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Conserved domains on  [gi|1958670239|ref|XP_038945888|]
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IQ domain-containing protein E isoform X10 [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 ...
 96-439 2.77e-08

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: 57.52  E-value: 2.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  96 REKEDMYDEIIELKKSLHMQKSDVDlmrTKLRRLEEENSRKDRQIEQLLDPGRGPDfvRTLAEKKPDTGWVITGLKQRIF 175
Cdd:pfam10174 411 RDKDKQLAGLKERVKSLQTDSSNTD---TALTTLEEALSEKERIIERLKEQRERED--RERLEELESLKKENKDLKEKVS 485

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 176 RLEQQCKEKDSTINKLQTDM---------KTTNLEEMRIAMETYYEEIHRLQTLLasseatgkKPILEKKMGVKRQKKMS 246
Cdd:pfam10174 486 ALQPELTEKESSLIDLKEHAsslassglkKDSKLKSLEIAVEQKKEECSKLENQL--------KKAHNAEEAVRTNPEIN 557

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 247 SALLNLTRSVQELTEENQSLKEDLDRMLSNSPTVSKIKGYVDwskprllRRIAELEKKVSSSESPKNSASELVKPNPVVP 326
Cdd:pfam10174 558 DRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKD-------KKIAELESLTLRQMKEQNKKVANIKHGQQEM 630

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 327 SPSNISvqkQLKGDQSKEDQPKVDPSEDQ-EHLQGTVKTLREELSALQEQLLgkdlEMKQMLQSK--------IDLEKEL 397
Cdd:pfam10174 631 KKKGAQ---LLEEARRREDNLADNSQQLQlEELMGALEKTRQELDATKARLS----STQQSLAEKdghltnlrAERRKQL 703

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 398 ETAREGEKE------------------SQEREQALREEVEALTKKCQELEEAKRQETQER 439
Cdd:pfam10174 704 EEILEMKQEallaaisekdaniallelSSSKKKKTQEEVMALKREKDRLVHQLKQQTQNR 763
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
362-533 1.35e-03

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


The actual alignment was detected with superfamily member COG4913:

Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  362 VKTLREELSALQEQLlgkdlemKQMLQSKIDLEkELETAREgekESQEREQALREEVEALTKKCQELEEaKRQETQERQD 441
Cdd:COG4913    663 VASAEREIAELEAEL-------ERLDASSDDLA-ALEEQLE---ELEAELEELEEELDELKGEIGRLEK-ELEQAEEELD 730

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  442 SFIAMTHEAhpevhapspcsrhsepdsdnnadnnagEDGGSQPPALCSEERREAAI-----RTLQAQWKAHRcKKRKAAL 516
Cdd:COG4913    731 ELQDRLEAA---------------------------EDLARLELRALLEERFAAALgdaveRELRENLEERI-DALRARL 782

                          170
                   ....*....|....*..
gi 1958670239  517 DEAATVLQAAFRGHLAR 533
Cdd:COG4913    783 NRAEEELERAMRAFNRE 799
 
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 ...
 96-439 2.77e-08

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: 57.52  E-value: 2.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  96 REKEDMYDEIIELKKSLHMQKSDVDlmrTKLRRLEEENSRKDRQIEQLLDPGRGPDfvRTLAEKKPDTGWVITGLKQRIF 175
Cdd:pfam10174 411 RDKDKQLAGLKERVKSLQTDSSNTD---TALTTLEEALSEKERIIERLKEQRERED--RERLEELESLKKENKDLKEKVS 485

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 176 RLEQQCKEKDSTINKLQTDM---------KTTNLEEMRIAMETYYEEIHRLQTLLasseatgkKPILEKKMGVKRQKKMS 246
Cdd:pfam10174 486 ALQPELTEKESSLIDLKEHAsslassglkKDSKLKSLEIAVEQKKEECSKLENQL--------KKAHNAEEAVRTNPEIN 557

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 247 SALLNLTRSVQELTEENQSLKEDLDRMLSNSPTVSKIKGYVDwskprllRRIAELEKKVSSSESPKNSASELVKPNPVVP 326
Cdd:pfam10174 558 DRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKD-------KKIAELESLTLRQMKEQNKKVANIKHGQQEM 630

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 327 SPSNISvqkQLKGDQSKEDQPKVDPSEDQ-EHLQGTVKTLREELSALQEQLLgkdlEMKQMLQSK--------IDLEKEL 397
Cdd:pfam10174 631 KKKGAQ---LLEEARRREDNLADNSQQLQlEELMGALEKTRQELDATKARLS----STQQSLAEKdghltnlrAERRKQL 703

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 398 ETAREGEKE------------------SQEREQALREEVEALTKKCQELEEAKRQETQER 439
Cdd:pfam10174 704 EEILEMKQEallaaisekdaniallelSSSKKKKTQEEVMALKREKDRLVHQLKQQTQNR 763
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 170-441 3.56e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 3.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 170 LKQRIFRLEQQCKEKDSTINKLQTDM--KTTNLEEMRIAMETYYEEIHRLQTLLASSEATGKKPILEKKMGVKRQKKMSS 247
Cdd:COG1196   237 LEAELEELEAELEELEAELEELEAELaeLEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 248 ALLNLTRSVQELTEENQSLKEDLDRMLSnsptvskikgyvdwSKPRLLRRIAELEKKVSSSESPKNSASELVKpnpvvps 327
Cdd:COG1196   317 RLEELEEELAELEEELEELEEELEELEE--------------ELEEAEEELEEAEAELAEAEEALLEAEAELA------- 375

