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Conserved domains on  [gi|254540105|ref|NP_001156888|]
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pentraxin-4 isoform 2 precursor [Mus musculus]

Protein Classification

LamG domain-containing protein( domain architecture ID 366259)

LamG (Laminin G) domain-containing protein may serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LamG super family cl22861
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
241-438 6.27e-69

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.


The actual alignment was detected with superfamily member cd00152:

Pssm-ID: 473984  Cd Length: 201  Bit Score: 217.91  E-value: 6.27e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540105 241 PVLIFPNTSTENVIFLSPGFLMPLRALSFCSWVRMA-TSHLGTLLSYATKDNDNKLVLHGRNslvPGSIHFVIGDPDFRE 319
Cdd:cd00152    7 KVFVFPKESDTSYVKLKPELPKPLQAFTLCLWVYTDlSTREYSLFSYATKGQDNELLLYKEK---DGGYSLYIGGKEVTF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540105 320 LSlkPLLDGQWHHICIIWTSVEGKYWLHIDRRLVATGSrFREGYEIPPGGSLVLGQEQDTVGGEFDSSEAFVGSISGLAI 399
Cdd:cd00152   84 KV--PESDGAWHHICVTWESTSGIAELWVNGKLSVRKS-LKKGYTVGPGGSIILGQEQDSYGGGFDATQSFVGEISDVNM 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 254540105 400 WDRALLPREVANLASGKELPTGAIL--TLTNVTSVGGFVQR 438
Cdd:cd00152  161 WDSVLSPEEIKNVYSEGGTLSGNILnwRALNYEINGGVVIK 201
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
31-160 1.30e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.66  E-value: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540105    31 ARQRKPFFERLRRLEEQSLVEQSQAVALAMNQsQAAIQGDVAHL------------KTWYRKSQRRSQKVDARLQALDLS 98
Cdd:TIGR02168  363 LEAELEELESRLEELEEQLETLRSKVAQLELQ-IASLNNEIERLearlerledrreRLQQEIEELLKKLEEAELKELQAE 441
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254540105    99 LSTKSRQWVEKEGEQKAQREAIASLALSVQALQDALASLTQQVHSQGARLAALEGQTQRASS 160
Cdd:TIGR02168  442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
 
Name Accession Description Interval E-value
PTX cd00152
Pentraxins are plasma proteins characterized by their pentameric discoid assembly and their ...
241-438 6.27e-69

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: 217.91  E-value: 6.27e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540105 241 PVLIFPNTSTENVIFLSPGFLMPLRALSFCSWVRMA-TSHLGTLLSYATKDNDNKLVLHGRNslvPGSIHFVIGDPDFRE 319
Cdd:cd00152    7 KVFVFPKESDTSYVKLKPELPKPLQAFTLCLWVYTDlSTREYSLFSYATKGQDNELLLYKEK---DGGYSLYIGGKEVTF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540105 320 LSlkPLLDGQWHHICIIWTSVEGKYWLHIDRRLVATGSrFREGYEIPPGGSLVLGQEQDTVGGEFDSSEAFVGSISGLAI 399
Cdd:cd00152   84 KV--PESDGAWHHICVTWESTSGIAELWVNGKLSVRKS-LKKGYTVGPGGSIILGQEQDSYGGGFDATQSFVGEISDVNM 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 254540105 400 WDRALLPREVANLASGKELPTGAIL--TLTNVTSVGGFVQR 438
Cdd:cd00152  161 WDSVLSPEEIKNVYSEGGTLSGNILnwRALNYEINGGVVIK 201
PTX smart00159
Pentraxin / C-reactive protein / pentaxin family; This family form a doscoid pentameric ...
238-443 3.50e-42

