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Conserved domains on  [gi|303313187|ref|XP_003066605|]
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hypothetical protein CPC735_058300 [Coccidioides posadasii C735 delta SOWgp]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 117-270 3.72e-05

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


The actual alignment was detected with superfamily member COG4942:

Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.75  E-value: 3.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303313187 117 ELEAQLALVKADLKERKKEVADLIEQMEKSGRDLASRYKKVQLQTTQLAELPSSISELENTIAELRASSAnASQSPESGD 196
Cdd:COG4942   31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE-AQKEELAEL 109

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 303313187 197 VPASQTLSLQDTLALLAEREaELASLNHQLSSVGPVLPRKAREAEAAEREIAGLERRRNEVVAQARETRRRKNE 270
Cdd:COG4942  110 LRALYRLGRQPPLALLLSPE-DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
 
Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 117-270 3.72e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.75  E-value: 3.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303313187 117 ELEAQLALVKADLKERKKEVADLIEQMEKSGRDLASRYKKVQLQTTQLAELPSSISELENTIAELRASSAnASQSPESGD 196
Cdd:COG4942   31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE-AQKEELAEL 109

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 303313187 197 VPASQTLSLQDTLALLAEREaELASLNHQLSSVGPVLPRKAREAEAAEREIAGLERRRNEVVAQARETRRRKNE 270
Cdd:COG4942  110 LRALYRLGRQPPLALLLSPE-DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
SNARE_NTD_Tlg1p-like cd21444
N-terminal domain of t-SNARE affecting a late Golgi compartment protein 1 and similar proteins; ...
 136-229 2.10e-03

N-terminal domain of t-SNARE affecting a late Golgi compartment protein 1 and similar proteins; t-SNARE affecting a late Golgi compartment protein 1 (Tlg1p), also called syntaxin TLG1, is a soluble NSF attachment protein receptor (SNARE) protein (of Qc type) involved in membrane fusion, probably in retrograde traffic of cytosolic double-membrane vesicles derived from both, early and possibly late endosomes/PVC (prevacuolar compartment) back to the trans-Golgi network (TGN or late Golgi). It has been reported to function both as a (target membrane) t-SNARE and as a (vesicle) v-SNARE. The model corresponds to the N-terminal domain of Tlg1p, which consists of a three-helix bundle.


Pssm-ID: 410570 [Multi-domain]  Cd Length: 93  Bit Score: 36.79  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303313187 136 VADLIEQMEkSGRDLASRYKKVQLqTTQLAELPSSISELENTIAELRASSANASQSPESGDVPASQtlslqdtlalLAER 215
Cdd:cd21444    7 QEDAWSQLE-RLRQLLTSYLRIPT-NEAKSDFENNIQELEETIEDLKQSVEISEADPERFGLDEEE----------ISER 74

                         90
                 ....*....|....
gi 303313187 216 EAELASLNHQLSSV 229
Cdd:cd21444   75 ERIVAELESQLDDL 88
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 116-269 3.04e-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: 3.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303313187   116 VELEAQLALVKADLKERKKEVADLIEQMEKSGRDLA-------SRYKKVQLQTTQLAELPSSISELENTIAELRASSANA 188
Cdd:TIGR02168  235 EELREELEELQEELKEAEEELEELTAELQELEEKLEelrlevsELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303313187   189 SQSPESGDVPASQTLS-LQDTLALLAEREAELASLNHQLSSVGPVLPRKAREAEAAEREIAGLERRRNEVVAQARETRRR 267
Cdd:TIGR02168  315 ERQLEELEAQLEELESkLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394


                   ..
gi 303313187   268 KN 269
Cdd:TIGR02168  395 IA 396
 
Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 117-270 3.72e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.75  E-value: 3.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303313187 117 ELEAQLALVKADLKERKKEVADLIEQMEKSGRDLASRYKKVQLQTTQLAELPSSISELENTIAELRASSAnASQSPESGD 196
Cdd:COG4942   31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE-AQKEELAEL 109

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 303313187 197 VPASQTLSLQDTLALLAEREaELASLNHQLSSVGPVLPRKAREAEAAEREIAGLERRRNEVVAQARETRRRKNE 270
Cdd:COG4942  110 LRALYRLGRQPPLALLLSPE-DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
SNARE_NTD_Tlg1p-like cd21444
N-terminal domain of t-SNARE affecting a late Golgi compartment protein 1 and similar proteins; ...
 136-229 2.10e-03

N-terminal domain of t-SNARE affecting a late Golgi compartment protein 1 and similar proteins; t-SNARE affecting a late Golgi compartment protein 1 (Tlg1p), also called syntaxin TLG1, is a soluble NSF attachment protein receptor (SNARE) protein (of Qc type) involved in membrane fusion, probably in retrograde traffic of cytosolic double-membrane vesicles derived from both, early and possibly late endosomes/PVC (prevacuolar compartment) back to the trans-Golgi network (TGN or late Golgi). It has been reported to function both as a (target membrane) t-SNARE and as a (vesicle) v-SNARE. The model corresponds to the N-terminal domain of Tlg1p, which consists of a three-helix bundle.


