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Conserved domains on  [gi|36054013|ref|NP_109614|]
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neuronal pentraxin receptor 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 ...
281-487 3.89e-93

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: 281.46  E-value: 3.89e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36054013    281 YSPPDAFKVSIPIRNNYMYARVRKALP-ELYAFTACMWLRSRSGGsGQGTPFSYSVPGQANEIVLLEAGLEPMELLINDK 359
Cdd:smart00159   1 QTDLTGKVFVFPKESDTSYVKLKPELPkPLQAFTVCLWFYSDLSP-RGYSLFSYATKGQDNELLLYKEKQGEYSLYIGGK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36054013    360 VAQLPLSLKDSNWHHICISWTTRDGLWSAYQDGELRgSGENLAAWHPIKPHGILILGQEQDTLGGRFDATQAFVGDIAQF 439
Cdd:smart00159  80 KVQFPVPESDGKWHHICTTWESSSGIAELWVDGKPG-VRKGLAKGYTVKPGGSIILGQEQDSYGGGFDATQSFVGEIGDL 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 36054013    440 NLWDHALTPAQVLGMANCTGPLMGNVLPWEDKLVEAFGGAKKAAFDVC 487
Cdd:smart00159 159 NMWDSVLSPEEIKSVYKGSTFSIGNILNWRALNYEVHGGVVIKPQEWC 206
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
106-276 2.75e-05

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 2.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36054013 106 AEQGDAAGERAELLLLQSTAEQLRQTALQQEARIRADRDTIRELTGKLGRCESGLPRGLQDAGPRRDTMADGAWDspalL 185
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE----L 325
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36054013 186 LELEDAVRALRDRIERIEQELpargnissapapampTALHSKMDELEGQLLAKVLALEKERAALSHGSHQQRQEVEKELN 265
Cdd:COG1196 326 AELEEELEELEEELEELEEEL---------------EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
                       170
                ....*....|.
gi 36054013 266 ALQGRVAELEH 276
Cdd:COG1196 391 ALRAAAELAAQ 401
 
Name Accession Description Interval E-value
PTX smart00159
Pentraxin / C-reactive protein / pentaxin family; This family form a doscoid pentameric ...
281-487 3.89e-93

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: 281.46  E-value: 3.89e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36054013    281 YSPPDAFKVSIPIRNNYMYARVRKALP-ELYAFTACMWLRSRSGGsGQGTPFSYSVPGQANEIVLLEAGLEPMELLINDK 359
Cdd:smart00159   1 QTDLTGKVFVFPKESDTSYVKLKPELPkPLQAFTVCLWFYSDLSP-RGYSLFSYATKGQDNELLLYKEKQGEYSLYIGGK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36054013    360 VAQLPLSLKDSNWHHICISWTTRDGLWSAYQDGELRgSGENLAAWHPIKPHGILILGQEQDTLGGRFDATQAFVGDIAQF 439
Cdd:smart00159  80 KVQFPVPESDGKWHHICTTWESSSGIAELWVDGKPG-VRKGLAKGYTVKPGGSIILGQEQDSYGGGFDATQSFVGEIGDL 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 36054013    440 NLWDHALTPAQVLGMANCTGPLMGNVLPWEDKLVEAFGGAKKAAFDVC 487
Cdd:smart00159 159 NMWDSVLSPEEIKSVYKGSTFSIGNILNWRALNYEVHGGVVIKPQEWC 206
PTX cd00152
Pentraxins are plasma proteins characterized by their pentameric discoid assembly and their ...
285-481 1.48e-89

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: 272.22  E-value: 1.48e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36054013 285 DAFKVSIPIRNNYMYARVRKALP-ELYAFTACMWLRSRSGgSGQGTPFSYSVPGQANEIVLLEAGLEPMELLINDKVAQL 363
Cdd:cd00152   5 SGKVFVFPKESDTSYVKLKPELPkPLQAFTLCLWVYTDLS-TREYSLFSYATKGQDNELLLYKEKDGGYSLYIGGKEVTF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36054013 364 PLSLKDSNWHHICISWTTRDGLWSAYQDGELRGSGEnLAAWHPIKPHGILILGQEQDTLGGRFDATQAFVGDIAQFNLWD 443
Cdd:cd00152  84 KVPESDGAWHHICVTWESTSGIAELWVNGKLSVRKS-LKKGYTVGPGGSIILGQEQDSYGGGFDATQSFVGEISDVNMWD 162
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 36054013 444 HALTPAQVLGMANCTGPLMGNVLPWEDKLVEAFGGAKK 481
Cdd:cd00152 163 SVLSPEEIKNVYSEGGTLSGNILNWRALNYEINGGVVI 200
Pentaxin pfam00354
Pentaxin family; Pentaxins are also known as pentraxins.
309-479 1.95e-28

Pentaxin family; Pentaxins are also known as pentraxins.


