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Conserved domains on  [gi|257153388|ref|NP_001158055|]
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auxilin isoform a [Mus musculus]

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 ...
 111-273 1.59e-113

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: 345.71  E-value: 1.59e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388 111 VSSYTKGDLDFTYVTSRIIVMSFPVDSVDIGFRNQVDDIRSFLDSRHLDHYTVYNLSPKSYRTAKFHSRVSECSWPIRQA 190
Cdd:cd14563    1 VASYTKGELDISYITSRIIVMSYPAEGVELGFRNHIEDVRSFLDSRHLDHYTVFNLSQKSYRSAKFHNRVSECSWPVRQA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388 191 PSLHNLFAVCRNMYNWLLQNPKNVCVVHCLDGRAASSILVGAMFIFCNLYSTPGPAVRLLYAKRPGIGLSPSHRRYLGYM 270
Cdd:cd14563   81 PSLHNLFAVCKNMHNWLQQNPKNVCVIHCMDGRAASAVLVSAMFCFCHLFSNPVPAMQLLNAKRPGIGLWPSHRRYIGYI 160


                 ...
gi 257153388 271 CDL 273
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 ...
 281-419 4.42e-36

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: 132.79  E-value: 4.42e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388  281 PHFKPLTIKAITVSPVPFFNKQrNGCRPYCDVLIGETKIYSTCTDFERMKEYRVQDGKIFIPLNITVQGDVIVSMYHLRS 360
Cdd:pfam10409   1 PPPKPLTLHSIILHGIPNFKSG-GGCRPYIRIYQNKKKVFSTSGKYKKLKEYQQDDCVILFPKGIPVQGDVLVEFYHKGS 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257153388  361 TIGSRlqakvtnTQIFQLQFHSGFIPldTTVLKFTKPELDACDVP---EKYPQLFQVTLDIE 419
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 ...
 916-961 4.92e-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: 4.92e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 257153388 916 TPEQVKKVYRRAVLVVHPDKATGQPyeqYAKMIFMELNDAWSEFEN 961
Cdd:cd06257   13 SDEEIKKAYRKLALKYHPDKNPDDP---EAEEKFKEINEAYEVLSD 55
PPE super family cl35037
PPE-repeat protein [Function unknown];
562-782 1.57e-05

PPE-repeat protein [Function unknown];


The actual alignment was detected with superfamily member COG5651:

Pssm-ID: 444372 [Multi-domain]  Cd Length: 385  Bit Score: 48.35  E-value: 1.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388 562 VSTNFSSLAAPPSNSELLSDLFGGVGATGPAQAGQAGVEDVFHPSGPVSAQSTPRRTATSASASPTlrvGEGATFDPFGA 641
Cdd:COG5651  173 TITNPGGLLGAQNAGSGNTSSNPGFANLGLTGLNQVGIGGLNSGSGPIGLNSGPGNTGFAGTGAAA---GAAAAAAAAAA 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388 642 PAKPPGQDLLGSFLNTSSASSDPFLQPTRSPS-----PTVHASSTPAVNIQPDIAGGWDWHTKPGGFGMGSKSAATSPTG 716
Cdd:COG5651  250 AAGAGASAALASLAATLLNASSLGLAATAASSaatnlGLAGSPLGLAGGGAGAAAATGLGLGAGGAAGAAGATGAGAALG 329

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 257153388 717 SSHGTPThqskpqtldpfADLGTLGSSSFASKPTTPTGLGGGFPPLSSPQKASPQPMGGGWQQPAG 782
Cdd:COG5651  330 AGAAAAA-----------AGAAAGAGAAAAAAAGGAGGGGGGALGAGGGGGSAGAAAGAASGGGAA 384
 
Name Accession Description Interval E-value
PTP_auxilin_N cd14563
N-terminal protein tyrosine phosphatase-like domain of auxilin; Auxilin, also called auxilin-1 ...
 111-273 1.59e-113

