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Conserved domains on  [gi|1958670243|ref|XP_038945889|]
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IQ domain-containing protein E isoform X17 [Rattus norvegicus]

Protein Classification

IQ calmodulin-binding motif-containing protein( domain architecture ID 10635649)

IQ calmodulin-binding motif-containing protein

Gene Ontology:  GO:0005516
PubMed:  9141499

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cast super family cl37807
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 141-484 1.50e-07

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


The actual alignment was detected with superfamily member pfam10174:

Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 54.83  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 141 REKEDMYDEIIELKKSLHMQKSDVDlmrTKLRRLEEENSRKDRQIEQLLDPGRGPDfvRTLAEKKPDTGWVITGLKQRIF 220
Cdd:pfam10174 411 RDKDKQLAGLKERVKSLQTDSSNTD---TALTTLEEALSEKERIIERLKEQRERED--RERLEELESLKKENKDLKEKVS 485

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 221 RLEQQCKEKDSTINKLQTDM---------KTTNLEEMRIAMETYYEEIHRLQTLLasseatgkKPILEKKMGVKRQKKMS 291
Cdd:pfam10174 486 ALQPELTEKESSLIDLKEHAsslassglkKDSKLKSLEIAVEQKKEECSKLENQL--------KKAHNAEEAVRTNPEIN 557

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 292 SALLNLTRSVQELTEENQSLKEDLDRMLSNSPTVSKIKGYVDwskprllRRIAELEKKVSSSESPKNSASELVKPNPVVP 371
Cdd:pfam10174 558 DRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKD-------KKIAELESLTLRQMKEQNKKVANIKHGQQEM 630

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 372 SPSNISvqkQLKGDQSKEDQPKVDPSEDQ-EHLQGTVKTLREELSALQEQLLgkdlEMKQMLQSK--------IDLEKEL 442
Cdd:pfam10174 631 KKKGAQ---LLEEARRREDNLADNSQQLQlEELMGALEKTRQELDATKARLS----STQQSLAEKdghltnlrAERRKQL 703

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 443 ETAREGEKE------------------SQEREQALREEVEALTKKCQELEEAKRQETQER 484
Cdd:pfam10174 704 EEILEMKQEallaaisekdaniallelSSSKKKKTQEEVMALKREKDRLVHQLKQQTQNR 763
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 563-584 1.88e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


:

Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 36.15  E-value: 1.88e-03
                           10        20
                   ....*....|....*....|..
gi 1958670243  563 EVSQAATVLQAAFRGHLARSKL 584
Cdd:smart00015   1 RLTRAAIIIQAAWRGYLARKRY 22
 
Name Accession Description Interval E-value
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 141-484 1.50e-07

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 54.83  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 141 REKEDMYDEIIELKKSLHMQKSDVDlmrTKLRRLEEENSRKDRQIEQLLDPGRGPDfvRTLAEKKPDTGWVITGLKQRIF 220
Cdd:pfam10174 411 RDKDKQLAGLKERVKSLQTDSSNTD---TALTTLEEALSEKERIIERLKEQRERED--RERLEELESLKKENKDLKEKVS 485

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 221 RLEQQCKEKDSTINKLQTDM---------KTTNLEEMRIAMETYYEEIHRLQTLLasseatgkKPILEKKMGVKRQKKMS 291
Cdd:pfam10174 486 ALQPELTEKESSLIDLKEHAsslassglkKDSKLKSLEIAVEQKKEECSKLENQL--------KKAHNAEEAVRTNPEIN 557

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 292 SALLNLTRSVQELTEENQSLKEDLDRMLSNSPTVSKIKGYVDwskprllRRIAELEKKVSSSESPKNSASELVKPNPVVP 371
Cdd:pfam10174 558 DRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKD-------KKIAELESLTLRQMKEQNKKVANIKHGQQEM 630

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 372 SPSNISvqkQLKGDQSKEDQPKVDPSEDQ-EHLQGTVKTLREELSALQEQLLgkdlEMKQMLQSK--------IDLEKEL 442
Cdd:pfam10174 631 KKKGAQ---LLEEARRREDNLADNSQQLQlEELMGALEKTRQELDATKARLS----STQQSLAEKdghltnlrAERRKQL 703

