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Conserved domains on  [gi|62078999|ref|NP_001014154|]
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TRAF3-interacting JNK-activating modulator isoform 1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CC1_T3JAM cd21912
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; ...
 190-234 2.10e-12

first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; TRAF3-interacting JNK-activating modulator (T3JAM), also called TRAF3-interacting protein 3 (TRAF3IP3), is a novel protein that specifically interacts with TRAF3 and promotes the activation of JNK. It may function as an adapter molecule that regulates TRAF3-mediated JNK activation. The model corresponds to a conserved region that shows high sequence similarity with the first CC (CC1) domain of Sarcolemmal membrane-associated protein (SLMAP), which is responsible for the binding of suppressor of IKBKE 1 (SIKE1).


:

Pssm-ID: 409288 [Multi-domain]  Cd Length: 45  Bit Score: 61.59  E-value: 2.10e-12
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 62078999 190 VLDKDIIQLSEYLKEALQRELILKQKMVILQDLLPALIRASDSSW 234
Cdd:cd21912   1 VLEKEILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 298-485 6.78e-10

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: 61.88  E-value: 6.78e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999 298 AEQQLQRAQLSLAVAEQKCQEWKSQYEALKEDWRTLGDQHRELESQLHVLQSKLQGADSRDSQMSQALRLLENEHQELQT 377
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999 378 KLESLQGDREQQSSETQDLQDQLKKSEEERQALMSRVQQLQSLLQNQSLQLREQEKLLKKDQglpvwnpKLSFDEVKPEG 457
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE-------EELEELAEELL 389

                       170       180
                ....*....|....*....|....*...
gi 62078999 458 TGKEKVEELRDQLQKETYQLQAKEKERQ 485
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLE 417
 
Name Accession Description Interval E-value
CC1_T3JAM cd21912
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; ...
 190-234 2.10e-12

first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; TRAF3-interacting JNK-activating modulator (T3JAM), also called TRAF3-interacting protein 3 (TRAF3IP3), is a novel protein that specifically interacts with TRAF3 and promotes the activation of JNK. It may function as an adapter molecule that regulates TRAF3-mediated JNK activation. The model corresponds to a conserved region that shows high sequence similarity with the first CC (CC1) domain of Sarcolemmal membrane-associated protein (SLMAP), which is responsible for the binding of suppressor of IKBKE 1 (SIKE1).


Pssm-ID: 409288 [Multi-domain]  Cd Length: 45  Bit Score: 61.59  E-value: 2.10e-12
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 62078999 190 VLDKDIIQLSEYLKEALQRELILKQKMVILQDLLPALIRASDSSW 234
Cdd:cd21912   1 VLEKEILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 298-485 6.78e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.88  E-value: 6.78e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999 298 AEQQLQRAQLSLAVAEQKCQEWKSQYEALKEDWRTLGDQHRELESQLHVLQSKLQGADSRDSQMSQALRLLENEHQELQT 377
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999 378 KLESLQGDREQQSSETQDLQDQLKKSEEERQALMSRVQQLQSLLQNQSLQLREQEKLLKKDQglpvwnpKLSFDEVKPEG 457
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE-------EELEELAEELL 389

                       170       180
                ....*....|....*....|....*...
gi 62078999 458 TGKEKVEELRDQLQKETYQLQAKEKERQ 485
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLE 417
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 241-410 9.64e-08

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: 55.06  E-value: 9.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999    241 DKLKGKLRSLENQLYTCLQKHSpwGMKKVLLDMENQRSSYEQK---AKASLQKVLEEKMCAEQQLQRAQLSLAVAEQKCQ 317
Cdd:TIGR02168  708 EELEEELEQLRKELEELSRQIS--ALRKDLARLEAEVEQLEERiaqLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999    318 EWKSQYEALKEDWRTLGDQHRELESQLHVLQSKLQGADSRDSQMSQALRLLENEHQELQTKLESLQGDREQQSSETQDLQ 397
Cdd:TIGR02168  786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE 865

