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Conserved domains on  [gi|1776769411|ref|XP_031419740|]
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TGF-beta-activated kinase 1 and MAP3K7-binding protein 1 isoform X1 [Clupea harengus]

Protein Classification

PP2C family serine/threonine-protein phosphatase( domain architecture ID 10065450)

PP2C family protein-serine/threonine phosphatase catalyzes the dephosphorylation of phosphoserine and phosphothreonine residues of specific protein substrates

CATH:  3.60.40.10
EC:  3.1.3.16
Gene Ontology:  GO:0004722|GO:0006470|GO:0046872
PubMed:  9192069|8819174
SCOP:  3000909

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PP2Cc cd00143
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
34-354 5.32e-30

Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity.


:

Pssm-ID: 238083 [Multi-domain]  Cd Length: 254  Bit Score: 117.81  E-value: 5.32e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776769411  34 VYGQDGKGAQSHPYEDGH---FRFRGEDCSLYGVFNGYDGSRVANFMSQCLTAELL-LGQLNTTHSDADVRRILSQAFDA 109
Cdd:cd00143     2 SAGVSDKGGDRKTNEDAVvikPNLNNEDGGLFGVFDGHGGHAAGEFASKLLVEELLeELEETLTLSEEDIEEALRKAFLR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776769411 110 VEKsyfetigdalaekanlqsqlpegaifhqlspqsqKLADRLAALEQEVNGGATAVVALILNNKLYIANVGTNRALLCK 189
Cdd:cd00143    82 ADE----------------------------------EILEEAQDEPDDARSGTTAVVALIRGNKLYVANVGDSRAVLCR 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776769411 190 StsdgqNQVIQIGRAHTTDNDDELTRLVQlaslkvtpppplvcasAGLDANRLRqtsLIAGQSSTRRIGDYKVKFnytdi 269
Cdd:cd00143   128 N-----GEAVQLTKDHKPVNEEERERIEK----------------AGGRVSNGR---VPGVLAVTRALGDFDLKP----- 178
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776769411 270 dvlsaaknkPIIAEAEIHGGQsLEGVTGFLLLMSEGLIKALEsahgpeqaNQEMVAMVAAELAQQStLEAAAQSVVERVK 349
Cdd:cd00143   179 ---------GVSAEPDVTVVK-LTEDDDFLILASDGLWDVLS--------NQEAVDIVRSELAKED-LQEAAQELVDLAL 239

                  ....*.
gi 1776769411 350 RL-HHD 354
Cdd:cd00143   240 RRgSHD 245
 
Name Accession Description Interval E-value
PP2Cc cd00143
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
34-354 5.32e-30

Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity.


Pssm-ID: 238083 [Multi-domain]  Cd Length: 254  Bit Score: 117.81  E-value: 5.32e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776769411  34 VYGQDGKGAQSHPYEDGH---FRFRGEDCSLYGVFNGYDGSRVANFMSQCLTAELL-LGQLNTTHSDADVRRILSQAFDA 109
Cdd:cd00143     2 SAGVSDKGGDRKTNEDAVvikPNLNNEDGGLFGVFDGHGGHAAGEFASKLLVEELLeELEETLTLSEEDIEEALRKAFLR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776769411 110 VEKsyfetigdalaekanlqsqlpegaifhqlspqsqKLADRLAALEQEVNGGATAVVALILNNKLYIANVGTNRALLCK 189
Cdd:cd00143    82 ADE----------------------------------EILEEAQDEPDDARSGTTAVVALIRGNKLYVANVGDSRAVLCR 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776769411 190 StsdgqNQVIQIGRAHTTDNDDELTRLVQlaslkvtpppplvcasAGLDANRLRqtsLIAGQSSTRRIGDYKVKFnytdi 269
Cdd:cd00143   128 N-----GEAVQLTKDHKPVNEEERERIEK----------------AGGRVSNGR---VPGVLAVTRALGDFDLKP----- 178
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776769411 270 dvlsaaknkPIIAEAEIHGGQsLEGVTGFLLLMSEGLIKALEsahgpeqaNQEMVAMVAAELAQQStLEAAAQSVVERVK 349
Cdd:cd00143   179 ---------GVSAEPDVTVVK-LTEDDDFLILASDGLWDVLS--------NQEAVDIVRSELAKED-LQEAAQELVDLAL 239

                  ....*.
gi 1776769411 350 RL-HHD 354
Cdd:cd00143   240 RRgSHD 245
PP2C pfam00481
Protein phosphatase 2C; Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine ...
66-348 1.49e-25

Protein phosphatase 2C; Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine/threonine phosphatase.