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 328 pSNISVQKQLKGDQSKEDQPKVDPSEDQEHLQGTVKTLREELSALQEQLLGKDLEMKQMLQSKIDLEKELETAREGEKES 407
Cdd:COG1196   376 -EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1958670239 408 QEREQALREEVEALTKKCQELEEAKRQETQERQD 441
Cdd:COG1196   455 EEEEEALLELLAELLEEAALLEAALAELLEELAE 488
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 149-457 1.36e-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: 51.98  E-value: 1.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  149 GPDFVRTLAEKKPDTGwvITGLKQRIFRLEQQCKEKDSTINKLQTdmkttNLEEMRIAMETYYEEIHRLQTLLASSEATG 228
Cdd:TIGR02168  656 RPGGVITGGSAKTNSS--ILERRREIEELEEKIEELEEKIAELEK-----ALAELRKELEELEEELEQLRKELEELSRQI 728

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  229 KKPILEKKMGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNSPTVSKIKGYVDWSKPRLLRRIAELEKKVSSS 308
Cdd:TIGR02168  729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  309 ESPKNSASELV--KPNPVVPSPSNISVQKQLKGDQSKEdqpKVDPSEDQEHLQGTVKTLREELSALQEQLLGKDLEMKQM 386
Cdd:TIGR02168  809 RAELTLLNEEAanLRERLESLERRIAATERRLEDLEEQ---IEELSEDIESLAAEIEELEELIEELESELEALLNERASL 885

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958670239  387 LQSKIDLEKELETAREGEKESQEREQALREEVEALTKKCQELE------EAKRQETQERQDSFIAMTHEAHPEVHAP 457
Cdd:TIGR02168  886 EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLElrleglEVRIDNLQERLSEEYSLTLEEAEALENK 962
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
170-431 1.10e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 170 LKQRIFRLEQQCKEKDSTINKL-----QTDMKTTNLEEMRIAMETYYEEIHRLQTLLASSEatGKKPILEKKMG--VKRQ 242
Cdd:PRK03918  191 IEELIKEKEKELEEVLREINEIsselpELREELEKLEKEVKELEELKEEIEELEKELESLE--GSKRKLEEKIRelEERI 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 243 KKMSSALLNLTRSVQELTE------ENQSLKEDLDRMLSNSPTVSKIKGyvdwskpRLLRRIAELEKKVSSSESPKNSAS 316
Cdd:PRK03918  269 EELKKEIEELEEKVKELKElkekaeEYIKLSEFYEEYLDELREIEKRLS-------RLEEEINGIEERIKELEEKEERLE 341

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 317 ELVKpnpvvpspsnisvqkqlkgdQSKEDQPKVDPSEDQEHLQGTVKTLREELSALQEQLLGKDLEmkqmlqskiDLEKE 396
Cdd:PRK03918  342 ELKK--------------------KLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPE---------KLEKE 392

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1958670239 397 LETAREGEKESQEREQALREEVEALTKKCQELEEA 431
Cdd:PRK03918  393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKA 427
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
362-533 1.35e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  362 VKTLREELSALQEQLlgkdlemKQMLQSKIDLEkELETAREgekESQEREQALREEVEALTKKCQELEEaKRQETQERQD 441
Cdd:COG4913    663 VASAEREIAELEAEL-------ERLDASSDDLA-ALEEQLE---ELEAELEELEEELDELKGEIGRLEK-ELEQAEEELD 730

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  442 SFIAMTHEAhpevhapspcsrhsepdsdnnadnnagEDGGSQPPALCSEERREAAI-----RTLQAQWKAHRcKKRKAAL 516
Cdd:COG4913    731 ELQDRLEAA---------------------------EDLARLELRALLEERFAAALgdaveRELRENLEERI-DALRARL 782

                          170
                   ....*....|....*..
gi 1958670239  517 DEAATVLQAAFRGHLAR 533
Cdd:COG4913    783 NRAEEELERAMRAFNRE 799
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 516-536 2.82e-03

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 35.76  E-value: 2.82e-03
                           10        20
                   ....*....|....*....|.
gi 1958670239  516 LDEAATVLQAAFRGHLARSKL 536
Cdd:smart00015   2 LTRAAIIIQAAWRGYLARKRY 22
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
 518-536 5.39e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 34.99  E-value: 5.39e-03
                          10
                  ....*....|....*....
gi 1958670239 518 EAATVLQAAFRGHLARSKL 536
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 ...
 96-439 2.77e-08

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: 57.52  E-value: 2.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  96 REKEDMYDEIIELKKSLHMQKSDVDlmrTKLRRLEEENSRKDRQIEQLLDPGRGPDfvRTLAEKKPDTGWVITGLKQRIF 175
Cdd:pfam10174 411 RDKDKQLAGLKERVKSLQTDSSNTD---TALTTLEEALSEKERIIERLKEQRERED--RERLEELESLKKENKDLKEKVS 485