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: 345.71  E-value: 1.59e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388 111 VSSYTKGDLDFTYVTSRIIVMSFPVDSVDIGFRNQVDDIRSFLDSRHLDHYTVYNLSPKSYRTAKFHSRVSECSWPIRQA 190
Cdd:cd14563    1 VASYTKGELDISYITSRIIVMSYPAEGVELGFRNHIEDVRSFLDSRHLDHYTVFNLSQKSYRSAKFHNRVSECSWPVRQA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388 191 PSLHNLFAVCRNMYNWLLQNPKNVCVVHCLDGRAASSILVGAMFIFCNLYSTPGPAVRLLYAKRPGIGLSPSHRRYLGYM 270
Cdd:cd14563   81 PSLHNLFAVCKNMHNWLQQNPKNVCVIHCMDGRAASAVLVSAMFCFCHLFSNPVPAMQLLNAKRPGIGLWPSHRRYIGYI 160


                 ...
gi 257153388 271 CDL 273
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 ...
 281-419 4.42e-36

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: 132.79  E-value: 4.42e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388  281 PHFKPLTIKAITVSPVPFFNKQrNGCRPYCDVLIGETKIYSTCTDFERMKEYRVQDGKIFIPLNITVQGDVIVSMYHLRS 360
Cdd:pfam10409   1 PPPKPLTLHSIILHGIPNFKSG-GGCRPYIRIYQNKKKVFSTSGKYKKLKEYQQDDCVILFPKGIPVQGDVLVEFYHKGS 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257153388  361 TIGSRlqakvtnTQIFQLQFHSGFIPldTTVLKFTKPELDACDVP---EKYPQLFQVTLDIE 419
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 ...
 916-961 4.92e-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: 4.92e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 257153388 916 TPEQVKKVYRRAVLVVHPDKATGQPyeqYAKMIFMELNDAWSEFEN 961
Cdd:cd06257   13 SDEEIKKAYRKLALKYHPDKNPDDP---EAEEKFKEINEAYEVLSD 55
DnaJ smart00271
DnaJ molecular chaperone homology domain;
916-962 3.38e-07

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 48.00  E-value: 3.38e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 257153388   916 TPEQVKKVYRRAVLVVHPDKATGQPYEqyAKMIFMELNDAWSEFENQ 962
Cdd:smart00271  14 SLDEIKKAYRKLALKYHPDKNPGDKEE--AEEKFKEINEAYEVLSDP 58
PPE COG5651
PPE-repeat protein [Function unknown];
562-782 1.57e-05

PPE-repeat protein [Function unknown];


Pssm-ID: 444372 [Multi-domain]  Cd Length: 385  Bit Score: 48.35  E-value: 1.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388 562 VSTNFSSLAAPPSNSELLSDLFGGVGATGPAQAGQAGVEDVFHPSGPVSAQSTPRRTATSASASPTlrvGEGATFDPFGA 641
Cdd:COG5651  173 TITNPGGLLGAQNAGSGNTSSNPGFANLGLTGLNQVGIGGLNSGSGPIGLNSGPGNTGFAGTGAAA---GAAAAAAAAAA 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388 642 PAKPPGQDLLGSFLNTSSASSDPFLQPTRSPS-----PTVHASSTPAVNIQPDIAGGWDWHTKPGGFGMGSKSAATSPTG 716
Cdd:COG5651  250 AAGAGASAALASLAATLLNASSLGLAATAASSaatnlGLAGSPLGLAGGGAGAAAATGLGLGAGGAAGAAGATGAGAALG 329

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 257153388 717 SSHGTPThqskpqtldpfADLGTLGSSSFASKPTTPTGLGGGFPPLSSPQKASPQPMGGGWQQPAG 782
Cdd:COG5651  330 AGAAAAA-----------AGAAAGAGAAAAAAAGGAGGGGGGALGAGGGGGSAGAAAGAASGGGAA 384
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 916-957 2.62e-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: 2.62e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 257153388  916 TPEQVKKVYRRAVLVVHPDKATGQPyeQYAKMiFMELNDAWS 957
Cdd:pfam00226  13 SDEEIKKAYRKLALKYHPDKNPGDP--EAEEK-FKEINEAYE 51
PHA03247 PHA03247
large tegument protein UL36; Provisional
 589-820 3.05e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.40  E-value: 3.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388  589 TGPAQAGQAGVEDVFHPSGPVSAQST---------PRRTATSASASPTlrvgegATFDPFGAPAK---PPGQDLLGSFLN 656
Cdd:PHA03247 2723 PGPAAARQASPALPAAPAPPAVPAGPatpggparpARPPTTAGPPAPA------PPAAPAAGPPRrltRPAVASLSESRE 2796

