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Conserved domains on  [gi|348605241|ref|NP_001014092|]
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kazrin isoform 2 [Rattus norvegicus]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000037)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 25-257 2.36e-09

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.57  E-value: 2.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241  25 NLRAELTATNRRLAELSGGGGGPGSGPGAATSASAAAVTVADSAVATMENHQhGAQVLLREEVVQLQEEVHLLRQMKEML 104
Cdd:COG1196  236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-AEEYELLAELARLEQDIARLEERRREL 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241 105 AKDLEESQGGKCSEVLSATELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIR- 183
Cdd:COG1196  315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRa 394

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 348605241 184 --NYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTK 257
Cdd:COG1196  395 aaELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 25-257 2.36e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.57  E-value: 2.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241  25 NLRAELTATNRRLAELSGGGGGPGSGPGAATSASAAAVTVADSAVATMENHQhGAQVLLREEVVQLQEEVHLLRQMKEML 104
Cdd:COG1196  236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-AEEYELLAELARLEQDIARLEERRREL 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241 105 AKDLEESQGGKCSEVLSATELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIR- 183
Cdd:COG1196  315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRa 394

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 348605241 184 --NYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTK 257
Cdd:COG1196  395 aaELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 21-257 2.53e-07

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: 53.14  E-value: 2.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241    21 QEVTNLRAELTATNRRLAELSGGGGGPGSGPGAATSASAAAVTVADSAVATMENhqhgaqvlLREEVVQLQEEVHLLRQM 100
Cdd:TIGR02168  691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ--------LEERIAQLSKELTELEAE 762

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241   101 KEMLAKDLEESQggkcsevLSATELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDL---VSQMQQLYATLESREEQ 177
Cdd:TIGR02168  763 IEELEERLEEAE-------EELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLESLERRIAA 835

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241   178 LRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATD-------HAAALRSQLDLKDNRMKELEAELAMAKQ 250
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNerasleeALALLRSELEELSEELRELESKRSELRR 915


                   ....*..
gi 348605241   251 SLATLTK 257
Cdd:TIGR02168  916 ELEELRE 922
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
82-257 2.14e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.49  E-value: 2.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241  82 LLREEVVQLQEEVHLLRQMKEMLAKDLEESQ----GGKCSE----------VLSATELRVQLVQKEQELARAREALQAMK 147
Cdd:PRK02224 416 ELREERDELREREAELEATLRTARERVEEAEalleAGKCPEcgqpvegsphVETIEEDRERVEELEAELEDLEEEVEEVE 495

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241 148 ADRKRLKgektDLVSqmqqlyatLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAAL 227
Cdd:PRK02224 496 ERLERAE----DLVE--------AEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEA 563

                        170       180       190
                 ....*....|....*....|....*....|
gi 348605241 228 RSQLDLKDNRMKELEAELAMAKQSLATLTK 257
Cdd:PRK02224 564 EEEAEEAREEVAELNSKLAELKERIESLER 593
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 125-267 6.36e-04

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: 42.12  E-value: 6.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241  125 LRVQLVQKEQELARAREALQAMKADRKRLKGEKTDL---VSQMQQLYATL-ESREEQLRDFIRNYEQHRKESEDAvkala 200
Cdd:pfam10174 406 LQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLeeaLSEKERIIERLkEQREREDRERLEELESLKKENKDL----- 480

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 348605241  201 KEK-DLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVPKRHSLAM 267
Cdd:pfam10174 481 KEKvSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEE 548
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 25-257 2.36e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.57  E-value: 2.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241  25 NLRAELTATNRRLAELSGGGGGPGSGPGAATSASAAAVTVADSAVATMENHQhGAQVLLREEVVQLQEEVHLLRQMKEML 104
Cdd:COG1196  236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-AEEYELLAELARLEQDIARLEERRREL 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241 105 AKDLEESQGGKCSEVLSATELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIR- 183
Cdd:COG1196  315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRa 394