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 176 RLEQQCKEKDSTINKLQTDM---------KTTNLEEMRIAMETYYEEIHRLQTLLasseatgkKPILEKKMGVKRQKKMS 246
Cdd:pfam10174 486 ALQPELTEKESSLIDLKEHAsslassglkKDSKLKSLEIAVEQKKEECSKLENQL--------KKAHNAEEAVRTNPEIN 557

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 247 SALLNLTRSVQELTEENQSLKEDLDRMLSNSPTVSKIKGYVDwskprllRRIAELEKKVSSSESPKNSASELVKPNPVVP 326
Cdd:pfam10174 558 DRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKD-------KKIAELESLTLRQMKEQNKKVANIKHGQQEM 630

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 327 SPSNISvqkQLKGDQSKEDQPKVDPSEDQ-EHLQGTVKTLREELSALQEQLLgkdlEMKQMLQSK--------IDLEKEL 397
Cdd:pfam10174 631 KKKGAQ---LLEEARRREDNLADNSQQLQlEELMGALEKTRQELDATKARLS----STQQSLAEKdghltnlrAERRKQL 703

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 398 ETAREGEKE------------------SQEREQALREEVEALTKKCQELEEAKRQETQER 439
Cdd:pfam10174 704 EEILEMKQEallaaisekdaniallelSSSKKKKTQEEVMALKREKDRLVHQLKQQTQNR 763
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 170-441 3.56e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 3.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 170 LKQRIFRLEQQCKEKDSTINKLQTDM--KTTNLEEMRIAMETYYEEIHRLQTLLASSEATGKKPILEKKMGVKRQKKMSS 247
Cdd:COG1196   237 LEAELEELEAELEELEAELEELEAELaeLEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 248 ALLNLTRSVQELTEENQSLKEDLDRMLSnsptvskikgyvdwSKPRLLRRIAELEKKVSSSESPKNSASELVKpnpvvps 327
Cdd:COG1196   317 RLEELEEELAELEEELEELEEELEELEE--------------ELEEAEEELEEAEAELAEAEEALLEAEAELA------- 375

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 328 pSNISVQKQLKGDQSKEDQPKVDPSEDQEHLQGTVKTLREELSALQEQLLGKDLEMKQMLQSKIDLEKELETAREGEKES 407
Cdd:COG1196   376 -EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1958670239 408 QEREQALREEVEALTKKCQELEEAKRQETQERQD 441
Cdd:COG1196   455 EEEEEALLELLAELLEEAALLEAALAELLEELAE 488
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 149-457 1.36e-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: 51.98  E-value: 1.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  149 GPDFVRTLAEKKPDTGwvITGLKQRIFRLEQQCKEKDSTINKLQTdmkttNLEEMRIAMETYYEEIHRLQTLLASSEATG 228
Cdd:TIGR02168  656 RPGGVITGGSAKTNSS--ILERRREIEELEEKIEELEEKIAELEK-----ALAELRKELEELEEELEQLRKELEELSRQI 728

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  229 KKPILEKKMGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNSPTVSKIKGYVDWSKPRLLRRIAELEKKVSSS 308
Cdd:TIGR02168  729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  309 ESPKNSASELV--KPNPVVPSPSNISVQKQLKGDQSKEdqpKVDPSEDQEHLQGTVKTLREELSALQEQLLGKDLEMKQM 386
Cdd:TIGR02168  809 RAELTLLNEEAanLRERLESLERRIAATERRLEDLEEQ---IEELSEDIESLAAEIEELEELIEELESELEALLNERASL 885

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958670239  387 LQSKIDLEKELETAREGEKESQEREQALREEVEALTKKCQELE------EAKRQETQERQDSFIAMTHEAHPEVHAP 457
Cdd:TIGR02168  886 EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLElrleglEVRIDNLQERLSEEYSLTLEEAEALENK 962
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 89-445 1.72e-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: 48.53  E-value: 1.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239   89 VSGTSVY-REKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEEN---------SRKDRQIEQLLDPGRgpdfVRTLAE 158
Cdd:TIGR02169  162 IAGVAEFdRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRERekaeryqalLKEKREYEGYELLKE----KEALER 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  159 KKPDTGWVITGLKQRIFRLEQQCKEKDSTINKLQTDMKTTNLEEMRIAMETYY---EEIHRLQTLLASSEATGKKPILEK 235
Cdd:TIGR02169  238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLrvkEKIGELEAEIASLERSIAEKEREL 317

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  236 KMGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDrmlsnsptvsKIKGYVDWSKPR---LLRRIAELEKKvsSSESPK 312
Cdd:TIGR02169  318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRD----------KLTEEYAELKEEledLRAELEEVDKE--FAETRD 385

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  313 NSASELVKPNPVvpspsnISVQKQLKGDQSKEDQPKVDPSEDQEHLQGTVKTLREELSALQEQLLGKDLEMKQmlqskid 392
Cdd:TIGR02169  386 ELKDYREKLEKL------KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKK------- 452

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958670239  393 LEKELETAREGEKESQEREQALREEVEALTKKCQELE------EAKRQETQERQDSFIA 445
Cdd:TIGR02169  453 QEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQrelaeaEAQARASEERVRGGRA 511
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 93-440 1.90e-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: 48.19  E-value: 1.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239   93 SVYREKEDMY-DEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDPGRGPDFVRTLAEKKPDTGW-VITGL 170
Cdd:pfam15921  331 SELREAKRMYeDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWdRDTGN 410