                          170
                   ....*....|...
gi 62078999    398 DQLKKSEEERQAL 410
Cdd:TIGR02168  866 ELIEELESELEAL 878
PRK12704 PRK12704
phosphodiesterase; Provisional
 285-414 1.14e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999  285 KASLQKVLEEKMCAEQQLQRAQLSLAVAEQKCQ-EWKSQYEALKEDWRtlgDQHRELESQLHVLQSKLQgadSRDSQMSQ 363
Cdd:PRK12704  27 KIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALlEAKEEIHKLRNEFE---KELRERRNELQKLEKRLL---QKEENLDR 100

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62078999  364 ALRLLENEHQELQTK---LESLQGDREQQSSETQDLQDQLKK---------SEEERQALMSRV 414
Cdd:PRK12704 101 KLELLEKREEELEKKekeLEQKQQELEKKEEELEELIEEQLQelerisgltAEEAKEILLEKV 163
 
Name Accession Description Interval E-value
CC1_T3JAM cd21912
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; ...
 190-234 2.10e-12

first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; TRAF3-interacting JNK-activating modulator (T3JAM), also called TRAF3-interacting protein 3 (TRAF3IP3), is a novel protein that specifically interacts with TRAF3 and promotes the activation of JNK. It may function as an adapter molecule that regulates TRAF3-mediated JNK activation. The model corresponds to a conserved region that shows high sequence similarity with the first CC (CC1) domain of Sarcolemmal membrane-associated protein (SLMAP), which is responsible for the binding of suppressor of IKBKE 1 (SIKE1).


Pssm-ID: 409288 [Multi-domain]  Cd Length: 45  Bit Score: 61.59  E-value: 2.10e-12
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 62078999 190 VLDKDIIQLSEYLKEALQRELILKQKMVILQDLLPALIRASDSSW 234
Cdd:cd21912   1 VLEKEILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
CC1_SLMAP cd21911
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal ...
 194-254 4.20e-11

first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal membrane-associated protein (SLMAP), also called Sarcolemmal membrane-associated protein, is a cardiac tail-anchored membrane protein that may play a role during myoblast fusion. SLMAP contains an N-terminal FHA domain followed by four coiled-coil (CC) domains and a transmembrane domain. The model corresponds to the first CC (CC1) domain that is responsible for the binding of suppressor of IKBKE 1 (SIKE1).


Pssm-ID: 409287 [Multi-domain]  Cd Length: 63  Bit Score: 58.46  E-value: 4.20e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62078999 194 DIIQLSEYLKEALQRELILKQKMVILQDLLPALIRASDSSWKGQLNEDKLKGKLRSLENQL 254
Cdd:cd21911   2 ELFQLQQYLQEALHREQILEQKLETLQRLLSSTQEASESSWQALIDEDRLLSRLELLENQL 62
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 298-485 6.78e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.88  E-value: 6.78e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999 298 AEQQLQRAQLSLAVAEQKCQEWKSQYEALKEDWRTLGDQHRELESQLHVLQSKLQGADSRDSQMSQALRLLENEHQELQT 377
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999 378 KLESLQGDREQQSSETQDLQDQLKKSEEERQALMSRVQQLQSLLQNQSLQLREQEKLLKKDQglpvwnpKLSFDEVKPEG 457
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE-------EELEELAEELL 389

                       170       180
                ....*....|....*....|....*...
gi 62078999 458 TGKEKVEELRDQLQKETYQLQAKEKERQ 485
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLE 417
CC1_SLMAP-like cd21868
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar ...
 197-234 5.27e-09

first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar proteins; The family includes Sarcolemmal membrane-associated protein (SLMAP), its paralog TRAF3-interacting JNK-activating modulator (T3JAM), and similar proteins. SLMAP, also called Sarcolemmal membrane-associated protein, is a cardiac tail-anchored membrane protein that may play a role during myoblast fusion. T3JAM, also called TRAF3-interacting protein 3 (TRAF3IP3), is a novel protein that specifically interacts with TRAF3 and promotes the activation of JNK. It may function as an adapter molecule that regulates TRAF3-mediated JNK activation. SLMAP contains an N-terminal FHA domain, followed by four coiled-coil (CC) domains and a transmembrane domain. The model corresponds to the first CC (CC1) domain that is responsible for the binding of suppressor of IKBKE 1 (SIKE1).


