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Conserved domains on  [gi|1958776351|ref|XP_038965846|]
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putative tyrosine-protein phosphatase auxilin isoform X3 [Rattus norvegicus]

Protein Classification

cyclin-G-associated kinase( domain architecture ID 12998533)

cyclin-G-associated kinase (GAK) is a serine/threonine-protein kinase that catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates; it phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2, and associates with cyclin G and CDK5

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_auxilin_N cd14563
N-terminal protein tyrosine phosphatase-like domain of auxilin; Auxilin, also called auxilin-1 ...
 43-205 2.79e-114

N-terminal protein tyrosine phosphatase-like domain of auxilin; Auxilin, also called auxilin-1 or DnaJ homolog subfamily C member 6 (DNAJC6), is a J-domain containing protein that recruits the ATP-dependent chaperone Hsc70 to newly budded clathrin-coated vesicles and promotes uncoating of clathrin-coated vesicles, driving the clathrin assembly#disassembly cycle. Mutations in the DNAJC6 gene, encoding auxilin, are associated with early-onset Parkinson's disease. Auxilin contains an N-terminal protein tyrosine phosphatase (PTP)-like domain similar to the PTP-like domain of PTEN, a phosphoinositide 3-phosphatase, and a C-terminal region with clathrin-binding and J domains.


:

Pssm-ID: 350411 [Multi-domain]  Cd Length: 163  Bit Score: 346.10  E-value: 2.79e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351  43 VSSYTKGDLDFTYVTSRIIVMSFPMDSVDIGFRNQVDDIRSFLDSRHLDHYTVYNLSPKSYRTAKFHSRVSECSWPIRQA 122
Cdd:cd14563     1 VASYTKGELDISYITSRIIVMSYPAEGVELGFRNHIEDVRSFLDSRHLDHYTVFNLSQKSYRSAKFHNRVSECSWPVRQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351 123 PSLHNLFAVCRNMYNWLLQNPKNVCVVHCLDGRAASSILVGAMFIFCNLYSTPGPAVRLLYAKRPGIGLSPSHRRYLGYM 202
Cdd:cd14563    81 PSLHNLFAVCKNMHNWLQQNPKNVCVIHCMDGRAASAVLVSAMFCFCHLFSNPVPAMQLLNAKRPGIGLWPSHRRYIGYI 160


                  ...
gi 1958776351 203 CDL 205
Cdd:cd14563   161 CDL 163
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 213-351 5.41e-37

C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key form, of the PTEN protein, phosphatidyl-inositol triphosphate phosphatase, and it is the C-terminus. This domain may well include a CBR3 loop which means it plays a central role in membrane binding. This domain associates across an extensive interface with the N-terminal phosphatase domain DSPc (pfam00782) suggesting that the C2 domain productively positions the catalytic part of the protein onto the membrane.


:

Pssm-ID: 463081  Cd Length: 133  Bit Score: 135.48  E-value: 5.41e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351 213 PHFKPLTIKAITVSPIPFFNKQrNGCRPYCDVLIGETKIFSTCTDFERMKEYRVQDGKIFIPLNITVQGDVIVSMYHLRS 292
Cdd:pfam10409   1 PPPKPLTLHSIILHGIPNFKSG-GGCRPYIRIYQNKKKVFSTSGKYKKLKEYQQDDCVILFPKGIPVQGDVLVEFYHKGS 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958776351 293 TIGSRlqakvtnTQIFQLQFHSGFIPldTTVLKFTKPELDACDVP---EKYPQLFQVTLDIE 351
Cdd:pfam10409  80 DLLSE-------EKMFRFWFNTSFIE--DNTLTLPKNELDKADKDkkdKRFPKDFKVELLFS 132
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 848-893 4.57e-09

DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.


:

Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 52.93  E-value: 4.57e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1958776351 848 TPEQVKKVYRRAVLVVHPDKATGQPyeqYAKMIFMELNDAWSEFEN 893
Cdd:cd06257    13 SDEEIKKAYRKLALKYHPDKNPDDP---EAEEKFKEINEAYEVLSD 55
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 521-752 7.87e-07

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.40  E-value: 7.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351  521 TGPAQAGQVGVEDVFHPSGPASAQST---------PRRATTSASASPTlrvgegATFDPFGAPAK---PPGQDLLGSFLN 588
Cdd:PHA03247  2723 PGPAAARQASPALPAAPAPPAVPAGPatpggparpARPPTTAGPPAPA------PPAAPAAGPPRrltRPAVASLSESRE 2796

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351  589 TSNASSDPFLQP--TRSPSPTVHASSTPAVNIQPDIAGGWDWHAKP-----------GGFGMGSKSAATSPTGSTHGTPT 655
Cdd:PHA03247  2797 SLPSPWDPADPPaaVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPpgppppslplgGSVAPGGDVRRRPPSRSPAAKPA 2876

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351  656 HQSKPQTldpfadlgtlgsSSFASKPTTPTGLGGGFPPLSSPQKASPQPMgggwQQPAGYNWQQAQPKPQssmPHSSPQN 735
Cdd:PHA03247  2877 APARPPV------------RRLARPAVSRSTESFALPPDQPERPPQPQAP----PPPQPQPQPPPPPQPQ---PPPPPPP 2937

                          250
                   ....*....|....*..
gi 1958776351  736 RPNYNVSFSAMPAGQSD 752
Cdd:PHA03247  2938 RPQPPLAPTTDPAGAGE 2954
 
Name Accession Description Interval E-value
PTP_auxilin_N cd14563
N-terminal protein tyrosine phosphatase-like domain of auxilin; Auxilin, also called auxilin-1 ...
 43-205 2.79e-114

N-terminal protein tyrosine phosphatase-like domain of auxilin; Auxilin, also called auxilin-1 or DnaJ homolog subfamily C member 6 (DNAJC6), is a J-domain containing protein that recruits the ATP-dependent chaperone Hsc70 to newly budded clathrin-coated vesicles and promotes uncoating of clathrin-coated vesicles, driving the clathrin assembly#disassembly cycle. Mutations in the DNAJC6 gene, encoding auxilin, are associated with early-onset Parkinson's disease. Auxilin contains an N-terminal protein tyrosine phosphatase (PTP)-like domain similar to the PTP-like domain of PTEN, a phosphoinositide 3-phosphatase, and a C-terminal region with clathrin-binding and J domains.