Pssm-ID: 278768  Cd Length: 194  Bit Score: 111.36  E-value: 1.95e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36054013   309 LYAFTACmwLRSRSGGSGQGTPFSYSVPGQANEIVLLEAglEPMELLINdkVAQLPLSLKDS----NWHHICISWTTRDG 384
Cdd:pfam00354  24 LQNFTLC--LRFYTDLSRSYSLFSYATKKQDNELLIFKE--KDGEYSFY--VGGAEVLFKVSeipvAPVHICTSWESSSG 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36054013   385 LWSAYQDGELRGSgENLAAWHPIKPHGILILGQEQDTLGGRFDATQAFVGDIAQFNLWDHALTPAQVLGMANCtGPLMGN 464
Cdd:pfam00354  98 IAEFWVDGKPWVR-KSLKKGYTVGAPPSIILGQEQDSYGGGFDASQSLVGEIGDLNMWDYVLTPEEINTVYKG-GPFSPN 175
                         170
                  ....*....|....*
gi 36054013   465 VLPWEDKLVEAFGGA 479
Cdd:pfam00354 176 ILDWRALNYEARGYV 190
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
106-276 2.75e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 2.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36054013 106 AEQGDAAGERAELLLLQSTAEQLRQTALQQEARIRADRDTIRELTGKLGRCESGLPRGLQDAGPRRDTMADGAWDspalL 185
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE----L 325
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36054013 186 LELEDAVRALRDRIERIEQELpargnissapapampTALHSKMDELEGQLLAKVLALEKERAALSHGSHQQRQEVEKELN 265
Cdd:COG1196 326 AELEEELEELEEELEELEEEL---------------EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
                       170
                ....*....|.
gi 36054013 266 ALQGRVAELEH 276
Cdd:COG1196 391 ALRAAAELAAQ 401
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
115-304 1.16e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 1.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36054013    115 RAELLLLQSTAEQLRQTALQQEARIRADRDTIRELTGKLGRCESGLPRGLQDAG--PRRDTMADGAWDSPALLLE-LEDA 191
Cdd:TIGR02168  781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAatERRLEDLEEQIEELSEDIEsLAAE 860
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36054013    192 VRALRDRIERIEQELPARGNISSApapaMPTALHSKMDELEgQLLAKVLALEKERAALSHGSHQQRQEVEK---ELNALQ 268
Cdd:TIGR02168  861 IEELEELIEELESELEALLNERAS----LEEALALLRSELE-ELSEELRELESKRSELRRELEELREKLAQlelRLEGLE 935
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 36054013    269 GRVAEL-----EHGSSAYSPPDAFKVSIPIRNNYMYARVRK 304
Cdd:TIGR02168  936 VRIDNLqerlsEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
114-275 3.17e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 39.88  E-value: 3.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36054013   114 ERAELLLLQSTAEQLRQTALQQEARIRADRD-TIRELTGKLGRCESGLPR-------------GLQDAGP----RRDTMA 175
Cdd:pfam07888  42 ERAELLQAQEAANRQREKEKERYKRDREQWErQRRELESRVAELKEELRQsrekheeleekykELSASSEelseEKDALL 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36054013   176 DGAWDSPALLLELEDAVRALRDRIERIEQELP------ARGNISSAPAPAMPTALHSKMDELEGQL--LAKVLALEKERA 247
Cdd:pfam07888 122 AQRAAHEARIRELEEDIKTLTQRVLERETELErmkeraKKAGAQRKEEEAERKQLQAKLQQTEEELrsLSKEFQELRNSL 201
                         170       180       190
                  ....*....|....*....|....*....|..
gi 36054013   248 ALSHGSHQQRQE----VEKELNALQGRVAELE 275
Cdd:pfam07888 202 AQRDTQVLQLQDtittLTQKLTTAHRKEAENE 233
 
Name Accession Description Interval E-value
PTX smart00159
Pentraxin / C-reactive protein / pentaxin family; This family form a doscoid pentameric ...
281-487 3.89e-93