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 443 ETAREGEKE------------------SQEREQALREEVEALTKKCQELEEAKRQETQER 484
Cdd:pfam10174 704 EEILEMKQEallaaisekdaniallelSSSKKKKTQEEVMALKREKDRLVHQLKQQTQNR 763
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 215-486 5.21e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 5.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 215 LKQRIFRLEQQCKEKDSTINKLQTDM--KTTNLEEMRIAMETYYEEIHRLQTLLASSEATGKKPILEKKMGVKRQKKMSS 292
Cdd:COG1196   237 LEAELEELEAELEELEAELEELEAELaeLEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 293 ALLNLTRSVQELTEENQSLKEDLDRMLSnsptvskikgyvdwSKPRLLRRIAELEKKVSSSESPKNSASELVKpnpvvps 372
Cdd:COG1196   317 RLEELEEELAELEEELEELEEELEELEE--------------ELEEAEEELEEAEAELAEAEEALLEAEAELA------- 375

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 373 pSNISVQKQLKGDQSKEDQPKVDPSEDQEHLQGTVKTLREELSALQEQLLGKDLEMKQMLQSKIDLEKELETAREGEKES 452
Cdd:COG1196   376 -EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1958670243 453 QEREQALREEVEALTKKCQELEEAKRQETQERQD 486
Cdd:COG1196   455 EEEEEALLELLAELLEEAALLEAALAELLEELAE 488
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 194-502 2.32e-06

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: 51.21  E-value: 2.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243  194 GPDFVRTLAEKKPDTGwvITGLKQRIFRLEQQCKEKDSTINKLQTdmkttNLEEMRIAMETYYEEIHRLQTLLASSEATG 273
Cdd:TIGR02168  656 RPGGVITGGSAKTNSS--ILERRREIEELEEKIEELEEKIAELEK-----ALAELRKELEELEEELEQLRKELEELSRQI 728

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243  274 KKPILEKKMGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNSPTVSKIKGYVDWSKPRLLRRIAELEKKVSSS 353
Cdd:TIGR02168  729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243  354 ESPKNSASELV--KPNPVVPSPSNISVQKQLKGDQSKEdqpKVDPSEDQEHLQGTVKTLREELSALQEQLLGKDLEMKQM 431
Cdd:TIGR02168  809 RAELTLLNEEAanLRERLESLERRIAATERRLEDLEEQ---IEELSEDIESLAAEIEELEELIEELESELEALLNERASL 885

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958670243  432 LQSKIDLEKELETAREGEKESQEREQALREEVEALTKKCQELE------EAKRQETQERQDSFIAMTHEAHPEVHAP 502
Cdd:TIGR02168  886 EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLElrleglEVRIDNLQERLSEEYSLTLEEAEALENK 962
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
215-476 1.85e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 215 LKQRIFRLEQQCKEKDSTINKL-----QTDMKTTNLEEMRIAMETYYEEIHRLQTLLASSEatGKKPILEKKMG--VKRQ 287
Cdd:PRK03918  191 IEELIKEKEKELEEVLREINEIsselpELREELEKLEKEVKELEELKEEIEELEKELESLE--GSKRKLEEKIRelEERI 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 288 KKMSSALLNLTRSVQELTE------ENQSLKEDLDRMLSNSPTVSKIKGyvdwskpRLLRRIAELEKKVSSSESPKNSAS 361
Cdd:PRK03918  269 EELKKEIEELEEKVKELKElkekaeEYIKLSEFYEEYLDELREIEKRLS-------RLEEEINGIEERIKELEEKEERLE 341

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 362 ELVKpnpvvpspsnisvqkqlkgdQSKEDQPKVDPSEDQEHLQGTVKTLREELSALQEQLLGKDLEmkqmlqskiDLEKE 441
Cdd:PRK03918  342 ELKK--------------------KLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPE---------KLEKE 392

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1958670243 442 LETAREGEKESQEREQALREEVEALTKKCQELEEA 476
Cdd:PRK03918  393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKA 427
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 563-584 1.88e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 36.15  E-value: 1.88e-03
                           10        20
                   ....*....|....*....|..
gi 1958670243  563 EVSQAATVLQAAFRGHLARSKL 584
Cdd:smart00015   1 RLTRAAIIIQAAWRGYLARKRY 22
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
 566-584 5.82e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 34.60  E-value: 5.82e-03
                          10
                  ....*....|....*....
gi 1958670243 566 QAATVLQAAFRGHLARSKL 584
Cdd:pfam00612   2 KAAIKIQAAWRGYLARKRY 20
 
Name Accession Description Interval E-value
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 141-484 1.50e-07

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 54.83  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 141 REKEDMYDEIIELKKSLHMQKSDVDlmrTKLRRLEEENSRKDRQIEQLLDPGRGPDfvRTLAEKKPDTGWVITGLKQRIF 220
Cdd:pfam10174 411 RDKDKQLAGLKERVKSLQTDSSNTD---TALTTLEEALSEKERIIERLKEQRERED--RERLEELESLKKENKDLKEKVS 485

