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Conserved domains on  [gi|1907157327|ref|XP_036020340|]
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kazrin isoform X10 [Mus musculus]

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]; ...
 113-345 1.32e-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: 60.72  E-value: 1.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 113 NLRAELTATNRRLAELSGGGGGPGSGPGAATSASAAAVTVADSAVATMENHQhGAQVLLREEVVQLQEEVHLLRQMKEML 192
Cdd:COG1196   236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-AEEYELLAELARLEQDIARLEERRREL 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 193 AKDLEESQGGKCSEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIR- 271
Cdd:COG1196   315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRa 394

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907157327 272 --NYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTK 345
Cdd:COG1196   395 aaELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 113-345 1.32e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 1.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 113 NLRAELTATNRRLAELSGGGGGPGSGPGAATSASAAAVTVADSAVATMENHQhGAQVLLREEVVQLQEEVHLLRQMKEML 192
Cdd:COG1196   236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-AEEYELLAELARLEQDIARLEERRREL 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 193 AKDLEESQGGKCSEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIR- 271
Cdd:COG1196   315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRa 394

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907157327 272 --NYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTK 345
Cdd:COG1196   395 aaELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 109-345 1.37e-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: 54.29  E-value: 1.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  109 QEVTNLRAELTATNRRLAELSGGGGGPGSGPGAATSASAAAVTVADSAVATMENhqhgaqvlLREEVVQLQEEVHLLRQM 188
Cdd:TIGR02168  691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ--------LEERIAQLSKELTELEAE 762

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  189 KEMLAKDLEESQggkcsevLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDL---VSQMQQLYATLESREEQ 265
Cdd:TIGR02168  763 IEELEERLEEAE-------EELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLESLERRIAA 835

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  266 LRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATD-------HAAALRSQLDLKDNRMKELEAELAMAKQ 338
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNerasleeALALLRSELEELSEELRELESKRSELRR 915


                   ....*..
gi 1907157327  339 SLATLTK 345
Cdd:TIGR02168  916 ELEELRE 922
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
170-345 1.74e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.26  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 170 LLREEVVQLQEEVHLLRQMKEMLAKDLEESQ----GGKCSE----------VLSATELRVQLVQKEQELARAKEALQAMK 235
Cdd:PRK02224  416 ELREERDELREREAELEATLRTARERVEEAEalleAGKCPEcgqpvegsphVETIEEDRERVEELEAELEDLEEEVEEVE 495

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 236 ADRKRLKgektDLVSqmqqlyatLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAAL 315
Cdd:PRK02224  496 ERLERAE----DLVE--------AEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEA 563

                         170       180       190
                  ....*....|....*....|....*....|
gi 1907157327 316 RSQLDLKDNRMKELEAELAMAKQSLATLTK 345
Cdd:PRK02224  564 EEEAEEAREEVAELNSKLAELKERIESLER 593
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 173-343 7.10e-04

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: 42.27  E-value: 7.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  173 EEVVQLQEEVHLLrqmkemLAKDLEESQGGKCSEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQm 252
Cdd:pfam02463  278 EKEKKLQEEELKL------LAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIK- 350

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  253 qqlYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQA----KEATDHAAALRSQLDLKDNRMKE 328
Cdd:pfam02463  351 ---REAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKseeeKEAQLLLELARQLEDLLKEEKKE 427

                          170
                   ....*....|....*
gi 1907157327  329 LEAELAMAKQSLATL 343
Cdd:pfam02463  428 ELEILEEEEESIELK 442
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 219-344 6.76e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 38.50  E-value: 6.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 219 QKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLrdfirnyeqhrKESEDAVKA-LAKEKDLLERE 297
Cdd:cd22656   111 ELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTAL-----------ETLEKALKDlLTDEGGAIARK 179

