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Conserved domains on  [gi|1720431023|ref|XP_030100097|]
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testis-expressed protein 9 isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 201-359 3.96e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.37  E-value: 3.96e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023  201 TEAQIRFLKAKLHVMQEELDSVVCECSKKEDKIQDLKSKVKNLEEDCVRQQRTVTSQQSQIEKYKNLFEEANKKCDELQQ 280
Cdd:TIGR02168  272 LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720431023  281 QLSSVERELESKRRLQKQAASSQSATEVRLNRAleeAEKYKVELSKLRQTNKDITNEDhQKIEVLKSENKKLERQKGEL 359
Cdd:TIGR02168  352 ELESLEAELEELEAELEELESRLEELEEQLETL---RSKVAQLELQIASLNNEIERLE-ARLERLEDRRERLQQEIEEL 426
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 201-359 3.96e-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: 52.37  E-value: 3.96e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023  201 TEAQIRFLKAKLHVMQEELDSVVCECSKKEDKIQDLKSKVKNLEEDCVRQQRTVTSQQSQIEKYKNLFEEANKKCDELQQ 280
Cdd:TIGR02168  272 LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720431023  281 QLSSVERELESKRRLQKQAASSQSATEVRLNRAleeAEKYKVELSKLRQTNKDITNEDhQKIEVLKSENKKLERQKGEL 359
Cdd:TIGR02168  352 ELESLEAELEELEAELEELESRLEELEEQLETL---RSKVAQLELQIASLNNEIERLE-ARLERLEDRRERLQQEIEEL 426
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 216-384 6.45e-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: 6.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023 216 QEELDSVVCECSKKEDKIQDLKSKVKNLEEDCVRQQRTVTSQQSQIEKYKNLFEEANKKCDELQQQLSSVERELESKR-R 294
Cdd:COG4942    26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKeE 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023 295 LQKQAASSQSATEVRLNRALEEAEKYKvELSKLRQTNKDITNEDHQKIEVLKSENKKLERQKGELMIGFKKQLKLIDILK 374
Cdd:COG4942   106 LAELLRALYRLGRQPPLALLLSPEDFL-DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELE 184

                         170
                  ....*....|
gi 1720431023 375 RQKMHIEAAK 384
Cdd:COG4942   185 EERAALEALK 194
46 PHA02562
endonuclease subunit; Provisional
 210-337 3.75e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 42.69  E-value: 3.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023 210 AKLHVMQEELDsvVC-EC----SKKEDKIQDLKSKVKNLeedcvrqqrtvtsqQSQIEKYKNLFEEANKKCDELQQQlSS 284
Cdd:PHA02562  275 QKVIKMYEKGG--VCpTCtqqiSEGPDRITKIKDKLKEL--------------QHSLEKLDTAIDELEEIMDEFNEQ-SK 337

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720431023 285 VERELESKRRLQKQAASSQSATEVRLNRALEEAEK----YKVELSKLRQTNKDITNE 337
Cdd:PHA02562  338 KLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAefvdNAEELAKLQDELDKIVKT 394
DUF4686 pfam15742
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ...
 208-377 1.44e-03

Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.


Pssm-ID: 464838 [Multi-domain]  Cd Length: 384  Bit Score: 40.43  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023 208 LKAKLHVMQEELDSVVCECSKKEDKIQDLKSKVKNLEEDCVRQQRTVTSQQSQIEKY---KNLFEEANKKCDELQQQLSS 284
Cdd:pfam15742  60 IKAELKQAQQKLLDSTKMCSSLTAEWKHCQQKIRELELEVLKQAQSIKSQNSLQEKLaqeKSRVADAEEKILELQQKLEH 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023 285 VereleSKRRLQKQAASSQSATEVRLNRALEEAEKYKVELSKLRQTNKDI---TNEDHQKIEVLKSENKKLERQKGELMI 361
Cdd:pfam15742 140 A-----HKVCLTDTCILEKKQLEERIKEASENEAKLKQQYQEEQQKRKLLdqnVNELQQQVRSLQDKEAQLEMTNSQQQL 214