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: 281.46  E-value: 3.89e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36054013    281 YSPPDAFKVSIPIRNNYMYARVRKALP-ELYAFTACMWLRSRSGGsGQGTPFSYSVPGQANEIVLLEAGLEPMELLINDK 359
Cdd:smart00159   1 QTDLTGKVFVFPKESDTSYVKLKPELPkPLQAFTVCLWFYSDLSP-RGYSLFSYATKGQDNELLLYKEKQGEYSLYIGGK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36054013    360 VAQLPLSLKDSNWHHICISWTTRDGLWSAYQDGELRgSGENLAAWHPIKPHGILILGQEQDTLGGRFDATQAFVGDIAQF 439
Cdd:smart00159  80 KVQFPVPESDGKWHHICTTWESSSGIAELWVDGKPG-VRKGLAKGYTVKPGGSIILGQEQDSYGGGFDATQSFVGEIGDL 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 36054013    440 NLWDHALTPAQVLGMANCTGPLMGNVLPWEDKLVEAFGGAKKAAFDVC 487
Cdd:smart00159 159 NMWDSVLSPEEIKSVYKGSTFSIGNILNWRALNYEVHGGVVIKPQEWC 206
PTX cd00152
Pentraxins are plasma proteins characterized by their pentameric discoid assembly and their ...
285-481 1.48e-89

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: 272.22  E-value: 1.48e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36054013 285 DAFKVSIPIRNNYMYARVRKALP-ELYAFTACMWLRSRSGgSGQGTPFSYSVPGQANEIVLLEAGLEPMELLINDKVAQL 363
Cdd:cd00152   5 SGKVFVFPKESDTSYVKLKPELPkPLQAFTLCLWVYTDLS-TREYSLFSYATKGQDNELLLYKEKDGGYSLYIGGKEVTF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36054013 364 PLSLKDSNWHHICISWTTRDGLWSAYQDGELRGSGEnLAAWHPIKPHGILILGQEQDTLGGRFDATQAFVGDIAQFNLWD 443
Cdd:cd00152  84 KVPESDGAWHHICVTWESTSGIAELWVNGKLSVRKS-LKKGYTVGPGGSIILGQEQDSYGGGFDATQSFVGEISDVNMWD 162
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 36054013 444 HALTPAQVLGMANCTGPLMGNVLPWEDKLVEAFGGAKK 481
Cdd:cd00152 163 SVLSPEEIKNVYSEGGTLSGNILNWRALNYEINGGVVI 200
Pentaxin pfam00354
Pentaxin family; Pentaxins are also known as pentraxins.
309-479 1.95e-28

Pentaxin family; Pentaxins are also known as pentraxins.


Pssm-ID: 278768  Cd Length: 194  Bit Score: 111.36  E-value: 1.95e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36054013   309 LYAFTACmwLRSRSGGSGQGTPFSYSVPGQANEIVLLEAglEPMELLINdkVAQLPLSLKDS----NWHHICISWTTRDG 384
Cdd:pfam00354  24 LQNFTLC--LRFYTDLSRSYSLFSYATKKQDNELLIFKE--KDGEYSFY--VGGAEVLFKVSeipvAPVHICTSWESSSG 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36054013   385 LWSAYQDGELRGSgENLAAWHPIKPHGILILGQEQDTLGGRFDATQAFVGDIAQFNLWDHALTPAQVLGMANCtGPLMGN 464
Cdd:pfam00354  98 IAEFWVDGKPWVR-KSLKKGYTVGAPPSIILGQEQDSYGGGFDASQSLVGEIGDLNMWDYVLTPEEINTVYKG-GPFSPN 175
                         170
                  ....*....|....*
gi 36054013   465 VLPWEDKLVEAFGGA 479
Cdd:pfam00354 176 ILDWRALNYEARGYV 190
Laminin_G_3 pfam13385
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ...
311-451 1.32e-13