Pssm-ID: 350411 [Multi-domain]  Cd Length: 163  Bit Score: 346.10  E-value: 2.79e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351  43 VSSYTKGDLDFTYVTSRIIVMSFPMDSVDIGFRNQVDDIRSFLDSRHLDHYTVYNLSPKSYRTAKFHSRVSECSWPIRQA 122
Cdd:cd14563     1 VASYTKGELDISYITSRIIVMSYPAEGVELGFRNHIEDVRSFLDSRHLDHYTVFNLSQKSYRSAKFHNRVSECSWPVRQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351 123 PSLHNLFAVCRNMYNWLLQNPKNVCVVHCLDGRAASSILVGAMFIFCNLYSTPGPAVRLLYAKRPGIGLSPSHRRYLGYM 202
Cdd:cd14563    81 PSLHNLFAVCKNMHNWLQQNPKNVCVIHCMDGRAASAVLVSAMFCFCHLFSNPVPAMQLLNAKRPGIGLWPSHRRYIGYI 160


                  ...
gi 1958776351 203 CDL 205
Cdd:cd14563   161 CDL 163
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 213-351 5.41e-37

C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key form, of the PTEN protein, phosphatidyl-inositol triphosphate phosphatase, and it is the C-terminus. This domain may well include a CBR3 loop which means it plays a central role in membrane binding. This domain associates across an extensive interface with the N-terminal phosphatase domain DSPc (pfam00782) suggesting that the C2 domain productively positions the catalytic part of the protein onto the membrane.


Pssm-ID: 463081  Cd Length: 133  Bit Score: 135.48  E-value: 5.41e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351 213 PHFKPLTIKAITVSPIPFFNKQrNGCRPYCDVLIGETKIFSTCTDFERMKEYRVQDGKIFIPLNITVQGDVIVSMYHLRS 292
Cdd:pfam10409   1 PPPKPLTLHSIILHGIPNFKSG-GGCRPYIRIYQNKKKVFSTSGKYKKLKEYQQDDCVILFPKGIPVQGDVLVEFYHKGS 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958776351 293 TIGSRlqakvtnTQIFQLQFHSGFIPldTTVLKFTKPELDACDVP---EKYPQLFQVTLDIE 351
Cdd:pfam10409  80 DLLSE-------EKMFRFWFNTSFIE--DNTLTLPKNELDKADKDkkdKRFPKDFKVELLFS 132
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 848-893 4.57e-09

DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.


Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 52.93  E-value: 4.57e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1958776351 848 TPEQVKKVYRRAVLVVHPDKATGQPyeqYAKMIFMELNDAWSEFEN 893
Cdd:cd06257    13 SDEEIKKAYRKLALKYHPDKNPDDP---EAEEKFKEINEAYEVLSD 55
DnaJ smart00271
DnaJ molecular chaperone homology domain;
848-894 3.14e-07

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 48.00  E-value: 3.14e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958776351  848 TPEQVKKVYRRAVLVVHPDKATGQPYEqyAKMIFMELNDAWSEFENQ 894
Cdd:smart00271  14 SLDEIKKAYRKLALKYHPDKNPGDKEE--AEEKFKEINEAYEVLSDP 58
PHA03247 PHA03247
large tegument protein UL36; Provisional
 521-752 7.87e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.40  E-value: 7.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351  521 TGPAQAGQVGVEDVFHPSGPASAQST---------PRRATTSASASPTlrvgegATFDPFGAPAK---PPGQDLLGSFLN 588
Cdd:PHA03247  2723 PGPAAARQASPALPAAPAPPAVPAGPatpggparpARPPTTAGPPAPA------PPAAPAAGPPRrltRPAVASLSESRE 2796

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351  589 TSNASSDPFLQP--TRSPSPTVHASSTPAVNIQPDIAGGWDWHAKP-----------GGFGMGSKSAATSPTGSTHGTPT 655
Cdd:PHA03247  2797 SLPSPWDPADPPaaVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPpgppppslplgGSVAPGGDVRRRPPSRSPAAKPA 2876

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351  656 HQSKPQTldpfadlgtlgsSSFASKPTTPTGLGGGFPPLSSPQKASPQPMgggwQQPAGYNWQQAQPKPQssmPHSSPQN 735
Cdd:PHA03247  2877 APARPPV------------RRLARPAVSRSTESFALPPDQPERPPQPQAP----PPPQPQPQPPPPPQPQ---PPPPPPP 2937

                          250
                   ....*....|....*..
gi 1958776351  736 RPNYNVSFSAMPAGQSD 752
Cdd:PHA03247  2938 RPQPPLAPTTDPAGAGE 2954
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 537-753 9.90e-06

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 49.38  E-value: 9.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351 537 PSGPASAQSTPRRATTS-ASASPTlrvGEGATFDPFGAPA-KPPGQDLLGSFLNTSNASSDPFLQPTRSPSPtvHASSTP 614
Cdd:pfam03154 177 QSGAASPPSPPPPGTTQaATAGPT---PSAPSVPPQGSPAtSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSP--HPPLQP 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351 615 AVNIQPDIAGGWDWHAKPGGFGMGSKSAATSPTGsthgtPTHQSKPQTLDPFADLGTLGSSSFASKPTTPTGLGGGFPPL 694
Cdd:pfam03154 252 MTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTG-----PSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIH 326

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958776351 695 SSPQKASPQPmgggwQQPAgynwqQAQPKPQSsmPHSSPQNRPNYNVSFSAMPAGQSDR 753
Cdd:pfam03154 327 TPPSQSQLQS-----QQPP-----REQPLPPA--PLSMPHIKPPPTTPIPQLPNPQSHK 373
PPE COG5651
PPE-repeat protein [Function unknown];
494-714 1.90e-05

PPE-repeat protein [Function unknown];


Pssm-ID: 444372 [Multi-domain]  Cd Length: 385  Bit Score: 47.97  E-value: 1.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351 494 VSTNFSPLAAPPSNSELLSDLFGGGGATGPAQAGQVGVEDVFHPSGPASAQSTPRRATTSASASPTlrvGEGATFDPFGA 573
Cdd:COG5651   173 TITNPGGLLGAQNAGSGNTSSNPGFANLGLTGLNQVGIGGLNSGSGPIGLNSGPGNTGFAGTGAAA---GAAAAAAAAAA 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351 574 PAKPPGQDLLGSFLNTSNASSDPFLQPTRSPSPtvhASSTPAVNIQPDIAGGWDWHAKPGGFGmgskSAATSPTGSTHGT 653
Cdd:COG5651   250 AAGAGASAALASLAATLLNASSLGLAATAASSA---ATNLGLAGSPLGLAGGGAGAAAATGLG----LGAGGAAGAAGAT 322

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958776351 654 PTHQSKPQTLDPFADLG-TLGSSSFASKPTTPTGLGGGFPPLSSPQKASPQPMGGGWQQPAG 714
Cdd:COG5651   323 GAGAALGAGAAAAAAGAaAGAGAAAAAAAGGAGGGGGGALGAGGGGGSAGAAAGAASGGGAA 384
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 848-889 2.43e-05

DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.


Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 42.85  E-value: 2.43e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958776351 848 TPEQVKKVYRRAVLVVHPDKATGQPyeQYAKMiFMELNDAWS 889
Cdd:pfam00226  13 SDEEIKKAYRKLALKYHPDKNPGDP--EAEEK-FKEINEAYE 51
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
847-888 1.86e-03

DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 37.85  E-value: 1.86e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1958776351 847 VTPEQVKKVYRRAVLVVHPDK-ATGQPYEQ--YAKMIFMELNDAW 888
Cdd:COG1076    16 ADDAELKRAYRKLQREHHPDRlAAGLPEEEqrLALQKAAAINEAY 60
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 546-694 4.04e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 41.13  E-value: 4.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351  546 TPRRATTSASASPTLRVGEGATFDPFGA-----PAKPPGQ----DLLGSFLNTSNASSDPflQPTRSPSPtvhASSTPAV 616
Cdd:TIGR00927  285 TPRRVESNSSTNHWGLVGKNNLTTPQGTvlehtPATSEGQvtisIMTGSSPAETKASTAA--WKIRNPLS---RTSAPAV 359

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351  617 NIQPdiAGGWDWHAKPggfgmgSKSAATSPTGSTHGTPTHQ------SKPQTLDPFADLGTLGSSSFASKPT-TPTGLGG 689
Cdd:TIGR00927  360 RIAS--ATFRGLEKNP------STAPSTPATPRVRAVLTTQvhhcvvVKPAPAVPTTPSPSLTTALFPEAPSpSPSALPP 431


                   ....*
gi 1958776351  690 GFPPL 694
Cdd:TIGR00927  432 GQPDL 436
 
Name Accession Description Interval E-value
PTP_auxilin_N cd14563
N-terminal protein tyrosine phosphatase-like domain of auxilin; Auxilin, also called auxilin-1 ...
 43-205 2.79e-114

N-terminal protein tyrosine phosphatase-like domain of auxilin; Auxilin, also called auxilin-1 or DnaJ homolog subfamily C member 6 (DNAJC6), is a J-domain containing protein that recruits the ATP-dependent chaperone Hsc70 to newly budded clathrin-coated vesicles and promotes uncoating of clathrin-coated vesicles, driving the clathrin assembly#disassembly cycle. Mutations in the DNAJC6 gene, encoding auxilin, are associated with early-onset Parkinson's disease. Auxilin contains an N-terminal protein tyrosine phosphatase (PTP)-like domain similar to the PTP-like domain of PTEN, a phosphoinositide 3-phosphatase, and a C-terminal region with clathrin-binding and J domains.


Pssm-ID: 350411 [Multi-domain]  Cd Length: 163  Bit Score: 346.10  E-value: 2.79e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351  43 VSSYTKGDLDFTYVTSRIIVMSFPMDSVDIGFRNQVDDIRSFLDSRHLDHYTVYNLSPKSYRTAKFHSRVSECSWPIRQA 122
Cdd:cd14563     1 VASYTKGELDISYITSRIIVMSYPAEGVELGFRNHIEDVRSFLDSRHLDHYTVFNLSQKSYRSAKFHNRVSECSWPVRQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351 123 PSLHNLFAVCRNMYNWLLQNPKNVCVVHCLDGRAASSILVGAMFIFCNLYSTPGPAVRLLYAKRPGIGLSPSHRRYLGYM 202
Cdd:cd14563    81 PSLHNLFAVCKNMHNWLQQNPKNVCVIHCMDGRAASAVLVSAMFCFCHLFSNPVPAMQLLNAKRPGIGLWPSHRRYIGYI 160


                  ...
gi 1958776351 203 CDL 205
Cdd:cd14563   161 CDL 163
PTP_auxilin-like cd14511
protein tyrosine phosphatase-like domain of auxilin and similar proteins; This subfamily ...
 43-205 4.67e-95

protein tyrosine phosphatase-like domain of auxilin and similar proteins; This subfamily contains proteins similar to auxilin, characterized by also containing a J domain. It includes auxilin, also called auxilin-1, and cyclin-G-associated kinase (GAK), also called auxilin-2. Auxilin-1 and -2 facilitate Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, while auxilin-1 which is nerve-specific. Both proteins contain a protein tyrosine phosphatase (PTP)-like domain similar to the PTP-like domain of PTEN (a phosphoinositide 3-phosphatase), and a C-terminal region with clathrin-binding and J domains. In addition, GAK contains an N-terminal protein kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2.


Pssm-ID: 350361 [Multi-domain]  Cd Length: 164  Bit Score: 295.80  E-value: 4.67e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351  43 VSSYTKGDLDFTYVTSRIIVMSFPMDSVDIGFR-NQVDDIRSFLDSRHLDHYTVYNLSPKSYRTAKFHSRVSECSWPIRQ 121
Cdd:cd14511     1 QQSYARNDLDISYITSRIIVMPFPAEGIESTYRkNNIEDVRAFLDSRHPQKYSVYNLSPRSYPTLRLPSRVVECSWPYRR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351 122 APSLHNLFAVCRNMYNWLLQNPKNVCVVHCLDGRAASSILVGAMFIFCNLYSTPGPAVRLLYAKRPGIGLSPSHRRYLGY 201
Cdd:cd14511    81 APSLHALYALCRDIYQWLNKDPKNVIVIHCTDGKAASATVVCALLVYCGLFKTPEDALQMFAVKRCPPGLSPSELRYLYY 160


                  ....
gi 1958776351 202 MCDL 205
Cdd:cd14511   161 FSDI 164
PTP_GAK cd14564
protein tyrosine phosphatase-like domain of cyclin-G-associated kinase; cyclin-G-associated ...
 43-205 1.41e-77

protein tyrosine phosphatase-like domain of cyclin-G-associated kinase; cyclin-G-associated kinase (GAK), also called auxilin-2, contains an N-terminal protein kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of a protein tyrosine phosphatase (PTP)-like domain similar to the PTP-like domain of PTEN (a phosphoinositide 3-phosphatase), and a C-terminal region with clathrin-binding and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor.