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  171 KQRIFRLEQQCKEKDSTINKLQTDMKTT------NLEEMRIAMETYYEEIHRLQTLLASSEATgkKPILEKKMGVKRQKK 244
Cdd:pfam15921  411 SITIDHLRRELDDRNMEVQRLEALLKAMksecqgQMERQMAAIQGKNESLEKVSSLTAQLEST--KEMLRKVVEELTAKK 488

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  245 MSsaLLNLTRSVQELTeenQSLKEDLDRMLSNSPTVSKIKGYVDWskprllrRIAELEKKVSSSESPKNSASE------- 317
Cdd:pfam15921  489 MT--LESSERTVSDLT---ASLQEKERAIEATNAEITKLRSRVDL-------KLQELQHLKNEGDHLRNVQTEcealklq 556

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  318 LVKPNPVVPS-PSNISVQKQLKGDQSKEDQPKvdpSEDQEHLQGTVKTLREELSALQEQLLGKDLEMKQMLQSKIDLEKE 396
Cdd:pfam15921  557 MAEKDKVIEIlRQQIENMTQLVGQHGRTAGAM---QVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELE 633

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958670239  397 --------LETAREGEKESQEREQAL------REEVEALTKKCQELEEAKRQETQERQ 440
Cdd:pfam15921  634 kvklvnagSERLRAVKDIKQERDQLLnevktsRNELNSLSEDYEVLKRNFRNKSEEME 691
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 102-434 5.35e-05

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: 46.97  E-value: 5.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  102 YDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDpgrgpdFVRTLAEKKPDTGWVITGLKQRIFRLEQQC 181
Cdd:TIGR02168  231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL------EVSELEEEIEELQKELYALANEISRLEQQK 304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  182 KEKDSTINKLQTDMKTTN--LEEMRIAMETYYEEIHRLQTLLASSEAtgkkpilEKKMGVKRQKKMSSALLNLTRSVQEL 259
Cdd:TIGR02168  305 QILRERLANLERQLEELEaqLEELESKLDELAEELAELEEKLEELKE-------ELESLEAELEELEAELEELESRLEEL 377

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  260 TEENQSLKEDLDRmlsnsptvskikgyvdwskprLLRRIAELEKKVSSSESPKNSASElvkpnpvvpspsniSVQKQlkg 339
Cdd:TIGR02168  378 EEQLETLRSKVAQ---------------------LELQIASLNNEIERLEARLERLED--------------RRERL--- 419

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  340 DQSKEDQPKVDPSEDQEHLQGTVKTLREELSALQEQLlgkdlemkqmlqskIDLEKELETAREGEKESQEREQALREEVE 419
Cdd:TIGR02168  420 QQEIEELLKKLEEAELKELQAELEELEEELEELQEEL--------------ERLEEALEELREELEEAEQALDAAERELA 485

                          330
                   ....*....|....*
gi 1958670239  420 ALTKKCQELEEAKRQ 434
Cdd:TIGR02168  486 QLQARLDSLERLQEN 500
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 353-453 5.66e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 5.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 353 EDQEHLQGTVKTLREELSALQEQLLGKDLEMKQMLQSKIDLEKELETAregEKESQEREQALREEVEALTKKCQELEEAK 432
Cdd:COG1196   309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA---EAELAEAEEALLEAEAELAEAEEELEELA 385

                          90       100
                  ....*....|....*....|.
gi 1958670239 433 RQETQERQDSFIAMTHEAHPE 453
Cdd:COG1196   386 EELLEALRAAAELAAQLEELE 406
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 352-443 6.26e-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: 6.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 352 SEDQEHLQGTVKTLREELSALQEQLLGKDLEMKQMLQSKIDLEKELETAREGEKESQEREQALREEVEALTKKcQELEEA 431
Cdd:COG1196   294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA-LLEAEA 372

                          90
                  ....*....|..
gi 1958670239 432 KRQETQERQDSF 443
Cdd:COG1196   373 ELAEAEEELEEL 384
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 96-441 9.07e-05

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: 46.20  E-value: 9.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239   96 REKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQI-EQLLDPGRGPDFVRTLAEKkpdtgwvITGLKQRI 174
Cdd:TIGR02168  684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIsALRKDLARLEAEVEQLEER-------IAQLSKEL 756

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  175 FRLEQQCKEKDSTINKLQtdmktTNLEEMRIAMETYYEEIHRLQTLLASSEatgkkpilekkmgvkrqkkmsSALLNLTR 254
Cdd:TIGR02168  757 TELEAEIEELEERLEEAE-----EELAEAEAEIEELEAQIEQLKEELKALR---------------------EALDELRA 810

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  255 SVQELTEENQSLKEDLDRMLSNSPTVSKIKGYVDWSKPRLLRRIAELEKKVSSSESPKNSASELVKpnpvvpSPSNISVQ 334
Cdd:TIGR02168  811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE------ALLNERAS 884

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  335 KQLKGDQSKEDQPKVdpSEDQEHLQGTVKTLREELSALQEQL--LGKDLE-MKQMLQSKID-----LEKELETAREGEKE 406
Cdd:TIGR02168  885 LEEALALLRSELEEL--SEELRELESKRSELRRELEELREKLaqLELRLEgLEVRIDNLQErlseeYSLTLEEAEALENK 962