Pssm-ID: 409286 [Multi-domain]  Cd Length: 38  Bit Score: 51.71  E-value: 5.27e-09
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 62078999 197 QLSEYLKEALQRELILKQKMVILQDLLPALIRASDSSW 234
Cdd:cd21868   1 QLNQYIQEALQREQSLENKLANLQEILEATKKAAEESW 38
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 241-410 9.64e-08

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: 55.06  E-value: 9.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999    241 DKLKGKLRSLENQLYTCLQKHSpwGMKKVLLDMENQRSSYEQK---AKASLQKVLEEKMCAEQQLQRAQLSLAVAEQKCQ 317
Cdd:TIGR02168  708 EELEEELEQLRKELEELSRQIS--ALRKDLARLEAEVEQLEERiaqLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999    318 EWKSQYEALKEDWRTLGDQHRELESQLHVLQSKLQGADSRDSQMSQALRLLENEHQELQTKLESLQGDREQQSSETQDLQ 397
Cdd:TIGR02168  786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE 865

                          170
                   ....*....|...
gi 62078999    398 DQLKKSEEERQAL 410
Cdd:TIGR02168  866 ELIEELESELEAL 878
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 242-433 1.39e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 1.39e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999 242 KLKGKLRSLENQLYtclqkhspwgmkkvLLDMENQRSSYE--QKAKASLQKVLEEkmcAEQQLQRAQLSLAVAEQKCQEW 319
Cdd:COG1196 217 ELKEELKELEAELL--------------LLKLRELEAELEelEAELEELEAELEE---LEAELAELEAELEELRLELEEL 279

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999 320 KSQYEALKEDWRTLGDQHRELESQLHVLQSKLQGADSRDSQMSQALRLLENEHQELQTKLESLQGDREQQSSETQDLQDQ 399
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359

                       170       180       190
                ....*....|....*....|....*....|....
gi 62078999 400 LKKSEEERQALMSRVQQLQSLLQNQSLQLREQEK 433
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 274-485 4.15e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 4.15e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999 274 ENQRSSYEQKAKASLQKVLEEKMCAEQQLQRAQLSLAVAEQKCQEWKSQYEALKEDWRTLGDQHRELESQLHVLQSKLQG 353
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999 354 ADSRDSQMSQALRLLENEHQELQTKLESLQGDREQQSSETQDLQDQLKKSEEERQALMSRVQQLQSLLQNQSLQLREQEK 433
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 62078999 434 LLKKDQGLPVWNPKLSFDEVKPEGTGKEKVEELRDQLQKETYQLQAKEKERQ 485
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
299-480 1.36e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.07  E-value: 1.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999  299 EQQLQRAQLSLAVAE---QKCQEWKSQYEALKEDWRTLGDQ------HRELESQLHVLQSKLQGADSRDSQmsqaLRLLE 369
Cdd:COG4913  616 EAELAELEEELAEAEerlEALEAELDALQERREALQRLAEYswdeidVASAEREIAELEAELERLDASSDD----LAALE 691

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999  370 NEHQELQTKLESLQGDREQQSSETQDLQDQLKKSEEERQALMSRVQQLqsllqnqslqlreqekllkkdQGLPVWNPKLS 449
Cdd:COG4913  692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA---------------------EDLARLELRAL 750

