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Conserved domains on  [gi|7949098|ref|NP_058069|]
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neuronal pentraxin-2 precursor [Mus musculus]

Protein Classification

PTX domain-containing protein( domain architecture ID 10639996)

PTX domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTX smart00159
Pentraxin / C-reactive protein / pentaxin family; This family form a doscoid pentameric ...
217-422 7.65e-104

Pentraxin / C-reactive protein / pentaxin family; This family form a doscoid pentameric structure. Human serum amyloid P demonstrates calcium-mediated ligand-binding.


:

Pssm-ID: 128463  Cd Length: 206  Bit Score: 306.50  E-value: 7.65e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098     217 FKSPDAFKVSLPLRTNYLYGKIKKTLP-ELYAFTICLWLRSSASPGIGTPFSYAVPGQANEIVLIEWGNNPIELLINDKV 295
Cdd:smart00159   1 QTDLTGKVFVFPKESDTSYVKLKPELPkPLQAFTVCLWFYSDLSPRGYSLFSYATKGQDNELLLYKEKQGEYSLYIGGKK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098     296 AQLPLFVSDGKWHHICITWTTRDGMWEAFQDGeKLGTGENLAPWHPIKPGGVLILGQEQDTVGGRFDATQAFVGELSQFN 375
Cdd:smart00159  81 VQFPVPESDGKWHHICTTWESSSGIAELWVDG-KPGVRKGLAKGYTVKPGGSIILGQEQDSYGGGFDATQSFVGEIGDLN 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 7949098     376 IWDRVLRAQEIINIANCSTNMPGNIIPWVDNNVDVFGGASKWPVETC 422
Cdd:smart00159 160 MWDSVLSPEEIKSVYKGSTFSIGNILNWRALNYEVHGGVVIKPQEWC 206
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
57-215 9.11e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


The actual alignment was detected with superfamily member COG4913:

Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 9.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098    57 EEELRAAVLQLRETVVQQKETLGAQREAIRELTGKLARceglAGGkargtgkDTMGDLPRDpghvVEQLSRSLQTLKDRL 136
Cdd:COG4913  297 LEELRAELARLEAELERLEARLDALREELDELEAQIRG----NGG-------DRLEQLERE----IERLERELEERERRR 361
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098   137 ESLELQLRTnvsnAGLPSDFREvlqRRLGELERQLLRKVAELEDEKSLLHNE-TSAHRQKTEST--LNALLQRVTELERG 213
Cdd:COG4913  362 ARLEALLAA----LGLPLPASA---EEFAALRAEAAALLEALEEELEALEEAlAEAEAALRDLRreLRELEAEIASLERR 434

                 ..
gi 7949098   214 NS 215
Cdd:COG4913  435 KS 436
 
Name Accession Description Interval E-value
PTX smart00159
Pentraxin / C-reactive protein / pentaxin family; This family form a doscoid pentameric ...
217-422 7.65e-104

Pentraxin / C-reactive protein / pentaxin family; This family form a doscoid pentameric structure. Human serum amyloid P demonstrates calcium-mediated ligand-binding.


Pssm-ID: 128463  Cd Length: 206  Bit Score: 306.50  E-value: 7.65e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098     217 FKSPDAFKVSLPLRTNYLYGKIKKTLP-ELYAFTICLWLRSSASPGIGTPFSYAVPGQANEIVLIEWGNNPIELLINDKV 295
Cdd:smart00159   1 QTDLTGKVFVFPKESDTSYVKLKPELPkPLQAFTVCLWFYSDLSPRGYSLFSYATKGQDNELLLYKEKQGEYSLYIGGKK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098     296 AQLPLFVSDGKWHHICITWTTRDGMWEAFQDGeKLGTGENLAPWHPIKPGGVLILGQEQDTVGGRFDATQAFVGELSQFN 375
Cdd:smart00159  81 VQFPVPESDGKWHHICTTWESSSGIAELWVDG-KPGVRKGLAKGYTVKPGGSIILGQEQDSYGGGFDATQSFVGEIGDLN 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 7949098     376 IWDRVLRAQEIINIANCSTNMPGNIIPWVDNNVDVFGGASKWPVETC 422
Cdd:smart00159 160 MWDSVLSPEEIKSVYKGSTFSIGNILNWRALNYEVHGGVVIKPQEWC 206
PTX cd00152
Pentraxins are plasma proteins characterized by their pentameric discoid assembly and their ...
221-417 3.99e-95