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 1958670239  407 SQEREQALREEVEALTKKCQEL--------EEAkrQETQERQD 441
Cdd:TIGR02168  963 IEDDEEEARRRLKRLENKIKELgpvnlaaiEEY--EELKERYD 1003
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 172-450 1.40e-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: 1.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  172 QRIFRLEQQCKEKDSTINKLQTDMKTTNLEEMRIAMETYYEEIHRLQTLLASSEAtgKKPILEKKMGVKRQKKMS--SAL 249
Cdd:TIGR02168  213 ERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEE--KLEELRLEVSELEEEIEElqKEL 290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  250 LNLTRSVQELTEENQSLKEDLDRmlsnsptvskikgyVDWSKPRLLRRIAELEKKvsssespKNSASElvkpnpvvpsps 329
Cdd:TIGR02168  291 YALANEISRLEQQKQILRERLAN--------------LERQLEELEAQLEELESK-------LDELAE------------ 337

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  330 nisvQKQLKGDQSKEDQPKVDP-SEDQEHLQGTVKTLREELSALQEQLLGKDLEMKQMLQSKIDLEKELETAREGEKESQ 408
Cdd:TIGR02168  338 ----ELAELEEKLEELKEELESlEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE 413

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1958670239  409 EREQALREEVEALTKKcqeLEEAKRQETQERQDSFIAMTHEA 450
Cdd:TIGR02168  414 DRRERLQQEIEELLKK---LEEAELKELQAELEELEEELEEL 452
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 167-440 1.58e-04

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: 45.40  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 167 ITGLKQRIFRLEQQCKEKDSTINKLQTDMKTTNLEEmriamETYYEEIHRLQTLLASSEATGKKPILEKKMGVKRQKKMS 246
Cdd:TIGR04523  77 IKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEI-----KNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKE 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 247 SALLNLTRSVQELTEENQSLKEDLDRMLSNsptVSKIKGYVDWSKPRLLR---RIAELEKKVSSSESPKNSASELVKPNp 323
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEELENELNLLEKE---KLNIQKNIDKIKNKLLKlelLLSNLKKKIQKNKSLESQISELKKQN- 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 324 vvpspSNISVQKQLKGDQSKEDQPKVDPSEDQehlqgtVKTLREELSALQEQLLGKDLEMKQMLQSKIDLEKELETAR-E 402
Cdd:TIGR04523 228 -----NQLKDNIEKKQQEINEKTTEISNTQTQ------LNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKsE 296

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1958670239 403 GEKESQEREQALREEV-EALTKKCQELEEAKRQETQERQ 440
Cdd:TIGR04523 297 ISDLNNQKEQDWNKELkSELKNQEKKLEEIQNQISQNNK 335
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 251-449 3.43e-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: 44.40  E-value: 3.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  251 NLTRSVQELTEENQSLKEDLDrmlsnspTVSKIKGYVDWSKPRLLRRIAELEKKVSSSESPKNSASE-LVKPNPVVPSPS 329
Cdd:pfam01576  374 NLEKAKQALESENAELQAELR-------TLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEkLSKLQSELESVS 446

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  330 NISVQKQLKGDQSKEDQPKVDPS--EDQEHLQ----------GTVKTLREELSALQEQL---------LGKDLEM--KQM 386
Cdd:pfam01576  447 SLLNEAEGKNIKLSKDVSSLESQlqDTQELLQeetrqklnlsTRLRQLEDERNSLQEQLeeeeeakrnVERQLSTlqAQL 526

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958670239  387 LQSKIDLEKE---LETAREGEKESQEREQALREEVEALTKKCQELEEAKRQETQERQDSFIAMTHE 449
Cdd:pfam01576  527 SDMKKKLEEDagtLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQ 592
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 97-440 4.39e-04

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: 43.79  E-value: 4.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  97 EKEDMYDEIIELKKSLhmQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDpgrgpdfvrTLAE--KKPDTGWVITGLKQRI 174
Cdd:COG5185   250 QTSDKLEKLVEQNTDL--RLEKLGENAESSKRLNENANNLIKQFENTKE---------KIAEytKSIDIKKATESLEEQL 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 175 FRLEqqcKEKDSTINKLQTDMKTTNLEemriametyyEEIHRLQTLLASSEATGKKPILEKKMGV---KRQKKMSSALLN 251
Cdd:COG5185   319 AAAE---AEQELEESKRETETGIQNLT----------AEIEQGQESLTENLEAIKEEIENIVGEVelsKSSEELDSFKDT 385

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 252 LTRSVQELTEENQSLKEDLDRMLSnspTVSKIKGYVDWSKPRLLRRIAELEKKVS-SSESPKNSASELVKPNPVVPSPSN 330
Cdd:COG5185   386 IESTKESLDEIPQNQRGYAQEILA---TLEDTLKAADRQIEELQRQIEQATSSNEeVSKLLNELISELNKVMREADEESQ 462

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 331 ISVQKQLKGDQSKEDQPKVDPSEDQEHLQGTVKTLREELsalqEQLLGKDLEMKQMLQSKIDLEKELETAREGEkESQER 410
Cdd:COG5185   463 SRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATL----EKLRAKLERQLEGVRSKLDQVAESLKDFMRA-RGYAH 537