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907157327 298 KWE-LRRQAKEAT-DHAAALRSQLDLKDNRMKELEAELAMAKQSLATLT 344
Cdd:cd22656   180 EIKdLQKELEKLNeEYAAKLKAKIDELKALIADDEAKLAAALRLIADLT 228
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 113-345 1.32e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 1.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 113 NLRAELTATNRRLAELSGGGGGPGSGPGAATSASAAAVTVADSAVATMENHQhGAQVLLREEVVQLQEEVHLLRQMKEML 192
Cdd:COG1196   236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-AEEYELLAELARLEQDIARLEERRREL 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 193 AKDLEESQGGKCSEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIR- 271
Cdd:COG1196   315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRa 394

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907157327 272 --NYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTK 345
Cdd:COG1196   395 aaELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
171-347 6.16e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.31  E-value: 6.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  171 LREEVVQLQEEVHLLRQMKEmLAKDLEESQGGKcsEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLvs 250
Cdd:COG4913    240 AHEALEDAREQIELLEPIRE-LAERYAAARERL--AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERL-- 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  251 qmQQLYATLESREEQLRdfirnyEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELE 330
Cdd:COG4913    315 --EARLDALREELDELE------AQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR 386

                          170
                   ....*....|....*..
gi 1907157327  331 AELAMAKQSLATLTKDV 347
Cdd:COG4913    387 AEAAALLEALEEELEAL 403
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 109-345 1.37e-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: 54.29  E-value: 1.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  109 QEVTNLRAELTATNRRLAELSGGGGGPGSGPGAATSASAAAVTVADSAVATMENhqhgaqvlLREEVVQLQEEVHLLRQM 188
Cdd:TIGR02168  691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ--------LEERIAQLSKELTELEAE 762

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  189 KEMLAKDLEESQggkcsevLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDL---VSQMQQLYATLESREEQ 265
Cdd:TIGR02168  763 IEELEERLEEAE-------EELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLESLERRIAA 835

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  266 LRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATD-------HAAALRSQLDLKDNRMKELEAELAMAKQ 338
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNerasleeALALLRSELEELSEELRELESKRSELRR 915


                   ....*..
gi 1907157327  339 SLATLTK 345
Cdd:TIGR02168  916 ELEELRE 922
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 171-345 1.78e-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: 50.45  E-value: 1.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  171 LREEVVQLQEEVHLLRQMKEMLAKDLEESQGGKCSEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVS 250
Cdd:TIGR02169  700 IENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEE 779

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  251 QMQQLYATL-ESREEQLRDFIRNYEQHRKESEDAVKALAK-------EKDLLEREKWELRRQAKEATDHAAALRSQLDLK 322
Cdd:TIGR02169  780 ALNDLEARLsHSRIPEIQAELSKLEEEVSRIEARLREIEQklnrltlEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENL 859

                          170       180
                   ....*....|....*....|...
gi 1907157327  323 DNRMKELEAELAMAKQSLATLTK 345
Cdd:TIGR02169  860 NGKKEELEEELEELEAALRDLES 882
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 64-342 2.41e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 2.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  64 EKETLKNSMILMRHLLMDAQAKILSMMEDNKQLALRIdgavQSASQEVTNLRAELTATNRRLAELSGGGGGPGSGPGAAT 143
Cdd:COG1196   296 ELARLEQDIARLEERRRELEERLEELEEELAELEEEL----EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 144 SASAAAVTVADSAVATMENHQHGAQVLLREEVVQLQEEVHLLRQMKEMLA--KDLEESQGGKCSEVLSATELRVQLVQKE 221
Cdd:COG1196   372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEelEELEEALAELEEEEEEEEEALEEAAEEE 451

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 222 QELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQH---RKESEDAVKALAKEKDLLEREK 298
Cdd:COG1196   452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFlegVKAALLLAGLRGLAGAVAVLIG 531