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388  657 TSSASSDPFLQP--TRSPSPTVHASSTPAVNIQPDIAggwdwhtkpggfgmgskSAATSPTGSSHGTPTHQSKPQTLDPF 734
Cdd:PHA03247 2797 SLPSPWDPADPPaaVLAPAAALPPAASPAGPLPPPTS-----------------AQPTAPPPPPGPPPPSLPLGGSVAPG 2859

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388  735 ADLGTLGSS-SFASKPTTPTGLGG---GFPPLSSPQKASPQPMGGGWQQPAGYNWQQTQSKPQ-----SSMPHSSPQNRP 805
Cdd:PHA03247 2860 GDVRRRPPSrSPAAKPAAPARPPVrrlARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQpppppQPQPPPPPPPRP 2939

                         250
                  ....*....|....*
gi 257153388  806 NYNVSFSAMPAGQSE 820
Cdd:PHA03247 2940 QPPLAPTTDPAGAGE 2954
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 605-821 8.18e-05

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: 46.68  E-value: 8.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388  605 PSGPVSAQSTPRRTATS-ASASPTlrvGEGATFDPFGAPA-KPPGQDLLGSFLNTSSASSDPFLQPTRSPSPtvHASSTP 682
Cdd:pfam03154 177 QSGAASPPSPPPPGTTQaATAGPT---PSAPSVPPQGSPAtSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSP--HPPLQP 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388  683 AVNIQPDIAGGWDWHTKPGGFGMGSKSAATSPTGsshgtPTHQSKPQTLDPFADLGTLGSSSFASKPTTPTGLGGGFPPL 762
Cdd:pfam03154 252 MTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTG-----PSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIH 326

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 257153388  763 SSPQKASPQPmgggwQQPAgynwqqtQSKPQSSMPHSSPQNRPNYNVSFSAMPAGQSER 821
Cdd:pfam03154 327 TPPSQSQLQS-----QQPP-------REQPLPPAPLSMPHIKPPPTTPIPQLPNPQSHK 373
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
915-956 2.01e-03

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 37.85  E-value: 2.01e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 257153388 915 VTPEQVKKVYRRAVLVVHPDK-ATGQPYEQ--YAKMIFMELNDAW 956
Cdd:COG1076   16 ADDAELKRAYRKLQREHHPDRlAAGLPEEEqrLALQKAAAINEAY 60
 
Name Accession Description Interval E-value
PTP_auxilin_N cd14563
N-terminal protein tyrosine phosphatase-like domain of auxilin; Auxilin, also called auxilin-1 ...
 111-273 1.59e-113

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: 345.71  E-value: 1.59e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388 111 VSSYTKGDLDFTYVTSRIIVMSFPVDSVDIGFRNQVDDIRSFLDSRHLDHYTVYNLSPKSYRTAKFHSRVSECSWPIRQA 190
Cdd:cd14563    1 VASYTKGELDISYITSRIIVMSYPAEGVELGFRNHIEDVRSFLDSRHLDHYTVFNLSQKSYRSAKFHNRVSECSWPVRQA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388 191 PSLHNLFAVCRNMYNWLLQNPKNVCVVHCLDGRAASSILVGAMFIFCNLYSTPGPAVRLLYAKRPGIGLSPSHRRYLGYM 270
Cdd:cd14563   81 PSLHNLFAVCKNMHNWLQQNPKNVCVIHCMDGRAASAVLVSAMFCFCHLFSNPVPAMQLLNAKRPGIGLWPSHRRYIGYI 160


                 ...
gi 257153388 271 CDL 273
Cdd:cd14563  161 CDL 163
PTP_auxilin-like cd14511
protein tyrosine phosphatase-like domain of auxilin and similar proteins; This subfamily ...
 111-273 1.44e-94