                        170       180       190
                 ....*....|....*....|....*....|.
gi 62078999  450 FDEVKPEGTGKEKVEELRDQLQKETYQLQAK 480
Cdd:COG4913  751 LEERFAAALGDAVERELRENLEERIDALRAR 781
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 277-414 3.19e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.06  E-value: 3.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999    277 RSSYEQKAKASLQKVLEEkmcAEQQLQRAQLSLAVAEQKCQEWKSQYEALKEDWRTLGDQHRELESQLHVLQSKLQGADS 356
Cdd:TIGR02168  219 KAELRELELALLVLRLEE---LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62078999    357 RDSQMSQALRLLENEHQELQTKLESLQGDREQQSS---------------------ETQDLQDQLKKSEEERQALMSRV 414
Cdd:TIGR02168  296 EISRLEQQKQILRERLANLERQLEELEAQLEELESkldelaeelaeleekleelkeELESLEAELEELEAELEELESRL 374
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 240-485 8.55e-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: 8.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999    240 EDKLKGKLRSLENQLYTCLQKHSPWGMKKVLLDMENQRSSYEQKAKASLQKVLE-EKMCAEQQLQRAQLSLAVAEQKCQE 318
Cdd:TIGR02168  248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEqQKQILRERLANLERQLEELEAQLEE 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999    319 WKSQYEALKEDWRTLGDQHRELESQLHVLQSKLQGADSRDSQMSQALRLLENEHQELQTKLESLQGDREQQSSETQDLQD 398
Cdd:TIGR02168  328 LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA 407

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999    399 QLKKSEEERQALmsrvqqlqsllqnqslqLREQEKLLKKDQGLPVWNPKLSFDEVKPEGTG-KEKVEELRDQLQKETYQL 477
Cdd:TIGR02168  408 RLERLEDRRERL-----------------QQEIEELLKKLEEAELKELQAELEELEEELEElQEELERLEEALEELREEL 470


                   ....*...
gi 62078999    478 QAKEKERQ 485
Cdd:TIGR02168  471 EEAEQALD 478
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 298-439 1.65e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 1.65e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999 298 AEQQLQRAQLSLAVAEQKCQEWKSQYEALKEDWRTLGDQHRELESQLHVLQSKLQGADSRDSQMSQALRLLENEHQELQ- 376
Cdd:COG1196 209 AEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQa 288

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62078999 377 ------TKLESLQGDREQQSSETQDLQDQLKKSEEERQALMSRVQQLQSLLQNQSLQLREQEKLLKKDQ 439
Cdd:COG1196 289 eeyellAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 242-438 4.96e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.21  E-value: 4.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999    242 KLKGKLRSLENQLYTCLQKhspwgmkkvLLDMENQRssyeQKAKASLQKVLEE-----KMCAEQQLQRAQLSLAVAEQK- 315
Cdd:TIGR02169  298 ELEAEIASLERSIAEKERE---------LEDAEERL----AKLEAEIDKLLAEieeleREIEEERKRRDKLTEEYAELKe 364

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999    316 ---------------CQEWKSQYEALKEDWRTLGDQHRELESQLHVLQSKLQGADSRDSQMSQALRLLENEHQELQT--- 377
Cdd:TIGR02169  365 eledlraeleevdkeFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEeke 444

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62078999    378 -----------KLESLQGDREQQSSETQDLQDQLKKSEEERQAL---MSRVQQLQSLLQNQSLQLREQEKLLKKD 438
Cdd:TIGR02169  445 dkaleikkqewKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLqreLAEAEAQARASEERVRGGRAVEEVLKAS 519
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
286-414 6.75e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 6.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999  286 ASLQKVLEEKmcaEQQLQRAQLS---LAVAEQKCQEWKSQYEALKEDWRTLGDQHRELESQLHVLQSKLQGADSRDSQMS 362
Cdd:COG4913  664 ASAEREIAEL---EAELERLDASsddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAE 740

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 62078999  363 QALRllENEHQELQTKLESLQGDrEQQSSETQDLQDQLKKSEEERQALMSRV 414
Cdd:COG4913  741 DLAR--LELRALLEERFAAALGD-AVERELRENLEERIDALRARLNRAEEEL 789
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 282-455 1.41e-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: 44.66  E-value: 1.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999    282 QKAKASLQKVLEEkmcAEQQLQRAQLSLAVAEQKCQEWKSQYEALKEDWRTLGDQHRELESQLHVLQSKLQGADSR---- 357
Cdd:TIGR02168  336 AEELAELEEKLEE---LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARlerl 412