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 221 RLEQQCKEKDSTINKLQTDM---------KTTNLEEMRIAMETYYEEIHRLQTLLasseatgkKPILEKKMGVKRQKKMS 291
Cdd:pfam10174 486 ALQPELTEKESSLIDLKEHAsslassglkKDSKLKSLEIAVEQKKEECSKLENQL--------KKAHNAEEAVRTNPEIN 557

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 292 SALLNLTRSVQELTEENQSLKEDLDRMLSNSPTVSKIKGYVDwskprllRRIAELEKKVSSSESPKNSASELVKPNPVVP 371
Cdd:pfam10174 558 DRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKD-------KKIAELESLTLRQMKEQNKKVANIKHGQQEM 630

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 372 SPSNISvqkQLKGDQSKEDQPKVDPSEDQ-EHLQGTVKTLREELSALQEQLLgkdlEMKQMLQSK--------IDLEKEL 442
Cdd:pfam10174 631 KKKGAQ---LLEEARRREDNLADNSQQLQlEELMGALEKTRQELDATKARLS----STQQSLAEKdghltnlrAERRKQL 703

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 443 ETAREGEKE------------------SQEREQALREEVEALTKKCQELEEAKRQETQER 484
Cdd:pfam10174 704 EEILEMKQEallaaisekdaniallelSSSKKKKTQEEVMALKREKDRLVHQLKQQTQNR 763
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 215-486 5.21e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 5.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 215 LKQRIFRLEQQCKEKDSTINKLQTDM--KTTNLEEMRIAMETYYEEIHRLQTLLASSEATGKKPILEKKMGVKRQKKMSS 292
Cdd:COG1196   237 LEAELEELEAELEELEAELEELEAELaeLEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 293 ALLNLTRSVQELTEENQSLKEDLDRMLSnsptvskikgyvdwSKPRLLRRIAELEKKVSSSESPKNSASELVKpnpvvps 372
Cdd:COG1196   317 RLEELEEELAELEEELEELEEELEELEE--------------ELEEAEEELEEAEAELAEAEEALLEAEAELA------- 375

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 373 pSNISVQKQLKGDQSKEDQPKVDPSEDQEHLQGTVKTLREELSALQEQLLGKDLEMKQMLQSKIDLEKELETAREGEKES 452
Cdd:COG1196   376 -EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1958670243 453 QEREQALREEVEALTKKCQELEEAKRQETQERQD 486
Cdd:COG1196   455 EEEEEALLELLAELLEEAALLEAALAELLEELAE 488
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 194-502 2.32e-06

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: 51.21  E-value: 2.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243  194 GPDFVRTLAEKKPDTGwvITGLKQRIFRLEQQCKEKDSTINKLQTdmkttNLEEMRIAMETYYEEIHRLQTLLASSEATG 273
Cdd:TIGR02168  656 RPGGVITGGSAKTNSS--ILERRREIEELEEKIEELEEKIAELEK-----ALAELRKELEELEEELEQLRKELEELSRQI 728

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243  274 KKPILEKKMGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNSPTVSKIKGYVDWSKPRLLRRIAELEKKVSSS 353
Cdd:TIGR02168  729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243  354 ESPKNSASELV--KPNPVVPSPSNISVQKQLKGDQSKEdqpKVDPSEDQEHLQGTVKTLREELSALQEQLLGKDLEMKQM 431
Cdd:TIGR02168  809 RAELTLLNEEAanLRERLESLERRIAATERRLEDLEEQ---IEELSEDIESLAAEIEELEELIEELESELEALLNERASL 885

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958670243  432 LQSKIDLEKELETAREGEKESQEREQALREEVEALTKKCQELE------EAKRQETQERQDSFIAMTHEAHPEVHAP 502
Cdd:TIGR02168  886 EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLElrleglEVRIDNLQERLSEEYSLTLEEAEALENK 962
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 134-490 2.97e-05

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: 47.37  E-value: 2.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243  134 VSGTSVY-REKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEEN---------SRKDRQIEQLLDPGRgpdfVRTLAE 203
Cdd:TIGR02169  162 IAGVAEFdRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRERekaeryqalLKEKREYEGYELLKE----KEALER 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243  204 KKPDTGWVITGLKQRIFRLEQQCKEKDSTINKLQTDMKTTNLEEMRIAMETYY---EEIHRLQTLLASSEATGKKPILEK 280
Cdd:TIGR02169  238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLrvkEKIGELEAEIASLERSIAEKEREL 317

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243  281 KMGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDrmlsnsptvsKIKGYVDWSKPR---LLRRIAELEKKvsSSESPK 357
Cdd:TIGR02169  318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRD----------KLTEEYAELKEEledLRAELEEVDKE--FAETRD 385