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 348605241 184 --NYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTK 257
Cdd:COG1196  395 aaELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
83-259 8.08e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.54  E-value: 8.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241   83 LREEVVQLQEEVHLLRQMKEmLAKDLEESQGGKcsEVLSATELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDLvs 162
Cdd:COG4913   240 AHEALEDAREQIELLEPIRE-LAERYAAARERL--AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERL-- 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241  163 qmQQLYATLESREEQLRdfirnyEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELE 242
Cdd:COG4913   315 --EARLDALREELDELE------AQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR 386

                         170
                  ....*....|....*..
gi 348605241  243 AELAMAKQSLATLTKDV 259
Cdd:COG4913   387 AEAAALLEALEEELEAL 403
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 21-257 2.53e-07

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: 53.14  E-value: 2.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241    21 QEVTNLRAELTATNRRLAELSGGGGGPGSGPGAATSASAAAVTVADSAVATMENhqhgaqvlLREEVVQLQEEVHLLRQM 100
Cdd:TIGR02168  691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ--------LEERIAQLSKELTELEAE 762

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241   101 KEMLAKDLEESQggkcsevLSATELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDL---VSQMQQLYATLESREEQ 177
Cdd:TIGR02168  763 IEELEERLEEAE-------EELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLESLERRIAA 835

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241   178 LRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATD-------HAAALRSQLDLKDNRMKELEAELAMAKQ 250
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNerasleeALALLRSELEELSEELRELESKRSELRR 915


                   ....*..
gi 348605241   251 SLATLTK 257
Cdd:TIGR02168  916 ELEELRE 922
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 83-259 1.91e-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: 50.44  E-value: 1.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241    83 LREEVVQLQEEVHLLRQMKEMLAKDL---------EESQGGKCSEVLSA-----TELRVQLVQKEQELARAREALQAMKA 148
Cdd:TIGR02168  703 LRKELEELEEELEQLRKELEELSRQIsalrkdlarLEAEVEQLEERIAQlskelTELEAEIEELEERLEEAEEELAEAEA 782

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241   149 DRKRLKGEKTDLVSQMQQL---YATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEAT---- 221
Cdd:TIGR02168  783 EIEELEAQIEQLKEELKALreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAaeie 862

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 348605241   222 ---DHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 259
Cdd:TIGR02168  863 eleELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 124-259 2.08e-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: 50.06  E-value: 2.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241   124 ELRVQLVQKEQELARAREALQAMK---ADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALA 200
Cdd:TIGR02168  688 ELEEKIAELEKALAELRKELEELEeelEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 348605241   201 K-------EKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 259
Cdd:TIGR02168  768 ErleeaeeELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 83-257 2.17e-06

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: 50.07  E-value: 2.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241    83 LREEVVQLQEEVHLLRQMKEMLAKDLEESQGGKCSEVLSATELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDLVS 162
Cdd:TIGR02169  700 IENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEE 779

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241   163 QMQQLYATL-ESREEQLRDFIRNYEQHRKESEDAVKALAK-------EKDLLEREKWELRRQAKEATDHAAALRSQLDLK 234
Cdd:TIGR02169  780 ALNDLEARLsHSRIPEIQAELSKLEEEVSRIEARLREIEQklnrltlEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENL 859

                          170       180
                   ....*....|....*....|...
gi 348605241   235 DNRMKELEAELAMAKQSLATLTK 257
Cdd:TIGR02169  860 NGKKEELEEELEELEAALRDLES 882
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 124-258 3.49e-06

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: 48.00  E-value: 3.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241 124 ELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDfIRNYEQhrkesedaVKALAKEK 203
Cdd:COG1579   28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-VRNNKE--------YEALQKEI 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 348605241 204 DLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKD 258
Cdd:COG1579   99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 83-258 4.28e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 4.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241  83 LREEVVQLQEEVHLLR-----QMKEMLAKDLEESQGGKCSEVLSATELRVQLVQKEQELARAREALQAMKADRKRLKGEK 157
Cdd:COG1196  218 LKEELKELEAELLLLKlreleAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241 158 TDLVSQM---QQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLK 234
Cdd:COG1196  298 ARLEQDIarlEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377