                         170
                  ....*....|....*.
gi 1720431023 362 GFKKQLKLIDILKRQK 377
Cdd:pfam15742 215 RIQQQEAQLKQLENEK 230
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 201-359 3.96e-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: 52.37  E-value: 3.96e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023  201 TEAQIRFLKAKLHVMQEELDSVVCECSKKEDKIQDLKSKVKNLEEDCVRQQRTVTSQQSQIEKYKNLFEEANKKCDELQQ 280
Cdd:TIGR02168  272 LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720431023  281 QLSSVERELESKRRLQKQAASSQSATEVRLNRAleeAEKYKVELSKLRQTNKDITNEDhQKIEVLKSENKKLERQKGEL 359
Cdd:TIGR02168  352 ELESLEAELEELEAELEELESRLEELEEQLETL---RSKVAQLELQIASLNNEIERLE-ARLERLEDRRERLQQEIEEL 426
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 204-359 5.17e-06

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: 48.48  E-value: 5.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023 204 QIRFLKAKLHVMQEELDSVVCECSKKEDKIQDLKSKVKNLEEDCVRQQRTVTSQQSQIEKYKNLFEEANKKCDELQQQLS 283
Cdd:TIGR04523 315 ELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIN 394

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720431023 284 SVERELESKRRLQKQAASSQSATEVRLNRALEEAEKYKVELSKLRQTNKDITNEDHQKIEVLKSENKKLERQKGEL 359
Cdd:TIGR04523 395 DLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQL 470
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 216-384 6.45e-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: 6.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023 216 QEELDSVVCECSKKEDKIQDLKSKVKNLEEDCVRQQRTVTSQQSQIEKYKNLFEEANKKCDELQQQLSSVERELESKR-R 294
Cdd:COG4942    26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKeE 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023 295 LQKQAASSQSATEVRLNRALEEAEKYKvELSKLRQTNKDITNEDHQKIEVLKSENKKLERQKGELMIGFKKQLKLIDILK 374
Cdd:COG4942   106 LAELLRALYRLGRQPPLALLLSPEDFL-DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELE 184

                         170
                  ....*....|
gi 1720431023 375 RQKMHIEAAK 384
Cdd:COG4942   185 EERAALEALK 194
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 202-329 4.38e-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: 4.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023  202 EAQIRFLKAKLHVMQEELDSVVCECSKKEDKIQDLKSKVKNLEEDCVRQQRTVTSQQSQIEKYKNLFEEANKKCDELQQQ 281
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1720431023  282 LSSVERELESKRRLQKQAASSQSATEVRLNRALEEAEKYKVELSKLRQ 329
Cdd:TIGR02168  381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 195-399 5.82e-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: 5.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023 195 VSKDIGTEAQIRFLKAKLHVMQEELDSVVCECSKKEDKIQDLKSKVKNLEEDCVRQQRTVTSQQSQIEKYKNLFEEANKK 274
Cdd:COG1196   294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023 275 CDELQQQLSSVERELESKRRLQKQAASSQSATEVRLNRALEEAEKYKVELSKLRQTNKDITNEDHQKIEVLKSENKKLER 354
Cdd:COG1196   374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1720431023 355 QKGELmigfKKQLKLIDILKRQKMHIEAAKMLSFSEEEFMKALEW 399
Cdd:COG1196   454 LEEEE----EALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 202-398 1.08e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023 202 EAQIRFLKAKLHVMQEELDSVVCECSKKEDKIQDLKSKVKNLEEDCVRQQRTVTSQQSQIEKYKNLFEEANKKCDELQQQ 281
Cdd:COG1196   238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023 282 LSSVERELESKRRLQKQAASSQSATEVRLNRALEEAEKYKVELSKLRQTNKDITNEDHQKIEVLKSENKKLERQKGELmI 361
Cdd:COG1196   318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA-A 396

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1720431023 362 GFKKQLK-----LIDILKRQKMHIEAAKMLSFSEEEFMKALE 398
Cdd:COG1196   397 ELAAQLEeleeaEEALLERLERLEEELEELEEALAELEEEEE 438
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 197-360 1.27e-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: 44.29  E-value: 1.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023  197 KDIGTEAQIRFlKAKLHVMQEELDSVVCECSKKEDKIQDLKSKVKNLEEDCVRQQRT-------VTSQQSQIEKYKNLFE 269
Cdd:TIGR02169  282 KDLGEEEQLRV-KEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEieelereIEEERKRRDKLTEEYA 360

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023  270 EANKKCDELQQQLSSVERELESKRRLQKQAASSQSATEVRLN-------RALEEAEKYKVELSKLRQTNKDITNEDHQKI 342
Cdd:TIGR02169  361 ELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINelkreldRLQEELQRLSEELADLNAAIAGIEAKINELE 440