Pentraxins are plasma proteins characterized by their pentameric discoid assembly and their Ca2+ dependent ligand binding, such as Serum amyloid P component (SAP) and C-reactive Protein (CRP), which are cytokine-inducible acute-phase proteins implicated in innate immunity. CRP binds to ligands containing phosphocholine, SAP binds to amyloid fibrils, DNA, chromatin, fibronectin, C4-binding proteins and glycosaminoglycans. "Long" pentraxins have N-terminal extensions to the common pentraxin domain; one group, the neuronal pentraxins, may be involved in synapse formation and remodeling, and they may also be able to form heteromultimers.


Pssm-ID: 238086  Cd Length: 201  Bit Score: 284.16  E-value: 3.99e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098  221 DAFKVSLPLRTNYLYGKIKKTLP-ELYAFTICLWLRSSASPGIGTPFSYAVPGQANEIVLIEWGNNPIELLINDKVAQLP 299
Cdd:cd00152   5 SGKVFVFPKESDTSYVKLKPELPkPLQAFTLCLWVYTDLSTREYSLFSYATKGQDNELLLYKEKDGGYSLYIGGKEVTFK 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098  300 LFVSDGKWHHICITWTTRDGMWEAFQDGEKLGTGEnLAPWHPIKPGGVLILGQEQDTVGGRFDATQAFVGELSQFNIWDR 379
Cdd:cd00152  85 VPESDGAWHHICVTWESTSGIAELWVNGKLSVRKS-LKKGYTVGPGGSIILGQEQDSYGGGFDATQSFVGEISDVNMWDS 163
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 7949098  380 VLRAQEIINIANCSTNMPGNIIPWVDNNVDVFGGASKW 417
Cdd:cd00152 164 VLSPEEIKNVYSEGGTLSGNILNWRALNYEINGGVVIK 201
Pentaxin pfam00354
Pentaxin family; Pentaxins are also known as pentraxins.
222-414 1.64e-32

Pentaxin family; Pentaxins are also known as pentraxins.


Pssm-ID: 278768  Cd Length: 194  Bit Score: 121.76  E-value: 1.64e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098    222 AFKVSLPLRTNYLYGKIKKTLPeLYAFTICLWLRSSASPGIGTpFSYAVPGQANEIvLIEWgNNPIELLINdkVAQLP-L 300
Cdd:pfam00354   2 VFVFPKESDTSYVSLIPELEKP-LQNFTLCLRFYTDLSRSYSL-FSYATKKQDNEL-LIFK-EKDGEYSFY--VGGAEvL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098    301 FVSDG---KWHHICITWTTRDGMWEAFQDGeKLGTGENLAPWHPIKPGGVLILGQEQDTVGGRFDATQAFVGELSQFNIW 377
Cdd:pfam00354  76 FKVSEipvAPVHICTSWESSSGIAEFWVDG-KPWVRKSLKKGYTVGAPPSIILGQEQDSYGGGFDASQSLVGEIGDLNMW 154
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 7949098    378 DRVLRAQEIINIANCSTnMPGNIIPWVDNNVDVFGGA 414
Cdd:pfam00354 155 DYVLTPEEINTVYKGGP-FSPNILDWRALNYEARGYV 190
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
57-215 9.11e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 9.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098    57 EEELRAAVLQLRETVVQQKETLGAQREAIRELTGKLARceglAGGkargtgkDTMGDLPRDpghvVEQLSRSLQTLKDRL 136
Cdd:COG4913  297 LEELRAELARLEAELERLEARLDALREELDELEAQIRG----NGG-------DRLEQLERE----IERLERELEERERRR 361
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098   137 ESLELQLRTnvsnAGLPSDFREvlqRRLGELERQLLRKVAELEDEKSLLHNE-TSAHRQKTEST--LNALLQRVTELERG 213
Cdd:COG4913  362 ARLEALLAA----LGLPLPASA---EEFAALRAEAAALLEALEEELEALEEAlAEAEAALRDLRreLRELEAEIASLERR 434