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1907157327 299 WELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLAT 342
Cdd:COG1196   532 VEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAT 575
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 212-346 3.89e-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: 3.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 212 ELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDfIRNYEQhrkesedaVKALAKEK 291
Cdd:COG1579    28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-VRNNKE--------YEALQKEI 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907157327 292 DLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKD 346
Cdd:COG1579    99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 212-347 4.11e-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: 49.28  E-value: 4.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  212 ELRVQLVQKEQELARAKEALQAMK---ADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALA 288
Cdd:TIGR02168  688 ELEEKIAELEKALAELRKELEELEeelEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907157327  289 K-------EKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 347
Cdd:TIGR02168  768 ErleeaeeELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
170-336 4.62e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 4.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  170 LLREEVVQLQEEVHLLRQMKEMLAKDLEESQGgkcsevlSATELRVQLVQKE-QELARAKEALQAMKADRKRLKGEKTDL 248
Cdd:COG4913    292 LLEAELEELRAELARLEAELERLEARLDALRE-------ELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARL 364

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  249 VSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKE 328
Cdd:COG4913    365 EALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLA 444


                   ....*...
gi 1907157327  329 LEAELAMA 336
Cdd:COG4913    445 LRDALAEA 452
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 171-347 5.75e-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: 48.90  E-value: 5.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  171 LREEVVQLQEEVHLLRQMKEMLAKDL---------EESQGGKCSEVLSA-----TELRVQLVQKEQELARAKEALQAMKA 236
Cdd:TIGR02168  703 LRKELEELEEELEQLRKELEELSRQIsalrkdlarLEAEVEQLEERIAQlskelTELEAEIEELEERLEEAEEELAEAEA 782

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  237 DRKRLKGEKTDLVSQMQQL---YATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEAT---- 309
Cdd:TIGR02168  783 EIEELEAQIEQLKEELKALreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAaeie 862

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1907157327  310 ---DHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 347
Cdd:TIGR02168  863 eleELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 173-349 6.50e-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: 6.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 173 EEVVQLQEEVHLLRQMKEMLAKDLEESQGgkcsevlSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQM 252
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKK-------EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 253 QQLYATLESREEQLRDFIRNYEQHRKESEDAV---------------------KALAKEKDLLEREKWELRRQAKEATDH 311
Cdd:COG4942    93 AELRAELEAQKEELAELLRALYRLGRQPPLALllspedfldavrrlqylkylaPARREQAEELRADLAELAALRAELEAE 172

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1907157327 312 AAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVPK 349
Cdd:COG4942   173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAE 210
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 64-290 7.48e-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: 47.84  E-value: 7.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  64 EKETLKNSMILMRHLLMDAQAKILSMMEDNKQLALRIDgavqSASQEVTNLRAELTATNRRLAELSGGGGGPGSGPGAAT 143
Cdd:COG4942    28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA----ALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 144 SASAAAVtvadsAVATMENHQHGAQVLLR-EEVVQLQEEVHLLRQMKEMLAKDLEESQggkcsevlsatELRVQLVQKEQ 222
Cdd:COG4942   104 EELAELL-----RALYRLGRQPPLALLLSpEDFLDAVRRLQYLKYLAPARREQAEELR-----------ADLAELAALRA 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907157327 223 ELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKE 290
Cdd:COG4942   168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 154-348 7.71e-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: 48.51  E-value: 7.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  154 DSAVATMENHQHGAQvllrEEVVQLQEEVHLLRQMKEMLAKDLEESQGGKCSEVLSATELRVQLVQKEQELARAKEALQA 233
Cdd:TIGR02168  273 RLEVSELEEEIEELQ----KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE 348

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  234 MKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAA 313
Cdd:TIGR02168  349 LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1907157327  314 AlrsqldLKDNRMKELEAELAMAKQSLATLTKDVP 348
Cdd:TIGR02168  429 K------LEEAELKELQAELEELEEELEELQEELE 457
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 171-346 1.03e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 171 LREEVVQLQEEVHLLR-----QMKEMLAKDLEESQGGKCSEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEK 245
Cdd:COG1196   218 LKEELKELEAELLLLKlreleAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 246 TDLVSQM---QQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLK 322
Cdd:COG1196   298 ARLEQDIarlEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377

