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Conserved domains on  [gi|17402888|ref|NP_055108|]
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neuronal pentraxin receptor precursor [Homo sapiens]

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 ...
288-494 3.28e-92

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: 279.15  E-value: 3.28e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402888    288 YSPPDAFKISIPIRNNYMYARVRKALP-ELYAFTACMWLRSRSSgTGQGTPFSYSVPGQANEIVLLEAGHEPMELLINDK 366
Cdd:smart00159   1 QTDLTGKVFVFPKESDTSYVKLKPELPkPLQAFTVCLWFYSDLS-PRGYSLFSYATKGQDNELLLYKEKQGEYSLYIGGK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402888    367 VAQLPLSLKDNGWHHICIAWTTRDGLWSAYQDGELqGSGENLAAWHPIKPHGILILGQEQDTLGGRFDATQAFVGDIAQF 446
Cdd:smart00159  80 KVQFPVPESDGKWHHICTTWESSSGIAELWVDGKP-GVRKGLAKGYTVKPGGSIILGQEQDSYGGGFDATQSFVGEIGDL 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 17402888    447 NLWDHALTPAQVLGIANCTAPLLGNVLPWEDKLVEAFGGATKAAFDVC 494
Cdd:smart00159 159 NMWDSVLSPEEIKSVYKGSTFSIGNILNWRALNYEVHGGVVIKPQEWC 206
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
120-291 6.83e-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: 45.68  E-value: 6.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402888  120 REELLLLQSTAEQLRQTALQQEARIRADQDTIRELTGKLGRCEsglpRGLQGAGPRRdtmadgpwdspalILELEDAVRA 199
Cdd:COG4913  287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELE----AQIRGNGGDR-------------LEQLEREIER 349
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402888  200 LRDRIDRLEQELpARVN--LSAAPAPVSAVPTGLHSKMDQLEgQLLAQVLALEKERVALSHSSRRQRQEVEKELDVLQGR 277
Cdd:COG4913  350 LERELEERERRR-ARLEalLAALGLPLPASAEEFAALRAEAA-ALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
                        170
                 ....*....|....
gi 17402888  278 VAELEHGSSAYSPP 291
Cdd:COG4913  428 IASLERRKSNIPAR 441
 
Name Accession Description Interval E-value
PTX smart00159
Pentraxin / C-reactive protein / pentaxin family; This family form a doscoid pentameric ...
288-494 3.28e-92

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: 279.15  E-value: 3.28e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402888    288 YSPPDAFKISIPIRNNYMYARVRKALP-ELYAFTACMWLRSRSSgTGQGTPFSYSVPGQANEIVLLEAGHEPMELLINDK 366
Cdd:smart00159   1 QTDLTGKVFVFPKESDTSYVKLKPELPkPLQAFTVCLWFYSDLS-PRGYSLFSYATKGQDNELLLYKEKQGEYSLYIGGK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402888    367 VAQLPLSLKDNGWHHICIAWTTRDGLWSAYQDGELqGSGENLAAWHPIKPHGILILGQEQDTLGGRFDATQAFVGDIAQF 446
Cdd:smart00159  80 KVQFPVPESDGKWHHICTTWESSSGIAELWVDGKP-GVRKGLAKGYTVKPGGSIILGQEQDSYGGGFDATQSFVGEIGDL 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 17402888    447 NLWDHALTPAQVLGIANCTAPLLGNVLPWEDKLVEAFGGATKAAFDVC 494
Cdd:smart00159 159 NMWDSVLSPEEIKSVYKGSTFSIGNILNWRALNYEVHGGVVIKPQEWC 206
PTX cd00152
Pentraxins are plasma proteins characterized by their pentameric discoid assembly and their ...
292-488 1.57e-86

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: 264.52  E-value: 1.57e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402888 292 DAFKISIPIRNNYMYARVRKALP-ELYAFTACMWLRSrSSGTGQGTPFSYSVPGQANEIVLLEAGHEPMELLINDKVAQL 370
Cdd:cd00152   5 SGKVFVFPKESDTSYVKLKPELPkPLQAFTLCLWVYT-DLSTREYSLFSYATKGQDNELLLYKEKDGGYSLYIGGKEVTF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402888 371 PLSLKDNGWHHICIAWTTRDGLWSAYQDGELQGSGEnLAAWHPIKPHGILILGQEQDTLGGRFDATQAFVGDIAQFNLWD 450
Cdd:cd00152  84 KVPESDGAWHHICVTWESTSGIAELWVNGKLSVRKS-LKKGYTVGPGGSIILGQEQDSYGGGFDATQSFVGEISDVNMWD 162
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 17402888 451 HALTPAQVLGIANCTAPLLGNVLPWEDKLVEAFGGATK 488
Cdd:cd00152 163 SVLSPEEIKNVYSEGGTLSGNILNWRALNYEINGGVVI 200
Pentaxin pfam00354
Pentaxin family; Pentaxins are also known as pentraxins.
316-487 2.95e-27

Pentaxin family; Pentaxins are also known as pentraxins.


