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Conserved domains on  [gi|61966763|ref|NP_001013680|]
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pentraxin-4 isoform 2 [Homo sapiens]

Protein Classification

pentraxin family protein( domain architecture ID 10066289)

pentraxin family protein is a LamG (Laminin G) domain-containing protein that may serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules; similar to jeltraxin and mucosal pentraxin

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTX cd00152
Pentraxins are plasma proteins characterized by their pentameric discoid assembly and their ...
265-462 5.11e-76

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: 236.78  E-value: 5.11e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61966763 265 GPTLVFPNASTRNVVFLSPGFVTALRALSFCSWVRTA-SGRLGTLLSYATEDNDNKLVLHGRDsllPGSIHFVIGDPAFR 343
Cdd:cd00152   6 GKVFVFPKESDTSYVKLKPELPKPLQAFTLCLWVYTDlSTREYSLFSYATKGQDNELLLYKEK---DGGYSLYIGGKEVT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61966763 344 ELPLQLllDGQWHHICVIWTSTQGRYWLHVDRRLVATGSrFREGYEIPPGGSLVLGQEQDSVGGGFDSSEAFVGSMSGLA 423
Cdd:cd00152  83 FKVPES--DGAWHHICVTWESTSGIAELWVNGKLSVRKS-LKKGYTVGPGGSIILGQEQDSYGGGFDATQSFVGEISDVN 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 61966763 424 IWDRALVPGEVANLAIGKEFPTGAIL--TLANAALAGGFVQ 462
Cdd:cd00152 160 MWDSVLSPEEIKNVYSEGGTLSGNILnwRALNYEINGGVVI 200
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
76-174 1.44e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61966763     76 EESQAVAQAVNRSQASVQGELAQLKAWVRKLQRRGRKVDTRLRALDLTLGERSQQRARerkaHKAQRDALQDSLARLEGL 155
Cdd:TIGR02168  270 EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE----LESKLDELAEELAELEEK 345
                           90
                   ....*....|....*....
gi 61966763    156 VHSQGARLAALEGRLPVAH 174
Cdd:TIGR02168  346 LEELKEELESLEAELEELE 364
 
Name Accession Description Interval E-value
PTX cd00152
Pentraxins are plasma proteins characterized by their pentameric discoid assembly and their ...
265-462 5.11e-76

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: 236.78  E-value: 5.11e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61966763 265 GPTLVFPNASTRNVVFLSPGFVTALRALSFCSWVRTA-SGRLGTLLSYATEDNDNKLVLHGRDsllPGSIHFVIGDPAFR 343
Cdd:cd00152   6 GKVFVFPKESDTSYVKLKPELPKPLQAFTLCLWVYTDlSTREYSLFSYATKGQDNELLLYKEK---DGGYSLYIGGKEVT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61966763 344 ELPLQLllDGQWHHICVIWTSTQGRYWLHVDRRLVATGSrFREGYEIPPGGSLVLGQEQDSVGGGFDSSEAFVGSMSGLA 423
Cdd:cd00152  83 FKVPES--DGAWHHICVTWESTSGIAELWVNGKLSVRKS-LKKGYTVGPGGSIILGQEQDSYGGGFDATQSFVGEISDVN 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 61966763 424 IWDRALVPGEVANLAIGKEFPTGAIL--TLANAALAGGFVQ 462
Cdd:cd00152 160 MWDSVLSPEEIKNVYSEGGTLSGNILnwRALNYEINGGVVI 200
PTX smart00159
Pentraxin / C-reactive protein / pentaxin family; This family form a doscoid pentameric ...
263-449 5.85e-43