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243  358 NSASELVKPNPVvpspsnISVQKQLKGDQSKEDQPKVDPSEDQEHLQGTVKTLREELSALQEQLLGKDLEMKQmlqskid 437
Cdd:TIGR02169  386 ELKDYREKLEKL------KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKK------- 452

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958670243  438 LEKELETAREGEKESQEREQALREEVEALTKKCQELE------EAKRQETQERQDSFIA 490
Cdd:TIGR02169  453 QEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQrelaeaEAQARASEERVRGGRA 511
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 138-485 6.00e-05

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 46.65  E-value: 6.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243  138 SVYREKEDMY-DEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDPGRGPDFVRTLAEKKPDTGW-VITGL 215
Cdd:pfam15921  331 SELREAKRMYeDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWdRDTGN 410

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243  216 KQRIFRLEQQCKEKDSTINKLQTDMKTT------NLEEMRIAMETYYEEIHRLQTLLASSEATgkKPILEKKMGVKRQKK 289
Cdd:pfam15921  411 SITIDHLRRELDDRNMEVQRLEALLKAMksecqgQMERQMAAIQGKNESLEKVSSLTAQLEST--KEMLRKVVEELTAKK 488

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243  290 MSsaLLNLTRSVQELTeenQSLKEDLDRMLSNSPTVSKIKGYVDWskprllrRIAELEKKVSSSESPKNSASE------- 362
Cdd:pfam15921  489 MT--LESSERTVSDLT---ASLQEKERAIEATNAEITKLRSRVDL-------KLQELQHLKNEGDHLRNVQTEcealklq 556

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243  363 LVKPNPVVPS-PSNISVQKQLKGDQSKEDQPKvdpSEDQEHLQGTVKTLREELSALQEQLLGKDLEMKQMLQSKIDLEKE 441
Cdd:pfam15921  557 MAEKDKVIEIlRQQIENMTQLVGQHGRTAGAM---QVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELE 633

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958670243  442 --------LETAREGEKESQEREQAL------REEVEALTKKCQELEEAKRQETQERQ 485
Cdd:pfam15921  634 kvklvnagSERLRAVKDIKQERDQLLnevktsRNELNSLSEDYEVLKRNFRNKSEEME 691
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 398-498 6.77e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 6.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 398 EDQEHLQGTVKTLREELSALQEQLLGKDLEMKQMLQSKIDLEKELETAregEKESQEREQALREEVEALTKKCQELEEAK 477
Cdd:COG1196   309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA---EAELAEAEEALLEAEAELAEAEEELEELA 385

                          90       100
                  ....*....|....*....|.
gi 1958670243 478 RQETQERQDSFIAMTHEAHPE 498
Cdd:COG1196   386 EELLEALRAAAELAAQLEELE 406
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 397-488 8.03e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 8.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 397 SEDQEHLQGTVKTLREELSALQEQLLGKDLEMKQMLQSKIDLEKELETAREGEKESQEREQALREEVEALTKKcQELEEA 476
Cdd:COG1196   294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA-LLEAEA 372

                          90
                  ....*....|..
gi 1958670243 477 KRQETQERQDSF 488
Cdd:COG1196   373 ELAEAEEELEEL 384
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 147-479 1.26e-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: 45.43  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243  147 YDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDpgrgpdFVRTLAEKKPDTGWVITGLKQRIFRLEQQC 226
Cdd:TIGR02168  231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL------EVSELEEEIEELQKELYALANEISRLEQQK 304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243  227 KEKDSTINKLQTDMKTTN--LEEMRIAMETYYEEIHRLQTLLASSEAtgkkpilEKKMGVKRQKKMSSALLNLTRSVQEL 304
Cdd:TIGR02168  305 QILRERLANLERQLEELEaqLEELESKLDELAEELAELEEKLEELKE-------ELESLEAELEELEAELEELESRLEEL 377

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243  305 TEENQSLKEDLDRmlsnsptvskikgyvdwskprLLRRIAELEKKVSSSESPKNSASElvkpnpvvpspsniSVQKQlkg 384
Cdd:TIGR02168  378 EEQLETLRSKVAQ---------------------LELQIASLNNEIERLEARLERLED--------------RRERL--- 419

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243  385 DQSKEDQPKVDPSEDQEHLQGTVKTLREELSALQEQLlgkdlemkqmlqskIDLEKELETAREGEKESQEREQALREEVE 464
Cdd:TIGR02168  420 QQEIEELLKKLEEAELKELQAELEELEEELEELQEEL--------------ERLEEALEELREELEEAEQALDAAERELA 485