Pssm-ID: 278768  Cd Length: 194  Bit Score: 108.28  E-value: 2.95e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402888   316 LYAFTACMWLRSRSSGTGqgTPFSYSVPGQANEIVLLEagHEPMELLINdkVAQLPLSLKDN----GWHHICIAWTTRDG 391
Cdd:pfam00354  24 LQNFTLCLRFYTDLSRSY--SLFSYATKKQDNELLIFK--EKDGEYSFY--VGGAEVLFKVSeipvAPVHICTSWESSSG 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402888   392 LWSAYQDGELQGSgENLAAWHPIKPHGILILGQEQDTLGGRFDATQAFVGDIAQFNLWDHALTPAQVLGIANCtAPLLGN 471
Cdd:pfam00354  98 IAEFWVDGKPWVR-KSLKKGYTVGAPPSIILGQEQDSYGGGFDASQSLVGEIGDLNMWDYVLTPEEINTVYKG-GPFSPN 175
                         170
                  ....*....|....*.
gi 17402888   472 VLPWEDKLVEAFGGAT 487
Cdd:pfam00354 176 ILDWRALNYEARGYVV 191
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
120-291 6.83e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 6.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402888  120 REELLLLQSTAEQLRQTALQQEARIRADQDTIRELTGKLGRCEsglpRGLQGAGPRRdtmadgpwdspalILELEDAVRA 199
Cdd:COG4913  287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELE----AQIRGNGGDR-------------LEQLEREIER 349
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402888  200 LRDRIDRLEQELpARVN--LSAAPAPVSAVPTGLHSKMDQLEgQLLAQVLALEKERVALSHSSRRQRQEVEKELDVLQGR 277
Cdd:COG4913  350 LERELEERERRR-ARLEalLAALGLPLPASAEEFAALRAEAA-ALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
                        170
                 ....*....|....
gi 17402888  278 VAELEHGSSAYSPP 291
Cdd:COG4913  428 IASLERRKSNIPAR 441
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
120-281 1.11e-03

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: 41.97  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402888    120 REELLLLQSTAEQLRQTALQQEARIRADQDTIRELTGKLGRCESGLPRGLQ--GAGPRRDTMADGPWDSPAL-ILELEDA 196
Cdd:TIGR02168  781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERriAATERRLEDLEEQIEELSEdIESLAAE 860
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402888    197 VRALRDRIDRLEQELPARVNLSAApapvsaVPTGLHSKMDQLEgQLLAQVLALEKERVALSHSSRRQRQEVEK---ELDV 273
Cdd:TIGR02168  861 IEELEELIEELESELEALLNERAS------LEEALALLRSELE-ELSEELRELESKRSELRRELEELREKLAQlelRLEG 933

                   ....*...
gi 17402888    274 LQGRVAEL 281
Cdd:TIGR02168  934 LEVRIDNL 941
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
117-282 7.76e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 7.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402888  117 PGEREELL-LLQSTAEQLRQTALQQEARIRADQDTIRELTGKL--GRC-ESGLPrgLQGAgPRRDTMADGPWDSPALILE 192
Cdd:PRK02224 407 LGNAEDFLeELREERDELREREAELEATLRTARERVEEAEALLeaGKCpECGQP--VEGS-PHVETIEEDRERVEELEAE 483
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402888  193 LEDA---VRALRDRIDRLEQ--ELPARV-----NLSAAPAPVSAVPTGLHSKMDQLEgQLLAQVLALEKERVALSHSSRR 262
Cdd:PRK02224 484 LEDLeeeVEEVEERLERAEDlvEAEDRIerleeRREDLEELIAERRETIEEKRERAE-ELRERAAELEAEAEEKREAAAE 562
                        170       180
                 ....*....|....*....|...
gi 17402888  263 QRQEVEK---ELDVLQGRVAELE 282
Cdd:PRK02224 563 AEEEAEEareEVAELNSKLAELK 585
 