                 ..
gi 7949098   214 NS 215
Cdd:COG4913  435 KS 436
CDC37_N smart01071
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
66-185 2.08e-03

Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domain corresponds to the N terminal domain which binds predominantly to protein kinases.and is found N terminal to the Hsp (Heat shocked protein) 90-binding domain. Expression of a construct consisting of only the N-terminal domain of Saccharomyces pombe Cdc37 results in cellular viability. This indicates that interactions with the cochaperone Hsp90 may not be essential for Cdc37 function.


Pssm-ID: 198139 [Multi-domain]  Cd Length: 154  Bit Score: 38.55  E-value: 2.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098      66 QLRETVVQQKETLGAQREAIRELTGKlarceglaggkargtgKDTMGDLPRDpghvvEQLSRSLQTLKDRLESLELQLRT 145
Cdd:smart01071  39 QARVERMEEIKNLKYELIMNDHLNKR----------------IDKLLKGLRE-----EELSPETPTYNEMLAELQDQLKK 97
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 7949098     146 NVSNA-GLPSDFREVLQRRLGEL---ERQLLRKVAELEDEKSLL 185
Cdd:smart01071  98 ELEEAnGDSEGLLEELKKHRDKLkkeQKELRKKLDELEKEEKKK 141
CCDC-167 pfam15188
Coiled-coil domain-containing protein 167; The function of this family of coiled-coil domains, ...
121-188 2.69e-03

Coiled-coil domain-containing protein 167; The function of this family of coiled-coil domains, has not, as yet, been determined. Members of this family remain uncharacterized. This family of proteins is found in eukaryotes. Proteins in this family are typically between and 103 amino acids in length.


Pssm-ID: 464553 [Multi-domain]  Cd Length: 82  Bit Score: 36.49  E-value: 2.69e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7949098    121 VVEQLSRSLQTLKDRLESLELQLRTnvsnAGLPSDfrevlQRRLGELERQLLRKVAE-LEDEKSLLHNE 188
Cdd:pfam15188   4 EIDRLEEKIASCRDRLERIEKKLRR----EELSEE-----DRRSLEKELLLLKKRLEkNEEELKLLRKE 63
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
58-171 2.84e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 2.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098    58 EELRAAVLQLRETVVQQKETLGAQREAIRELTGKL--ARCEGLAGGKARG-------TGK-----DTMGDLPRDPGHVVE 123
Cdd:PRK02224 609 ERLREKREALAELNDERRERLAEKRERKRELEAEFdeARIEEAREDKERAeeyleqvEEKldelrEERDDLQAEIGAVEN 688
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 7949098   124 QLSRsLQTLKDRLESLE---LQLRTNVSNAG--------LPSDFRevlQRRLGELERQL 171
Cdd:PRK02224 689 ELEE-LEELRERREALEnrvEALEALYDEAEelesmygdLRAELR---QRNVETLERML 743
growth_prot_Scy NF041483
polarized growth protein Scy;
68-201 5.70e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 39.04  E-value: 5.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098     68 RETVVQQKETLGAQREAIReltGKL--ARcEGLAGGKARGTGkdtmgdlprDPGHVVEQLSRSLQTLKDRLES-LELQLR 144
Cdd:NF041483   31 REKAVQHAEDLGYQVEVLR---AKLheAR-RSLASRPAYDGA---------DIGYQAEQLLRNAQIQADQLRAdAERELR 97
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7949098    145 tnvsnaglpsDFREVLQRRLGELERQLLRKVAELEDE----KSLLHNETSAHRQKTESTLN 201
Cdd:NF041483   98 ----------DARAQTQRILQEHAEHQARLQAELHTEavqrRQQLDQELAERRQTVESHVN 148
 