                          170
                   ....*....|....*...
gi 1720431023  343 EVLKSENKKLERQKGELM 360
Cdd:TIGR02169  441 EEKEDKALEIKKQEWKLE 458
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 202-375 1.63e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 1.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023  202 EAQIRFLKAKLHVMQEELDSVVCECSKKEDKIQDLKSKVKNLEEDcvrqqrtVTSQQSQIEKYKNLFEEANKKCDELQQQ 281
Cdd:TIGR02168  224 ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEK-------LEELRLEVSELEEEIEELQKELYALANE 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023  282 LSSVERElesKRRLQKQAASSQsATEVRLNRALEEAEKYKVELSKLRQTNKDITNEDHQKIEVLKSENKKLERQKGELMI 361
Cdd:TIGR02168  297 ISRLEQQ---KQILRERLANLE-RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372

                          170
                   ....*....|....
gi 1720431023  362 GFKKQLKLIDILKR 375
Cdd:TIGR02168  373 RLEELEEQLETLRS 386
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 225-384 1.71e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.28  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023 225 ECSKKEDKIQDLKSKVKNLEEDCVRQQRTVTSQQSQIEKYKNLFEEANKKCDELQQQLSSVERELESKR-RLQKQAASSQ 303
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERReELGERARALY 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023 304 -SATEVRLNRALEEAEKYKVELSKLRQTNKdITNEDHQKIEVLKSENKKLERQKGELMIGFKKQLKLIDILKRQKMHIEA 382
Cdd:COG3883    97 rSGGSVSYLDVLLGSESFSDFLDRLSALSK-IADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175


                  ..
gi 1720431023 383 AK 384
Cdd:COG3883   176 QQ 177
46 PHA02562
endonuclease subunit; Provisional
 210-337 3.75e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 42.69  E-value: 3.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023 210 AKLHVMQEELDsvVC-EC----SKKEDKIQDLKSKVKNLeedcvrqqrtvtsqQSQIEKYKNLFEEANKKCDELQQQlSS 284
Cdd:PHA02562  275 QKVIKMYEKGG--VCpTCtqqiSEGPDRITKIKDKLKEL--------------QHSLEKLDTAIDELEEIMDEFNEQ-SK 337

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720431023 285 VERELESKRRLQKQAASSQSATEVRLNRALEEAEK----YKVELSKLRQTNKDITNE 337
Cdd:PHA02562  338 KLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAefvdNAEELAKLQDELDKIVKT 394
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 200-359 5.66e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 5.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023  200 GTEAQIRFLKAKLHVMQEELDSVVCECSKKEDKIQDLKSKVKNLEEDCVRQQRTVTSQQSQIEKYKNLFEEANKKCDELQ 279
Cdd:TIGR02168  730 ALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR 809

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023  280 QQLSSVERELESKRRLQKQAASSQSATEVRLNRALEEAEKYKVELSKLRQTNKDIT---NEDHQKIEVLKSENKKLERQK 356
Cdd:TIGR02168  810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEeliEELESELEALLNERASLEEAL 889


                   ...
gi 1720431023  357 GEL 359
Cdd:TIGR02168  890 ALL 892
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 201-385 6.73e-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: 6.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023  201 TEAQIRFLKAKLHVMQEELDSV-------VCECSKKEDKIQDLKSKVKNL-EEDCVRQQRTVTSQQSQIEKYKNLFEEAN 272
Cdd:TIGR02169  235 LERQKEAIERQLASLEEELEKLteeiselEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKE 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023  273 KKCDELQQQLSSVERELESKRRLQKQAASSQSATEVRLNRALEEAEKYKVELSKLRQTNKDITNEDHQKIEVLKSENKKL 352
Cdd:TIGR02169  315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1720431023  353 ERQKGELMIGFKKQLKLIDILKRQKMHIEAAKM 385
Cdd:TIGR02169  395 EKLKREINELKRELDRLQEELQRLSEELADLNA 427
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 232-359 1.11e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.29  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023 232 KIQDLKSKVKNLEEDCVRQQRTVTSQQSQIEKYKNLFEEANKKCDELQQQLSSV---------ERELESKRRLQKQAASS 302
Cdd:COG1579    32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeyealQKEIESLKRRISDLEDE 111

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720431023 303 QSATEVRLNRALEEAEKYKVELSKLRQTNKDITNEDHQKIEVLKSENKKLERQKGEL 359
Cdd:COG1579   112 ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 249-398 1.21e-03