Pssm-ID: 395385  Cd Length: 252  Bit Score: 105.50  E-value: 1.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776769411  66 NGYDGSRVANFMSQCLTAELLLGQLNTthSDADVRRILSQAFDAVEKSYFETIGDA-LAEKANLQSQLPEGAIF-HQLSP 143
Cdd:pfam00481   1 IDLGGPRMQGWRKSMEDAHIDLPNLNS--SSGKDSWSFFAVFDGHGGSEAAKYCGKhLHTILALRRSFLEGEKLeDALRK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776769411 144 QSQKLAD--RLAALEQEVNGGATAVVALILNNKLYIANVGTNRALLCKSTSDGQnqviQIGRAHTTDNDDELTRLVQlas 221
Cdd:pfam00481  79 SFLEDTDevLRSAEKEDLDSGCTAVVALISGNKLYVANVGDSRAVLCRNGNAIK----RLTKDHKPSDEDERRRIRA--- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776769411 222 lkvtpppplvcasAGLDANRLRQtslIAGQ-SSTRRIGDYKVKfnytdidvlsaAKNKPIIAEAEIHGGQSLEGvTGFLL 300
Cdd:pfam00481 152 -------------AGGFVSRNGR---VNGVlAVSRAFGDFELK-----------PGEQAVSAEPDITSHTITED-DEFLI 203
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1776769411 301 LMSEGLIKALESAHGPEQANQEMVAMVAAELAQQSTL-EAAAQSVVERV 348
Cdd:pfam00481 204 LACDGLWDVLSDQEVVDLVRSELSDGGSPMEAAEELRdEAIAYGSEDNI 252
PP2Cc smart00332
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
31-376 4.46e-22

Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity.


Pssm-ID: 214625 [Multi-domain]  Cd Length: 252  Bit Score: 95.52  E-value: 4.46e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776769411   31 PNCVYGQDGKGAQSHPYEDGHFRF--RGEDCSLYGVFNGYDGSRVANFMSQCLTAELLLGQLNTTHSDADVRRILSQAFD 108
Cdd:smart00332   7 LGLRYGLSSMQGVRKPMEDAHVITpdLSDSGGFFGVFDGHGGSEAAKFLSKNLPEILAEELIKEKDELEDVEEALRKAFL 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776769411  109 AVEKsyfetigdALAEKAnlqsqlpegaifhqlspqsqkladrlaaleqEVNGGATAVVALILNNKLYIANVGTNRALLC 188
Cdd:smart00332  87 STDE--------EILEEL-------------------------------EALSGSTAVVALISGNKLYVANVGDSRAVLC 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776769411  189 KstsdgQNQVIQIGRAHTTDNDDELTRLVQLASlkvtpppplvcasagldanRLRQTSLIAGQSSTRRIGDYKVKfnytd 268
Cdd:smart00332 128 R-----NGKAVQLTEDHKPSNEDERARIEAAGG-------------------FVINGRVNGVLALSRAIGDFFLK----- 178
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776769411  269 idvlsaaknKPIIAEAEIHgGQSLEGVTGFLLLMSEGLIKALEsahgpeqaNQEMVAMVaaelaqQSTLEAAAQsvvERV 348
Cdd:smart00332 179 ---------PYVSAEPDVT-VVELTEKDDFLILASDGLWDVLS--------NQEVVDIV------RKHLSKDPK---EAA 231
                          330       340
                   ....*....|....*....|....*...
gi 1776769411  349 KRLHHDAFVSGrqrashcsRHEDMTLLV 376
Cdd:smart00332 232 KRLIDLALARG--------SKDNITVVV 251
 
Name Accession Description Interval E-value
PP2Cc cd00143
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
34-354 5.32e-30

Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity.


Pssm-ID: 238083 [Multi-domain]  Cd Length: 254  Bit Score: 117.81  E-value: 5.32e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776769411  34 VYGQDGKGAQSHPYEDGH---FRFRGEDCSLYGVFNGYDGSRVANFMSQCLTAELL-LGQLNTTHSDADVRRILSQAFDA 109
Cdd:cd00143     2 SAGVSDKGGDRKTNEDAVvikPNLNNEDGGLFGVFDGHGGHAAGEFASKLLVEELLeELEETLTLSEEDIEEALRKAFLR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776769411 110 VEKsyfetigdalaekanlqsqlpegaifhqlspqsqKLADRLAALEQEVNGGATAVVALILNNKLYIANVGTNRALLCK 189
Cdd:cd00143    82 ADE----------------------------------EILEEAQDEPDDARSGTTAVVALIRGNKLYVANVGDSRAVLCR 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776769411 190 StsdgqNQVIQIGRAHTTDNDDELTRLVQlaslkvtpppplvcasAGLDANRLRqtsLIAGQSSTRRIGDYKVKFnytdi 269
Cdd:cd00143   128 N-----GEAVQLTKDHKPVNEEERERIEK----------------AGGRVSNGR---VPGVLAVTRALGDFDLKP----- 178
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776769411 270 dvlsaaknkPIIAEAEIHGGQsLEGVTGFLLLMSEGLIKALEsahgpeqaNQEMVAMVAAELAQQStLEAAAQSVVERVK 349
Cdd:cd00143   179 ---------GVSAEPDVTVVK-LTEDDDFLILASDGLWDVLS--------NQEAVDIVRSELAKED-LQEAAQELVDLAL 239