                         170       180
                  ....*....|....*....|....
gi 1907157327 323 DNRMKELEAELAMAKQSLATLTKD 346
Cdd:COG1196   378 EEELEELAEELLEALRAAAELAAQ 401
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
171-333 2.36e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 2.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  171 LREEVVQLQEEVHLLRQMKEMLAKDLEESQGGKCS----EVLSATELRV-----QLVQKEQELARAKEA---LQAMKADR 238
Cdd:COG4913    615 LEAELAELEEELAEAEERLEALEAELDALQERREAlqrlAEYSWDEIDVasaerEIAELEAELERLDASsddLAALEEQL 694

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  239 KRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQ 318
Cdd:COG4913    695 EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEER 774

                          170
                   ....*....|....*
gi 1907157327  319 LDLKDNRMKELEAEL 333
Cdd:COG4913    775 IDALRARLNRAEEEL 789
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 212-347 5.26e-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: 45.82  E-value: 5.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  212 ELRVQLVQKEQELA-----RAKEALQAMKADRKRLKGEKTDLVSQMQqlyaTLESREEQLRDFIRNYEQHRKESEDAVKA 286
Cdd:TIGR02168  217 ELKAELRELELALLvlrleELREELEELQEELKEAEEELEELTAELQ----ELEEKLEELRLEVSELEEEIEELQKELYA 292

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907157327  287 LAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 347
Cdd:TIGR02168  293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
212-334 8.08e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 8.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  212 ELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLvSQMQQLY------ATLESREEQLRDFIRNYEqhrkESEDAVK 285
Cdd:COG4913    614 ALEAELAELEEELAEAEERLEALEAELDALQERREAL-QRLAEYSwdeidvASAEREIAELEAELERLD----ASSDDLA 688

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1907157327  286 ALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELA 334
Cdd:COG4913    689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 206-347 8.51e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 8.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 206 EVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVK 285
Cdd:COG1196   223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907157327 286 ALAKEKDL-------LEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 347
Cdd:COG1196   303 DIARLEERrreleerLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 63-303 8.74e-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: 45.05  E-value: 8.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327   63 TEKETLKNSMILMRHLLMDAQAKILSMMEDNKQLALRIDGAVQSASQEVTNLRAELTATNRRLAELSGGGGGPGSGPGAA 142
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  143 TSASAAAVTVADSAVATME--NHQHGAQVLLREE-----------VVQLQEEVHLLRQMKEMLAKDLEESQGGKcsevls 209
Cdd:TIGR02168  837 ERRLEDLEEQIEELSEDIEslAAEIEELEELIEEleseleallneRASLEEALALLRSELEELSEELRELESKR------ 910

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  210 aTELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVS----QMQQLYATLESREEQLRDFIRNYEQHRKE------ 279
Cdd:TIGR02168  911 -SELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSltleEAEALENKIEDDEEEARRRLKRLENKIKElgpvnl 989

                          250       260
                   ....*....|....*....|....*
gi 1907157327  280 -SEDAVKALAKEKDLLEREKWELRR 303
Cdd:TIGR02168  990 aAIEEYEELKERYDFLTAQKEDLTE 1014
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
173-344 1.25e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 173 EEVVQLQEEVHLLRQMKEMLAKDLEESQggkcsEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQM 252
Cdd:COG4717    88 EEYAELQEELEELEEELEELEAELEELR-----EELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELE 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 253 QQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRM--KELE 330
Cdd:COG4717   163 EELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELeaAALE 242

                         170
                  ....*....|....
gi 1907157327 331 AELAMAKQSLATLT 344
Cdd:COG4717   243 ERLKEARLLLLIAA 256
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
214-347 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 1907157327  214 RVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQmQQLYATLESREEQLRDfIRNYEQHRKESEDAVKALAKEKDL 293
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYSWDEID-VASAEREIAELEAELERLDASSDD 686