Pssm-ID: 350412 [Multi-domain]  Cd Length: 163  Bit Score: 249.05  E-value: 1.41e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351  43 VSSYTKGDLDFTYVTSRIIVMSFPMDSVDIGFRNQVDDIRSFLDSRHLDHYTVYNLSPKSYRTAKFHSRVSECSWPIRQA 122
Cdd:cd14564     1 VANYAKGDLDISYITSRIAVMSFPAEGVESAIKNNIEDVRLFLDSRHPGHYAVYNLSQRTYRPSRFHNRVSECGWPARRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351 123 PSLHNLFAVCRNMYNWLLQNPKNVCVVHCLDGRAASSILVGAMFIFCNLYSTPGPAVRLLYAKRPGIGLSPSHRRYLGYM 202
Cdd:cd14564    81 PNLQNLYSICKNMHLWLKQDQKNICIVHCLDGRAASAVVVCSFLCFCRLFTTAEAAVYMFSMKRCPPGIWPSHKRYIEYM 160


                  ...
gi 1958776351 203 CDL 205
Cdd:cd14564   161 CDM 163
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 52-205 4.19e-61

protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar proteins; Phosphatase and tensin homolog (PTEN) is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It dephosphorylates phosphoinositide trisphosphate. In addition to PTEN, this family includes tensins, voltage-sensitive phosphatases (VSPs), and auxilins. They all contain a protein tyrosine phosphatase-like domain although not all are active phosphatases. Tensins are intracellular proteins that act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility, and they may or may not have phosphatase activity. VSPs are phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. Auxilins are J domain-containing proteins that facilitate Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles, and they do not exhibit phosphatase activity.


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 204.35  E-value: 4.19e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351  52 DFTYVTSRIIVMSFPMDSV-DIGFRNQVDDIRSFLDSRHLDHYTVYNLSPKSYR-TAKFHSRVSECSWPIRQAPSLHNLF 129
Cdd:cd14497     1 DLSYITPRIIAMSFPATGYpESLYRNSIDDVANFLNTHHPDHYMIFNLSEEEYDdDSKFEGRVLHYGFPDHHPPPLGLLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351 130 AVCRNMYNWLLQNPKNVCVVHCLDGRAASSILVGAMFIFCNLYSTPGPAVRLLYAKRPGIGL----SPSHRRYLGYMCDL 205
Cdd:cd14497    81 EIVDDIDSWLSEDPNNVAVVHCKAGKGRTGTVICAYLLYYGQYSTADEALEYFAKKRFKEGLpgvtIPSQLRYLQYFERL 160
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 213-351 5.41e-37

C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key form, of the PTEN protein, phosphatidyl-inositol triphosphate phosphatase, and it is the C-terminus. This domain may well include a CBR3 loop which means it plays a central role in membrane binding. This domain associates across an extensive interface with the N-terminal phosphatase domain DSPc (pfam00782) suggesting that the C2 domain productively positions the catalytic part of the protein onto the membrane.


Pssm-ID: 463081  Cd Length: 133  Bit Score: 135.48  E-value: 5.41e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351 213 PHFKPLTIKAITVSPIPFFNKQrNGCRPYCDVLIGETKIFSTCTDFERMKEYRVQDGKIFIPLNITVQGDVIVSMYHLRS 292
Cdd:pfam10409   1 PPPKPLTLHSIILHGIPNFKSG-GGCRPYIRIYQNKKKVFSTSGKYKKLKEYQQDDCVILFPKGIPVQGDVLVEFYHKGS 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958776351 293 TIGSRlqakvtnTQIFQLQFHSGFIPldTTVLKFTKPELDACDVP---EKYPQLFQVTLDIE 351
Cdd:pfam10409  80 DLLSE-------EKMFRFWFNTSFIE--DNTLTLPKNELDKADKDkkdKRFPKDFKVELLFS 132
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 52-201 5.44e-36

protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; Phosphatase and tensin homolog (PTEN), also phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN or mutated in multiple advanced cancers 1 (MMAC1), is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It is a critical endogenous inhibitor of phosphoinositide signaling. It dephosphorylates phosphoinositide trisphosphate, and therefore, has the function of negatively regulating Akt. The PTEN/PI3K/AKT pathway regulates the signaling of multiple biological processes such as apoptosis, metabolism, cell proliferation, and cell growth. PTEN contains an N-terminal PIP-binding domain, a protein tyrosine phosphatase (PTP)-like catalytic domain, a regulatory C2 domain responsible for its cellular location, a C-tail containing phosphorylation sites, and a C-terminal PDZ domain.


Pssm-ID: 350359 [Multi-domain]  Cd Length: 158  Bit Score: 133.48  E-value: 5.44e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351  52 DFTYVTSRIIVMSFPMDSVDIGFRNQVDDIRSFLDSRHLDHYTVYNL-SPKSYRTAKFHSRVSECSWPIRQAPSLHNLFA 130
Cdd:cd14509     1 DLTYITPNIIAMGFPAEGVEGVYRNPIDDVQRFLETKHKGHYKVYNLcSERSYDPSKFNGRVAEYPFDDHNPPPLELIKP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958776351 131 VCRNMYNWLLQNPKNVCVVHCLDGRAASSILVGAMFIFCNLYSTPGPAVRLLYAKRP--GIGLS-PSHRRYLGY 201
Cdd:cd14509    81 FCEDVDEWLKEDEKNVAAVHCKAGKGRTGVMICCYLLYLGKFPSAKEALDFYGAKRTknKKGVTiPSQRRYVYY 154
PTP_tensin cd14508
protein tyrosine phosphatase-like domain of tensins; The tensin family of intracellular ...
 52-205 7.19e-36

protein tyrosine phosphatase-like domain of tensins; The tensin family of intracellular proteins (tensin-1, -2, -3 and -4) act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. Dysregulation of tensin expression has been implicated in human cancer. Tensin-1, -2, and -3 contain an N-terminal region with a protein tyrosine phosphatase (PTP)-like domain followed by a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains. In addition, tensin-2 contains a zinc finger N-terminal to its PTP domain. Tensin-4 is not included in this model as it does not contain a PTP-like domain.