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: 1.44e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388 111 VSSYTKGDLDFTYVTSRIIVMSFPVDSVDIGFR-NQVDDIRSFLDSRHLDHYTVYNLSPKSYRTAKFHSRVSECSWPIRQ 189
Cdd:cd14511    1 QQSYARNDLDISYITSRIIVMPFPAEGIESTYRkNNIEDVRAFLDSRHPQKYSVYNLSPRSYPTLRLPSRVVECSWPYRR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388 190 APSLHNLFAVCRNMYNWLLQNPKNVCVVHCLDGRAASSILVGAMFIFCNLYSTPGPAVRLLYAKRPGIGLSPSHRRYLGY 269
Cdd:cd14511   81 APSLHALYALCRDIYQWLNKDPKNVIVIHCTDGKAASATVVCALLVYCGLFKTPEDALQMFAVKRCPPGLSPSELRYLYY 160


                 ....
gi 257153388 270 MCDL 273
Cdd:cd14511  161 FSDI 164
PTP_GAK cd14564
protein tyrosine phosphatase-like domain of cyclin-G-associated kinase; cyclin-G-associated ...
 111-273 2.49e-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: 249.43  E-value: 2.49e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388 111 VSSYTKGDLDFTYVTSRIIVMSFPVDSVDIGFRNQVDDIRSFLDSRHLDHYTVYNLSPKSYRTAKFHSRVSECSWPIRQA 190
Cdd:cd14564    1 VANYAKGDLDISYITSRIAVMSFPAEGVESAIKNNIEDVRLFLDSRHPGHYAVYNLSQRTYRPSRFHNRVSECGWPARRA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388 191 PSLHNLFAVCRNMYNWLLQNPKNVCVVHCLDGRAASSILVGAMFIFCNLYSTPGPAVRLLYAKRPGIGLSPSHRRYLGYM 270
Cdd:cd14564   81 PNLQNLYSICKNMHLWLKQDQKNICIVHCLDGRAASAVVVCSFLCFCRLFTTAEAAVYMFSMKRCPPGIWPSHKRYIEYM 160


                 ...
gi 257153388 271 CDL 273
Cdd:cd14564  161 CDM 163
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 120-273 6.96e-62

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: 207.05  E-value: 6.96e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388 120 DFTYVTSRIIVMSFPVDSV-DIGFRNQVDDIRSFLDSRHLDHYTVYNLSPKSYR-TAKFHSRVSECSWPIRQAPSLHNLF 197
Cdd:cd14497    1 DLSYITPRIIAMSFPATGYpESLYRNSIDDVANFLNTHHPDHYMIFNLSEEEYDdDSKFEGRVLHYGFPDHHPPPLGLLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388 198 AVCRNMYNWLLQNPKNVCVVHCLDGRAASSILVGAMFIFCNLYSTPGPAVRLLYAKRPGIGL----SPSHRRYLGYMCDL 273
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 ...
 281-419 4.42e-36

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: 132.79  E-value: 4.42e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388  281 PHFKPLTIKAITVSPVPFFNKQrNGCRPYCDVLIGETKIYSTCTDFERMKEYRVQDGKIFIPLNITVQGDVIVSMYHLRS 360
Cdd:pfam10409   1 PPPKPLTLHSIILHGIPNFKSG-GGCRPYIRIYQNKKKVFSTSGKYKKLKEYQQDDCVILFPKGIPVQGDVLVEFYHKGS 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257153388  361 TIGSRlqakvtnTQIFQLQFHSGFIPldTTVLKFTKPELDACDVP---EKYPQLFQVTLDIE 419
Cdd:pfam10409  80 DLLSE-------EKMFRFWFNTSFIE--DNTLTLPKNELDKADKDkkdKRFPKDFKVELLFS 132
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 120-269 4.88e-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: 133.87  E-value: 4.88e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388 120 DFTYVTSRIIVMSFPVDSVDIGFRNQVDDIRSFLDSRHLDHYTVYNL-SPKSYRTAKFHSRVSECSWPIRQAPSLHNLFA 198
Cdd:cd14509    1 DLTYITPNIIAMGFPAEGVEGVYRNPIDDVQRFLETKHKGHYKVYNLcSERSYDPSKFNGRVAEYPFDDHNPPPLELIKP 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 257153388 199 VCRNMYNWLLQNPKNVCVVHCLDGRAASSILVGAMFIFCNLYSTPGPAVRLLYAKRP--GIGLS-PSHRRYLGY 269
Cdd:cd14509   81 FCEDVDEWLKEDEKNVAAVHCKAGKGRTGVMICCYLLYLGKFPSAKEALDFYGAKRTknKKGVTiPSQRRYVYY 154
PTP_tensin cd14508
protein tyrosine phosphatase-like domain of tensins; The tensin family of intracellular ...
 120-273 1.14e-35