                        170       180
                 ....*....|....*....|....
gi 348605241 235 DNRMKELEAELAMAKQSLATLTKD 258
Cdd:COG1196  378 EEELEELAEELLEALRAAAELAAQ 401
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 85-261 5.60e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.22  E-value: 5.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241  85 EEVVQLQEEVHLLRQMKEMLAKDLEESQGgkcsevlSATELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDLVSQM 164
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKK-------EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241 165 QQLYATLESREEQLRDFIRNYEQHRKESEDAV---------------------KALAKEKDLLEREKWELRRQAKEATDH 223
Cdd:COG4942   93 AELRAELEAQKEELAELLRALYRLGRQPPLALllspedfldavrrlqylkylaPARREQAEELRADLAELAALRAELEAE 172

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 348605241 224 AAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVPK 261
Cdd:COG4942  173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAE 210
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 3-254 6.55e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 6.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241   3 EDNKQLALRIDGAVQSASQEVTNLRAELTATNRRLAELSGGGGGPGSGPGAATSASAAAVTVADSAVATMENHQHGAQVL 82
Cdd:COG1196  312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241  83 LREEVVQLQEEVHLLRQMKEML---------AKDLEESQGGKCSEVLSATELRVQLVQKEQELARAREALQAMKADRKRL 153
Cdd:COG1196  392 LRAAAELAAQLEELEEAEEALLerlerleeeLEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241 154 KGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQH---RKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQ 230
Cdd:COG1196  472 AALLEAALAELLEELAEAAARLLLLLEAEADYEGFlegVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNI 551

                        250       260
                 ....*....|....*....|....
gi 348605241 231 LDLKDNRMKELEAELAMAKQSLAT 254
Cdd:COG1196  552 VVEDDEVAAAAIEYLKAAKAGRAT 575
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
82-248 1.12e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241   82 LLREEVVQLQEEVHLLRQMKEMLAKDLEESQGgkcsevlSATELRVQLVQKE-QELARAREALQAMKADRKRLKGEKTDL 160
Cdd:COG4913   292 LLEAELEELRAELARLEAELERLEARLDALRE-------ELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARL 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241  161 VSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKE 240
Cdd:COG4913   365 EALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLA 444


                  ....*...
gi 348605241  241 LEAELAMA 248
Cdd:COG4913   445 LRDALAEA 452
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 66-260 1.37e-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: 47.74  E-value: 1.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241    66 DSAVATMENHQHGAQvllrEEVVQLQEEVHLLRQMKEMLAKDLEESQGGKCSEVLSATELRVQLVQKEQELARAREALQA 145
Cdd:TIGR02168  273 RLEVSELEEEIEELQ----KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE 348

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241   146 MKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAA 225
Cdd:TIGR02168  349 LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 348605241   226 AlrsqldLKDNRMKELEAELAMAKQSLATLTKDVP 260
Cdd:TIGR02168  429 K------LEEAELKELQAELEELEEELEELQEELE 457
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
83-245 1.52e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241   83 LREEVVQLQEEVHLLRQMKEMLAKDLEESQGGKCS----EVLSATELRV-----QLVQKEQELARAREA---LQAMKADR 150
Cdd:COG4913   615 LEAELAELEEELAEAEERLEALEAELDALQERREAlqrlAEYSWDEIDVasaerEIAELEAELERLDASsddLAALEEQL 694

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241  151 KRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQ 230
Cdd:COG4913   695 EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEER 774