Name Accession Description Interval E-value
PTX smart00159
Pentraxin / C-reactive protein / pentaxin family; This family form a doscoid pentameric ...
217-422 7.65e-104

Pentraxin / C-reactive protein / pentaxin family; This family form a doscoid pentameric structure. Human serum amyloid P demonstrates calcium-mediated ligand-binding.


Pssm-ID: 128463  Cd Length: 206  Bit Score: 306.50  E-value: 7.65e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098     217 FKSPDAFKVSLPLRTNYLYGKIKKTLP-ELYAFTICLWLRSSASPGIGTPFSYAVPGQANEIVLIEWGNNPIELLINDKV 295
Cdd:smart00159   1 QTDLTGKVFVFPKESDTSYVKLKPELPkPLQAFTVCLWFYSDLSPRGYSLFSYATKGQDNELLLYKEKQGEYSLYIGGKK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098     296 AQLPLFVSDGKWHHICITWTTRDGMWEAFQDGeKLGTGENLAPWHPIKPGGVLILGQEQDTVGGRFDATQAFVGELSQFN 375
Cdd:smart00159  81 VQFPVPESDGKWHHICTTWESSSGIAELWVDG-KPGVRKGLAKGYTVKPGGSIILGQEQDSYGGGFDATQSFVGEIGDLN 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 7949098     376 IWDRVLRAQEIINIANCSTNMPGNIIPWVDNNVDVFGGASKWPVETC 422
Cdd:smart00159 160 MWDSVLSPEEIKSVYKGSTFSIGNILNWRALNYEVHGGVVIKPQEWC 206
PTX cd00152
Pentraxins are plasma proteins characterized by their pentameric discoid assembly and their ...
221-417 3.99e-95

Pentraxins are plasma proteins characterized by their pentameric discoid assembly and their Ca2+ dependent ligand binding, such as Serum amyloid P component (SAP) and C-reactive Protein (CRP), which are cytokine-inducible acute-phase proteins implicated in innate immunity. CRP binds to ligands containing phosphocholine, SAP binds to amyloid fibrils, DNA, chromatin, fibronectin, C4-binding proteins and glycosaminoglycans. "Long" pentraxins have N-terminal extensions to the common pentraxin domain; one group, the neuronal pentraxins, may be involved in synapse formation and remodeling, and they may also be able to form heteromultimers.


Pssm-ID: 238086  Cd Length: 201  Bit Score: 284.16  E-value: 3.99e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098  221 DAFKVSLPLRTNYLYGKIKKTLP-ELYAFTICLWLRSSASPGIGTPFSYAVPGQANEIVLIEWGNNPIELLINDKVAQLP 299
Cdd:cd00152   5 SGKVFVFPKESDTSYVKLKPELPkPLQAFTLCLWVYTDLSTREYSLFSYATKGQDNELLLYKEKDGGYSLYIGGKEVTFK 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098  300 LFVSDGKWHHICITWTTRDGMWEAFQDGEKLGTGEnLAPWHPIKPGGVLILGQEQDTVGGRFDATQAFVGELSQFNIWDR 379
Cdd:cd00152  85 VPESDGAWHHICVTWESTSGIAELWVNGKLSVRKS-LKKGYTVGPGGSIILGQEQDSYGGGFDATQSFVGEISDVNMWDS 163
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 7949098  380 VLRAQEIINIANCSTNMPGNIIPWVDNNVDVFGGASKW 417
Cdd:cd00152 164 VLSPEEIKNVYSEGGTLSGNILNWRALNYEINGGVVIK 201
Pentaxin pfam00354
Pentaxin family; Pentaxins are also known as pentraxins.
222-414 1.64e-32

Pentaxin family; Pentaxins are also known as pentraxins.