                          330
                   ....*....|....*
gi 1958670243  465 ALTKKCQELEEAKRQ 479
Cdd:TIGR02168  486 QLQARLDSLERLQEN 500
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 141-486 2.35e-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: 2.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243  141 REKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDpgrgpDFVRTLAEkkpdtgwvITGLKQRIF 220
Cdd:TIGR02168  684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRK-----DLARLEAE--------VEQLEERIA 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243  221 RLEQQCKEKDSTINKLQTDmkttnLEEMRIAMETYYEEIHRLQTLLASSEAtgkkpilekkmgvkRQKKMSSALLNLTRS 300
Cdd:TIGR02168  751 QLSKELTELEAEIEELEER-----LEEAEEELAEAEAEIEELEAQIEQLKE--------------ELKALREALDELRAE 811

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243  301 VQELTEENQSLKEDLDRMLSNSPTVSKIKGYVDWSKPRLLRRIAELEKKVSSSESPKNSASELVKpnpvvpSPSNISVQK 380
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE------ALLNERASL 885

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243  381 QLKGDQSKEDQPKVdpSEDQEHLQGTVKTLREELSALQEQL--LGKDLE-MKQMLQSKID-----LEKELETAREGEKES 452
Cdd:TIGR02168  886 EEALALLRSELEEL--SEELRELESKRSELRRELEELREKLaqLELRLEgLEVRIDNLQErlseeYSLTLEEAEALENKI 963

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1958670243  453 QEREQALREEVEALTKKCQEL--------EEAkrQETQERQD 486
Cdd:TIGR02168  964 EDDEEEARRRLKRLENKIKELgpvnlaaiEEY--EELKERYD 1003
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 217-495 3.01e-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: 44.28  E-value: 3.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243  217 QRIFRLEQQCKEKDSTINKLQTDMKTTNLEEMRIAMETYYEEIHRLQTLLASSEAtgKKPILEKKMGVKRQKKMS--SAL 294
Cdd:TIGR02168  213 ERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEE--KLEELRLEVSELEEEIEElqKEL 290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243  295 LNLTRSVQELTEENQSLKEDLDRmlsnsptvskikgyVDWSKPRLLRRIAELEKKvsssespKNSASElvkpnpvvpsps 374
Cdd:TIGR02168  291 YALANEISRLEQQKQILRERLAN--------------LERQLEELEAQLEELESK-------LDELAE------------ 337

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243  375 nisvQKQLKGDQSKEDQPKVDP-SEDQEHLQGTVKTLREELSALQEQLLGKDLEMKQMLQSKIDLEKELETAREGEKESQ 453
Cdd:TIGR02168  338 ----ELAELEEKLEELKEELESlEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE 413

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1958670243  454 EREQALREEVEALTKKcqeLEEAKRQETQERQDSFIAMTHEA 495
Cdd:TIGR02168  414 DRRERLQQEIEELLKK---LEEAELKELQAELEELEEELEEL 452
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 116-488 4.42e-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: 43.51  E-value: 4.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243  116 EAVRAKRADLRRSSSHGHVSGTSVYREKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDPGRGP 195
Cdd:TIGR02168  694 AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243  196 DFVRTLAEKKpdtgwvITGLKQRIFRLEQQCKEKDSTINKLQTDMKTTNleemriametyyEEIHRLQTLLASSEATGKK 275
Cdd:TIGR02168  774 EEELAEAEAE------IEELEAQIEQLKEELKALREALDELRAELTLLN------------EEAANLRERLESLERRIAA 835

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243  276 PILEKKMGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRmlsnsptVSKIKGYVDWSKPRLLRRIAELEKKVSSSES 355
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA-------LLNERASLEEALALLRSELEELSEELRELES 908

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243  356 pknsaselvkpnpvvpspsnisVQKQLKGDQSKEDQPKVDPSEDQEHLQGTVKTLREELSALQEQLLGKDLEMKQMLQSK 435
Cdd:TIGR02168  909 ----------------------KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDD 966

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958670243  436 --------IDLEKELE-------TAREGEKESQEREQALREEVEALTKKCQELEEAKRQ---ETQER-QDSF 488
Cdd:TIGR02168  967 eeearrrlKRLENKIKelgpvnlAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEidrEARERfKDTF 1038
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 408-486 8.24e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 8.24e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958670243 408 KTLREELSALQEQLLGKDLEMKQMLQSKIDLEKELETAREGEKESQEREQALREEVEALTKKCQELEEAKRQETQERQD 486
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 296-494 8.28e-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: 42.85  E-value: 8.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243  296 NLTRSVQELTEENQSLKEDLDrmlsnspTVSKIKGYVDWSKPRLLRRIAELEKKVSSSESPKNSASE-LVKPNPVVPSPS 374
Cdd:pfam01576  374 NLEKAKQALESENAELQAELR-------TLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEkLSKLQSELESVS 446