                         170
                  ....*....|....*
gi 348605241  231 LDLKDNRMKELEAEL 245
Cdd:COG4913   775 IDALRARLNRAEEEL 789
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 5-202 3.30e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.91  E-value: 3.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241   5 NKQLAlRIDGAVQSASQEVTNLRAELTATNRRLAELSGGGGGPGSGPGAATSASAAAVtvadsAVATMENHQHGAQVLLR 84
Cdd:COG4942   54 LKQLA-ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL-----RALYRLGRQPPLALLLS 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241  85 -EEVVQLQEEVHLLRQMKEMLAKDLEESQggkcsevlsatELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDLVSQ 163
Cdd:COG4942  128 pEDFLDAVRRLQYLKYLAPARREQAEELR-----------ADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 348605241 164 MQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKE 202
Cdd:COG4942  197 RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 124-259 3.52e-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: 3.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241   124 ELRVQLVQKEQELARAReaLQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQL---RDFIRNYEQHRKESEDAVKALA 200
Cdd:TIGR02168  217 ELKAELRELELALLVLR--LEELREELEELQEELKEAEEELEELTAELQELEEKLeelRLEVSELEEEIEELQKELYALA 294

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 348605241   201 KEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 259
Cdd:TIGR02168  295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
85-256 8.55e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.76  E-value: 8.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241  85 EEVVQLQEEVHLLRQMKEMLAKDLEESQggkcsEVLSATELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDLVSQM 164
Cdd:COG4717   88 EEYAELQEELEELEEELEELEAELEELR-----EELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELE 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241 165 QQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRM--KELE 242
Cdd:COG4717  163 EELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELeaAALE 242

                        170
                 ....*....|....
gi 348605241 243 AELAMAKQSLATLT 256
Cdd:COG4717  243 ERLKEARLLLLIAA 256
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
117-259 9.97e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 9.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241 117 SEVLSATELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAV 196
Cdd:COG4372   35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 348605241 197 KALAKekdlLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 259
Cdd:COG4372  115 EELEE----LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL 173
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
124-246 1.10e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241  124 ELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDLvSQMQQLY------ATLESREEQLRDFIRNYEqhrkESEDAVK 197
Cdd:COG4913   614 ALEAELAELEEELAEAEERLEALEAELDALQERREAL-QRLAEYSwdeidvASAEREIAELEAELERLD----ASSDDLA 688

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 348605241  198 ALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELA 246
Cdd:COG4913   689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
126-259 1.34e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241  126 RVQLVQKEQELARAREALQAMKADRKRLKGEKTDLVSQmQQLYATLESREEQLRDfIRNYEQHRKESEDAVKALAKEKDL 205
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYSWDEID-VASAEREIAELEAELERLDASSDD 686

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 348605241  206 LErekwELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 259
Cdd:COG4913   687 LA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
82-257 2.14e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.49  E-value: 2.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241  82 LLREEVVQLQEEVHLLRQMKEMLAKDLEESQ----GGKCSE----------VLSATELRVQLVQKEQELARAREALQAMK 147
Cdd:PRK02224 416 ELREERDELREREAELEATLRTARERVEEAEalleAGKCPEcgqpvegsphVETIEEDRERVEELEAELEDLEEEVEEVE 495

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241 148 ADRKRLKgektDLVSqmqqlyatLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAAL 227
Cdd:PRK02224 496 ERLERAE----DLVE--------AEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEA 563

                        170       180       190
                 ....*....|....*....|....*....|
gi 348605241 228 RSQLDLKDNRMKELEAELAMAKQSLATLTK 257
Cdd:PRK02224 564 EEEAEEAREEVAELNSKLAELKERIESLER 593
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
124-259 2.78e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 2.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241 124 ELRVQLVQKEQELARAREALQAMKADRKRLKGEKT--DLVSQMQQLYATLESREEQLRDfIRNYEQHRKESEDAVKALAK 201
Cdd:COG4717   92 ELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEE-LEERLEELRELEEELEELEA 170

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 348605241 202 EKDLLEREKWELRRQAKEATDHAAA-LRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 259
Cdd:COG4717  171 ELAELQEELEELLEQLSLATEEELQdLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 122-255 3.38e-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: 3.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241 122 ATELRVQLVQKEQELARAReaLQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDA------ 195
Cdd:COG1196  215 YRELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeeye 292