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: 148.18  E-value: 3.50e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540105   238 NTDP---VLIFPNTSTENVIFLSPGFLMPLRALSFCSWVRM-ATSHLGTLLSYATKDNDNKLVLHGRNslvPGSIHFVIG 313
Cdd:smart00159   1 QTDLtgkVFVFPKESDTSYVKLKPELPKPLQAFTVCLWFYSdLSPRGYSLFSYATKGQDNELLLYKEK---QGEYSLYIG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540105   314 DPdfrELSLK-PLLDGQWHHICIIWTSVEGKYWLHID-RRLVATGSRfrEGYEIPPGGSLVLGQEQDTVGGEFDSSEAFV 391
Cdd:smart00159  78 GK---KVQFPvPESDGKWHHICTTWESSSGIAELWVDgKPGVRKGLA--KGYTVKPGGSIILGQEQDSYGGGFDATQSFV 152
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 254540105   392 GSISGLAIWDRALLPREVANLASGKELPTGAILT--LTNVTSVGGFVQRAKCTC 443
Cdd:smart00159 153 GEIGDLNMWDSVLSPEEIKSVYKGSTFSIGNILNwrALNYEVHGGVVIKPQEWC 206
Pentaxin pfam00354
Pentaxin family; Pentaxins are also known as pentraxins.
242-419 3.43e-27

Pentaxin family; Pentaxins are also known as pentraxins.


Pssm-ID: 278768  Cd Length: 194  Bit Score: 107.51  E-value: 3.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540105  242 VLIFPNTSTENVIFLSPGFLMPLRALSFCSWVRMATSHLGTLLSYATKDNDNKLVLHGRNslvPGSIHFVIG-DPDFREL 320
Cdd:pfam00354   2 VFVFPKESDTSYVSLIPELEKPLQNFTLCLRFYTDLSRSYSLFSYATKKQDNELLIFKEK---DGEYSFYVGgAEVLFKV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540105  321 SLKPLldgQWHHICIIWTSVEGKYWLHID-RRLVATGSRfrEGYEIPPGGSLVLGQEQDTVGGEFDSSEAFVGSISGLAI 399
Cdd:pfam00354  79 SEIPV---APVHICTSWESSSGIAEFWVDgKPWVRKSLK--KGYTVGAPPSIILGQEQDSYGGGFDASQSLVGEIGDLNM 153
                         170       180
                  ....*....|....*....|
gi 254540105  400 WDRALLPREVANLASGKELP 419
Cdd:pfam00354 154 WDYVLTPEEINTVYKGGPFS 173
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
31-160 1.30e-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: 44.66  E-value: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540105    31 ARQRKPFFERLRRLEEQSLVEQSQAVALAMNQsQAAIQGDVAHL------------KTWYRKSQRRSQKVDARLQALDLS 98
Cdd:TIGR02168  363 LEAELEELESRLEELEEQLETLRSKVAQLELQ-IASLNNEIERLearlerledrreRLQQEIEELLKKLEEAELKELQAE 441
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254540105    99 LSTKSRQWVEKEGEQKAQREAIASLALSVQALQDALASLTQQVHSQGARLAALEGQTQRASS 160
Cdd:TIGR02168  442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
28-199 2.80e-04

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 43.64  E-value: 2.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540105   28 AHPARQRKPFFERL-----------RRLEE-----QSLVEQSQAVALAMNQSQAAIQGDVAHLKTWYRKSQR----RSQK 87
Cdd:PRK10246  286 AQPARQLRPHWERIqeqsaalahtrQQIEEvntrlQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRfrqwNNEL 365
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540105   88 VDARLQALDLSlSTKS--RQWVEKEGEQKAQREAI--ASLALSVQALQDALASLTQQVHSQgARLAALEGQTQRASSGTV 163
Cdd:PRK10246  366 AGWRAQFSQQT-SDREqlRQWQQQLTHAEQKLNALpaITLTLTADEVAAALAQHAEQRPLR-QRLVALHGQIVPQQKRLA 443
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 254540105  164 ALGLTTAPNPTQLAQRgpgSLQLWRDRQVAKSSPQH 199
Cdd:PRK10246  444 QLQVAIQNVTQEQTQR---NAALNEMRQRYKEKTQQ 476
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
38-177 3.17e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 3.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540105   38 FERLRRLEEQSLVEQSQAVAL----AMNQSQAAIQGDVAHLKT-----WYRKSQRRSQKVDARLQALDLSLSTKSRQWVE 108
Cdd:COG4913   234 FDDLERAHEALEDAREQIELLepirELAERYAAARERLAELEYlraalRLWFAQRRLELLEAELEELRAELARLEAELER 313
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540105  109 KEGEQKAQREAIASLALSVQALQ-DALASLTQQVHSQGARLAALEGQTQRASSGTVALGLTTAPNPTQLA 177
Cdd:COG4913   314 LEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFA 383
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
23-152 8.84e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 41.70  E-value: 8.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540105    23 TPSQEAHPARQRKPFFERLRRLEEQslVEQSQAVALAMNQSQAAIQGDVAHLKTWYR-------KSQRRSQKVDARLQAL 95
Cdd:pfam01576  340 TRSHEAQLQEMRQKHTQALEELTEQ--LEQAKRNKANLEKAKQALESENAELQAELRtlqqakqDSEHKRKKLEGQLQEL 417
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254540105    96 DLSLSTKSRQWVE-------------------KEGEQKAQREA--IASLALSVQALQDALASLTQQVHSQGARLAALE 152
Cdd:pfam01576  418 QARLSESERQRAElaeklsklqselesvssllNEAEGKNIKLSkdVSSLESQLQDTQELLQEETRQKLNLSTRLRQLE 495
 