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243  375 NISVQKQLKGDQSKEDQPKVDPS--EDQEHLQ----------GTVKTLREELSALQEQL---------LGKDLEM--KQM 431
Cdd:pfam01576  447 SLLNEAEGKNIKLSKDVSSLESQlqDTQELLQeetrqklnlsTRLRQLEDERNSLQEQLeeeeeakrnVERQLSTlqAQL 526

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958670243  432 LQSKIDLEKE---LETAREGEKESQEREQALREEVEALTKKCQELEEAKRQETQERQDSFIAMTHE 494
Cdd:pfam01576  527 SDMKKKLEEDagtLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQ 592
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
398-484 9.04e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 9.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 398 EDQEHLQGTVKTLREELSALQEQL-LGKDLEMKQMLQSKIDLEKELETAREGEKESQEREQALREEVEALTKKCQELEEA 476
Cdd:COG4717   163 EELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242


                  ....*...
gi 1958670243 477 KRQETQER 484
Cdd:COG4717   243 ERLKEARL 250
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 212-485 1.08e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.31  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 212 ITGLKQRIFRLEQQCKEKDSTINKLQTDMKTTNLEEmriamETYYEEIHRLQTLLASSEATGKKPILEKKMGVKRQKKMS 291
Cdd:TIGR04523  77 IKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEI-----KNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKE 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 292 SALLNLTRSVQELTEENQSLKEDLDRMLSNSPTVSKIKGYVDWSKPRLLRRIAELEKKVSSSESPKNSASELVKPNpvvp 371
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQN---- 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 372 spSNISVQKQLKGDQSKEDQPKVDPSEDQehlqgtVKTLREELSALQEQLLGKDLEMKQMLQSKIDLEKELETAR-EGEK 450
Cdd:TIGR04523 228 --NQLKDNIEKKQQEINEKTTEISNTQTQ------LNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKsEISD 299

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1958670243 451 ESQEREQALREEV-EALTKKCQELEEAKRQETQERQ 485
Cdd:TIGR04523 300 LNNQKEQDWNKELkSELKNQEKKLEEIQNQISQNNK 335
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 142-485 1.64e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 41.48  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 142 EKEDMYDEIIELKKSLhmQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDpgrgpdfvrTLAE--KKPDTGWVITGLKQRI 219
Cdd:COG5185   250 QTSDKLEKLVEQNTDL--RLEKLGENAESSKRLNENANNLIKQFENTKE---------KIAEytKSIDIKKATESLEEQL 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 220 FRLEqqcKEKDSTINKLQTDMKTTNLEemriametyyEEIHRLQTLLASSEATGKKPILEKKMGV---KRQKKMSSALLN 296
Cdd:COG5185   319 AAAE---AEQELEESKRETETGIQNLT----------AEIEQGQESLTENLEAIKEEIENIVGEVelsKSSEELDSFKDT 385

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 297 LTRSVQELTEENQSLKEDLDRMLSnspTVSKIKGYVDWSKPRLLRRIAELEKKVS-SSESPKNSASELVKPNPVVPSPSN 375
Cdd:COG5185   386 IESTKESLDEIPQNQRGYAQEILA---TLEDTLKAADRQIEELQRQIEQATSSNEeVSKLLNELISELNKVMREADEESQ 462

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 376 ISVQKQLKGDQSKEDQPKVDPSEDQEHLQGTVKTLREELsalqEQLLGKDLEMKQMLQSKIDLEKELETAREGEkESQER 455
Cdd:COG5185   463 SRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATL----EKLRAKLERQLEGVRSKLDQVAESLKDFMRA-RGYAH 537

                         330       340       350
                  ....*....|....*....|....*....|
gi 1958670243 456 EQALREEVEALTKKCQELEEAKRQETQERQ 485
Cdd:COG5185   538 ILALENLIPASELIQASNAKTDGQAANLRT 567
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
215-476 1.85e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 215 LKQRIFRLEQQCKEKDSTINKL-----QTDMKTTNLEEMRIAMETYYEEIHRLQTLLASSEatGKKPILEKKMG--VKRQ 287
Cdd:PRK03918  191 IEELIKEKEKELEEVLREINEIsselpELREELEKLEKEVKELEELKEEIEELEKELESLE--GSKRKLEEKIRelEERI 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 288 KKMSSALLNLTRSVQELTE------ENQSLKEDLDRMLSNSPTVSKIKGyvdwskpRLLRRIAELEKKVSSSESPKNSAS 361
Cdd:PRK03918  269 EELKKEIEELEEKVKELKElkekaeEYIKLSEFYEEYLDELREIEKRLS-------RLEEEINGIEERIKELEEKEERLE 341