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 348605241 196 ----VKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATL 255
Cdd:COG1196  293 llaeLARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 128-282 5.40e-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: 42.31  E-value: 5.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241  128 QLVQKEQELARAREALQamKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALA-KEKDLL 206
Cdd:TIGR04523 422 ELLEKEIERLKETIIKN--NSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKsKEKELK 499

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 348605241  207 E--REKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLtKDVPKRHSLampgETVLNGNQEWVVQ 282
Cdd:TIGR04523 500 KlnEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKD-DFELKKENL----EKEIDEKNKEIEE 572
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
83-245 5.93e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.33  E-value: 5.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241  83 LREEVVQLQEEVHLLRQMKEMLAKDLEESQGGKCS-EVLSAT--ELRVQLVQKEQELARAREALQAMKADRKRLKGEKTD 159
Cdd:PRK02224 218 LDEEIERYEEQREQARETRDEADEVLEEHEERREElETLEAEieDLRETIAETEREREELAEEVRDLRERLEELEEERDD 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241 160 LVSQ----------MQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRS 229
Cdd:PRK02224 298 LLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEARE 377

                        170
                 ....*....|....*.
gi 348605241 230 QLDLKDNRMKELEAEL 245
Cdd:PRK02224 378 AVEDRREEIEELEEEI 393
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 125-267 6.36e-04

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: 42.12  E-value: 6.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241  125 LRVQLVQKEQELARAREALQAMKADRKRLKGEKTDL---VSQMQQLYATL-ESREEQLRDFIRNYEQHRKESEDAvkala 200
Cdd:pfam10174 406 LQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLeeaLSEKERIIERLkEQREREDRERLEELESLKKENKDL----- 480

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 348605241  201 KEK-DLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVPKRHSLAM 267
Cdd:pfam10174 481 KEKvSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEE 548
PTZ00121 PTZ00121
MAEBL; Provisional
 79-244 6.51e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 6.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241   79 AQVLLREEVVQLQEEVHLLRQMKEmlAKDLEESQGGKCSEVLSATELRVQLVQKEQELARAREALQAMKADRKRLKGEKT 158
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEEAKK--AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL 1625

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241  159 DLVSQMQQLYATLESREEQLrdfIRNYEQHRKESEDAVKALAKEKDLLEREK---WELRRQAKEATDHAAALRSQLD--L 233
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEE---KKKAEELKKAEEENKIKAAEEAKKAEEDKkkaEEAKKAEEDEKKAAEALKKEAEeaK 1702

                         170
                  ....*....|.
gi 348605241  234 KDNRMKELEAE 244
Cdd:PTZ00121 1703 KAEELKKKEAE 1713
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
83-218 1.10e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241  83 LREEVVQLQEEVHLLRQMKEMLAKDLEESQggkCSEVLSATELRV-QLVQKEQELARAREALQAMKADRKRLKGEKTDLV 161
Cdd:COG4717  107 LEAELEELREELEKLEKLLQLLPLYQELEA---LEAELAELPERLeELEERLEELRELEEELEELEAELAELQEELEELL 183

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 348605241 162 SQ----MQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAK 218
Cdd:COG4717  184 EQlslaTEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 85-255 1.10e-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: 41.50  E-value: 1.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241    85 EEVVQLQEEVHLLrqmkemLAKDLEESQGGKCSEVLSATELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDLVSQm 164
Cdd:pfam02463  278 EKEKKLQEEELKL------LAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIK- 350

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241   165 qqlYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQA----KEATDHAAALRSQLDLKDNRMKE 240
Cdd:pfam02463  351 ---REAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKseeeKEAQLLLELARQLEDLLKEEKKE 427