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907157327  294 LErekwELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 347
Cdd:COG4913    687 LA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
170-345 1.74e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.26  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 170 LLREEVVQLQEEVHLLRQMKEMLAKDLEESQ----GGKCSE----------VLSATELRVQLVQKEQELARAKEALQAMK 235
Cdd:PRK02224  416 ELREERDELREREAELEATLRTARERVEEAEalleAGKCPEcgqpvegsphVETIEEDRERVEELEAELEDLEEEVEEVE 495

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 236 ADRKRLKgektDLVSqmqqlyatLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAAL 315
Cdd:PRK02224  496 ERLERAE----DLVE--------AEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEA 563

                         170       180       190
                  ....*....|....*....|....*....|
gi 1907157327 316 RSQLDLKDNRMKELEAELAMAKQSLATLTK 345
Cdd:PRK02224  564 EEEAEEAREEVAELNSKLAELKERIESLER 593
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 210-343 3.35e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 3.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 210 ATELRVQLVQKEQELARAKeaLQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDA------ 283
Cdd:COG1196   215 YRELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeeye 292

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907157327 284 ----VKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATL 343
Cdd:COG1196   293 llaeLARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
171-342 3.62e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 3.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 171 LREEVVQLQEEVHLLRQMKEMLAKDLEESQggkcsEVLSATElrvqlvQKEQELARAKEALQAMKADRKRLKGEKTDLVS 250
Cdd:PRK02224  211 LESELAELDEEIERYEEQREQARETRDEAD-----EVLEEHE------ERREELETLEAEIEDLRETIAETEREREELAE 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 251 QMQQLYATLESREEQLRDFIRNYEQHRKESEdavkALAKEKDLLEREKWELRR--------------QAKEATDHAAALR 316
Cdd:PRK02224  280 EVRDLRERLEELEEERDDLLAEAGLDDADAE----AVEARREELEDRDEELRDrleecrvaaqahneEAESLREDADDLE 355

                         170       180
                  ....*....|....*....|....*.
gi 1907157327 317 SQLDLKDNRMKELEAELAMAKQSLAT 342
Cdd:PRK02224  356 ERAEELREEAAELESELEEAREAVED 381
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
171-333 3.78e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 3.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 171 LREEVVQLQEEVHLLRQMKEMLAKDLEESQGGKCS-EVLSAT--ELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTD 247
Cdd:PRK02224  218 LDEEIERYEEQREQARETRDEADEVLEEHEERREElETLEAEieDLRETIAETEREREELAEEVRDLRERLEELEEERDD 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 248 LVSQ----------MQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRS 317
Cdd:PRK02224  298 LLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEARE 377

                         170
                  ....*....|....*.
gi 1907157327 318 QLDLKDNRMKELEAEL 333
Cdd:PRK02224  378 AVEDRREEIEELEEEI 393
PTZ00121 PTZ00121
MAEBL; Provisional
 167-332 5.38e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 5.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  167 AQVLLREEVVQLQEEVHLLRQMKEmlAKDLEESQGGKCSEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKT 246
Cdd:PTZ00121  1548 ADELKKAEELKKAEEKKKAEEAKK--AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL 1625

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  247 DLVSQMQQLYATLESREEQLrdfIRNYEQHRKESEDAVKALAKEKDLLEREKW---ELRRQAKEATDHAAALRSQLD--L 321
Cdd:PTZ00121  1626 KKAEEEKKKVEQLKKKEAEE---KKKAEELKKAEEENKIKAAEEAKKAEEDKKkaeEAKKAEEDEKKAAEALKKEAEeaK 1702

                          170
                   ....*....|.
gi 1907157327  322 KDNRMKELEAE 332
Cdd:PTZ00121  1703 KAEELKKKEAE 1713
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
212-347 5.40e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 5.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 212 ELRVQLVQKEQELARAKEALQAMKADRKRLKGEKT--DLVSQMQQLYATLESREEQLRDfIRNYEQHRKESEDAVKALAK 289
Cdd:COG4717    92 ELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEE-LEERLEELRELEEELEELEA 170