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999    358 --------DSQMSQALRLLENEHQELQTKLESLQGDREQQSSETQDLQDQLKKSEEE----RQALMSRVQQLQSLLQNQS 425
Cdd:TIGR02168  413 edrrerlqQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEleeaEQALDAAERELAQLQARLD 492

                          170       180       190
                   ....*....|....*....|....*....|.
gi 62078999    426 LQLREQEKLLKKDQGLP-VWNPKLSFDEVKP 455
Cdd:TIGR02168  493 SLERLQENLEGFSEGVKaLLKNQSGLSGILG 523
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
241-410 4.97e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.70  E-value: 4.97e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999 241 DKLKGKLRSLENQLYTCLQKHSpwgmkkvLLDMENQRSSYEQKAKAslqkvleekmcAEQQLQRAQLSLAVAEQKCQEWK 320
Cdd:COG3206 185 PELRKELEEAEAALEEFRQKNG-------LVDLSEEAKLLLQQLSE-----------LESQLAEARAELAEAEARLAALR 246

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999 321 SQYEALKEDWRTLGD--QHRELESQLHVLQSKLQGADSR-----------DSQMSQALRLLEnehQELQTKLESLQGDRE 387
Cdd:COG3206 247 AQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARytpnhpdvialRAQIAALRAQLQ---QEAQRILASLEAELE 323

                       170       180
                ....*....|....*....|...
gi 62078999 388 QQSSETQDLQDQLKKSEEERQAL 410
Cdd:COG3206 324 ALQAREASLQAQLAQLEARLAEL 346
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 286-488 7.97e-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: 7.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999    286 ASLQKVLEEKmcaEQQLQRAQLSLAVAEQKCQEWKSQYEALKEDWRTLGDQHRELESQLHVLQSKLQGADSRDSQMSQAL 365
Cdd:TIGR02169  304 ASLERSIAEK---ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF 380

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999    366 RLLENEHQELQTKLESLQGDREQQSSETQDLQDQLKKSEEERQALMSRVQQLQSLLQNQSLQLRE-QEKLLKKDQGLPVW 444
Cdd:TIGR02169  381 AETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDkALEIKKQEWKLEQL 460

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 62078999    445 NPKLSFDEVKPEGTgKEKVEELRDQLQKETYQLQAKEKERQCSQ 488
Cdd:TIGR02169  461 AADLSKYEQELYDL-KEEYDRVEKELSKLQRELAEAEAQARASE 503
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 282-439 8.70e-04

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: 41.67  E-value: 8.70e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999 282 QKAKASLQKVLEEKMCAEQQLQRAQLSLAVAEQKCQEWKSQYEALKEDWRTLGDQHRELESQLHVLQSKL---------- 351
Cdd:COG4942  37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELaellralyrl 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999 352 ---------------QGADSRDSQMSQALRLLENEHQELQTKLESLQGDREQQSSETQDLQDQLKKSEEERQALMSRVQQ 416
Cdd:COG4942 117 grqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196

                       170       180
                ....*....|....*....|...
gi 62078999 417 LQSLLQNQSLQLREQEKLLKKDQ 439
Cdd:COG4942 197 RQKLLARLEKELAELAAELAELQ 219
PRK12704 PRK12704
phosphodiesterase; Provisional
 285-414 1.14e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999  285 KASLQKVLEEKMCAEQQLQRAQLSLAVAEQKCQ-EWKSQYEALKEDWRtlgDQHRELESQLHVLQSKLQgadSRDSQMSQ 363
Cdd:PRK12704  27 KIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALlEAKEEIHKLRNEFE---KELRERRNELQKLEKRLL---QKEENLDR 100