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 362 ELVKpnpvvpspsnisvqkqlkgdQSKEDQPKVDPSEDQEHLQGTVKTLREELSALQEQLLGKDLEmkqmlqskiDLEKE 441
Cdd:PRK03918  342 ELKK--------------------KLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPE---------KLEKE 392

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1958670243 442 LETAREGEKESQEREQALREEVEALTKKCQELEEA 476
Cdd:PRK03918  393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKA 427
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 563-584 1.88e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 36.15  E-value: 1.88e-03
                           10        20
                   ....*....|....*....|..
gi 1958670243  563 EVSQAATVLQAAFRGHLARSKL 584
Cdd:smart00015   1 RLTRAAIIIQAAWRGYLARKRY 22
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
398-486 2.12e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 2.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 398 EDQEHLQGTVKTLREELSALQEQLLGKDLEMKQMLQSKIDLEKELETAREGEKESQEREQALREEVEALTKKCQELEEAK 477
Cdd:COG4372    45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124


                  ....*....
gi 1958670243 478 RQETQERQD 486
Cdd:COG4372   125 QDLEQQRKQ 133
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 398-487 2.25e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 398 EDQEHLQGTVKTLREELSALQEQLLGKDLEMKQMLQSKIDLEKELETAREGEKESQEREQALREEVEALTKKCQELEEAK 477
Cdd:COG1196   274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353

                          90
                  ....*....|
gi 1958670243 478 RQETQERQDS 487
Cdd:COG1196   354 EEAEAELAEA 363
Leu_zip pfam15294
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ...
 291-444 2.41e-03

Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).


Pssm-ID: 464620 [Multi-domain]  Cd Length: 276  Bit Score: 40.46  E-value: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 291 SSALLNLtrSVQELTEENQSLKEDLdRMLSnsptvSKIKGYVDwSKPRLLRRIAELEKKVSSSESPKNSASELVKpnpvv 370
Cdd:pfam15294 127 GSALLHM--EIERLKEENEKLKERL-KTLE-----SQATQALD-EKSKLEKALKDLQKEQGAKKDVKSNLKEISD----- 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 371 pspsnisVQKQLKGDQSKEDQPKVDPSEDQEHLQGTVKTLREELSALQEQL--LGKDLE-----------MKQMLQSKID 437
Cdd:pfam15294 193 -------LEEKMAALKSDLEKTLNASTALQKSLEEDLASTKHELLKVQEQLemAEKELEkkfqqtaayrnMKEMLTKKNE 265


                  ....*..
gi 1958670243 438 LEKELET 444
Cdd:pfam15294 266 QIKELRK 272
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
407-581 3.78e-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: 3.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243  407 VKTLREELSALQEQLlgkdlemKQMLQSKIDLEkELETAREgekESQEREQALREEVEALTKKCQELEEaKRQETQERQD 486
Cdd:COG4913    663 VASAEREIAELEAEL-------ERLDASSDDLA-ALEEQLE---ELEAELEELEEELDELKGEIGRLEK-ELEQAEEELD 730

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243  487 SFIAMTHEAhpevhapspcsrhsepdsdnnadnnagEDGGSQPPALCSEERREAAI-----RTLQAQWKAHrckkRKAAL 561
Cdd:COG4913    731 ELQDRLEAA---------------------------EDLARLELRALLEERFAAALgdaveRELRENLEER----IDALR 779

                          170       180
                   ....*....|....*....|
gi 1958670243  562 DEVSQAATVLQAAFRGHLAR 581
Cdd:COG4913    780 ARLNRAEEELERAMRAFNRE 799
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
406-479 3.79e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.39  E-value: 3.79e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958670243 406 TVKTLREELSALQEQLLgkdlemKQMLQSKIDLEKELETAREGEKESQEREQALREEVEALTKKCQELEEAKRQ 479
Cdd:COG3206   292 DVIALRAQIAALRAQLQ------QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLERE 359
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
141-486 3.89e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 3.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 141 REKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDpgRGPDFVRTLAEKKPDTGWV---ITGLKQ 217
Cdd:PRK02224  272 REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELED--RDEELRDRLEECRVAAQAHneeAESLRE 349

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 218 RIFRLEQQCKEKDSTINKLQTDmkttnLEEMRIAMETYYEEIHRLQTLLASSEAtgkkpilekkmgvkrqkkmssALLNL 297
Cdd:PRK02224  350 DADDLEERAEELREEAAELESE-----LEEAREAVEDRREEIEELEEEIEELRE---------------------RFGDA 403