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: 132.90  E-value: 1.14e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388 120 DFTYVTSRIIVMSFPVDSVDIGFRNQVDDIRSFLDSRHLDHYTVYNLSPKSYRTAKFHSRVSECSWPIRQAPSLHNLFAV 199
Cdd:cd14508    1 DLTYITERIIALSFPSTCSEQTYRHNLREAAHLLQSKHGDNYMVFNLSERRHDLRSLNPKVLDFGWPELHAPPLEKLCSI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257153388 200 CRNMYNWLLQNPKNVCVVHCLDGRAASSILVGAMFIFCNLYSTPGPAVRLLYAKR-----PGIGLSPSHRRYLGYMCDL 273
Cdd:cd14508   81 CKNMDSWLNADPQNVVVLHCKGGKGRLGVVVSAYMHYSKISATADQALDRFAMKRfyddkVGPLGQPSQKRYVGYFSGL 159
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 114-269 9.60e-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: 9.60e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388 114 YTKG--DLDFTYVTSRIIVMSFPVDSVDIGFRNQVDDIRSFLDSRHLDHYTVYNL-SPKSYRTAKFHSRVSECSWPIRQA 190
Cdd:cd14510    7 YQKDgfDLDLTYVTDRVIAMSFPSSGKQAFYRNPIEEVVRFLDTKHPDHYKVYNLcSERGYDPKYFHNRVERVPIDDHNV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388 191 PSLHNLFAVCRNMYNWLLQNPKNVCVVHCLDGRAASSILVGAMFIFCNLYSTPGPAVRLLYAKRPGIGLS--------PS 262
Cdd:cd14510   87 PTLDEMLSFTAEVREWMAADPKNVVAIHCKGGKGRTGTMVCAWLIYSGQFESAKEALEYFGERRTDKSVSskfqgvetPS 166


                 ....*..
gi 257153388 263 HRRYLGY 269
Cdd:cd14510  167 QSRYVGY 173
PTP_tensin-3 cd14561
protein tyrosine phosphatase-like domain of tensin-3; Tensin-3 (TNS3) is also called ...
 120-273 5.34e-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: 5.34e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388 120 DFTYVTSRIIVMSFPVDSVDIGFRNQVDDIRSFLDSRHLDHYTVYNLSPKSYRTAKFHSRVSECSWPIRQAPSLHNLFAV 199
Cdd:cd14561    1 DLTYITERIIAVSFPADCSEETYLHNLQDVTRMLKSKHGDNYLVLNLSEKRYELTKLNPKIMDVGWPDLHAPPLDKMCTI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257153388 200 CRNMYNWLLQNPKNVCVVHCLDGRAASSILVGAMFIFCNLYSTPGPAV-----RLLYAKRPGIGLSPSHRRYLGYMCDL 273
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 ...
 120-273 2.67e-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: 2.67e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388 120 DFTYVTSRIIVMSFPVDSVDIGFRNQVDDIRSFLDSRHLDHYTVYNLSPKSYRTAKFHSRVSECSWPIRQAPSLHNLFAV 199
Cdd:cd14560    1 DLVYITERIISVSFPSTAEEPSFRSNLKEVAQMLKSKHGDNYLLFNLSERRHDISKLHPKVLDFGWPDLHAPALEKICSI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388 200 CRNMYNWLLQNPKNVCVVHCLDGRAASSILVGAMFIFCNLYSTPGPAVRLLYAKR-------PgIGlSPSHRRYLGYMCD 272
Cdd:cd14560   81 CKAMDTWLNADPHNVVVIHNKGNRGRTGVVIAAYMHYSNISASADQALDRFAMKRfyedkvvP-VG-QPSQKRYVHYFSG 158