                         330       340       350
                  ....*....|....*....|....*....|
gi 1958670239 411 EQALREEVEALTKKCQELEEAKRQETQERQ 440
Cdd:COG5185   538 ILALENLIPASELIQASNAKTDGQAANLRT 567
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
353-439 4.60e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 4.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 353 EDQEHLQGTVKTLREELSALQEQL-LGKDLEMKQMLQSKIDLEKELETAREGEKESQEREQALREEVEALTKKCQELEEA 431
Cdd:COG4717   163 EELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242


                  ....*...
gi 1958670239 432 KRQETQER 439
Cdd:COG4717   243 ERLKEARL 250
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
353-441 5.85e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 5.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 353 EDQEHLQGTVKTLREELSALQEQLLGKDLEMKQMLQSKIDLEKELETAREGEKESQEREQALREEVEALTKKCQELEEAK 432
Cdd:COG4372    45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124


                  ....*....
gi 1958670239 433 RQETQERQD 441
Cdd:COG4372   125 QDLEQQRKQ 133
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 96-430 6.21e-04

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: 43.47  E-value: 6.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  96 REKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDPgrgpdfVRTLAEKKPDTGWVITGLKQRIF 175
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNE------IEKLKKENQSYKQEIKNLESQIN 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 176 RLEQQCKEKDSTINKLQTDMKTTNLEEmriamETYYEEIHRLQTLLASSEATGKKpiLEKKMGVKRQKkmssallnltrs 255
Cdd:TIGR04523 395 DLESKIQNQEKLNQQKDEQIKKLQQEK-----ELLEKEIERLKETIIKNNSEIKD--LTNQDSVKELI------------ 455

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 256 VQELTEENQSLKEDLDrMLSNSptVSKIKGYVDWSKPRLLRRIAELEKKVSSSESPKNSASELVKPNPvvpspSNISVQK 335
Cdd:TIGR04523 456 IKNLDNTRESLETQLK-VLSRS--INKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIS-----SLKEKIE 527

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 336 QLKGDQSKEDQpKVDPSEDQehlqgtVKTLREEL--SALQEQLLGKDLEMKQMLQSKIDLEKELETAREGEKESQEREQA 413
Cdd:TIGR04523 528 KLESEKKEKES-KISDLEDE------LNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKD 600

                         330
                  ....*....|....*..
gi 1958670239 414 LREEVEALTKKCQELEE 430
Cdd:TIGR04523 601 LIKEIEEKEKKISSLEK 617
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 96-444 6.60e-04

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: 43.09  E-value: 6.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  96 REKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQlldpgrgpdfVRTLAEKkpdtgwvITGLKQRIF 175
Cdd:TIGR04523 166 KQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQK----------NKSLESQ-------ISELKKQNN 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 176 RLEQQCKEKDSTINKLQTDMKTTNlEEMRIAMETYYEEIHRLQTLLASSEATGKKpILEKKMGVKRQKKMSSALLN---- 251
Cdd:TIGR04523 229 QLKDNIEKKQQEINEKTTEISNTQ-TQLNQLKDEQNKIKKQLSEKQKELEQNNKK-IKELEKQLNQLKSEISDLNNqkeq 306

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 252 -LTRSVQELTEENQSLKEDLDRMLSNS--------PTVSKIKGYVDWSKPRLLRRIAELEKKVSSSESPKNSASELVKPN 322
Cdd:TIGR04523 307 dWNKELKSELKNQEKKLEEIQNQISQNnkiisqlnEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 323 PVVPSPSNI---SVQKQLKGDQSKEDQPKVDPSE------DQEHLQGTVKTLREELSALQEQLLGKDLEMKQMLQSKIDL 393
Cdd:TIGR04523 387 KNLESQINDlesKIQNQEKLNQQKDEQIKKLQQEkellekEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESL 466

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958670239 394 EKELET-AREGEKESQEREQALRE------EVEALTKKCQELEEaKRQETQERQDSFI 444
Cdd:TIGR04523 467 ETQLKVlSRSINKIKQNLEQKQKElkskekELKKLNEEKKELEE-KVKDLTKKISSLK 523
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 363-441 7.09e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 7.09e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958670239 363 KTLREELSALQEQLLGKDLEMKQMLQSKIDLEKELETAREGEKESQEREQALREEVEALTKKCQELEEAKRQETQERQD 441
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
333-441 9.44e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 9.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 333 VQKQLKGDQSKEDQPKvdpsEDQEHLQGTVKTLREELSALQEQLLGKDLEMKQMLQSKIDLEKELETAREGEKESQEREQ 412
Cdd:COG4372    43 LQEELEQLREELEQAR----EELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118

                          90       100
                  ....*....|....*....|....*....
gi 1958670239 413 ALREEVEALTKKCQELEEAKRQETQERQD 441
Cdd:COG4372   119 ELQKERQDLEQQRKQLEAQIAELQSEIAE 147
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 167-441 9.69e-04