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: 150.88  E-value: 5.85e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61966763    263 GVGPTLVFPNASTRNVVFLSPGFVTALRALSFCSWVRT-ASGRLGTLLSYATEDNDNKLVLHGRDsllPGSIHFVIGDPa 341
Cdd:smart00159   4 LTGKVFVFPKESDTSYVKLKPELPKPLQAFTVCLWFYSdLSPRGYSLFSYATKGQDNELLLYKEK---QGEYSLYIGGK- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61966763    342 frELPLQLLL-DGQWHHICVIWTSTQGRYWLHVD-RRLVATGSRfrEGYEIPPGGSLVLGQEQDSVGGGFDSSEAFVGSM 419
Cdd:smart00159  80 --KVQFPVPEsDGKWHHICTTWESSSGIAELWVDgKPGVRKGLA--KGYTVKPGGSIILGQEQDSYGGGFDATQSFVGEI 155
                          170       180       190
                   ....*....|....*....|....*....|
gi 61966763    420 SGLAIWDRALVPGEVANLAIGKEFPTGAIL 449
Cdd:smart00159 156 GDLNMWDSVLSPEEIKSVYKGSTFSIGNIL 185
Pentaxin pfam00354
Pentaxin family; Pentaxins are also known as pentraxins.
269-444 2.24e-27

Pentaxin family; Pentaxins are also known as pentraxins.


Pssm-ID: 278768  Cd Length: 194  Bit Score: 108.28  E-value: 2.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61966763   269 VFPNASTRNVVFLSPGFVTALRALSFCSWVRTASGRLGTLLSYATEDNDNKLVLHGRDsllPGSIHFVIG-DPA-FRELP 346
Cdd:pfam00354   4 VFPKESDTSYVSLIPELEKPLQNFTLCLRFYTDLSRSYSLFSYATKKQDNELLIFKEK---DGEYSFYVGgAEVlFKVSE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61966763   347 LQLlldgQWHHICVIWTSTQGRYWLHVD-RRLVATGSRfrEGYEIPPGGSLVLGQEQDSVGGGFDSSEAFVGSMSGLAIW 425
Cdd:pfam00354  81 IPV----APVHICTSWESSSGIAEFWVDgKPWVRKSLK--KGYTVGAPPSIILGQEQDSYGGGFDASQSLVGEIGDLNMW 154
                         170
                  ....*....|....*....
gi 61966763   426 DRALVPGEVANLAIGKEFP 444
Cdd:pfam00354 155 DYVLTPEEINTVYKGGPFS 173
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
76-174 1.44e-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: 41.20  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61966763     76 EESQAVAQAVNRSQASVQGELAQLKAWVRKLQRRGRKVDTRLRALDLTLGERSQQRARerkaHKAQRDALQDSLARLEGL 155
Cdd:TIGR02168  270 EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE----LESKLDELAEELAELEEK 345
                           90
                   ....*....|....*....
gi 61966763    156 VHSQGARLAALEGRLPVAH 174
Cdd:TIGR02168  346 LEELKEELESLEAELEELE 364
TolC COG1538
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
64-211 2.26e-03

Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441147 [Multi-domain]  Cd Length: 367  Bit Score: 40.02  E-value: 2.26e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61966763  64 SYNVDVRFRSLAEESQAVAQaVNRSQASVQGELAQLKAWVRK----LQRRGRKVDTRLRALDLTlgERSQQRARERKAH- 138
Cdd:COG1538  40 SQELDLGGKRRARIEAAKAQ-AEAAEADLRAARLDLAAEVAQayfdLLAAQEQLALAEENLALA--EELLELARARYEAg 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61966763 139 ----------KAQRDALQDSLARLEGLVHSQGARLAALEGRLPvahPGTAALGPALVPTPTQPEELGPTSLKLQRDRQEL 208
Cdd:COG1538 117 lasrldvlqaEAQLAQARAQLAQAEAQLAQARNALALLLGLPP---PAPLDLPDPLPPLPPLPPSLPGLPSEALERRPDL 193