Pssm-ID: 278768  Cd Length: 194  Bit Score: 121.76  E-value: 1.64e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098    222 AFKVSLPLRTNYLYGKIKKTLPeLYAFTICLWLRSSASPGIGTpFSYAVPGQANEIvLIEWgNNPIELLINdkVAQLP-L 300
Cdd:pfam00354   2 VFVFPKESDTSYVSLIPELEKP-LQNFTLCLRFYTDLSRSYSL-FSYATKKQDNEL-LIFK-EKDGEYSFY--VGGAEvL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098    301 FVSDG---KWHHICITWTTRDGMWEAFQDGeKLGTGENLAPWHPIKPGGVLILGQEQDTVGGRFDATQAFVGELSQFNIW 377
Cdd:pfam00354  76 FKVSEipvAPVHICTSWESSSGIAEFWVDG-KPWVRKSLKKGYTVGAPPSIILGQEQDSYGGGFDASQSLVGEIGDLNMW 154
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 7949098    378 DRVLRAQEIINIANCSTnMPGNIIPWVDNNVDVFGGA 414
Cdd:pfam00354 155 DYVLTPEEINTVYKGGP-FSPNILDWRALNYEARGYV 190
Laminin_G_3 pfam13385
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ...
247-386 5.49e-16

Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.


Pssm-ID: 463865 [Multi-domain]  Cd Length: 151  Bit Score: 74.73  E-value: 5.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098    247 AFTICLWLRSSASPGIGTPFsyAVPGQANEIVLIEWGNNPIELLIND-----KVAQLPLFVSDGKWHHICITWttRDGMW 321
Cdd:pfam13385  18 DFTVSAWVKPDSLPGWARAI--ISSSGGGGYSLGLDGDGRLRFAVNGgnggwDTVTSGASVPLGQWTHVAVTY--DGGTL 93
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7949098    322 EAFQDGEKLGTGENLAPWhPIKPGGVLILGqeqdtvgGRFDATQAFVGELSQFNIWDRVLRAQEI 386
Cdd:pfam13385  94 RLYVNGVLVGSSTLTGGP-PPGTGGPLYIG-------RSPGGDDYFNGLIDEVRIYDRALSAAEI 150
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
57-215 9.11e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 9.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098    57 EEELRAAVLQLRETVVQQKETLGAQREAIRELTGKLARceglAGGkargtgkDTMGDLPRDpghvVEQLSRSLQTLKDRL 136
Cdd:COG4913  297 LEELRAELARLEAELERLEARLDALREELDELEAQIRG----NGG-------DRLEQLERE----IERLERELEERERRR 361
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098   137 ESLELQLRTnvsnAGLPSDFREvlqRRLGELERQLLRKVAELEDEKSLLHNE-TSAHRQKTEST--LNALLQRVTELERG 213
Cdd:COG4913  362 ARLEALLAA----LGLPLPASA---EEFAALRAEAAALLEALEEELEALEEAlAEAEAALRDLRreLRELEAEIASLERR 434

                 ..
gi 7949098   214 NS 215
Cdd:COG4913  435 KS 436
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
248-377 1.56e-04

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 41.63  E-value: 1.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098  248 FTICLWLRSSASPGIgtPFSYAVPGQANEIVL--------IEWGNNPIELLINDKVAqlplfVSDGKWHHICITWTTRDG 319
Cdd:cd00110  22 LSISFSFRTTSPNGL--LLYAGSQNGGDFLALeledgrlvLRYDLGSGSLVLSSKTP-----LNDGQWHSVSVERNGRSV 94
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098  320 MweaFQ-DGEKLGTGENLAPWHPIKPGGVLILGQEQDTVGGRFDA-TQAFVGELSQFNIW 377
Cdd:cd00110  95 T---LSvDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPvSPGFVGCIRDLKVN 151
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
57-212 2.15e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 2.15e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098   57 EEELRAAVLQLRE--TVVQQKETLGAQREAIR----ELTGKLARCEGLAGgkargtgkdtmgdlPRDPGHVVEQLSRSLQ 130
Cdd:COG4717  77 EEELKEAEEKEEEyaELQEELEELEEELEELEaeleELREELEKLEKLLQ--------------LLPLYQELEALEAELA 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098  131 TLKDRLESLELQLRTnvsnaglpsdfREVLQRRLGELERQLLRKVAELEDEKSLLHNETSAHRQKTESTLNALLQRVTEL 210
Cdd:COG4717 143 ELPERLEELEERLEE-----------LRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211