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907157327 290 EKDLLEREKWELRRQAKEATDHAAA-LRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 347
Cdd:COG4717   171 ELAELQEELEELLEQLSLATEEELQdLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 171-348 5.79e-04

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: 42.36  E-value: 5.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  171 LREEVVQLQEEVHLLRQMKEMLAKDleesqggkcsevlsATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVS 250
Cdd:TIGR02169  355 LTEEYAELKEELEDLRAELEEVDKE--------------FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  251 QMQQLYATLESREEQLrdfirnyeqhrKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELE 330
Cdd:TIGR02169  421 ELADLNAAIAGIEAKI-----------NELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489

                          170
                   ....*....|....*...
gi 1907157327  331 AELAMAKQSLATLTKDVP 348
Cdd:TIGR02169  490 RELAEAEAQARASEERVR 507
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 173-343 7.10e-04

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: 42.27  E-value: 7.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  173 EEVVQLQEEVHLLrqmkemLAKDLEESQGGKCSEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQm 252
Cdd:pfam02463  278 EKEKKLQEEELKL------LAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIK- 350

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  253 qqlYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQA----KEATDHAAALRSQLDLKDNRMKE 328
Cdd:pfam02463  351 ---REAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKseeeKEAQLLLELARQLEDLLKEEKKE 427

                          170
                   ....*....|....*
gi 1907157327  329 LEAELAMAKQSLATL 343
Cdd:pfam02463  428 ELEILEEEEESIELK 442
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 55-348 9.21e-04

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: 41.98  E-value: 9.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327   55 EDDDPFLPTEKETLKNSMILMRHLLMDAQAKILSMMEDNKQLALRIDGAV----------QSASQEVTNLRAELTATNRR 124
Cdd:TIGR02169  687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKerleeleedlSSLEQEIENVKSELKELEAR 766

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  125 LAELSGGGGGPGSgpgaatsasaaavtvadsAVATMENHQHGAQVllrEEVVQLQEEVHLLRQMKEMLAKDLEESqggkc 204
Cdd:TIGR02169  767 IEELEEDLHKLEE------------------ALNDLEARLSHSRI---PEIQAELSKLEEEVSRIEARLREIEQK----- 820

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  205 sevLSATELRVQLVQKE-QELARAKEALQAMKADRKRlkgEKTDLVSQMQQLYATLESREEQLRDfirnyeqhrkeseda 283
Cdd:TIGR02169  821 ---LNRLTLEKEYLEKEiQELQEQRIDLKEQIKSIEK---EIENLNGKKEELEEELEELEAALRD--------------- 879

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907157327  284 vkaLAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVP 348
Cdd:TIGR02169  880 ---LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKG 941
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 213-355 1.04e-03

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: 41.73  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 213 LRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDL---VSQMQQLYATL-ESREEQLRDFIRNYEQHRKESEDAvkala 288
Cdd:pfam10174 406 LQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLeeaLSEKERIIERLkEQREREDRERLEELESLKKENKDL----- 480

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907157327 289 KEK-DLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVPKRHSLAM 355
Cdd:pfam10174 481 KEKvSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEE 548
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 219-370 1.05e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.54  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 219 QKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALA-KEKDLLE-- 295
Cdd:TIGR04523 423 LLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKsKEKELKKln 502

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907157327 296 REKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLtKDVPKRHSLampgETVLNGNQEWVVQ 370
Cdd:TIGR04523 503 EEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKD-DFELKKENL----EKEIDEKNKEIEE 572
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 213-348 1.88e-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: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 213 LRVQLVQKEQELARAKEALQAMKADRKRLKGEKtDLVSQmqqlyatleSREEQLRDFIrnyEQHRKESEDAvkalakekd 292
Cdd:COG0542   402 VRMEIDSKPEELDELERRLEQLEIEKEALKKEQ-DEASF---------ERLAELRDEL---AELEEELEAL--------- 459