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 298 TRSVQELTEENQSLKEDLDRmlsnsptvskikgyvdwskprLLRRIAELEKKVSSSESPKNSASELVKPNpvvpspsnis 377
Cdd:PRK02224  404 PVDLGNAEDFLEELREERDE---------------------LREREAELEATLRTARERVEEAEALLEAG---------- 452

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 378 vqKQLKGDQSKEDQPKVDPSEDQ----EHLQGTVKTLREELSALQEQL-LGKDL-----EMKQMLQSKIDLEKELETARE 447
Cdd:PRK02224  453 --KCPECGQPVEGSPHVETIEEDrervEELEAELEDLEEEVEEVEERLeRAEDLveaedRIERLEERREDLEELIAERRE 530

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1958670243 448 GEKESQEREQALREEVEALTKKCQELEEAKRQETQERQD 486
Cdd:PRK02224  531 TIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEE 569
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
398-486 4.21e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 4.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 398 EDQEHLQGTVKTLREELSALQEQLLGKDLEMKQMLQSKIDLEKELETAREGEKESQEREQALREEVEALTKKCQELEEAK 477
Cdd:COG4372    59 EELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQI 138


                  ....*....
gi 1958670243 478 RQETQERQD 486
Cdd:COG4372   139 AELQSEIAE 147
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 398-486 5.30e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.14  E-value: 5.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 398 EDQEHLQGTVKTLREELSALQEQLL-GKDLEMKQMLQSKID-LEKELETAREGEKESQEREQALREEVEALTKKCQELEE 475
Cdd:COG1579    59 KEIKRLELEIEEVEARIKKYEEQLGnVRNNKEYEALQKEIEsLKRRISDLEDEILELMERIEELEEELAELEAELAELEA 138

                          90
                  ....*....|.
gi 1958670243 476 AKRQETQERQD 486
Cdd:COG1579   139 ELEEKKAELDE 149
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
 566-584 5.82e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 34.60  E-value: 5.82e-03
                          10
                  ....*....|....*....
gi 1958670243 566 QAATVLQAAFRGHLARSKL 584
Cdd:pfam00612   2 KAAIKIQAAWRGYLARKRY 20
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 278-480 7.42e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 39.57  E-value: 7.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243  278 LEKKMGVK-RQKKMSSALLNLTRSVQELTE------ENQSLKEDLDRMLSNSPTVSKIKGYVDWSKPRLLRRIAELEKKV 350
Cdd:pfam02463  175 LKKLIEETeNLAELIIDLEELKLQELKLKEqakkalEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIE 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243  351 SSSESPKNSASELVKpnpvvpSPSNISVQKQLKGDQSKEDqpkvDPSEDQEHLQGTVKTLREELSALQEQLLGKDLEMKQ 430
Cdd:pfam02463  255 SSKQEIEKEEEKLAQ------VLKENKEEEKEKKLQEEEL----KLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK 324

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958670243  431 MLQSKIDLEKELETAREGEKESQEREQALREEVEALTKKCQELEEAKRQE 480
Cdd:pfam02463  325 KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEE 374
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 141-475 9.01e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 39.23  E-value: 9.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 141 REKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDPgrgpdfVRTLAEKKPDTGWVITGLKQRIF 220
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNE------IEKLKKENQSYKQEIKNLESQIN 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 221 RLEQQCKEKDSTINKLQTDMKTTNLEEmriamETYYEEIHRLQTLLASSEATGKKpiLEKKMGVKRQKkmssallnltrs 300
Cdd:TIGR04523 395 DLESKIQNQEKLNQQKDEQIKKLQQEK-----ELLEKEIERLKETIIKNNSEIKD--LTNQDSVKELI------------ 455

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 301 VQELTEENQSLKEDLDrMLSNSptVSKIKGYVDWSKPRLLRRIAELEKKVSSSESPKNSASELVKPNPvvpspSNISVQK 380
Cdd:TIGR04523 456 IKNLDNTRESLETQLK-VLSRS--INKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIS-----SLKEKIE 527

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670243 381 QLKGDQSKEDQpKVDPSEDQehlqgtVKTLREEL--SALQEQLLGKDLEMKQMLQSKIDLEKELETAREGEKESQEREQA 458
Cdd:TIGR04523 528 KLESEKKEKES-KISDLEDE------LNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKD 600

                         330
                  ....*....|....*..
gi 1958670243 459 LREEVEALTKKCQELEE 475
Cdd:TIGR04523 601 LIKEIEEKEKKISSLEK 617
 
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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