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: 41.20  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023  249 RQQRTVTSQQSQIEKYKNL---------------FEEANKKCDELQQQLSSVERELESKRRLQKQAASSQSATEVRLNRA 313
Cdd:TIGR02168  200 RQLKSLERQAEKAERYKELkaelrelelallvlrLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023  314 LEEAEKYKVELSKLRQTNKDITNEDHQKIEVLKSENKKLERQKGELMIGFKKQLKLIDILKRQKMHIEAAKMLSFSEEEF 393
Cdd:TIGR02168  280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359


                   ....*
gi 1720431023  394 MKALE 398
Cdd:TIGR02168  360 LEELE 364
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 261-382 1.39e-03

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: 40.81  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023  261 IEKYKNLFEEANKKCDELQQQLSSVE---RELESK-RRLQKQAASSQSATEV--------------RLNRALEEAEKYKV 322
Cdd:TIGR02168  167 ISKYKERRKETERKLERTRENLDRLEdilNELERQlKSLERQAEKAERYKELkaelrelelallvlRLEELREELEELQE 246

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720431023  323 ELSKLRQTNKDIT---NEDHQKIEVLKSENKKLERQKGELMIGFKKQLKLIDILKRQKMHIEA 382
Cdd:TIGR02168  247 ELKEAEEELEELTaelQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309
DUF4686 pfam15742
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ...
 208-377 1.44e-03

Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.


Pssm-ID: 464838 [Multi-domain]  Cd Length: 384  Bit Score: 40.43  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023 208 LKAKLHVMQEELDSVVCECSKKEDKIQDLKSKVKNLEEDCVRQQRTVTSQQSQIEKY---KNLFEEANKKCDELQQQLSS 284
Cdd:pfam15742  60 IKAELKQAQQKLLDSTKMCSSLTAEWKHCQQKIRELELEVLKQAQSIKSQNSLQEKLaqeKSRVADAEEKILELQQKLEH 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023 285 VereleSKRRLQKQAASSQSATEVRLNRALEEAEKYKVELSKLRQTNKDI---TNEDHQKIEVLKSENKKLERQKGELMI 361
Cdd:pfam15742 140 A-----HKVCLTDTCILEKKQLEERIKEASENEAKLKQQYQEEQQKRKLLdqnVNELQQQVRSLQDKEAQLEMTNSQQQL 214

                         170
                  ....*....|....*.
gi 1720431023 362 GFKKQLKLIDILKRQK 377
Cdd:pfam15742 215 RIQQQEAQLKQLENEK 230
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 202-359 1.58e-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: 40.82  E-value: 1.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023  202 EAQIRFLKAKLHVMQEELDSVVCECSKKEDKIQDLKSKVKNLEEDcvrqqrtvtSQQSQIEKYKNLFEEANKKCDELQQQ 281
Cdd:TIGR02169  743 EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR---------LSHSRIPEIQAELSKLEEEVSRIEAR 813

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023  282 LSSVERELEsKRRLQKQAASSQSATEVRLNRALEE---AEKYKVELSKLRQTNKDITNEDHQ-KIEVLKSENKKLERQKG 357
Cdd:TIGR02169  814 LREIEQKLN-RLTLEKEYLEKEIQELQEQRIDLKEqikSIEKEIENLNGKKEELEEELEELEaALRDLESRLGDLKKERD 892


                   ..
gi 1720431023  358 EL 359
Cdd:TIGR02169  893 EL 894
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 202-329 2.41e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.14  E-value: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023 202 EAQIRFLKAKLHVMQEELDSVVCECSKKEDKIQDLKSKVKNLEE--DCVRQQRTVTSQQSQIEKYKNLFEEANKKCDELQ 279
Cdd:COG1579    37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlGNVRNNKEYEALQKEIESLKRRISDLEDEILELM 116

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720431023 280 QQLSSVERELESKRRLQKQAASSQSATEVRLNRALEEAEKYKVELSKLRQ 329
Cdd:COG1579   117 ERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAERE 166
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 228-395 3.96e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 39.72  E-value: 3.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023  228 KKEDKIQDLKSKVKNLEEDCVrqqRTVTSQQSQIEKYKNLFEEANKKCDELQ---QQLSSVERELESKRRLQKQAASSQS 304
Cdd:pfam15921  615 KKDAKIRELEARVSDLELEKV---KLVNAGSERLRAVKDIKQERDQLLNEVKtsrNELNSLSEDYEVLKRNFRNKSEEME 691