Name Accession Description Interval E-value
PTX cd00152
Pentraxins are plasma proteins characterized by their pentameric discoid assembly and their ...
241-438 6.27e-69

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: 217.91  E-value: 6.27e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540105 241 PVLIFPNTSTENVIFLSPGFLMPLRALSFCSWVRMA-TSHLGTLLSYATKDNDNKLVLHGRNslvPGSIHFVIGDPDFRE 319
Cdd:cd00152    7 KVFVFPKESDTSYVKLKPELPKPLQAFTLCLWVYTDlSTREYSLFSYATKGQDNELLLYKEK---DGGYSLYIGGKEVTF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540105 320 LSlkPLLDGQWHHICIIWTSVEGKYWLHIDRRLVATGSrFREGYEIPPGGSLVLGQEQDTVGGEFDSSEAFVGSISGLAI 399
Cdd:cd00152   84 KV--PESDGAWHHICVTWESTSGIAELWVNGKLSVRKS-LKKGYTVGPGGSIILGQEQDSYGGGFDATQSFVGEISDVNM 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 254540105 400 WDRALLPREVANLASGKELPTGAIL--TLTNVTSVGGFVQR 438
Cdd:cd00152  161 WDSVLSPEEIKNVYSEGGTLSGNILnwRALNYEINGGVVIK 201
PTX smart00159
Pentraxin / C-reactive protein / pentaxin family; This family form a doscoid pentameric ...
238-443 3.50e-42

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: 148.18  E-value: 3.50e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540105   238 NTDP---VLIFPNTSTENVIFLSPGFLMPLRALSFCSWVRM-ATSHLGTLLSYATKDNDNKLVLHGRNslvPGSIHFVIG 313
Cdd:smart00159   1 QTDLtgkVFVFPKESDTSYVKLKPELPKPLQAFTVCLWFYSdLSPRGYSLFSYATKGQDNELLLYKEK---QGEYSLYIG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540105   314 DPdfrELSLK-PLLDGQWHHICIIWTSVEGKYWLHID-RRLVATGSRfrEGYEIPPGGSLVLGQEQDTVGGEFDSSEAFV 391
Cdd:smart00159  78 GK---KVQFPvPESDGKWHHICTTWESSSGIAELWVDgKPGVRKGLA--KGYTVKPGGSIILGQEQDSYGGGFDATQSFV 152
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 254540105   392 GSISGLAIWDRALLPREVANLASGKELPTGAILT--LTNVTSVGGFVQRAKCTC 443
Cdd:smart00159 153 GEIGDLNMWDSVLSPEEIKSVYKGSTFSIGNILNwrALNYEVHGGVVIKPQEWC 206
Pentaxin pfam00354
Pentaxin family; Pentaxins are also known as pentraxins.
242-419 3.43e-27

Pentaxin family; Pentaxins are also known as pentraxins.