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62078999  364 ALRLLENEHQELQTK---LESLQGDREQQSSETQDLQDQLKK---------SEEERQALMSRV 414
Cdd:PRK12704 101 KLELLEKREEELEKKekeLEQKQQELEKKEEELEELIEEQLQelerisgltAEEAKEILLEKV 163
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
274-435 2.02e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 2.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999 274 ENQRSSYEQKAKAsLQKVLEEKMCAEQQLQRAQLSLAVAEQKCQEWK--SQYEALKEDWRTLGDQHRELESQLHVLQSKL 351
Cdd:COG4717  84 EEKEEEYAELQEE-LEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRELE 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999 352 QGADSRDSQMSQALRLLENEHQELQTK----LESLQGDREQQSSETQDLQDQLKKSEEERQALMSRVQQLQSLLQNQSLQ 427
Cdd:COG4717 163 EELEELEAELAELQEELEELLEQLSLAteeeLQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242


                ....*...
gi 62078999 428 LREQEKLL 435
Cdd:COG4717 243 ERLKEARL 250
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 288-437 2.45e-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: 2.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999    288 LQKVLEEKMcaeQQLQRAQLSLAVAE--QKCQEWKSQYEA--LKEDWRTLGDQHRELESQLHVLQSKLQGADSRDSQ--- 360
Cdd:TIGR02169  189 LDLIIDEKR---QQLERLRREREKAEryQALLKEKREYEGyeLLKEKEALERQKEAIERQLASLEEELEKLTEEISElek 265

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999    361 -MSQALRLL-----------ENEHQELQTKLESLQGDREQQSSETQDLQDQLKKSEEERQALMSRVQQLQSLLQNQSLQL 428
Cdd:TIGR02169  266 rLEEIEQLLeelnkkikdlgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREI 345


                   ....*....
gi 62078999    429 REQEKLLKK 437
Cdd:TIGR02169  346 EEERKRRDK 354
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 191-414 2.56e-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: 2.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999    191 LDKDIIQLSEYLKEALQRELILKQKMVILQDLLpALIRASDSSWKGQLNEdkLKGKLRSLENQLYTCLQKHspwgmkkvl 270
Cdd:TIGR02168  314 LERQLEELEAQLEELESKLDELAEELAELEEKL-EELKEELESLEAELEE--LEAELEELESRLEELEEQL--------- 381

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999    271 ldmENQRSSY--EQKAKASLQKVLEEkmcAEQQLQRAQLSLA--VAEQKCQEWKSQYEALKEDWRTLGDQHRELE---SQ 343
Cdd:TIGR02168  382 ---ETLRSKVaqLELQIASLNNEIER---LEARLERLEDRRErlQQEIEELLKKLEEAELKELQAELEELEEELEelqEE 455

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62078999    344 LHVLQSKLQGADSRDSQMSQALRLLENEHQELQTKLESLQGDREQQSSETQDLQdQLKKSEEERQALMSRV 414
Cdd:TIGR02168  456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVK-ALLKNQSGLSGILGVL 525
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
240-402 4.43e-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: 4.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999  240 EDKLKGKLRSLENQLYTCLQKHSpwGMKKVLLDMENQRSSYEQKAKASLQKVLEEkmcAEQQLQRAQLSLAVAEQKCQEW 319
Cdd:COG4913  297 LEELRAELARLEAELERLEARLD--ALREELDELEAQIRGNGGDRLEQLEREIER---LERELEERERRRARLEALLAAL 371

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999  320 KSQYEALKEDWRtlgDQHRELESQLHVLQSKLQGADSRDSQMSQALRLLENEHQELQTKLESLQGDREQQSSETQDLQDQ 399
Cdd:COG4913  372 GLPLPASAEEFA---ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDA 448


                 ...
gi 62078999  400 LKK 402
Cdd:COG4913  449 LAE 451
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 191-414 5.71e-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: 39.67  E-value: 5.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999    191 LDKDIIQLSEYLKEALQRELILKQKMVILQDLLPALIrasdsSWKGQLNED--KLKGKLRSLENQLytclqKHSPWGMKK 268
Cdd:TIGR02169  728 LEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE-----ARIEELEEDlhKLEEALNDLEARL-----SHSRIPEIQ 797