Pssm-ID: 350358 [Multi-domain]  Cd Length: 159  Bit Score: 133.28  E-value: 7.19e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351  52 DFTYVTSRIIVMSFPMDSVDIGFRNQVDDIRSFLDSRHLDHYTVYNLSPKSYRTAKFHSRVSECSWPIRQAPSLHNLFAV 131
Cdd:cd14508     1 DLTYITERIIALSFPSTCSEQTYRHNLREAAHLLQSKHGDNYMVFNLSERRHDLRSLNPKVLDFGWPELHAPPLEKLCSI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958776351 132 CRNMYNWLLQNPKNVCVVHCLDGRAASSILVGAMFIFCNLYSTPGPAVRLLYAKR-----PGIGLSPSHRRYLGYMCDL 205
Cdd:cd14508    81 CKNMDSWLNADPQNVVVLHCKGGKGRLGVVVSAYMHYSKISATADQALDRFAMKRfyddkVGPLGQPSQKRYVGYFSGL 159
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 46-201 9.72e-34

protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase/transmembrane phosphatase with tensin homology; Voltage-sensitive phosphatase (VSP) proteins comprise a family of phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. This family is conserved in deuterostomes; VSP was first identified as a sperm flagellar plasma membrane protein in Ciona intestinalis. Gene duplication events in primates resulted in the presence of paralogs, transmembrane phosphatase with tensin homology (TPTE) and TPTE2, that retain protein domain architecture but, in the case of TPTE, have lost catalytic activity. TPTE, also called cancer/testis antigen 44 (CT44), may play a role in the signal transduction pathways of the endocrine or spermatogenic function of the testis. TPTE2, also called TPTE and PTEN homologous inositol lipid phosphatase (TPIP), occurs in several differentially spliced forms; TPIP alpha displays phosphoinositide 3-phosphatase activity and is localized on the endoplasmic reticulum, while TPIP beta is cytosolic and lacks detectable phosphatase activity. VSP/TPTE proteins contain an N-terminal voltage sensor consisting of four transmembrane segments, a protein tyrosine phosphatase (PTP)-like phosphoinositide phosphatase catalytic domain, followed by a regulatory C2 domain.


Pssm-ID: 350360 [Multi-domain]  Cd Length: 177  Bit Score: 127.86  E-value: 9.72e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351  46 YTKG--DLDFTYVTSRIIVMSFPMDSVDIGFRNQVDDIRSFLDSRHLDHYTVYNL-SPKSYRTAKFHSRVSECSWPIRQA 122
Cdd:cd14510     7 YQKDgfDLDLTYVTDRVIAMSFPSSGKQAFYRNPIEEVVRFLDTKHPDHYKVYNLcSERGYDPKYFHNRVERVPIDDHNV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351 123 PSLHNLFAVCRNMYNWLLQNPKNVCVVHCLDGRAASSILVGAMFIFCNLYSTPGPAVRLLYAKRPGIGLS--------PS 194
Cdd:cd14510    87 PTLDEMLSFTAEVREWMAADPKNVVAIHCKGGKGRTGTMVCAWLIYSGQFESAKEALEYFGERRTDKSVSskfqgvetPS 166


                  ....*..
gi 1958776351 195 HRRYLGY 201
Cdd:cd14510   167 QSRYVGY 173
PTP_tensin-3 cd14561
protein tyrosine phosphatase-like domain of tensin-3; Tensin-3 (TNS3) is also called ...
 52-205 4.97e-27

protein tyrosine phosphatase-like domain of tensin-3; Tensin-3 (TNS3) is also called tensin-like SH2 domain-containing protein 1 (TENS1) or tumor endothelial marker (TEM6). It is part of the tensin family of intracellular proteins (tensin-1, -2, -3 and -4), which act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. Tensin-3 contributes to cell migration, anchorage-independent growth, tumorigenesis, and metastasis of cancer cells. It cooperates with Dock5, an exchange factor for the small GTPase Rac, for osteoclast activity to ensure the correct organization of podosomes. Tensin-3 contains an N-terminal region with a protein tyrosine phosphatase (PTP)-like domain followed by a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains.


Pssm-ID: 350409 [Multi-domain]  Cd Length: 159  Bit Score: 107.72  E-value: 4.97e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351  52 DFTYVTSRIIVMSFPMDSVDIGFRNQVDDIRSFLDSRHLDHYTVYNLSPKSYRTAKFHSRVSECSWPIRQAPSLHNLFAV 131
Cdd:cd14561     1 DLTYITERIIAVSFPADCSEETYLHNLQDVTRMLKSKHGDNYLVLNLSEKRYELTKLNPKIMDVGWPDLHAPPLDKMCTI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958776351 132 CRNMYNWLLQNPKNVCVVHCLDGRAASSILVGAMFIFCNLYSTPGPAV-----RLLYAKRPGIGLSPSHRRYLGYMCDL 205
Cdd:cd14561    81 CKAMESWLNSDPLHVVVIHCRGGKGRIGVVISSYMHFTNVSASADQALdrfamKKFYDDKVSALMQPSQKRYVQFLSGL 159
PTP_tensin-1 cd14560
protein tyrosine phosphatase-like domain of tensin-1; Tensin-1 (TNS1) is part of the tensin ...
 52-205 2.66e-25

protein tyrosine phosphatase-like domain of tensin-1; Tensin-1 (TNS1) is part of the tensin family of intracellular proteins (tensin-1, -2, -3 and -4), which act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. It plays an essential role in TGF-beta-induced myofibroblast differentiation and myofibroblast-mediated formation of extracellular fibronectin and collagen matrix. It also positively regulates RhoA activity through its interaction with DLC1, a RhoGAP-containing tumor suppressor; the tensin-1-DLC1-RhoA signaling axis is critical in regulating cellular functions that lead to angiogenesis. Tensin-1 contains an N-terminal region with a protein tyrosine phosphatase (PTP)-like domain followed by a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains.