Pssm-ID: 278768  Cd Length: 194  Bit Score: 107.51  E-value: 3.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540105  242 VLIFPNTSTENVIFLSPGFLMPLRALSFCSWVRMATSHLGTLLSYATKDNDNKLVLHGRNslvPGSIHFVIG-DPDFREL 320
Cdd:pfam00354   2 VFVFPKESDTSYVSLIPELEKPLQNFTLCLRFYTDLSRSYSLFSYATKKQDNELLIFKEK---DGEYSFYVGgAEVLFKV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540105  321 SLKPLldgQWHHICIIWTSVEGKYWLHID-RRLVATGSRfrEGYEIPPGGSLVLGQEQDTVGGEFDSSEAFVGSISGLAI 399
Cdd:pfam00354  79 SEIPV---APVHICTSWESSSGIAEFWVDgKPWVRKSLK--KGYTVGAPPSIILGQEQDSYGGGFDASQSLVGEIGDLNM 153
                         170       180
                  ....*....|....*....|
gi 254540105  400 WDRALLPREVANLASGKELP 419
Cdd:pfam00354 154 WDYVLTPEEINTVYKGGPFS 173
Laminin_G_3 pfam13385
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ...
258-410 2.94e-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: 70.11  E-value: 2.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540105  258 PGFLMPLRALSFCSWVRM-ATSHLGTLLSYATKDNdnklvlhGRNSLVP--GSIHFVIGDPDFRE---LSLKPLLDGQWH 331
Cdd:pfam13385  10 PDALLPTSDFTVSAWVKPdSLPGWARAIISSSGGG-------GYSLGLDgdGRLRFAVNGGNGGWdtvTSGASVPLGQWT 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254540105  332 HICIIWTSVEGKywLHIDRRLVATGSRFregYEIPPGGSLVLgqeqdTVGGEFDSSEAFVGSISGLAIWDRALLPREVA 410
Cdd:pfam13385  83 HVAVTYDGGTLR--LYVNGVLVGSSTLT---GGPPPGTGGPL-----YIGRSPGGDDYFNGLIDEVRIYDRALSAAEIA 151
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
281-400 8.61e-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: 51.26  E-value: 8.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540105 281 GTLLSYATKDNDNKLVLHgrnsLVPGSIHFVIGDPDFR-ELSLKPLL-DGQWHHICIIWTSVEGKywLHIDRRLVATGSR 358
Cdd:cd00110   35 GLLLYAGSQNGGDFLALE----LEDGRLVLRYDLGSGSlVLSSKTPLnDGQWHSVSVERNGRSVT--LSVDGERVVESGS 108
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 254540105 359 FREGYEIPPGGSLVLGQEQDTVGGEFD-SSEAFVGSISGLAIW 400
Cdd:cd00110  109 PGGSALLNLDGPLYLGGLPEDLKSPGLpVSPGFVGCIRDLKVN 151
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
31-160 1.30e-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: 44.66  E-value: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540105    31 ARQRKPFFERLRRLEEQSLVEQSQAVALAMNQsQAAIQGDVAHL------------KTWYRKSQRRSQKVDARLQALDLS 98
Cdd:TIGR02168  363 LEAELEELESRLEELEEQLETLRSKVAQLELQ-IASLNNEIERLearlerledrreRLQQEIEELLKKLEEAELKELQAE 441
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254540105    99 LSTKSRQWVEKEGEQKAQREAIASLALSVQALQDALASLTQQVHSQGARLAALEGQTQRASS 160
Cdd:TIGR02168  442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
LamG smart00282
Laminin G domain;
277-402 2.75e-04

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 40.79  E-value: 2.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540105   277 TSHLGTLLSYATKDNDNKLVLHgrnsLVPGSIHFVI--GDPDFR-ELSLKPLLDGQWHHICIIWTsvEGKYWLHIDRRLV 353
Cdd:smart00282   9 TSPNGLLLYAGSKGGGDYLALE----LRDGRLVLRYdlGSGPARlTSDPTPLNDGQWHRVAVERN--GRSVTLSVDGGNR 82
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 254540105   354 ATGSRFREGYEIPPGGSLVLGQEQDTVGGEFD-SSEAFVGSISGLAIWDR 402
Cdd:smart00282  83 VSGESPGGLTILNLDGPLYLGGLPEDLKLPPLpVTPGFRGCIRNLKVNGK 132
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
28-199 2.80e-04