                 .
gi 257153388 273 L 273
Cdd:cd14560  159 L 159
PTP_tensin-2 cd14562
protein tyrosine phosphatase-like domain of tensin-2; Tensin-2 (TNS2) is also called ...
 120-273 2.47e-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: 2.47e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388 120 DFTYVTSRIIVMSFPVDSVDIGFRNQVDDIRSFLDSRHLDHYTVYNLSPKSYRTAKFHSRVSECSWPIRQAPSLHNLFAV 199
Cdd:cd14562    1 DLTYITERIISVFFPPALEEQRYRGNLREVAQMLKSKHEDKYLLFNLSEKRHDITRLNPKVQDFGWPDLHAPPLDKICSI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257153388 200 CRNMYNWLLQNPKNVCVVHCLDGRAASSILVGAMFIFCNLYSTPGPAVRLLYAK-----RPGIGLSPSHRRYLGYMCDL 273
Cdd:cd14562   81 CKAMETWLNADPQHVVVLHCKGNKGKTGVIVAAYMHYSKISAGADQALSTLAMRkfcedKVATSLQPSQRRYISYFGGL 159
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 916-961 4.92e-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: 4.92e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 257153388 916 TPEQVKKVYRRAVLVVHPDKATGQPyeqYAKMIFMELNDAWSEFEN 961
Cdd:cd06257   13 SDEEIKKAYRKLALKYHPDKNPDDP---EAEEKFKEINEAYEVLSD 55
DnaJ smart00271
DnaJ molecular chaperone homology domain;
916-962 3.38e-07

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 48.00  E-value: 3.38e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 257153388   916 TPEQVKKVYRRAVLVVHPDKATGQPYEqyAKMIFMELNDAWSEFENQ 962
Cdd:smart00271  14 SLDEIKKAYRKLALKYHPDKNPGDKEE--AEEKFKEINEAYEVLSDP 58
PPE COG5651
PPE-repeat protein [Function unknown];
562-782 1.57e-05

PPE-repeat protein [Function unknown];


Pssm-ID: 444372 [Multi-domain]  Cd Length: 385  Bit Score: 48.35  E-value: 1.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388 562 VSTNFSSLAAPPSNSELLSDLFGGVGATGPAQAGQAGVEDVFHPSGPVSAQSTPRRTATSASASPTlrvGEGATFDPFGA 641
Cdd:COG5651  173 TITNPGGLLGAQNAGSGNTSSNPGFANLGLTGLNQVGIGGLNSGSGPIGLNSGPGNTGFAGTGAAA---GAAAAAAAAAA 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388 642 PAKPPGQDLLGSFLNTSSASSDPFLQPTRSPS-----PTVHASSTPAVNIQPDIAGGWDWHTKPGGFGMGSKSAATSPTG 716
Cdd:COG5651  250 AAGAGASAALASLAATLLNASSLGLAATAASSaatnlGLAGSPLGLAGGGAGAAAATGLGLGAGGAAGAAGATGAGAALG 329

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 257153388 717 SSHGTPThqskpqtldpfADLGTLGSSSFASKPTTPTGLGGGFPPLSSPQKASPQPMGGGWQQPAG 782
Cdd:COG5651  330 AGAAAAA-----------AGAAAGAGAAAAAAAGGAGGGGGGALGAGGGGGSAGAAAGAASGGGAA 384
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 916-957 2.62e-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: 2.62e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 257153388  916 TPEQVKKVYRRAVLVVHPDKATGQPyeQYAKMiFMELNDAWS 957
Cdd:pfam00226  13 SDEEIKKAYRKLALKYHPDKNPGDP--EAEEK-FKEINEAYE 51
PHA03247 PHA03247
large tegument protein UL36; Provisional
 589-820 3.05e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.40  E-value: 3.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388  589 TGPAQAGQAGVEDVFHPSGPVSAQST---------PRRTATSASASPTlrvgegATFDPFGAPAK---PPGQDLLGSFLN 656
Cdd:PHA03247 2723 PGPAAARQASPALPAAPAPPAVPAGPatpggparpARPPTTAGPPAPA------PPAAPAAGPPRrltRPAVASLSESRE 2796