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: 68.18  E-value: 1.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36054013   311 AFTACMWLRSRSGGSGQGTpfsYSVPGQANEIVLLEAGLEPMELLIND-----KVAQLPLSLKDSNWHHICISWttRDGL 385
Cdd:pfam13385  18 DFTVSAWVKPDSLPGWARA---IISSSGGGGYSLGLDGDGRLRFAVNGgnggwDTVTSGASVPLGQWTHVAVTY--DGGT 92
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 36054013   386 WSAYQDGELRGSGENLAAWhPIKPHGILilgqeqdTLGGRFDATQAFVGDIAQFNLWDHALTPAQV 451
Cdd:pfam13385  93 LRLYVNGVLVGSSTLTGGP-PPGTGGPL-------YIGRSPGGDDYFNGLIDEVRIYDRALSAAEI 150
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
106-276 2.75e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 2.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36054013 106 AEQGDAAGERAELLLLQSTAEQLRQTALQQEARIRADRDTIRELTGKLGRCESGLPRGLQDAGPRRDTMADGAWDspalL 185
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE----L 325
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36054013 186 LELEDAVRALRDRIERIEQELpargnissapapampTALHSKMDELEGQLLAKVLALEKERAALSHGSHQQRQEVEKELN 265
Cdd:COG1196 326 AELEEELEELEEELEELEEEL---------------EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
                       170
                ....*....|.
gi 36054013 266 ALQGRVAELEH 276
Cdd:COG1196 391 ALRAAAELAAQ 401
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
115-304 1.16e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 1.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36054013    115 RAELLLLQSTAEQLRQTALQQEARIRADRDTIRELTGKLGRCESGLPRGLQDAG--PRRDTMADGAWDSPALLLE-LEDA 191
Cdd:TIGR02168  781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAatERRLEDLEEQIEELSEDIEsLAAE 860
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36054013    192 VRALRDRIERIEQELPARGNISSApapaMPTALHSKMDELEgQLLAKVLALEKERAALSHGSHQQRQEVEK---ELNALQ 268
Cdd:TIGR02168  861 IEELEELIEELESELEALLNERAS----LEEALALLRSELE-ELSEELRELESKRSELRRELEELREKLAQlelRLEGLE 935
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 36054013    269 GRVAEL-----EHGSSAYSPPDAFKVSIPIRNNYMYARVRK 304
Cdd:TIGR02168  936 VRIDNLqerlsEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
103-275 9.48e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.98  E-value: 9.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36054013    103 PSGA----------EQGDAAGERAELLLLQSTAEQL---RQTALQQEARIR----ADRDTIRELTGKLGRCESGLPRGLQ 165
Cdd:TIGR02169  651 KSGAmtggsraprgGILFSRSEPAELQRLRERLEGLkreLSSLQSELRRIEnrldELSQELSDASRKIGEIEKEIEQLEQ 730
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36054013    166 DAGprrdtmadgawdspALLLELEDavraLRDRIERIEQELpargnissapapampTALHSKMDELEGQLLAKVLALEKE 245
Cdd:TIGR02169  731 EEE--------------KLKERLEE----LEEDLSSLEQEI---------------ENVKSELKELEARIEELEEDLHKL 777
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 36054013    246 RAALS----HGSHQQRQE-------VEKELNALQGRVAELE 275
Cdd:TIGR02169  778 EEALNdleaRLSHSRIPEiqaelskLEEEVSRIEARLREIE 818
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
115-284 1.97e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36054013  115 RAELLLLQSTAEQLRQTALQQEARIRADRDTIRELTGKLGRCEsglpRGLQDAGPRRdtmadgawdspalLLELEDAVRA 194
Cdd:COG4913  287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELE----AQIRGNGGDR-------------LEQLEREIER 349
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36054013  195 LRDRIERIEQElpaRGNISSA------PAPAMPTALHSKMDELEgQLLAKVLALEKERAALSHGSHQQRQEVEKELNALQ 268
Cdd:COG4913  350 LERELEERERR---RARLEALlaalglPLPASAEEFAALRAEAA-ALLEALEEELEALEEALAEAEAALRDLRRELRELE 425
                        170
                 ....*....|....*.
gi 36054013  269 GRVAELEHGSSAYSPP 284
Cdd:COG4913  426 AEIASLERRKSNIPAR 441
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
114-275 3.17e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 39.88  E-value: 3.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36054013   114 ERAELLLLQSTAEQLRQTALQQEARIRADRD-TIRELTGKLGRCESGLPR-------------GLQDAGP----RRDTMA 175
Cdd:pfam07888  42 ERAELLQAQEAANRQREKEKERYKRDREQWErQRRELESRVAELKEELRQsrekheeleekykELSASSEelseEKDALL 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36054013   176 DGAWDSPALLLELEDAVRALRDRIERIEQELP------ARGNISSAPAPAMPTALHSKMDELEGQL--LAKVLALEKERA 247
Cdd:pfam07888 122 AQRAAHEARIRELEEDIKTLTQRVLERETELErmkeraKKAGAQRKEEEAERKQLQAKLQQTEEELrsLSKEFQELRNSL 201
                         170       180       190
                  ....*....|....*....|....*....|..
gi 36054013   248 ALSHGSHQQRQE----VEKELNALQGRVAELE 275
Cdd:pfam07888 202 AQRDTQVLQLQDtittLTQKLTTAHRKEAENE 233
 
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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