
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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