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388  657 TSSASSDPFLQP--TRSPSPTVHASSTPAVNIQPDIAggwdwhtkpggfgmgskSAATSPTGSSHGTPTHQSKPQTLDPF 734
Cdd:PHA03247 2797 SLPSPWDPADPPaaVLAPAAALPPAASPAGPLPPPTS-----------------AQPTAPPPPPGPPPPSLPLGGSVAPG 2859

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388  735 ADLGTLGSS-SFASKPTTPTGLGG---GFPPLSSPQKASPQPMGGGWQQPAGYNWQQTQSKPQ-----SSMPHSSPQNRP 805
Cdd:PHA03247 2860 GDVRRRPPSrSPAAKPAAPARPPVrrlARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQpppppQPQPPPPPPPRP 2939

                         250
                  ....*....|....*
gi 257153388  806 NYNVSFSAMPAGQSE 820
Cdd:PHA03247 2940 QPPLAPTTDPAGAGE 2954
PHA03247 PHA03247
large tegument protein UL36; Provisional
 570-803 7.92e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.86  E-value: 7.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388  570 AAPPSNSELLSDLFGGVGATGPAQAGQAGvedvfhPSGPVSAQSTPRRTATSASASPTLRVGEGATFDPfgAPAKPPGQD 649
Cdd:PHA03247 2740 APPAVPAGPATPGGPARPARPPTTAGPPA------PAPPAAPAAGPPRRLTRPAVASLSESRESLPSPW--DPADPPAAV 2811

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388  650 LLGSFLNTSSASSDPFLQPTRSPSPTvhASSTPAVNIQPDIA-GGWdwhTKPGG---FGMGSKSAATSPTGSSHGTPTHQ 725
Cdd:PHA03247 2812 LAPAAALPPAASPAGPLPPPTSAQPT--APPPPPGPPPPSLPlGGS---VAPGGdvrRRPPSRSPAAKPAAPARPPVRRL 2886

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388  726 SKP---QTLDPFA----DLGTLGSSSFASKPTTPtglgggfPPLSSPQKASPQPMGGGWQQPAGYNWQQTQSKPQSSMPH 798
Cdd:PHA03247 2887 ARPavsRSTESFAlppdQPERPPQPQAPPPPQPQ-------PQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAV 2959


                  ....*
gi 257153388  799 SSPQN 803
Cdd:PHA03247 2960 PQPWL 2964
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 605-821 8.18e-05

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: 46.68  E-value: 8.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388  605 PSGPVSAQSTPRRTATS-ASASPTlrvGEGATFDPFGAPA-KPPGQDLLGSFLNTSSASSDPFLQPTRSPSPtvHASSTP 682
Cdd:pfam03154 177 QSGAASPPSPPPPGTTQaATAGPT---PSAPSVPPQGSPAtSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSP--HPPLQP 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388  683 AVNIQPDIAGGWDWHTKPGGFGMGSKSAATSPTGsshgtPTHQSKPQTLDPFADLGTLGSSSFASKPTTPTGLGGGFPPL 762
Cdd:pfam03154 252 MTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTG-----PSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIH 326

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 257153388  763 SSPQKASPQPmgggwQQPAgynwqqtQSKPQSSMPHSSPQNRPNYNVSFSAMPAGQSER 821
Cdd:pfam03154 327 TPPSQSQLQS-----QQPP-------REQPLPPAPLSMPHIKPPPTTPIPQLPNPQSHK 373
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 563-848 8.45e-05

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 46.45  E-value: 8.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388  563 STNFSSLAAPPSNSELLSDLFGGVGATGPAQAGqagvedvfhPSGPVSAQSTPRRTATSASASPtlrVGEGATFDPFGAP 642
Cdd:pfam05109 433 TLNTTGFAAPNTTTGLPSSTHVPTNLTAPASTG---------PTVSTADVTSPTPAGTTSGASP---VTPSPSPRDNGTE 500

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388  643 AKPPgqdllgSFLNTSSASSDPFLQPTrSPSPTVhasSTPAVNIQPDIAGgwdwHTKPGGFGMGSKSAATSPTGSShGTP 722
Cdd:pfam05109 501 SKAP------DMTSPTSAVTTPTPNAT-SPTPAV---TTPTPNATSPTLG----KTSPTSAVTTPTPNATSPTPAV-TTP 565