                          170
                   ....*....|....*
gi 348605241   241 LEAELAMAKQSLATL 255
Cdd:pfam02463  428 ELEILEEEEESIELK 442
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
83-261 1.13e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241  83 LREEVVQLQEEVHLLRQMKEMLA-----KDLEESQGGKCSEVLSATELRV-QLVQKEQELARAREALQAMKADRK---RL 153
Cdd:PRK03918 219 LREELEKLEKEVKELEELKEEIEelekeLESLEGSKRKLEEKIRELEERIeELKKEIEELEEKVKELKELKEKAEeyiKL 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241 154 KGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQhRKESEDAVKALAKEKDLLEREKWELRRQAKEATDhAAALRSQLD- 232
Cdd:PRK03918 299 SEFYEEYLDELREIEKRLSRLEEEINGIEERIKE-LEEKEERLEELKKKLKELEKRLEELEERHELYEE-AKAKKEELEr 376

                        170       180       190
                 ....*....|....*....|....*....|...
gi 348605241 233 ----LKDNRMKELEAELAMAKQSLATLTKDVPK 261
Cdd:PRK03918 377 lkkrLTGLTPEKLEKELEELEKAKEEIEEEISK 409
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
83-254 1.47e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241  83 LREEVVQLQEEVHLLRQMKEMLAKDLEESQggkcsEVLSATElrvqlvQKEQELARAREALQAMKADRKRLKGEKTDLVS 162
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEAD-----EVLEEHE------ERREELETLEAEIEDLRETIAETEREREELAE 279

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241 163 QMQQLYATLESREEQLRDFIRNYEQHRKESEdavkALAKEKDLLEREKWELRR--------------QAKEATDHAAALR 228
Cdd:PRK02224 280 EVRDLRERLEELEEERDDLLAEAGLDDADAE----AVEARREELEDRDEELRDrleecrvaaqahneEAESLREDADDLE 355

                        170       180
                 ....*....|....*....|....*.
gi 348605241 229 SQLDLKDNRMKELEAELAMAKQSLAT 254
Cdd:PRK02224 356 ERAEELREEAAELESELEEAREAVED 381
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 125-260 1.53e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.84  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241 125 LRVQLVQKEQELARAREALQAMKADRKRLKGEKtDLVSQmqqlyatleSREEQLRDFIrnyEQHRKESEDAvkalakekd 204
Cdd:COG0542  402 VRMEIDSKPEELDELERRLEQLEIEKEALKKEQ-DEASF---------ERLAELRDEL---AELEEELEAL--------- 459

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 348605241 205 lleREKWElrrQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVP 260
Cdd:COG0542  460 ---KARWE---AEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLR 509
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
108-259 2.09e-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: 2.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241 108 LEESQGGKCSEVLSATE-LRVQLVQKEQELARAREALQAMKADRK--RLKGEKTDLVSQMQQL---YATLESREEQLRDF 181
Cdd:COG3206  162 LEQNLELRREEARKALEfLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELesqLAEARAELAEAEAR 241

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 348605241 182 IRNYEQHRKESEDAVKALAKEKDLLErekweLRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 259
Cdd:COG3206  242 LAALRAQLGSGPDALPELLQSPVIQQ-----LRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI 314
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 83-260 2.10e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 2.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241    83 LREEVVQLQEEVHLLRQMKEMLAKDleesqggkcsevlsATELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDLVS 162
Cdd:TIGR02169  355 LTEEYAELKEELEDLRAELEEVDKE--------------FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241   163 QMQQLYATLESREEQLrdfirnyeqhrKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELE 242
Cdd:TIGR02169  421 ELADLNAAIAGIEAKI-----------NELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489

                          170
                   ....*....|....*...
gi 348605241   243 AELAMAKQSLATLTKDVP 260
Cdd:TIGR02169  490 RELAEAEAQARASEERVR 507
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 16-260 2.28e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 2.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241    16 VQSASQEVTNLRAELTATNRRLAELSGGGGGPGSgpgaatsasaaavtvadsAVATMENHQHGAQVllrEEVVQLQEEVH 95
Cdd:TIGR02169  746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEE------------------ALNDLEARLSHSRI---PEIQAELSKLE 804

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241    96 LLRQMKEMLAKDLEESqggkcsevLSATELRVQLVQKE-QELARAREALQAMKADRKRlkgEKTDLVSQMQQLYATLESR 174
Cdd:TIGR02169  805 EEVSRIEARLREIEQK--------LNRLTLEKEYLEKEiQELQEQRIDLKEQIKSIEK---EIENLNGKKEELEEELEEL 873