Pssm-ID: 350408 [Multi-domain]  Cd Length: 159  Bit Score: 103.14  E-value: 2.66e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351  52 DFTYVTSRIIVMSFPMDSVDIGFRNQVDDIRSFLDSRHLDHYTVYNLSPKSYRTAKFHSRVSECSWPIRQAPSLHNLFAV 131
Cdd:cd14560     1 DLVYITERIISVSFPSTAEEPSFRSNLKEVAQMLKSKHGDNYLLFNLSERRHDISKLHPKVLDFGWPDLHAPALEKICSI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351 132 CRNMYNWLLQNPKNVCVVHCLDGRAASSILVGAMFIFCNLYSTPGPAVRLLYAKR-------PgIGlSPSHRRYLGYMCD 204
Cdd:cd14560    81 CKAMDTWLNADPHNVVVIHNKGNRGRTGVVIAAYMHYSNISASADQALDRFAMKRfyedkvvP-VG-QPSQKRYVHYFSG 158


                  .
gi 1958776351 205 L 205
Cdd:cd14560   159 L 159
PTP_tensin-2 cd14562
protein tyrosine phosphatase-like domain of tensin-2; Tensin-2 (TNS2) is also called ...
 52-205 2.68e-23

protein tyrosine phosphatase-like domain of tensin-2; Tensin-2 (TNS2) is also called tensin-like C1 domain-containing phosphatase (TENC1) or C1 domain-containing phosphatase and tensin homolog (C1-TEN). It is part of the tensin family of intracellular proteins (tensin-1, -2, -3 and -4), which act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. Tensin-2 is an essential component for the maintenance of glomerular basement membrane (GBM) structures. It also modulates cell contractility and remodeling of collagen fibers through the DLC1, a RhoGAP that binds to tensins in focal adhesions. Tensin-2 may have phosphatase activity; it reduces AKT1 phosphorylation. It contains an N-terminal region with a zinc finger, a protein tyrosine phosphatase (PTP)-like domain and a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains.


Pssm-ID: 350410 [Multi-domain]  Cd Length: 159  Bit Score: 97.33  E-value: 2.68e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351  52 DFTYVTSRIIVMSFPMDSVDIGFRNQVDDIRSFLDSRHLDHYTVYNLSPKSYRTAKFHSRVSECSWPIRQAPSLHNLFAV 131
Cdd:cd14562     1 DLTYITERIISVFFPPALEEQRYRGNLREVAQMLKSKHEDKYLLFNLSEKRHDITRLNPKVQDFGWPDLHAPPLDKICSI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958776351 132 CRNMYNWLLQNPKNVCVVHCLDGRAASSILVGAMFIFCNLYSTPGPAVRLLYAK-----RPGIGLSPSHRRYLGYMCDL 205
Cdd:cd14562    81 CKAMETWLNADPQHVVVLHCKGNKGKTGVIVAAYMHYSKISAGADQALSTLAMRkfcedKVATSLQPSQRRYISYFGGL 159
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 848-893 4.57e-09

DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.


Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 52.93  E-value: 4.57e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1958776351 848 TPEQVKKVYRRAVLVVHPDKATGQPyeqYAKMIFMELNDAWSEFEN 893
Cdd:cd06257    13 SDEEIKKAYRKLALKYHPDKNPDDP---EAEEKFKEINEAYEVLSD 55
DnaJ smart00271
DnaJ molecular chaperone homology domain;
848-894 3.14e-07

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 48.00  E-value: 3.14e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958776351  848 TPEQVKKVYRRAVLVVHPDKATGQPYEqyAKMIFMELNDAWSEFENQ 894
Cdd:smart00271  14 SLDEIKKAYRKLALKYHPDKNPGDKEE--AEEKFKEINEAYEVLSDP 58
PHA03247 PHA03247
large tegument protein UL36; Provisional
 521-752 7.87e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.40  E-value: 7.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351  521 TGPAQAGQVGVEDVFHPSGPASAQST---------PRRATTSASASPTlrvgegATFDPFGAPAK---PPGQDLLGSFLN 588
Cdd:PHA03247  2723 PGPAAARQASPALPAAPAPPAVPAGPatpggparpARPPTTAGPPAPA------PPAAPAAGPPRrltRPAVASLSESRE 2796

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351  589 TSNASSDPFLQP--TRSPSPTVHASSTPAVNIQPDIAGGWDWHAKP-----------GGFGMGSKSAATSPTGSTHGTPT 655
Cdd:PHA03247  2797 SLPSPWDPADPPaaVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPpgppppslplgGSVAPGGDVRRRPPSRSPAAKPA 2876

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351  656 HQSKPQTldpfadlgtlgsSSFASKPTTPTGLGGGFPPLSSPQKASPQPMgggwQQPAGYNWQQAQPKPQssmPHSSPQN 735
Cdd:PHA03247  2877 APARPPV------------RRLARPAVSRSTESFALPPDQPERPPQPQAP----PPPQPQPQPPPPPQPQ---PPPPPPP 2937

                          250
                   ....*....|....*..
gi 1958776351  736 RPNYNVSFSAMPAGQSD 752
Cdd:PHA03247  2938 RPQPPLAPTTDPAGAGE 2954
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 537-753 9.90e-06

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 49.38  E-value: 9.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351 537 PSGPASAQSTPRRATTS-ASASPTlrvGEGATFDPFGAPA-KPPGQDLLGSFLNTSNASSDPFLQPTRSPSPtvHASSTP 614
Cdd:pfam03154 177 QSGAASPPSPPPPGTTQaATAGPT---PSAPSVPPQGSPAtSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSP--HPPLQP 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351 615 AVNIQPDIAGGWDWHAKPGGFGMGSKSAATSPTGsthgtPTHQSKPQTLDPFADLGTLGSSSFASKPTTPTGLGGGFPPL 694
Cdd:pfam03154 252 MTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTG-----PSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIH 326

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958776351 695 SSPQKASPQPmgggwQQPAgynwqQAQPKPQSsmPHSSPQNRPNYNVSFSAMPAGQSDR 753
Cdd:pfam03154 327 TPPSQSQLQS-----QQPP-----REQPLPPA--PLSMPHIKPPPTTPIPQLPNPQSHK 373
PPE COG5651
PPE-repeat protein [Function unknown];
494-714 1.90e-05

PPE-repeat protein [Function unknown];


Pssm-ID: 444372 [Multi-domain]  Cd Length: 385  Bit Score: 47.97  E-value: 1.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351 494 VSTNFSPLAAPPSNSELLSDLFGGGGATGPAQAGQVGVEDVFHPSGPASAQSTPRRATTSASASPTlrvGEGATFDPFGA 573
Cdd:COG5651   173 TITNPGGLLGAQNAGSGNTSSNPGFANLGLTGLNQVGIGGLNSGSGPIGLNSGPGNTGFAGTGAAA---GAAAAAAAAAA 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351 574 PAKPPGQDLLGSFLNTSNASSDPFLQPTRSPSPtvhASSTPAVNIQPDIAGGWDWHAKPGGFGmgskSAATSPTGSTHGT 653
Cdd:COG5651   250 AAGAGASAALASLAATLLNASSLGLAATAASSA---ATNLGLAGSPLGLAGGGAGAAAATGLG----LGAGGAAGAAGAT 322

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958776351 654 PTHQSKPQTLDPFADLG-TLGSSSFASKPTTPTGLGGGFPPLSSPQKASPQPMGGGWQQPAG 714
Cdd:COG5651   323 GAGAALGAGAAAAAAGAaAGAGAAAAAAAGGAGGGGGGALGAGGGGGSAGAAAGAASGGGAA 384
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 848-889 2.43e-05

DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.


Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 42.85  E-value: 2.43e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958776351 848 TPEQVKKVYRRAVLVVHPDKATGQPyeQYAKMiFMELNDAWS 889
Cdd:pfam00226  13 SDEEIKKAYRKLALKYHPDKNPGDP--EAEEK-FKEINEAYE 51
PHA03247 PHA03247
large tegument protein UL36; Provisional
 491-735 3.35e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 3.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351  491 GSDVSTNFSPLAAPPSNSELLSdlfgGGGATGPAQAGQVGVEdvfHPSGPASAQSTPRRATTSASASPTLRVGEGATFDP 570
Cdd:PHA03247  2730 QASPALPAAPAPPAVPAGPATP----GGPARPARPPTTAGPP---APAPPAAPAAGPPRRLTRPAVASLSESRESLPSPW 2802

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351  571 fgAPAKPPGQDLLGSFLNTSNASSDPFLQPTRSPSPTvhASSTPAVNIQPDIA-GGWdwhAKPGG---FGMGSKSAATSP 646
Cdd:PHA03247  2803 --DPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPT--APPPPPGPPPPSLPlGGS---VAPGGdvrRRPPSRSPAAKP 2875

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351  647 TGSTHGTPTHQSKP---QTLDPFA----DLGTLGSSSFASKPTTPtglgggfPPLSSPQKASPQPMGGGWQQPAGYNWQQ 719
Cdd:PHA03247  2876 AAPARPPVRRLARPavsRSTESFAlppdQPERPPQPQAPPPPQPQ-------PQPPPPPQPQPPPPPPPRPQPPLAPTTD 2948

                          250
                   ....*....|....*.
gi 1958776351  720 AQPKPQSSMPHSSPQN 735
Cdd:PHA03247  2949 PAGAGEPSGAVPQPWL 2964
PHA03378 PHA03378
EBNA-3B; Provisional
 500-767 1.40e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 45.83  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351 500 PLAAPPSNSELLSDLfgGGGATGPAQAGQVGVEDVFHPSGPAS-----AQSTPRRATTSASASPTLRVG-EGATFDPFG- 572
Cdd:PHA03378  571 PLQIQPLTSPTTSQL--ASSAPSYAQTPWPVPHPSQTPEPPTTqshipETSAPRQWPMPLRPIPMRPLRmQPITFNVLVf 648

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351 573 -APAKPPGQDLLGSFLNTSNASSDPFLQPTRSPSPTVHASSTPAVNIQPDIAGGWDWHAKPGGFGMGSKSAATSPTGSTH 651
Cdd:PHA03378  649 pTPHQPPQVEITPYKPTWTQIGHIPYQPSPTGANTMLPIQWAPGTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRARPPA 728

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351 652 GTPTHQSKPQTLD-----PFADLGTLGSSSFASKPTTPTGLGGGFPPLSSPQKASPQPMGGGWQQPAGYNWQQAQPKPQS 726
Cdd:PHA03378  729 AAPGRARPPAAAPgrarpPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRGAPTPQPPPQAGPTSMQ 808

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1958776351 727 SMPHSSPQNRPNYNVSFSAMPAGQSDRGKGSTNLEG---KQKAA 767
Cdd:PHA03378  809 LMPRAAPGQQGPTKQILRQLLTGGVKRGRPSLKKPAaleRQAAA 852
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 527-734 9.50e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.05  E-value: 9.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351 527 GQVGVEDVFHPSGPASAQSTPRRATTSASASPTLRVGEGAtfdpfgAPAKPPGQDllgsflnTSNASSDPFLQPTRSPSP 606
Cdd:PRK07764  580 GDWQVEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPA------APAAPAAPA-------PAGAAAAPAEASAAPAPG 646

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351 607 TVHASSTPAVNIQPDI-AGGWDWHAKPGGFGMGSKSAATSPTGSTHGTPTHQSKPQTLDPFADLGTLGSSSFASKPTTPT 685
Cdd:PRK07764  647 VAAPEHHPKHVAVPDAsDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQ 726

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958776351 686 GLGGGFPPLSSPQKASPQPMGGGWQQPAGYNWQQAQPKPQSSMPHSSPQ 734
Cdd:PRK07764  727 GASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPP 775
PHA03247 PHA03247
large tegument protein UL36; Provisional
 457-736 1.42e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351  457 ADGDKPHGAKKPGKKQQEPAappppeevdllglegsdvstnfSPLAAPPSNSELLSDLFGGGGATGP--------AQAGQ 528
Cdd:PHA03247  2603 DDRGDPRGPAPPSPLPPDTH----------------------APDPPPPSPSPAANEPDPHPPPTVPpperprddPAPGR 2660

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351  529 VGV-EDVFHPSGPASAQSTPRRATTSAsASPTlrVGEGATF----DPFGAPAKPPGQDLLGSFLNTSNAS---SDPFLQP 600
Cdd:PHA03247  2661 VSRpRRARRLGRAAQASSPPQRPRRRA-ARPT--VGSLTSLadppPPPPTPEPAPHALVSATPLPPGPAAarqASPALPA 2737

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351  601 TRSPSPTVHASSTPAVN---IQPDIAGGWDWHAKPGGFGMGSKSAATSPTGSThGTPTHQSKPQTLDPfADLGTLGSSSF 677
Cdd:PHA03247  2738 APAPPAVPAGPATPGGParpARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVAS-LSESRESLPSPWDP-ADPPAAVLAPA 2815