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999    269 VLLD-MENQRSSYE---QKAKASLQKVLEEKMCAEQQLQRAQlslavaeQKCQEWKSQYEALKEDWRTLGDQHRELESQL 344
Cdd:TIGR02169  798 AELSkLEEEVSRIEarlREIEQKLNRLTLEKEYLEKEIQELQ-------EQRIDLKEQIKSIEKEIENLNGKKEELEEEL 870

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999    345 HVLQSKLQGADSRdsqmsqaLRLLENEHQELQTKLESLQGDREQQSSETQDLQDQLKKSEEERQALMSRV 414
Cdd:TIGR02169  871 EELEAALRDLESR-------LGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 267-414 6.14e-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: 39.23  E-value: 6.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999   267 KKVLLDMENQRSSYEQKakasLQKVLEEKMCAEQQLQRAQLSLAVAEQkcqewksQYEALKEDWRTLGDQHRELESQLHV 346
Cdd:TIGR04523 383 KQEIKNLESQINDLESK----IQNQEKLNQQKDEQIKKLQQEKELLEK-------EIERLKETIIKNNSEIKDLTNQDSV 451

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62078999   347 LQSKLQGADSRDSQMSQALRLLENEHQELQTKLESLQGDREQQSSETQDLQDQLKKSEEERQALMSRV 414
Cdd:TIGR04523 452 KELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKI 519
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
282-414 6.24e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 6.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999  282 QKAKASLQKVLEEkmcAEQQLQRAQLSLAVAEQKCQEWKSQYEALKEDWRTL-GDQHRELESQLHVLQSKLQGADSRDSQ 360
Cdd:COG4913  287 QRRLELLEAELEE---LRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRAR 363

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 62078999  361 MSQALRLLeneHQELQTKLESLQGDREQQSSETQDLQDQLKKSEEERQALMSRV 414
Cdd:COG4913  364 LEALLAAL---GLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAAL 414
PTZ00121 PTZ00121
MAEBL; Provisional
 274-485 8.01e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 8.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999   274 ENQRSSYEQKAKA-SLQKVLEEKMCAEQQLQRAQLSLAVAEQ---KCQEWKSQYEALKEDWRTLGDQHRELESQLHVLQS 349
Cdd:PTZ00121 1460 EEAKKKAEEAKKAdEAKKKAEEAKKADEAKKKAEEAKKKADEakkAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEA 1539

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999   350 KLQGADSRDSQMSQALRLLENEHQElqtkleslqgDREQQSSETQDLQDQLKKSEEERQALMSRVQQLQSLLqnqslqlr 429
Cdd:PTZ00121 1540 KKAEEKKKADELKKAEELKKAEEKK----------KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLY-------- 1601

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 62078999   430 EQEKLLKKDQGLPVWNPKLSFDEVKPEGTGKEKVEELRDQLQKETYQLQAKEKERQ 485
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE 1657
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 298-485 8.59e-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: 38.59  E-value: 8.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999 298 AEQQLQRAQLSLAVAEQKCQEWKSQYEALKEDWRTLGDQHRELESQLHVLQSKLQGADSRDSQMSQALRLLENEHQELQT 377
Cdd:COG4942  18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078999 378 KLESLQGD-----REQQSSETQDLQDQLKKSEE-----ERQALMSRVQQLQSLLQNQSLQLREQEKLLKKDQglpvwnpk 447
Cdd:COG4942  98 ELEAQKEElaellRALYRLGRQPPLALLLSPEDfldavRRLQYLKYLAPARREQAEELRADLAELAALRAEL-------- 169

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 62078999 448 lsfdevkpeGTGKEKVEELRDQLQKETYQLQAKEKERQ 485
Cdd:COG4942 170 ---------EAERAELEALLAELEEERAALEALKAERQ 198
 
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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