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907157327 293 lleREKWElrrQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVP 348
Cdd:COG0542   460 ---KARWE---AEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLR 509
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
167-314 1.90e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 1.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  167 AQVLLREEVVQLQEEVHLLRQMKEMLAKDLEE------SQGGKCSEVLSA--TELRVQLVQKEQELARAKEALQAMKADR 238
Cdd:COG4913    296 ELEELRAELARLEAELERLEARLDALREELDEleaqirGNGGDRLEQLEReiERLERELEERERRRARLEALLAALGLPL 375

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  239 KRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKW-------ELRRQAKEATDH 311
Cdd:COG4913    376 PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSniparllALRDALAEALGL 455


                   ...
gi 1907157327  312 AAA 314
Cdd:COG4913    456 DEA 458
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
171-349 2.60e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 2.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 171 LREEVVQLQEEVHLLRQMKEMLA-----KDLEESQGGKCSEVLSATELRV-QLVQKEQELARAKEALQAMKADRK---RL 241
Cdd:PRK03918  219 LREELEKLEKEVKELEELKEEIEelekeLESLEGSKRKLEEKIRELEERIeELKKEIEELEEKVKELKELKEKAEeyiKL 298

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 242 KGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQhRKESEDAVKALAKEKDLLEREKWELRRQAKEATDhAAALRSQLD- 320
Cdd:PRK03918  299 SEFYEEYLDELREIEKRLSRLEEEINGIEERIKE-LEEKEERLEELKKKLKELEKRLEELEERHELYEE-AKAKKEELEr 376

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1907157327 321 ----LKDNRMKELEAELAMAKQSLATLTKDVPK 349
Cdd:PRK03918  377 lkkrLTGLTPEKLEKELEELEKAKEEIEEEISK 409
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
109-304 3.29e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 3.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  109 QEVTNLRAELTATNRRLAELSGGGGGPGSGPGAATSASAAAVTVADSAVAtmenhqhgaqvllREEVVQLQEEVHLLRQM 188
Cdd:COG4913    617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASA-------------EREIAELEAELERLDAS 683

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  189 KEMLAkdleesqggkcsevlsatELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRD 268
Cdd:COG4913    684 SDDLA------------------ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1907157327  269 FIRNY--EQHRKESEDAV-----KALAKEKDLLEREKWELRRQ 304
Cdd:COG4913    746 ELRALleERFAAALGDAVerelrENLEERIDALRARLNRAEEE 788
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 210-436 4.06e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.43  E-value: 4.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 210 ATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIR-NYEQHR----------- 277
Cdd:COG3883    32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARaLYRSGGsvsyldvllgs 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 278 ------------------------KESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAEL 333
Cdd:COG3883   112 esfsdfldrlsalskiadadadllEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEE 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 334 AMAKQSLATL--TKDVPKRHSLAMPGETVLNGNQEWVVQADLPLTAAIRQSQQTLYHSHPPHPADRQAVRVSPCHSRQPS 411
Cdd:COG3883   192 AAAEAQLAELeaELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGA 271

                         250       260
                  ....*....|....*....|....*
gi 1907157327 412 VISDASAAEGDRSSTPSDINSPRHR 436
Cdd:COG3883   272 AGAGAAAASAAGGGAGGAGGGGGGG 296
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 96-348 4.52e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 4.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  96 LALRIDGAVQSASQEVTNLRAELTATNRRLAELSGGGGGPGSGPGAATSASAAAVTVADSAVATMENHQHGAQVL----- 170
Cdd:COG4942     7 LALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALeaela 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 171 -LREEVVQLQEEvhlLRQMKEMLAKDLEESQggkcsevLSATELRVQLVQKEQELARAKEALQAMKAdrkrlkgektdLV 249
Cdd:COG4942    87 eLEKEIAELRAE---LEAQKEELAELLRALY-------RLGRQPPLALLLSPEDFLDAVRRLQYLKY-----------LA 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 250 SQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKEL 329
Cdd:COG4942   146 PARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225