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958776351  678 ASKPTTPTGLGGGFPPLSSPQKASPQPMG--------GGWQQPAGYNWQQAQPKPQSSMPHSSPQNR 736
Cdd:PHA03247  2816 AALPPAASPAGPLPPPTSAQPTAPPPPPGppppslplGGSVAPGGDVRRRPPSRSPAAKPAAPARPP 2882
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
847-888 1.86e-03

DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 37.85  E-value: 1.86e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1958776351 847 VTPEQVKKVYRRAVLVVHPDK-ATGQPYEQ--YAKMIFMELNDAW 888
Cdd:COG1076    16 ADDAELKRAYRKLQREHHPDRlAAGLPEEEqrLALQKAAAINEAY 60
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
848-888 2.10e-03

Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 38.16  E-value: 2.10e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958776351 848 TPEQVKKVYRRAVLVVHPDkaTGQPYEQYAKMIFMELNDAW 888
Cdd:COG2214    18 SLEEIRQAYRRLAKLLHPD--RGGELKALAEELFQRLNEAY 56
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
491-696 2.13e-03

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 41.66  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351 491 GSDVSTNFSPLAAPPSNSELLSDLFGGGGATGPAQAGQVGVEDvfhpSGPASAQSTPRRATTSASASPTLRVGegATFDP 570
Cdd:COG3469    15 ASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSA----GSGTGTTAASSTAATSSTTSTTATAT--AAAAA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351 571 FGAPAKPPGQDLLGSFLNTSNASSDPFLQPTRSPSPTVHASSTPAVNIQPDIAGGWDWHAKPGGFGMGSKSAATSPTGST 650
Cdd:COG3469    89 ATSTSATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTETATGGTTTTST 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1958776351 651 HGTPTHQSKPQTLDPFADLGTLGSSSFASKPTTPTGLGGGFPPLSS 696
Cdd:COG3469   169 TTTTTSASTTPSATTTATATTASGATTPSATTTATTTGPPTPGLPK 214
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 537-733 2.71e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.70  E-value: 2.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351  537 PSGPASAQSTPRRATTSASASPTLRVGEG---ATFDPFGAPAKPPGQDLLGS--------FLNTSNASSDPflqpTRSPS 605
Cdd:PHA03307   222 PAPGRSAADDAGASSSDSSSSESSGCGWGpenECPLPRPAPITLPTRIWEASgwngpssrPGPASSSSSPR----ERSPS 297

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351  606 PTVHASSTPAVNIQPDIAGGW-----DWHAKPGGFGMGSKSAATSPTGSTHGTPTHQSKPQTLDPfadlgtlgsssfASK 680
Cdd:PHA03307   298 PSPSSPGSGPAPSSPRASSSSsssreSSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADP------------SSP 365

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958776351  681 PTTPTGLGGgfPPLSSPQKASPQPMGGGWQQPAGYNWQQAQPKPQSSMPHSSP 733
Cdd:PHA03307   366 RKRPRPSRA--PSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSP 416
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 546-694 4.04e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 41.13  E-value: 4.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351  546 TPRRATTSASASPTLRVGEGATFDPFGA-----PAKPPGQ----DLLGSFLNTSNASSDPflQPTRSPSPtvhASSTPAV 616
Cdd:TIGR00927  285 TPRRVESNSSTNHWGLVGKNNLTTPQGTvlehtPATSEGQvtisIMTGSSPAETKASTAA--WKIRNPLS---RTSAPAV 359

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351  617 NIQPdiAGGWDWHAKPggfgmgSKSAATSPTGSTHGTPTHQ------SKPQTLDPFADLGTLGSSSFASKPT-TPTGLGG 689
Cdd:TIGR00927  360 RIAS--ATFRGLEKNP------STAPSTPATPRVRAVLTTQvhhcvvVKPAPAVPTTPSPSLTTALFPEAPSpSPSALPP 431


                   ....*
gi 1958776351  690 GFPPL 694
Cdd:TIGR00927  432 GQPDL 436
DUF1373 pfam07117
Protein of unknown function (DUF1373); This family consists of several hypothetical proteins ...
 679-775 4.94e-03

Protein of unknown function (DUF1373); This family consists of several hypothetical proteins which seem to be specific to Oryzias latipes (Japanese ricefish). Members of this family are typically around 200 residues in length. The function of this family is unknown.


Pssm-ID: 462093 [Multi-domain]  Cd Length: 212  Bit Score: 39.39  E-value: 4.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351 679 SKPTTPTGLGGGFPPLSSPQKASPQPMGGGWQQP---AGYNWQ-QAQPKPQSSMPHSSPQNRPNYNVSFSAMPAGQSDRG 754
Cdd:pfam07117  43 PRPEEEEGQGGGGGTFPFPGSPEPEPGGGGSGPMpmsASAPEPePAKAKPQRPAPAQGHGHGGGGDSDSSGSGSGHQGSG 122

                          90       100
                  ....*....|....*....|.
gi 1958776351 755 KGSTNLEGKQKAADFEDLLSS 775
Cdd:pfam07117 123 GAGAGAGAPGHQHEQEQESSS 143
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 121-199 5.16e-03

protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or PTP localized to the mitochondrion 1 (PTPMT1), also called phosphoinositide lipid phosphatase (PLIP), phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1, or PTEN-like phosphatase, is a lipid phosphatase or phosphatidylglycerophosphatase (EC 3.1.3.27) which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG). It is targeted to the mitochondrion by an N-terminal signal sequence and is found anchored to the matrix face of the inner membrane. It is essential for the biosynthesis of cardiolipin, a mitochondrial-specific phospholipid regulating the membrane integrity and activities of the organelle. PTPMT1 also plays a crucial role in hematopoietic stem cell (HSC) function, and has been shown to display activity toward phosphoprotein substrates.


Pssm-ID: 350374 [Multi-domain]  Cd Length: 149  Bit Score: 38.40  E-value: 5.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776351 121 QAPSLHNLF-AVcrnmyNWLL-QNPKNVCV-VHCLDGRAASSILVGAMFIFCNLYsTPGPAVRLLYAKRPGIGLSPSHRR 197
Cdd:cd14524    68 GVPSLEDLEkGV-----DFILkHREKGKSVyVHCKAGRGRSATIVACYLIQHKGW-SPEEAQEFLRSKRPHILLRLSQRE 141


                  ..
gi 1958776351 198 YL 199
Cdd:cd14524   142 VL 143
 
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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