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: 42.70  E-value: 9.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 167 ITGLKQRIFRLEQQCKEKDSTINKLQTDM--KTTNLEEMRIAMETYYEEIHRLQTLLASSEATGKKPILEKKMGVKRQKK 244
Cdd:TIGR04523 337 ISQLNEQISQLKKELTNSESENSEKQRELeeKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKK 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 245 MSSALLNLTRSVQELTEENQSLKEDLDRmLSNSPTVSKIKgyvdwsKPRLLRRIAELEKKVSS-SESPKNSASELVKpnp 323
Cdd:TIGR04523 417 LQQEKELLEKEIERLKETIIKNNSEIKD-LTNQDSVKELI------IKNLDNTRESLETQLKVlSRSINKIKQNLEQ--- 486

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 324 vvpspsnisVQKQLKgdqSKEDQPKVDPSEDQEhLQGTVKTLREELSALQEQLLGKDLEMKQMLQSKIDLEKELETAREG 403
Cdd:TIGR04523 487 ---------KQKELK---SKEKELKKLNEEKKE-LEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFE 553

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1958670239 404 ------EKESQEREQ---ALREEVEALTKKCQELEEAKRQETQERQD 441
Cdd:TIGR04523 554 lkkenlEKEIDEKNKeieELKQTQKSLKKKQEEKQELIDQKEKEKKD 600
Leu_zip pfam15294
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ...
 246-399 1.02e-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: 41.61  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 246 SSALLNLtrSVQELTEENQSLKEDLdRMLSnsptvSKIKGYVDwSKPRLLRRIAELEKKVSSSESPKNSASELVKpnpvv 325
Cdd:pfam15294 127 GSALLHM--EIERLKEENEKLKERL-KTLE-----SQATQALD-EKSKLEKALKDLQKEQGAKKDVKSNLKEISD----- 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 326 pspsnisVQKQLKGDQSKEDQPKVDPSEDQEHLQGTVKTLREELSALQEQL--LGKDLE-----------MKQMLQSKID 392
Cdd:pfam15294 193 -------LEEKMAALKSDLEKTLNASTALQKSLEEDLASTKHELLKVQEQLemAEKELEkkfqqtaayrnMKEMLTKKNE 265


                  ....*..
gi 1958670239 393 LEKELET 399
Cdd:pfam15294 266 QIKELRK 272
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
170-431 1.10e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 170 LKQRIFRLEQQCKEKDSTINKL-----QTDMKTTNLEEMRIAMETYYEEIHRLQTLLASSEatGKKPILEKKMG--VKRQ 242
Cdd:PRK03918  191 IEELIKEKEKELEEVLREINEIsselpELREELEKLEKEVKELEELKEEIEELEKELESLE--GSKRKLEEKIRelEERI 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 243 KKMSSALLNLTRSVQELTE------ENQSLKEDLDRMLSNSPTVSKIKGyvdwskpRLLRRIAELEKKVSSSESPKNSAS 316
Cdd:PRK03918  269 EELKKEIEELEEKVKELKElkekaeEYIKLSEFYEEYLDELREIEKRLS-------RLEEEINGIEERIKELEEKEERLE 341

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 317 ELVKpnpvvpspsnisvqkqlkgdQSKEDQPKVDPSEDQEHLQGTVKTLREELSALQEQLLGKDLEmkqmlqskiDLEKE 396
Cdd:PRK03918  342 ELKK--------------------KLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPE---------KLEKE 392

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1958670239 397 LETAREGEKESQEREQALREEVEALTKKCQELEEA 431
Cdd:PRK03918  393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKA 427
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
362-533 1.35e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  362 VKTLREELSALQEQLlgkdlemKQMLQSKIDLEkELETAREgekESQEREQALREEVEALTKKCQELEEaKRQETQERQD 441
Cdd:COG4913    663 VASAEREIAELEAEL-------ERLDASSDDLA-ALEEQLE---ELEAELEELEEELDELKGEIGRLEK-ELEQAEEELD 730

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  442 SFIAMTHEAhpevhapspcsrhsepdsdnnadnnagEDGGSQPPALCSEERREAAI-----RTLQAQWKAHRcKKRKAAL 516
Cdd:COG4913    731 ELQDRLEAA---------------------------EDLARLELRALLEERFAAALgdaveRELRENLEERI-DALRARL 782

                          170
                   ....*....|....*..
gi 1958670239  517 DEAATVLQAAFRGHLAR 533
Cdd:COG4913    783 NRAEEELERAMRAFNRE 799
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 353-442 2.02e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 353 EDQEHLQGTVKTLREELSALQEQLLGKDLEMKQMLQSKIDLEKELETAREGEKESQEREQALREEVEALTKKCQELEEAK 432
Cdd:COG1196   274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353

                          90
                  ....*....|
gi 1958670239 433 RQETQERQDS 442
Cdd:COG1196   354 EEAEAELAEA 363
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
361-440 2.53e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.16  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 361 TVKTLREELSALQEQLLgkdlemKQMLQSKIDLEKELETAREGEKESQEREQALREEVEALTKKCQELEEAKRQ-ETQER 439
Cdd:COG3206   292 DVIALRAQIAALRAQLQ------QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREvEVARE 365


                  .
gi 1958670239 440 Q 440
Cdd:COG3206   366 L 366
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
96-438 2.79e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 2.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  96 REKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDpgRGPDFVRTLAEKKPDTGWV---ITGLKQ 172
Cdd:PRK02224  272 REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELED--RDEELRDRLEECRVAAQAHneeAESLRE 349