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023  305 ATEVRLNRALEEAEKykvELSKLRQTNKDITNEDHQKIEVLKSENKKLERQKGElmigfkkqlklIDILKRQKMHIEAAK 384
Cdd:pfam15921  692 TTTNKLKMQLKSAQS---ELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQ-----------IDALQSKIQFLEEAM 757

                          170
                   ....*....|.
gi 1720431023  385 MLSFSEEEFMK 395
Cdd:pfam15921  758 TNANKEKHFLK 768
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 204-352 4.47e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 39.32  E-value: 4.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023 204 QIRFLKAKLHVMQEELDSVVCECSKKEDKIqdlKSKVKNLEEDCVRQQRTVTSQQSQIEKYKNlfeeankKCDELQQQLS 283
Cdd:pfam05483 535 QIENLEEKEMNLRDELESVREEFIQKGDEV---KCKLDKSEENARSIEYEVLKKEKQMKILEN-------KCNNLKKQIE 604

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720431023 284 SVERELESKRRLQKQAASSQSATEVRLNRALEEAEKYKVELSKLRQTNKDITNEDHQKIEVLKSENKKL 352
Cdd:pfam05483 605 NKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKL 673
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 202-368 4.82e-03

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: 39.27  E-value: 4.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023  202 EAQIRFLKAKLHVMQEELDSVVCECSKKEDKIQDLKSKVKNLEEDCVRQQRTVTSQQSQIEKYKNLFEEANKKCDELQQQ 281
Cdd:TIGR02168  322 EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023  282 LSSVERELE-SKRRLQKQaasSQSATEVRLNRALEEAEKYKVELSKLRQTNKDITNEDHQKIEVLKSEnKKLERQKGELM 360
Cdd:TIGR02168  402 IERLEARLErLEDRRERL---QQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEEL-REELEEAEQAL 477


                   ....*...
gi 1720431023  361 IGFKKQLK 368
Cdd:TIGR02168  478 DAAERELA 485
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 261-384 5.05e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 39.04  E-value: 5.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023 261 IEKYKNLFEEANKKCDELQQQLSSVERELESKRRlqkqaassqsatevRLNRALEEAEKYKVELSKLRQTNKDI------ 334
Cdd:PRK00409  504 IEEAKKLIGEDKEKLNELIASLEELERELEQKAE--------------EAEALLKEAEKLKEELEEKKEKLQEEedklle 569

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720431023 335 --TNEDHQKIEVLKSENKKLERQKGELMIGFKKQLK---LIDILKRQKMHIEAAK 384
Cdd:PRK00409  570 eaEKEAQQAIKEAKKEADEIIKELRQLQKGGYASVKaheLIEARKRLNKANEKKE 624
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 225-359 5.44e-03

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 38.95  E-value: 5.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023 225 ECSKKEDKIQDLKSKVKNLEEDCVRQQRTVTSQQSQIEKYKNLFEEANKKCDELQQQLSSVERELESKRRLQKQAASSqS 304
Cdd:pfam05557 319 ELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHN-E 397

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023 305 ATEVRLNRALEEAEKYK-------VELSKLRQTN--------KDITNEDHQKIEVLKSENKKLERQKGEL 359
Cdd:pfam05557 398 EMEAQLSVAEEELGGYKqqaqtleRELQALRQQEsladpsysKEEVDSLRRKLETLELERQRLREQKNEL 467
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 233-353 5.75e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 39.04  E-value: 5.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023 233 IQDLKSKVKNLEEDCVRQQRtvtSQQSQIEKYKNLFEEANKKCDELQQQLSSVERELESKRRLQKQAAssQSAtevrLNR 312
Cdd:PRK00409  511 IGEDKEKLNELIASLEELER---ELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEA--QQA----IKE 581