                ..
gi 7949098  211 ER 212
Cdd:COG4717 212 EE 213
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
58-212 3.95e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 3.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098    58 EELRAAVLQLRETVVQQKETLGAQREAIRELTGKLARCEGLAGgkargtgkdtMGDLPRDpghvVEQLSRSLQTLKDRLE 137
Cdd:COG4913  613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAE----------YSWDEID----VASAEREIAELEAELE 678
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7949098   138 SLELqlrtnvSNAGLpsdfrEVLQRRLGELERQLlrkvAELEDEKsllhNETSAHRQKTESTLNALLQRVTELER 212
Cdd:COG4913  679 RLDA------SSDDL-----AALEEQLEELEAEL----EELEEEL----DELKGEIGRLEKELEQAEEELDELQD 734
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
52-212 1.71e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.77  E-value: 1.71e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098   52 GALSPEEELRAAVLQLRETVVQQKETlgaqREAIRELTGKLARCEglaggKARGTGKDTMGDLPRDPghvveqlsrSLQT 131
Cdd:COG3206 206 GLVDLSEEAKLLLQQLSELESQLAEA----RAELAEAEARLAALR-----AQLGSGPDALPELLQSP---------VIQQ 267
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098  132 LKDRLESLELQLRTnvsnaglpsdfrevLQRRLGELERQLLRKVAELEDEKSLLHNETSAHRQKTESTLNALLQRVTELE 211
Cdd:COG3206 268 LRAQLAELEAELAE--------------LSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQ 333

                .
gi 7949098  212 R 212
Cdd:COG3206 334 A 334
CDC37_N smart01071
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
66-185 2.08e-03

Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domain corresponds to the N terminal domain which binds predominantly to protein kinases.and is found N terminal to the Hsp (Heat shocked protein) 90-binding domain. Expression of a construct consisting of only the N-terminal domain of Saccharomyces pombe Cdc37 results in cellular viability. This indicates that interactions with the cochaperone Hsp90 may not be essential for Cdc37 function.


Pssm-ID: 198139 [Multi-domain]  Cd Length: 154  Bit Score: 38.55  E-value: 2.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098      66 QLRETVVQQKETLGAQREAIRELTGKlarceglaggkargtgKDTMGDLPRDpghvvEQLSRSLQTLKDRLESLELQLRT 145
Cdd:smart01071  39 QARVERMEEIKNLKYELIMNDHLNKR----------------IDKLLKGLRE-----EELSPETPTYNEMLAELQDQLKK 97
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 7949098     146 NVSNA-GLPSDFREVLQRRLGEL---ERQLLRKVAELEDEKSLL 185
Cdd:smart01071  98 ELEEAnGDSEGLLEELKKHRDKLkkeQKELRKKLDELEKEEKKK 141
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
36-211 2.11e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 40.71  E-value: 2.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098    36 EAARAGCPLPAmpmqggaLSPE------EELRAAVLQLRETVVQQKETLGAQREAIRELTGKLARCEGLAGGKARGTGKD 109
Cdd:COG3096  423 EKARALCGLPD-------LTPEnaedylAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVERSQAWQ 495
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098   110 TMGDLPRDpghvveqlSRSLQTLKDRLESLELQLRTNVSNAGLPSDFREVLQ---RRLG-------ELERQLLRKVAELE 179
Cdd:COG3096  496 TARELLRR--------YRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEefcQRIGqqldaaeELEELLAELEAQLE 567
                        170       180       190
                 ....*....|....*....|....*....|..
gi 7949098   180 DEKSLLhNETSAHRQKTESTLNALLQRVTELE 211
Cdd:COG3096  568 ELEEQA-AEAVEQRSELRQQLEQLRARIKELA 598
CCDC-167 pfam15188
Coiled-coil domain-containing protein 167; The function of this family of coiled-coil domains, ...
121-188 2.69e-03