                  ....*.
gi 1776769411 350 RL-HHD 354
Cdd:cd00143   240 RRgSHD 245
PP2C pfam00481
Protein phosphatase 2C; Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine ...
66-348 1.49e-25

Protein phosphatase 2C; Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine/threonine phosphatase.


Pssm-ID: 395385  Cd Length: 252  Bit Score: 105.50  E-value: 1.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776769411  66 NGYDGSRVANFMSQCLTAELLLGQLNTthSDADVRRILSQAFDAVEKSYFETIGDA-LAEKANLQSQLPEGAIF-HQLSP 143
Cdd:pfam00481   1 IDLGGPRMQGWRKSMEDAHIDLPNLNS--SSGKDSWSFFAVFDGHGGSEAAKYCGKhLHTILALRRSFLEGEKLeDALRK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776769411 144 QSQKLAD--RLAALEQEVNGGATAVVALILNNKLYIANVGTNRALLCKSTSDGQnqviQIGRAHTTDNDDELTRLVQlas 221
Cdd:pfam00481  79 SFLEDTDevLRSAEKEDLDSGCTAVVALISGNKLYVANVGDSRAVLCRNGNAIK----RLTKDHKPSDEDERRRIRA--- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776769411 222 lkvtpppplvcasAGLDANRLRQtslIAGQ-SSTRRIGDYKVKfnytdidvlsaAKNKPIIAEAEIHGGQSLEGvTGFLL 300
Cdd:pfam00481 152 -------------AGGFVSRNGR---VNGVlAVSRAFGDFELK-----------PGEQAVSAEPDITSHTITED-DEFLI 203
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1776769411 301 LMSEGLIKALESAHGPEQANQEMVAMVAAELAQQSTL-EAAAQSVVERV 348
Cdd:pfam00481 204 LACDGLWDVLSDQEVVDLVRSELSDGGSPMEAAEELRdEAIAYGSEDNI 252
PP2Cc smart00332
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
31-376 4.46e-22

Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity.


Pssm-ID: 214625 [Multi-domain]  Cd Length: 252  Bit Score: 95.52  E-value: 4.46e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776769411   31 PNCVYGQDGKGAQSHPYEDGHFRF--RGEDCSLYGVFNGYDGSRVANFMSQCLTAELLLGQLNTTHSDADVRRILSQAFD 108
Cdd:smart00332   7 LGLRYGLSSMQGVRKPMEDAHVITpdLSDSGGFFGVFDGHGGSEAAKFLSKNLPEILAEELIKEKDELEDVEEALRKAFL 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776769411  109 AVEKsyfetigdALAEKAnlqsqlpegaifhqlspqsqkladrlaaleqEVNGGATAVVALILNNKLYIANVGTNRALLC 188
Cdd:smart00332  87 STDE--------EILEEL-------------------------------EALSGSTAVVALISGNKLYVANVGDSRAVLC 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776769411  189 KstsdgQNQVIQIGRAHTTDNDDELTRLVQLASlkvtpppplvcasagldanRLRQTSLIAGQSSTRRIGDYKVKfnytd 268
Cdd:smart00332 128 R-----NGKAVQLTEDHKPSNEDERARIEAAGG-------------------FVINGRVNGVLALSRAIGDFFLK----- 178
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776769411  269 idvlsaaknKPIIAEAEIHgGQSLEGVTGFLLLMSEGLIKALEsahgpeqaNQEMVAMVaaelaqQSTLEAAAQsvvERV 348
Cdd:smart00332 179 ---------PYVSAEPDVT-VVELTEKDDFLILASDGLWDVLS--------NQEVVDIV------RKHLSKDPK---EAA 231
                          330       340
                   ....*....|....*....|....*...
gi 1776769411  349 KRLHHDAFVSGrqrashcsRHEDMTLLV 376
Cdd:smart00332 232 KRLIDLALARG--------SKDNITVVV 251
 
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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