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 43.64  E-value: 2.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540105   28 AHPARQRKPFFERL-----------RRLEE-----QSLVEQSQAVALAMNQSQAAIQGDVAHLKTWYRKSQR----RSQK 87
Cdd:PRK10246  286 AQPARQLRPHWERIqeqsaalahtrQQIEEvntrlQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRfrqwNNEL 365
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540105   88 VDARLQALDLSlSTKS--RQWVEKEGEQKAQREAI--ASLALSVQALQDALASLTQQVHSQgARLAALEGQTQRASSGTV 163
Cdd:PRK10246  366 AGWRAQFSQQT-SDREqlRQWQQQLTHAEQKLNALpaITLTLTADEVAAALAQHAEQRPLR-QRLVALHGQIVPQQKRLA 443
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 254540105  164 ALGLTTAPNPTQLAQRgpgSLQLWRDRQVAKSSPQH 199
Cdd:PRK10246  444 QLQVAIQNVTQEQTQR---NAALNEMRQRYKEKTQQ 476
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
281-397 2.97e-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: 40.48  E-value: 2.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540105  281 GTLLsYATKDNDNKLVLhgrnSLVPGSIHFVI--GDPDFRELSL-KPLLDGQWHHICIIWTSVEGKywLHIDRRLVATGS 357
Cdd:pfam02210   8 GLLL-YAGGGGSDFLAL----ELVNGRLVLRYdlGSGPESLLSSgKNLNDGQWHSVRVERNGNTLT--LSVDGQTVVSSL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 254540105  358 RFREGYEIPPGGSLVLG--QEQDTVGGEfDSSEAFVGSISGL 397
Cdd:pfam02210  81 PPGESLLLNLNGPLYLGglPPLLLLPAL-PVRAGFVGCIRDV 121
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
38-177 3.17e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 3.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540105   38 FERLRRLEEQSLVEQSQAVAL----AMNQSQAAIQGDVAHLKT-----WYRKSQRRSQKVDARLQALDLSLSTKSRQWVE 108
Cdd:COG4913   234 FDDLERAHEALEDAREQIELLepirELAERYAAARERLAELEYlraalRLWFAQRRLELLEAELEELRAELARLEAELER 313
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540105  109 KEGEQKAQREAIASLALSVQALQ-DALASLTQQVHSQGARLAALEGQTQRASSGTVALGLTTAPNPTQLA 177
Cdd:COG4913   314 LEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFA 383
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
23-152 8.84e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 41.70  E-value: 8.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540105    23 TPSQEAHPARQRKPFFERLRRLEEQslVEQSQAVALAMNQSQAAIQGDVAHLKTWYR-------KSQRRSQKVDARLQAL 95
Cdd:pfam01576  340 TRSHEAQLQEMRQKHTQALEELTEQ--LEQAKRNKANLEKAKQALESENAELQAELRtlqqakqDSEHKRKKLEGQLQEL 417
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254540105    96 DLSLSTKSRQWVE-------------------KEGEQKAQREA--IASLALSVQALQDALASLTQQVHSQGARLAALE 152
Cdd:pfam01576  418 QARLSESERQRAElaeklsklqselesvssllNEAEGKNIKLSkdVSSLESQLQDTQELLQEETRQKLNLSTRLRQLE 495
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
40-159 1.68e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 1.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540105  40 RLRRLEEQSlveqSQAV-ALAMNQSQAAIQGDVAHLKtwYRKSQRRSQKVDARLQALDLSLSTKSRQWVEKEGEQKAQRE 118
Cdd:COG1196  201 QLEPLERQA----EKAErYRELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 254540105 119 AIASLALSVQALQDALASLTQQVHSQGARLAALEGQTQRAS 159
Cdd:COG1196  275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
39-160 2.32e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 2.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540105   39 ERLRRLEEQ--SLVEQSQAVALAMNQSQ----AAIQGDVAHLKTWYRKSQRRSQKVDARLQALDLSLSTKSRQWVEkege 112
Cdd:COG4913   309 AELERLEARldALREELDELEAQIRGNGgdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAA---- 384
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 254540105  113 qkaQREAIASLAlsvQALQDALASLTQQVHSQGARLAALEGQTQRASS 160
Cdd:COG4913   385 ---LRAEAAALL---EALEEELEALEEALAEAEAALRDLRRELRELEA 426
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
31-157 3.14e-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: 39.75  E-value: 3.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540105  31 ARQRKPFFERLRRLEEQSLVEQSQAVALAMNQSQAAIQGDVAHLKTWYRKSQRRSQKVD-ARLQALDLSLSTKSRQWVEK 109
Cdd:COG4942  100 EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADlAELAALRAELEAERAELEAL 179
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 254540105 110 EGEQKAQREAIASLalsVQALQDALASLTQQVHSQGARLAALEGQTQR 157
Cdd:COG4942  180 LAELEEERAALEAL---KAERQKLLARLEKELAELAAELAELQQEAEE 224
 
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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