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241   175 EEQLRDfirnyeqhrkesedavkaLAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLAT 254
Cdd:TIGR02169  874 EAALRD------------------LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE 935


                   ....*.
gi 348605241   255 LTKDVP 260
Cdd:TIGR02169  936 IEDPKG 941
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 83-348 2.39e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 2.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241  83 LREEVVQLQEEVHLLRQMKEMLAKDLEESQGgkcsevlSATELRVQLVQKEQELARAREALQAMKADRKRlKGEKTDLVS 162
Cdd:COG3883   35 AQAELDALQAELEELNEEYNELQAELEALQA-------EIDKLQAEIAEAEAEIEERREELGERARALYR-SGGSVSYLD 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241 163 QM--QQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKE 240
Cdd:COG3883  107 VLlgSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQ 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241 241 LEAELAMAKQSLATL--TKDVPKRHSLAMPGETVLNGNQEWVVQADLPLTAAIRQSQQTLYHSHPPHPADRQAVRVSPCH 318
Cdd:COG3883  187 LSAEEAAAEAQLAELeaELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAG 266

                        250       260       270
                 ....*....|....*....|....*....|
gi 348605241 319 SRQPSVISDASAAEGDRSSTPSDINSPRHR 348
Cdd:COG3883  267 AAAGAAGAGAAAASAAGGGAGGAGGGGGGG 296
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
21-230 2.41e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241   21 QEVTNLRAELTATNRRLAELSGGGGGPGSGPGAATSASAAAVTVADSAVAtmenhqhgaqvllREEVVQLQEEVHLLRQM 100
Cdd:COG4913   617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASA-------------EREIAELEAELERLDAS 683

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241  101 KEMLAkdleesqggkcsevlsatELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRD 180
Cdd:COG4913   684 SDDLA------------------ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 348605241  181 FIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQ 230
Cdd:COG4913   746 ELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
79-226 2.76e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 2.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241   79 AQVLLREEVVQLQEEVHLLRQMKEMLAKDLEE------SQGGKCSEVLSA--TELRVQLVQKEQELARAREALQAMKADR 150
Cdd:COG4913   296 ELEELRAELARLEAELERLEARLDALREELDEleaqirGNGGDRLEQLEReiERLERELEERERRRARLEALLAALGLPL 375

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241  151 KRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKW-------ELRRQAKEATDH 223
Cdd:COG4913   376 PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSniparllALRDALAEALGL 455


                  ...
gi 348605241  224 AAA 226
Cdd:COG4913   456 DEA 458
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 124-252 3.08e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 37.21  E-value: 3.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241  124 ELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDLVSQMQQLyatlesreeqlrdfirnyEQHRKESEDAVKALAKEK 203
Cdd:pfam20492  10 ELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERL------------------EQKRQEAEEEKERLEESA 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 348605241  204 DLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSL 252
Cdd:pfam20492  72 EMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 126-259 4.33e-03

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 39.28  E-value: 4.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241  126 RVQLVQKEQELARAREALQAMKADRKRLkgekTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDL 205
Cdd:pfam19220  47 KSRLLELEALLAQERAAYGKLRRELAGL----TRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEA 122

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 348605241  206 LEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 259
Cdd:pfam19220 123 LERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQEN 176
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
133-249 4.94e-03

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 38.27  E-value: 4.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241 133 EQELARAREALQAMKADRKRLKgektdlvSQMQQLYATLESREEQLRDFIrnyeqhRKESEDAVKALAKEKDLLEREKWE 212
Cdd:COG1842   36 EEDLVEARQALAQVIANQKRLE-------RQLEELEAEAEKWEEKARLAL------EKGREDLAREALERKAELEAQAEA 102