Name Accession Description Interval E-value
PTX smart00159
Pentraxin / C-reactive protein / pentaxin family; This family form a doscoid pentameric ...
288-494 3.28e-92

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: 279.15  E-value: 3.28e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402888    288 YSPPDAFKISIPIRNNYMYARVRKALP-ELYAFTACMWLRSRSSgTGQGTPFSYSVPGQANEIVLLEAGHEPMELLINDK 366
Cdd:smart00159   1 QTDLTGKVFVFPKESDTSYVKLKPELPkPLQAFTVCLWFYSDLS-PRGYSLFSYATKGQDNELLLYKEKQGEYSLYIGGK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402888    367 VAQLPLSLKDNGWHHICIAWTTRDGLWSAYQDGELqGSGENLAAWHPIKPHGILILGQEQDTLGGRFDATQAFVGDIAQF 446
Cdd:smart00159  80 KVQFPVPESDGKWHHICTTWESSSGIAELWVDGKP-GVRKGLAKGYTVKPGGSIILGQEQDSYGGGFDATQSFVGEIGDL 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 17402888    447 NLWDHALTPAQVLGIANCTAPLLGNVLPWEDKLVEAFGGATKAAFDVC 494
Cdd:smart00159 159 NMWDSVLSPEEIKSVYKGSTFSIGNILNWRALNYEVHGGVVIKPQEWC 206
PTX cd00152
Pentraxins are plasma proteins characterized by their pentameric discoid assembly and their ...
292-488 1.57e-86

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: 264.52  E-value: 1.57e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402888 292 DAFKISIPIRNNYMYARVRKALP-ELYAFTACMWLRSrSSGTGQGTPFSYSVPGQANEIVLLEAGHEPMELLINDKVAQL 370
Cdd:cd00152   5 SGKVFVFPKESDTSYVKLKPELPkPLQAFTLCLWVYT-DLSTREYSLFSYATKGQDNELLLYKEKDGGYSLYIGGKEVTF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402888 371 PLSLKDNGWHHICIAWTTRDGLWSAYQDGELQGSGEnLAAWHPIKPHGILILGQEQDTLGGRFDATQAFVGDIAQFNLWD 450
Cdd:cd00152  84 KVPESDGAWHHICVTWESTSGIAELWVNGKLSVRKS-LKKGYTVGPGGSIILGQEQDSYGGGFDATQSFVGEISDVNMWD 162
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 17402888 451 HALTPAQVLGIANCTAPLLGNVLPWEDKLVEAFGGATK 488
Cdd:cd00152 163 SVLSPEEIKNVYSEGGTLSGNILNWRALNYEINGGVVI 200
Pentaxin pfam00354
Pentaxin family; Pentaxins are also known as pentraxins.
316-487 2.95e-27

Pentaxin family; Pentaxins are also known as pentraxins.


Pssm-ID: 278768  Cd Length: 194  Bit Score: 108.28  E-value: 2.95e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402888   316 LYAFTACMWLRSRSSGTGqgTPFSYSVPGQANEIVLLEagHEPMELLINdkVAQLPLSLKDN----GWHHICIAWTTRDG 391
Cdd:pfam00354  24 LQNFTLCLRFYTDLSRSY--SLFSYATKKQDNELLIFK--EKDGEYSFY--VGGAEVLFKVSeipvAPVHICTSWESSSG 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402888   392 LWSAYQDGELQGSgENLAAWHPIKPHGILILGQEQDTLGGRFDATQAFVGDIAQFNLWDHALTPAQVLGIANCtAPLLGN 471
Cdd:pfam00354  98 IAEFWVDGKPWVR-KSLKKGYTVGAPPSIILGQEQDSYGGGFDASQSLVGEIGDLNMWDYVLTPEEINTVYKG-GPFSPN 175
                         170
                  ....*....|....*.
gi 17402888   472 VLPWEDKLVEAFGGAT 487
Cdd:pfam00354 176 ILDWRALNYEARGYVV 191
Laminin_G_3 pfam13385
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ...
318-458 1.20e-14