                         250
                  ....*....|....*....
gi 1907157327 330 EAELAMAKQSLATLTKDVP 348
Cdd:COG4942   226 EALIARLEAEAAAAAERTP 244
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
196-347 6.75e-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: 6.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 196 LEESQGGKCSEVLSATE-LRVQLVQKEQELARAKEALQAMKADRK--RLKGEKTDLVSQMQQL---YATLESREEQLRDF 269
Cdd:COG3206   162 LEQNLELRREEARKALEfLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELesqLAEARAELAEAEAR 241

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907157327 270 IRNYEQHRKESEDAVKALAKEKDLLErekweLRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 347
Cdd:COG3206   242 LAALRAQLGSGPDALPELLQSPVIQQ-----LRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI 314
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 219-344 6.76e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 38.50  E-value: 6.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 219 QKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLrdfirnyeqhrKESEDAVKA-LAKEKDLLERE 297
Cdd:cd22656   111 ELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTAL-----------ETLEKALKDlLTDEGGAIARK 179

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907157327 298 KWE-LRRQAKEAT-DHAAALRSQLDLKDNRMKELEAELAMAKQSLATLT 344
Cdd:cd22656   180 EIKdLQKELEKLNeEYAAKLKAKIDELKALIADDEAKLAAALRLIADLT 228
PTZ00121 PTZ00121
MAEBL; Provisional
 167-332 6.85e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 6.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  167 AQVLLREEVVQLQEEVHLLRQMKEMLAKDL--EESQGGKCSEVLSATELR----------------VQLVQKEQELARAK 228
Cdd:PTZ00121  1583 AEEAKKAEEARIEEVMKLYEEEKKMKAEEAkkAEEAKIKAEELKKAEEEKkkveqlkkkeaeekkkAEELKKAEEENKIK 1662

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327  229 EALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRdfiRNYEQHRKESEDAVKA---LAKEKDLLEREKWELRRQA 305
Cdd:PTZ00121  1663 AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA---KKAEELKKKEAEEKKKaeeLKKAEEENKIKAEEAKKEA 1739

                          170       180
                   ....*....|....*....|....*..
gi 1907157327  306 KEATDHAAALRSQLDLKdNRMKELEAE 332
Cdd:PTZ00121  1740 EEDKKKAEEAKKDEEEK-KKIAHLKKE 1765
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 212-340 6.90e-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: 36.43  E-value: 6.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 212 ELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLyatlesreeqlrdfirnyEQHRKESEDAVKALAKEK 291
Cdd:pfam20492  10 ELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERL------------------EQKRQEAEEEKERLEESA 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907157327 292 DLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSL 340
Cdd:pfam20492  72 EMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 212-345 8.88e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 38.46  E-value: 8.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 212 ELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQmqqlyatlesreeqlrdfIRNYEQHRKESEDAVKALAKEK 291
Cdd:TIGR04523 360 EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK------------------IQNQEKLNQQKDEQIKKLQQEK 421

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907157327 292 DLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTK 345
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSR 475
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
171-337 9.38e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.51  E-value: 9.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 171 LREEVVQLQEEVHLLRQMKEMLAKDLEEsQGGKCSEVLSAT--ELRvQLVQKEQELARAKEALQAMKADRKRLKGEKTDL 248
Cdd:PRK03918  554 LKKKLAELEKKLDELEEELAELLKELEE-LGFESVEELEERlkELE-PFYNEYLELKDAEKELEREEKELKKLEEELDKA 631

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157327 249 VSQMQQLYATLESREEQLRDFIRNY--EQHRKESEDAVKaLAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRM 326
Cdd:PRK03918  632 FEELAETEKRLEELRKELEELEKKYseEEYEELREEYLE-LSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAK 710

                         170
                  ....*....|..
gi 1907157327 327 KELEA-ELAMAK 337
Cdd:PRK03918  711 KELEKlEKALER 722
 
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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