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 348605241 213 LRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAK 249
Cdd:COG1842  103 LEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLK 139
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 8-260 5.38e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.98  E-value: 5.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241   8 LALRIDGAVQSASQEVTNLRAELTATNRRLAELSGGGGGPGSGPGAATSASAAAVTVADSAVATMENHQHGAQVL----- 82
Cdd:COG4942    7 LALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALeaela 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241  83 -LREEVVQLQEEvhlLRQMKEMLAKDLEESQggkcsevLSATELRVQLVQKEQELARAREALQAMKAdrkrlkgektdLV 161
Cdd:COG4942   87 eLEKEIAELRAE---LEAQKEELAELLRALY-------RLGRQPPLALLLSPEDFLDAVRRLQYLKY-----------LA 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241 162 SQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKEL 241
Cdd:COG4942  146 PARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225

                        250
                 ....*....|....*....
gi 348605241 242 EAELAMAKQSLATLTKDVP 260
Cdd:COG4942  226 EALIARLEAEAAAAAERTP 244
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
83-247 7.00e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 38.84  E-value: 7.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241  83 LREEVVQLQEEVHLLRQMKEMLAKDLEESQGGKCSEVLSatELRVQLVQKEQELARARE----------ALQAMKAD-RK 151
Cdd:COG3206  228 LAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQ--QLRAQLAELEAELAELSArytpnhpdviALRAQIAAlRA 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241 152 RLKGEKTDLVSQMQQLYATLESREEQLRdfiRNYEQHRKESEDAVKALAKEKDlLEREkwelrrqakeatdhAAALRSQL 231
Cdd:COG3206  306 QLQQEAQRILASLEAELEALQAREASLQ---AQLAQLEARLAELPELEAELRR-LERE--------------VEVARELY 367

                        170
                 ....*....|....*.
gi 348605241 232 DLKDNRMKELEAELAM 247
Cdd:COG3206  368 ESLLQRLEEARLAEAL 383
PTZ00121 PTZ00121
MAEBL; Provisional
 79-244 7.15e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 7.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241   79 AQVLLREEVVQLQEEVHLLRQMKEMLAKDL--EESQGGKCSEVLSATELR----------------VQLVQKEQELARAR 140
Cdd:PTZ00121 1583 AEEAKKAEEARIEEVMKLYEEEKKMKAEEAkkAEEAKIKAEELKKAEEEKkkveqlkkkeaeekkkAEELKKAEEENKIK 1662

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241  141 EALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRdfiRNYEQHRKESEDAVKA---LAKEKDLLEREKWELRRQA 217
Cdd:PTZ00121 1663 AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA---KKAEELKKKEAEEKKKaeeLKKAEEENKIKAEEAKKEA 1739

                         170       180
                  ....*....|....*....|....*..
gi 348605241  218 KEATDHAAALRSQLDLKdNRMKELEAE 244
Cdd:PTZ00121 1740 EEDKKKAEEAKKDEEEK-KKIAHLKKE 1765
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
84-245 9.23e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.48  E-value: 9.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241  84 REEVVQLQEEVHLLRQMKEMLAKDLEESqggkcsEVLSATELRVQLVQKEQELARAREALQAMKADRKRLKGE-----KT 158
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERLERA------EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEelrerAA 547

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241 159 DLVSQMQQLYA---TLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLL------EREKWELRRQAKEATDHAAALRS 229
Cdd:PRK02224 548 ELEAEAEEKREaaaEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLaaiadaEDEIERLREKREALAELNDERRE 627

                        170
                 ....*....|....*.
gi 348605241 230 QLDLKDNRMKELEAEL 245
Cdd:PRK02224 628 RLAEKRERKRELEAEF 643
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
83-253 9.89e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 37.96  E-value: 9.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241  83 LREEVVQLQEEVHLLRQMKEMLAKDLEESQGGKCSEVLSATELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDLVS 162
Cdd:COG4372   57 AREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEA 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348605241 163 QMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAK-EKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKEL 241
Cdd:COG4372  137 QIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAlSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPREL 216

                        170
                 ....*....|..
gi 348605241 242 EAELAMAKQSLA 253
Cdd:COG4372  217 AEELLEAKDSLE 228
 
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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