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: 71.26  E-value: 1.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402888   318 AFTACMWLRSRSSGTGQGTpfsYSVPGQANEIVLLEAGHEPMELLIND-----KVAQLPLSLKDNGWHHIciAWTTRDGL 392
Cdd:pfam13385  18 DFTVSAWVKPDSLPGWARA---IISSSGGGGYSLGLDGDGRLRFAVNGgnggwDTVTSGASVPLGQWTHV--AVTYDGGT 92
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17402888   393 WSAYQDGELQGSGENLAAWhPIKPHGILilgqeqdTLGGRFDATQAFVGDIAQFNLWDHALTPAQV 458
Cdd:pfam13385  93 LRLYVNGVLVGSSTLTGGP-PPGTGGPL-------YIGRSPGGDDYFNGLIDEVRIYDRALSAAEI 150
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
120-291 6.83e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 6.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402888  120 REELLLLQSTAEQLRQTALQQEARIRADQDTIRELTGKLGRCEsglpRGLQGAGPRRdtmadgpwdspalILELEDAVRA 199
Cdd:COG4913  287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELE----AQIRGNGGDR-------------LEQLEREIER 349
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402888  200 LRDRIDRLEQELpARVN--LSAAPAPVSAVPTGLHSKMDQLEgQLLAQVLALEKERVALSHSSRRQRQEVEKELDVLQGR 277
Cdd:COG4913  350 LERELEERERRR-ARLEalLAALGLPLPASAEEFAALRAEAA-ALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
                        170
                 ....*....|....
gi 17402888  278 VAELEHGSSAYSPP 291
Cdd:COG4913  428 IASLERRKSNIPAR 441
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
120-281 1.11e-03

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: 41.97  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402888    120 REELLLLQSTAEQLRQTALQQEARIRADQDTIRELTGKLGRCESGLPRGLQ--GAGPRRDTMADGPWDSPAL-ILELEDA 196
Cdd:TIGR02168  781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERriAATERRLEDLEEQIEELSEdIESLAAE 860
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402888    197 VRALRDRIDRLEQELPARVNLSAApapvsaVPTGLHSKMDQLEgQLLAQVLALEKERVALSHSSRRQRQEVEK---ELDV 273
Cdd:TIGR02168  861 IEELEELIEELESELEALLNERAS------LEEALALLRSELE-ELSEELRELESKRSELRRELEELREKLAQlelRLEG 933

                   ....*...
gi 17402888    274 LQGRVAEL 281
Cdd:TIGR02168  934 LEVRIDNL 941
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
119-282 5.00e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 5.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402888 119 EREELLLLQSTAEQLRQTALQQEARIRADQDTIRELTGKLGRCESGLPRGLQGAGPRRDTmadgpwdspalILELEDAVR 198
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER-----------LEELEEELA 326
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402888 199 ALRDRIDRLEQELPArvnlsaapapvsavptgLHSKMDQLEGQLLAQVLALEKERVALSHSSRRQRQEVEKELDVLQGRV 278
Cdd:COG1196 327 ELEEELEELEEELEE-----------------LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389

                ....
gi 17402888 279 AELE 282
Cdd:COG1196 390 EALR 393
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
117-282 7.76e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 7.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402888  117 PGEREELL-LLQSTAEQLRQTALQQEARIRADQDTIRELTGKL--GRC-ESGLPrgLQGAgPRRDTMADGPWDSPALILE 192
Cdd:PRK02224 407 LGNAEDFLeELREERDELREREAELEATLRTARERVEEAEALLeaGKCpECGQP--VEGS-PHVETIEEDRERVEELEAE 483
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402888  193 LEDA---VRALRDRIDRLEQ--ELPARV-----NLSAAPAPVSAVPTGLHSKMDQLEgQLLAQVLALEKERVALSHSSRR 262
Cdd:PRK02224 484 LEDLeeeVEEVEERLERAEDlvEAEDRIerleeRREDLEELIAERRETIEEKRERAE-ELRERAAELEAEAEEKREAAAE 562
                        170       180
                 ....*....|....*....|...
gi 17402888  263 QRQEVEK---ELDVLQGRVAELE 282
Cdd:PRK02224 563 AEEEAEEareEVAELNSKLAELK 585
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
192-283 9.80e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 9.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402888  192 ELEDAVRALRDRIDRLEQELPARVNLSAAPAPVSAVP------TGLHSKMDQLEGQLLA------QVLALEKERVALshs 259
Cdd:COG4913  621 ELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvASAEREIAELEAELERldassdDLAALEEQLEEL--- 697
                         90       100
                 ....*....|....*....|....
gi 17402888  260 sRRQRQEVEKELDVLQGRVAELEH 283
Cdd:COG4913  698 -EAELEELEEELDELKGEIGRLEK 720
 
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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