Coiled-coil domain-containing protein 167; The function of this family of coiled-coil domains, has not, as yet, been determined. Members of this family remain uncharacterized. This family of proteins is found in eukaryotes. Proteins in this family are typically between and 103 amino acids in length.


Pssm-ID: 464553 [Multi-domain]  Cd Length: 82  Bit Score: 36.49  E-value: 2.69e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7949098    121 VVEQLSRSLQTLKDRLESLELQLRTnvsnAGLPSDfrevlQRRLGELERQLLRKVAE-LEDEKSLLHNE 188
Cdd:pfam15188   4 EIDRLEEKIASCRDRLERIEKKLRR----EELSEE-----DRRSLEKELLLLKKRLEkNEEELKLLRKE 63
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
58-171 2.84e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 2.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098    58 EELRAAVLQLRETVVQQKETLGAQREAIRELTGKL--ARCEGLAGGKARG-------TGK-----DTMGDLPRDPGHVVE 123
Cdd:PRK02224 609 ERLREKREALAELNDERRERLAEKRERKRELEAEFdeARIEEAREDKERAeeyleqvEEKldelrEERDDLQAEIGAVEN 688
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 7949098   124 QLSRsLQTLKDRLESLE---LQLRTNVSNAG--------LPSDFRevlQRRLGELERQL 171
Cdd:PRK02224 689 ELEE-LEELRERREALEnrvEALEALYDEAEelesmygdLRAELR---QRNVETLERML 743
growth_prot_Scy NF041483
polarized growth protein Scy;
68-201 5.70e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 39.04  E-value: 5.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098     68 RETVVQQKETLGAQREAIReltGKL--ARcEGLAGGKARGTGkdtmgdlprDPGHVVEQLSRSLQTLKDRLES-LELQLR 144
Cdd:NF041483   31 REKAVQHAEDLGYQVEVLR---AKLheAR-RSLASRPAYDGA---------DIGYQAEQLLRNAQIQADQLRAdAERELR 97
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7949098    145 tnvsnaglpsDFREVLQRRLGELERQLLRKVAELEDE----KSLLHNETSAHRQKTESTLN 201
Cdd:NF041483   98 ----------DARAQTQRILQEHAEHQARLQAELHTEavqrRQQLDQELAERRQTVESHVN 148
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
58-212 6.69e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 6.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098   58 EELRAAVLQLRETVVQQKETLGAQREAIRELTGKLARCEglaGGKARgtGKDTMGDLPRDpghvVEQLSRSLQTLKDRLE 137
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLE---QDIAR--LEERRRELEER----LEELEEELAELEEELE 333
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7949098  138 SLELQLRTNVSNAGLPSDFREVLQRRLGELERQLLRKVAELEDEKSLLHNETSAHRQKtESTLNALLQRVTELER 212
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA-LRAAAELAAQLEELEE 407
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
58-195 8.78e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 37.60  E-value: 8.78e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949098   58 EELRAAVLQLRETVVQQKETLGAQREAIRELTGKLARCEG-LAGGKAR-GTGKDtmgdlPRDpghvVEQLSRSLQTLKDR 135
Cdd:COG1579  34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEArIKKYEEQlGNVRN-----NKE----YEALQKEIESLKRR 104
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7949098  136 LESLE---LQLRTNVSNAglpSDFREVLQRRLGELERQLLRKVAELEDEKSLLHNETSAHRQK 195
Cdd:COG1579 105 ISDLEdeiLELMERIEEL---EEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
 
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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