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1720431023 313 ALEEAEKYKVELSKLRQtNKDITNEDHQKIEVLKSENKKLE 353
Cdd:PRK00409  582 AKKEADEIIKELRQLQK-GGYASVKAHELIEARKRLNKANE 621
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 239-359 6.01e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 6.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023 239 KVKNLEEDCVRQQRTVTSQQSQIEKYKNLFEEANKKCDELQQQLSSVERELESKRRLQKQAASSQSATEVRLNRALEEAE 318
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1720431023 319 KYKVELSKLRQTNKDITNEDHQKIEVLKSENKKLERQKGEL 359
Cdd:COG1196   313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 201-355 7.31e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.27  E-value: 7.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023 201 TEAQIRFLKAKLHVMQEELDSVVCECSKKEDKIQDLKSKVKNLEEDCVRQQRTVTSQQSQIEK-----YKN--------- 266
Cdd:COG3883    28 LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraralYRSggsvsyldv 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023 267 ---------------LFEEANKKCDELQQQLSSVERELESKRRLQKQAASSQSATEVRLNRALEEAEKYKVELSKLRQTN 331
Cdd:COG3883   108 llgsesfsdfldrlsALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQL 187

                         170       180
                  ....*....|....*....|....
gi 1720431023 332 KDITNEDHQKIEVLKSENKKLERQ 355
Cdd:COG3883   188 SAEEAAAEAQLAELEAELAAAEAA 211
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 202-377 8.03e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 38.56  E-value: 8.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023  202 EAQIRFLKAKLHVMQEELDSVVCECSKKEDKIQDLKSKVKNL--EEDCVRQQRTVTSQQSQIEK--YKNLFEEANKKCDE 277
Cdd:pfam15921  617 DAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLlnEVKTSRNELNSLSEDYEVLKrnFRNKSEEMETTTNK 696

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023  278 LQQQLSSVERELESKRR------------------LQKQAASSQSATEVRLNRA--LEEA------EKY--KVELSKLRQ 329
Cdd:pfam15921  697 LKMQLKSAQSELEQTRNtlksmegsdghamkvamgMQKQITAKRGQIDALQSKIqfLEEAmtnankEKHflKEEKNKLSQ 776

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720431023  330 TNKDITNEDHQ---KIEVLKSENKKLERQKGELMIGFKKQ----LKLIDILKRQK 377
Cdd:pfam15921  777 ELSTVATEKNKmagELEVLRSQERRLKEKVANMEVALDKAslqfAECQDIIQRQE 831
PRK12704 PRK12704
phosphodiesterase; Provisional
 196-327 8.30e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.22  E-value: 8.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023 196 SKDIGTEAQIRFLKAKlhvmqEELDSvvcECSKKEDKIQDLKSKVKNLEEdcvrqqrTVTSQQSQIEKYKNLFEEANKKC 275
Cdd:PRK12704   55 KKEALLEAKEEIHKLR-----NEFEK---ELRERRNELQKLEKRLLQKEE-------NLDRKLELLEKREEELEKKEKEL 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720431023 276 DELQQQLSSVERELESKRRLQKQA---ASSQSATEVRlNRALEEAE-KYKVELSKL 327
Cdd:PRK12704  120 EQKQQELEKKEEELEELIEEQLQElerISGLTAEEAK-EILLEKVEeEARHEAAVL 174
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 166-377 8.81e-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: 38.51  E-value: 8.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023  166 SLAKTISRIEGQLDE--------DGLPECAEDDSFCGVSKDIGTEAQIRFLKAKLHVMQ---EELDSVVCECSKK----E 230
Cdd:TIGR02169  802 KLEEEVSRIEARLREieqklnrlTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNgkkEELEEELEELEAAlrdlE 881

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023  231 DKIQDLKSKVKNLEEDCVRQQRTVTSQQSQIEKYKNLFEEANKKCDELQQQLSSVEREleskrrlqKQAASSQSATEVRL 310
Cdd:TIGR02169  882 SRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDP--------KGEDEEIPEEELSL 953

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720431023  311 NRALEEAEKYKVELSKLrqtnKDITNEDHQKIEVLKSENKKLERQKGELMIGFKKQLKLIDILKRQK 377
Cdd:TIGR02169  954 EDVQAELQRVEEEIRAL----EPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKK 1016
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
225-340 9.70e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 38.30  E-value: 9.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431023 225 ECSKKEDKIQDLKSKVKNLEEdcvrqqrtvtsqqsQIEKYKNLFEEANKKCDELQQQLSSVERELESKRRLQKQAASSQS 304
Cdd:COG2433   407 ELTEEEEEIRRLEEQVERLEA--------------EVEELEAELEEKDERIERLERELSEARSEERREIRKDREISRLDR 472

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1720431023 305 ATEvRLNRALEEAEKYKVELSKLRQTNKDITNEDHQ 340
Cdd:COG2433   473 EIE-RLERELEEERERIEELKRKLERLKELWKLEHS 507
 
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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