                ...
gi 61966763 209 RAA 211
Cdd:COG1538 194 RAA 196
PRK12472 PRK12472
hypothetical protein; Provisional
75-166 8.17e-03

hypothetical protein; Provisional


Pssm-ID: 237110 [Multi-domain]  Cd Length: 508  Bit Score: 38.70  E-value: 8.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61966763   75 AEESQAVAQAVNRSQASVQGELAQLKAWVRKLQRRGRKVDTRLRALDLTLG----ERSQQRARERKAHKAQRDAlqDSLA 150
Cdd:PRK12472 199 AEDAARAADEAKTAAAAAAREAAPLKASLRKLERAKARADAELKRADKALAaaktDEAKARAEERQQKAAQQAA--EAAT 276
                         90
                 ....*....|....*.
gi 61966763  151 RLEGLVHSQGARLAAL 166
Cdd:PRK12472 277 QLDTAKADAEAKRAAA 292
 
Name Accession Description Interval E-value
PTX cd00152
Pentraxins are plasma proteins characterized by their pentameric discoid assembly and their ...
265-462 5.11e-76

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: 236.78  E-value: 5.11e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61966763 265 GPTLVFPNASTRNVVFLSPGFVTALRALSFCSWVRTA-SGRLGTLLSYATEDNDNKLVLHGRDsllPGSIHFVIGDPAFR 343
Cdd:cd00152   6 GKVFVFPKESDTSYVKLKPELPKPLQAFTLCLWVYTDlSTREYSLFSYATKGQDNELLLYKEK---DGGYSLYIGGKEVT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61966763 344 ELPLQLllDGQWHHICVIWTSTQGRYWLHVDRRLVATGSrFREGYEIPPGGSLVLGQEQDSVGGGFDSSEAFVGSMSGLA 423
Cdd:cd00152  83 FKVPES--DGAWHHICVTWESTSGIAELWVNGKLSVRKS-LKKGYTVGPGGSIILGQEQDSYGGGFDATQSFVGEISDVN 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 61966763 424 IWDRALVPGEVANLAIGKEFPTGAIL--TLANAALAGGFVQ 462
Cdd:cd00152 160 MWDSVLSPEEIKNVYSEGGTLSGNILnwRALNYEINGGVVI 200
PTX smart00159
Pentraxin / C-reactive protein / pentaxin family; This family form a doscoid pentameric ...
263-449 5.85e-43

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: 150.88  E-value: 5.85e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61966763    263 GVGPTLVFPNASTRNVVFLSPGFVTALRALSFCSWVRT-ASGRLGTLLSYATEDNDNKLVLHGRDsllPGSIHFVIGDPa 341
Cdd:smart00159   4 LTGKVFVFPKESDTSYVKLKPELPKPLQAFTVCLWFYSdLSPRGYSLFSYATKGQDNELLLYKEK---QGEYSLYIGGK- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61966763    342 frELPLQLLL-DGQWHHICVIWTSTQGRYWLHVD-RRLVATGSRfrEGYEIPPGGSLVLGQEQDSVGGGFDSSEAFVGSM 419
Cdd:smart00159  80 --KVQFPVPEsDGKWHHICTTWESSSGIAELWVDgKPGVRKGLA--KGYTVKPGGSIILGQEQDSYGGGFDATQSFVGEI 155
                          170       180       190
                   ....*....|....*....|....*....|
gi 61966763    420 SGLAIWDRALVPGEVANLAIGKEFPTGAIL 449
Cdd:smart00159 156 GDLNMWDSVLSPEEIKSVYKGSTFSIGNIL 185
Pentaxin pfam00354
Pentaxin family; Pentaxins are also known as pentraxins.
269-444 2.24e-27

Pentaxin family; Pentaxins are also known as pentraxins.


Pssm-ID: 278768  Cd Length: 194  Bit Score: 108.28  E-value: 2.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61966763   269 VFPNASTRNVVFLSPGFVTALRALSFCSWVRTASGRLGTLLSYATEDNDNKLVLHGRDsllPGSIHFVIG-DPA-FRELP 346
Cdd:pfam00354   4 VFPKESDTSYVSLIPELEKPLQNFTLCLRFYTDLSRSYSLFSYATKKQDNELLIFKEK---DGEYSFYVGgAEVlFKVSE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61966763   347 LQLlldgQWHHICVIWTSTQGRYWLHVD-RRLVATGSRfrEGYEIPPGGSLVLGQEQDSVGGGFDSSEAFVGSMSGLAIW 425
Cdd:pfam00354  81 IPV----APVHICTSWESSSGIAEFWVDgKPWVRKSLK--KGYTVGAPPSIILGQEQDSYGGGFDASQSLVGEIGDLNMW 154
                         170
                  ....*....|....*....
gi 61966763   426 DRALVPGEVANLAIGKEFP 444
Cdd:pfam00354 155 DYVLTPEEINTVYKGGPFS 173
Laminin_G_3 pfam13385
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ...
283-435 7.26e-12