Pssm-ID: 410570 [Multi-domain]  Cd Length: 93  Bit Score: 36.79  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303313187 136 VADLIEQMEkSGRDLASRYKKVQLqTTQLAELPSSISELENTIAELRASSANASQSPESGDVPASQtlslqdtlalLAER 215
Cdd:cd21444    7 QEDAWSQLE-RLRQLLTSYLRIPT-NEAKSDFENNIQELEETIEDLKQSVEISEADPERFGLDEEE----------ISER 74

                         90
                 ....*....|....
gi 303313187 216 EAELASLNHQLSSV 229
Cdd:cd21444   75 ERIVAELESQLDDL 88
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 116-269 3.04e-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: 3.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303313187   116 VELEAQLALVKADLKERKKEVADLIEQMEKSGRDLA-------SRYKKVQLQTTQLAELPSSISELENTIAELRASSANA 188
Cdd:TIGR02168  235 EELREELEELQEELKEAEEELEELTAELQELEEKLEelrlevsELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303313187   189 SQSPESGDVPASQTLS-LQDTLALLAEREAELASLNHQLSSVGPVLPRKAREAEAAEREIAGLERRRNEVVAQARETRRR 267
Cdd:TIGR02168  315 ERQLEELEAQLEELESkLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394


                   ..
gi 303313187   268 KN 269
Cdd:TIGR02168  395 IA 396
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 117-201 4.98e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.21  E-value: 4.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303313187 117 ELEAQLALVKADLKERKKEVADLIEQMEKSGRDLASRYKKVQLQTTQLAELPSSISELENTIAELRASSANASQSPESGD 196
Cdd:COG4942  168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247


                 ....*
gi 303313187 197 VPASQ 201
Cdd:COG4942  248 FAALK 252
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 117-270 6.80e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 37.99  E-value: 6.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303313187 117 ELEAQLALVKADLKERKKEVADLIEQMEKSGRDLASRYKKVQLQTTQLAELPSSISELENTIAELRASSANASQspesgd 196
Cdd:COG1196  264 ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE------ 337

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 303313187 197 vpasqtlSLQDTLALLAEREAELASLNHQLSSVGPVLPRKAREAEAAEREIAGLERRRNEVVAQARETRRRKNE 270
Cdd:COG1196  338 -------ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 117-271 7.90e-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: 37.44  E-value: 7.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303313187 117 ELEAQLALVKADLKERKKEVADLIEQMEKSGR--------------DLASRYKKVQLQTTQLAELpssISELENTIAELR 182
Cdd:COG4942   87 ELEKEIAELRAELEAQKEELAELLRALYRLGRqpplalllspedflDAVRRLQYLKYLAPARREQ---AEELRADLAELA 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303313187 183 ASSANASQSPESGDVPASQTLSLQDTL-ALLAEREAELASLNHQLSSVGPVLPRKAREAEAAEREIAGLERRRNEVVAQA 261
Cdd:COG4942  164 ALRAELEAERAELEALLAELEEERAALeALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243

                        170
                 ....*....|
gi 303313187 262 RETRRRKNEG 271
Cdd:COG4942  244 PAAGFAALKG 253
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 113-276 8.19e-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: 37.73  E-value: 8.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303313187   113 NDNVELEAQLALVKADLKERKKEVADLIEQMEKSGR---DLASRYKKVQLQTT-----------QLAELPSSISELENTI 178
Cdd:TIGR02168  330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAeleELESRLEELEEQLEtlrskvaqlelQIASLNNEIERLEARL 409

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303313187   179 AELRASSANASQSPESGDvPASQTLSLQDTLALLAEREAELASLNHQLSSVGPVLPRKAREAEAAEREIAGLERRRNEVV 258
Cdd:TIGR02168  410 ERLEDRRERLQQEIEELL-KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488

                          170       180
                   ....*....|....*....|
gi 303313187   259 AQAR--ETRRRKNEGESDGL 276
Cdd:TIGR02168  489 ARLDslERLQENLEGFSEGV 508
 
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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