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 173 RIFRLEQQCKEKDSTINKLQTDmkttnLEEMRIAMETYYEEIHRLQTLLASSEAtgkkpilekkmgvkrqkkmssALLNL 252
Cdd:PRK02224  350 DADDLEERAEELREEAAELESE-----LEEAREAVEDRREEIEELEEEIEELRE---------------------RFGDA 403

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 253 TRSVQELTEENQSLKEDLDRmlsnsptvskikgyvdwskprLLRRIAELEKKVSSSESPKNSASELVKPNpvvpspsnis 332
Cdd:PRK02224  404 PVDLGNAEDFLEELREERDE---------------------LREREAELEATLRTARERVEEAEALLEAG---------- 452

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 333 vqKQLKGDQSKEDQPKVDPSEDQ----EHLQGTVKTLREELSALQEQL-LGKDL-----EMKQMLQSKIDLEKELETARE 402
Cdd:PRK02224  453 --KCPECGQPVEGSPHVETIEEDrervEELEAELEDLEEEVEEVEERLeRAEDLveaedRIERLEERREDLEELIAERRE 530

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1958670239 403 GEKESQEREQALREEVEALTKKCQELEEA---KRQETQE 438
Cdd:PRK02224  531 TIEEKRERAEELRERAAELEAEAEEKREAaaeAEEEAEE 569
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 516-536 2.82e-03

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 35.76  E-value: 2.82e-03
                           10        20
                   ....*....|....*....|.
gi 1958670239  516 LDEAATVLQAAFRGHLARSKL 536
Cdd:smart00015   2 LTRAAIIIQAAWRGYLARKRY 22
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 233-435 2.94e-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: 41.11  E-value: 2.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  233 LEKKMGVK-RQKKMSSALLNLTRSVQELTE------ENQSLKEDLDRMLSNSPTVSKIKGYVDWSKPRLLRRIAELEKKV 305
Cdd:pfam02463  175 LKKLIEETeNLAELIIDLEELKLQELKLKEqakkalEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIE 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  306 SSSESPKNSASELVKpnpvvpSPSNISVQKQLKGDQSKEDqpkvDPSEDQEHLQGTVKTLREELSALQEQLLGKDLEMKQ 385
Cdd:pfam02463  255 SSKQEIEKEEEKLAQ------VLKENKEEEKEKKLQEEEL----KLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK 324

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958670239  386 MLQSKIDLEKELETAREGEKESQEREQALREEVEALTKKCQELEEAKRQE 435
Cdd:pfam02463  325 KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEE 374
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 353-441 3.23e-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: 39.91  E-value: 3.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 353 EDQEHLQGTVKTLREELSALQEQLL-GKDLEMKQMLQSKID-LEKELETAREGEKESQEREQALREEVEALTKKCQELEE 430
Cdd:COG1579    59 KEIKRLELEIEEVEARIKKYEEQLGnVRNNKEYEALQKEIEsLKRRISDLEDEILELMERIEELEEELAELEAELAELEA 138

                          90
                  ....*....|.
gi 1958670239 431 AKRQETQERQD 441
Cdd:COG1579   139 ELEEKKAELDE 149
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
98-433 4.90e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 4.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239  98 KEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLldpgrgpdfvRTLAEKkpdtgwvITGLKQRIFRL 177
Cdd:PRK03918  188 TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL----------EELKEE-------IEELEKELESL 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 178 EQQCKekdstinKLQTDMKttNLEEMRIAMETYYEEihrlqtllasseatgkkpiLEKKmgVKRQKKmssallnltrsVQ 257
Cdd:PRK03918  251 EGSKR-------KLEEKIR--ELEERIEELKKEIEE-------------------LEEK--VKELKE-----------LK 289

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 258 ELTEENQSLKEDLDRMLSNSPTVSKIKGyvdwskpRLLRRIAELEKKVSSSESPKNSASELVKpnpvvpspsnisvqkql 337
Cdd:PRK03918  290 EKAEEYIKLSEFYEEYLDELREIEKRLS-------RLEEEINGIEERIKELEEKEERLEELKK----------------- 345

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 338 kgdQSKEDQPKVDPSEDQEHLQGTVKTLREELSALQEQLLGKDLE-MKQMLQSkidLEKELETAREGEKESQEREQALRE 416
Cdd:PRK03918  346 ---KLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEkLEKELEE---LEKAKEEIEEEISKITARIGELKK 419

                         330
                  ....*....|....*..
gi 1958670239 417 EVEALTKKCQELEEAKR 433
Cdd:PRK03918  420 EIKELKKAIEELKKAKG 436
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
 518-536 5.39e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 34.99  E-value: 5.39e-03
                          10
                  ....*....|....*....
gi 1958670239 518 EAATVLQAAFRGHLARSKL 536
Cdd:pfam00612   2 KAAIKIQAAWRGYLARKRY 20
PRK12704 PRK12704
phosphodiesterase; Provisional
 362-449 9.21e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.38  E-value: 9.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958670239 362 VKTLREELSALQEQLLgkdlemkqmlQSKIDLEKELETAREGEKESQEREQALREEVEALTKKCQELEEaKRQETQERQD 441
Cdd:PRK12704   77 LRERRNELQKLEKRLL----------QKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEE-LIEEQLQELE 145


                  ....*...
gi 1958670239 442 SFIAMTHE 449
Cdd:PRK12704  146 RISGLTAE 153
 
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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