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: 63.17  E-value: 7.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61966763   283 PGFVTALRALSFCSWVRTASGRLGTLLsYATEDNDNKLVLHGRDSllpGSIHFVIGDPAFRELPLQL---LLDGQWHHIC 359
Cdd:pfam13385  10 PDALLPTSDFTVSAWVKPDSLPGWARA-IISSSGGGGYSLGLDGD---GRLRFAVNGGNGGWDTVTSgasVPLGQWTHVA 85
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 61966763   360 VIWTSTQGRywLHVDRRLVATGSRFregYEIPPGGSLVLgqeqdSVGGGFDSSEAFVGSMSGLAIWDRALVPGEVA 435
Cdd:pfam13385  86 VTYDGGTLR--LYVNGVLVGSSTLT---GGPPPGTGGPL-----YIGRSPGGDDYFNGLIDEVRIYDRALSAAEIA 151
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
292-425 1.72e-08

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: 53.58  E-value: 1.72e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61966763 292 LSFcsWVRTASGRlGTLLSYATEDNDNKLVLHGRDsllpGSIHFVIGDPAFREL--PLQLLLDGQWHHICVIWTSTQGRy 369
Cdd:cd00110  24 ISF--SFRTTSPN-GLLLYAGSQNGGDFLALELED----GRLVLRYDLGSGSLVlsSKTPLNDGQWHSVSVERNGRSVT- 95
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 61966763 370 wLHVDRRLVATGSRFREGYEIPPGGSLVLGQEQDSVGGGFD-SSEAFVGSMSGLAIW 425
Cdd:cd00110  96 -LSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLpVSPGFVGCIRDLKVN 151
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
298-422 1.88e-04

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 41.25  E-value: 1.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61966763   298 VRTASGRlGTLLsYATEDNDNKLVLhgrdSLLPGSIHFVI----GDPAFRELPlQLLLDGQWHHICVIWTSTQGRywLHV 373
Cdd:pfam02210   1 FRTRQPN-GLLL-YAGGGGSDFLAL----ELVNGRLVLRYdlgsGPESLLSSG-KNLNDGQWHSVRVERNGNTLT--LSV 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 61966763   374 DRRLVATGSRFREGYEIPPGGSLVLG-QEQDSVGGGFDSSEAFVGSMSGL 422
Cdd:pfam02210  72 DGQTVVSSLPPGESLLLNLNGPLYLGgLPPLLLLPALPVRAGFVGCIRDV 121
LamG smart00282
Laminin G domain;
292-427 3.25e-04

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 40.79  E-value: 3.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61966763    292 LSFcsWVRTASGRlGTLLSYATEDNDNKLVLHGRDsllpGSIHFVI---GDPAFRELPLQLLLDGQWHHICVIWTSTQGR 368
Cdd:smart00282   2 ISF--SFRTTSPN-GLLLYAGSKGGGDYLALELRD----GRLVLRYdlgSGPARLTSDPTPLNDGQWHRVAVERNGRSVT 74
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 61966763    369 ywLHVDRRLVATGSRFREGYEIPPGGSLVLG-----QEQDSVGggfdSSEAFVGSMSGLAIWDR 427
Cdd:smart00282  75 --LSVDGGNRVSGESPGGLTILNLDGPLYLGglpedLKLPPLP----VTPGFRGCIRNLKVNGK 132
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
76-174 1.44e-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: 41.20  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61966763     76 EESQAVAQAVNRSQASVQGELAQLKAWVRKLQRRGRKVDTRLRALDLTLGERSQQRARerkaHKAQRDALQDSLARLEGL 155
Cdd:TIGR02168  270 EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE----LESKLDELAEELAELEEK 345
                           90
                   ....*....|....*....
gi 61966763    156 VHSQGARLAALEGRLPVAH 174
Cdd:TIGR02168  346 LEELKEELESLEAELEELE 364
TolC COG1538
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
64-211 2.26e-03

Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441147 [Multi-domain]  Cd Length: 367  Bit Score: 40.02  E-value: 2.26e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61966763  64 SYNVDVRFRSLAEESQAVAQaVNRSQASVQGELAQLKAWVRK----LQRRGRKVDTRLRALDLTlgERSQQRARERKAH- 138
Cdd:COG1538  40 SQELDLGGKRRARIEAAKAQ-AEAAEADLRAARLDLAAEVAQayfdLLAAQEQLALAEENLALA--EELLELARARYEAg 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61966763 139 ----------KAQRDALQDSLARLEGLVHSQGARLAALEGRLPvahPGTAALGPALVPTPTQPEELGPTSLKLQRDRQEL 208
Cdd:COG1538 117 lasrldvlqaEAQLAQARAQLAQAEAQLAQARNALALLLGLPP---PAPLDLPDPLPPLPPLPPSLPGLPSEALERRPDL 193

                ...
gi 61966763 209 RAA 211
Cdd:COG1538 194 RAA 196
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
79-170 2.57e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 2.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61966763   79 QAVAQAVNRSQASVQGELAQLKAWVRKLQRRGRKVDTRLRALDLTLGERSQQRARERKAHKAQRDALQDSLARLEGLVHS 158
Cdd:COG4913  330 AQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAE 409
                         90
                 ....*....|..
gi 61966763  159 QGARLAALEGRL 170
Cdd:COG4913  410 AEAALRDLRREL 421
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
66-171 4.47e-03

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: 39.67  E-value: 4.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61966763     66 NVDVRFRSLAEESQAVA---QAVNRSQASVQGELAQLKAWVRKLQRRGRKVDTRLRALDLTLGERSQ---QRARERKAHK 139
Cdd:TIGR02169  326 KLEAEIDKLLAEIEELEreiEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREkleKLKREINELK 405
                           90       100       110
                   ....*....|....*....|....*....|..
gi 61966763    140 AQRDALQDSLARLEGLVHSQGARLAALEGRLP 171
Cdd:TIGR02169  406 RELDRLQEELQRLSEELADLNAAIAGIEAKIN 437
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
71-178 5.28e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.98  E-value: 5.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61966763  71 FRSLAEESQAVAQAVNRSQASVQGELAQLKAWVRKLQRRGRKVDTRLRALDLTLGERSQQRAR---ERKAHKAQRDALQD 147
Cdd:COG4942 141 LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARlekELAELAAELAELQQ 220
                        90       100       110
                ....*....|....*....|....*....|.
gi 61966763 148 SLARLEGLVHSQGARLAALEGRLPVAHPGTA 178
Cdd:COG4942 221 EAEELEALIARLEAEAAAAAERTPAAGFAAL 251
PRK12472 PRK12472
hypothetical protein; Provisional
75-166 8.17e-03

hypothetical protein; Provisional


Pssm-ID: 237110 [Multi-domain]  Cd Length: 508  Bit Score: 38.70  E-value: 8.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61966763   75 AEESQAVAQAVNRSQASVQGELAQLKAWVRKLQRRGRKVDTRLRALDLTLG----ERSQQRARERKAHKAQRDAlqDSLA 150
Cdd:PRK12472 199 AEDAARAADEAKTAAAAAAREAAPLKASLRKLERAKARADAELKRADKALAaaktDEAKARAEERQQKAAQQAA--EAAT 276
                         90
                 ....*....|....*.
gi 61966763  151 RLEGLVHSQGARLAAL 166
Cdd:PRK12472 277 QLDTAKADAEAKRAAA 292
 
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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