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388  723 ThqskpqtldPFADLGTLGSSSFASKPTTPTglgggfPPLSSPQKASPQPMGGGWQQPAGynwqQTQSKPQSSMPhssPQ 802
Cdd:pfam05109 566 T---------PNATIPTLGKTSPTSAVTTPT------PNATSPTVGETSPQANTTNHTLG----GTSSTPVVTSP---PK 623

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 257153388  803 NrpnynvSFSAMPAGQSERGKGSTNLEGKQKAADFEDLLSSQGFNA 848
Cdd:pfam05109 624 N------ATSAVTTGQHNITSSSTSSMSLRPSSISETLSPSTSDNS 663
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
559-764 2.70e-04

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 44.74  E-value: 2.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388 559 GSDVSTNFSSLAAPPSNSELLSDLFGGVGATGPAQAGQAGVedvfhpSGPVSAQSTPRRTATSASASPTLRVGEGATFDP 638
Cdd:COG3469   15 ASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASG------SAGSGTGTTAASSTAATSSTTSTTATATAAAAA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388 639 FGAPAKPPGQDLLGSFLNTSSASSDPFLQPTRSPSPTVHASSTPAVNIQPDIAGGWDWHTKPGGFGMGSKSAATSPTGSS 718
Cdd:COG3469   89 ATSTSATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTETATGGTTTTST 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 257153388 719 HGTPTHQSKPQTLDPFADLGTLGSSSFASKPTTPTGLGGGFPPLSS 764
Cdd:COG3469  169 TTTTTSASTTPSATTTATATTASGATTPSATTTATTTGPPTPGLPK 214
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
915-956 2.01e-03

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 37.85  E-value: 2.01e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 257153388 915 VTPEQVKKVYRRAVLVVHPDK-ATGQPYEQ--YAKMIFMELNDAW 956
Cdd:COG1076   16 ADDAELKRAYRKLQREHHPDRlAAGLPEEEqrLALQKAAAINEAY 60
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
916-956 2.43e-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: 2.43e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 257153388 916 TPEQVKKVYRRAVLVVHPDkaTGQPYEQYAKMIFMELNDAW 956
Cdd:COG2214   18 SLEEIRQAYRRLAKLLHPD--RGGELKALAEELFQRLNEAY 56
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 189-267 5.58e-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: 5.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388 189 QAPSLHNLF-AVcrnmyNWLL-QNPKNVCV-VHCLDGRAASSILVGAMFIFCNLYsTPGPAVRLLYAKRPGIGLSPSHRR 265
Cdd:cd14524   68 GVPSLEDLEkGV-----DFILkHREKGKSVyVHCKAGRGRSATIVACYLIQHKGW-SPEEAQEFLRSKRPHILLRLSQRE 141


                 ..
gi 257153388 266 YL 267
Cdd:cd14524  142 VL 143
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 605-815 9.51e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.15  E-value: 9.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388  605 PSGPVSAQSTPRRTATSASASPTLRVGEG---ATFDPFGAPAKPPGQDLLGS--------FLNTSSASSDPflqpTRSPS 673
Cdd:PHA03307  222 PAPGRSAADDAGASSSDSSSSESSGCGWGpenECPLPRPAPITLPTRIWEASgwngpssrPGPASSSSSPR----ERSPS 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257153388  674 PTVHASSTPAVNIQPDIAGGWDWHTKpggfgmgSKSAATSPTG-SSHGTPTHQSKPQTLDPfADLGTLGSSSFASKPTTP 752
Cdd:PHA03307  298 PSPSSPGSGPAPSSPRASSSSSSSRE-------SSSSSTSSSSeSSRGAAVSPGPSPSRSP-SPSRPPPPADPSSPRKRP 369

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 257153388  753 TGLGGgfPPLSSPQKASPQPMGGGWQQPAGYNWQQ-----TQSKPQSSMPHSS------PQNRPNYNVSFSAMP 815
Cdd:PHA03307  370 RPSRA--PSSPAASAGRPTRRRARAAVAGRARRRDatgrfPAGRPRPSPLDAGaasgafYARYPLLTPSGEPWP 441
 
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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