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Conserved domains on  [gi|767938181|ref|XP_011532775|]
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NEDD4-binding protein 3 isoform X1 [Homo sapiens]

Protein Classification

DUF812 and Fez1 domain-containing protein( domain architecture ID 12072568)

DUF812 and Fez1 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Fez1 pfam06818
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ...
368-526 2.61e-46

Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper region with similarity to the DNA-binding domain of the cAMP-responsive activating-transcription factor 5. There is evidence that Fez1 inhibits cancer cell growth through regulation of mitosis, and that its alterations result in abnormal cell growth. Note that some family members contain more than one copy of this region.


:

Pssm-ID: 462015 [Multi-domain]  Cd Length: 198  Bit Score: 160.93  E-value: 2.61e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  368 WEVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVRLREAVRS------------------- 428
Cdd:pfam06818   3 WEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSktlelevcenelqrkknea 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  429 --LQEQAPREEAP-----------------GSCETDDCKSRGLLGEAGGSEARDsAEQLRAELLQERLRGQEQALRFEQE 489
Cdd:pfam06818  83 elLREKVGKLEEEvsglrealsdvspsgyeSVYESDEAKEQRQEEADLGSLRRE-VERLRAELREERQRRERQASSFEQE 161
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 767938181  490 RRTWQEEKERVLRYQREIQGGYMDMYRRNQALEQELR 526
Cdd:pfam06818 162 RRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
260-438 3.46e-03

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


The actual alignment was detected with superfamily member COG4717:

Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 3.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181 260 AVLPETCEELKRGLGDEDGSNP---FTQVLEERQRLWLAELKRLYVERLHEVTQKAERSERNLQLQLFMAQQEQRRLRKE 336
Cdd:COG4717   45 AMLLERLEKEADELFKPQGRKPelnLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181 337 LRAQQGLAPEPRAPGTLPEADPSARPEEEARWEVCQKTAEISLLKQQLREAQAELAQKL--------AEIFSLKTQLRGS 408
Cdd:COG4717  125 LQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLeqlslateEELQDLAEELEEL 204
                        170       180       190
                 ....*....|....*....|....*....|
gi 767938181 409 RAQAQAQDAELVRLREAVRSLQEQAPREEA 438
Cdd:COG4717  205 QQRLAELEEELEEAQEELEELEEELEQLEN 234
 
Name Accession Description Interval E-value
Fez1 pfam06818
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ...
368-526 2.61e-46

Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper region with similarity to the DNA-binding domain of the cAMP-responsive activating-transcription factor 5. There is evidence that Fez1 inhibits cancer cell growth through regulation of mitosis, and that its alterations result in abnormal cell growth. Note that some family members contain more than one copy of this region.


Pssm-ID: 462015 [Multi-domain]  Cd Length: 198  Bit Score: 160.93  E-value: 2.61e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  368 WEVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVRLREAVRS------------------- 428
Cdd:pfam06818   3 WEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSktlelevcenelqrkknea 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  429 --LQEQAPREEAP-----------------GSCETDDCKSRGLLGEAGGSEARDsAEQLRAELLQERLRGQEQALRFEQE 489
Cdd:pfam06818  83 elLREKVGKLEEEvsglrealsdvspsgyeSVYESDEAKEQRQEEADLGSLRRE-VERLRAELREERQRRERQASSFEQE 161
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 767938181  490 RRTWQEEKERVLRYQREIQGGYMDMYRRNQALEQELR 526
Cdd:pfam06818 162 RRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
278-530 2.83e-11

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: 66.62  E-value: 2.83e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181   278 GSNPFTQVLEERQRlwlaELkrlyvERLHEVTQKAERSERNLQLQLFMAQQEQRRLRKELRAQQGLAPEPRAPGTLPEAD 357
Cdd:TIGR02168  664 GSAKTNSSILERRR----EI-----EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181   358 PSARPEEEARW---------EVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVRLREAVRS 428
Cdd:TIGR02168  735 LARLEAEVEQLeeriaqlskELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL 814
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181   429 LQE---QAPREEAPGSCETDDCKSRGLLGEAGGSEARDSAEQLRAEL--LQERLRGQEQALRFEQERRTWQEEKERVLRY 503
Cdd:TIGR02168  815 LNEeaaNLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIeeLEELIEELESELEALLNERASLEEALALLRS 894
                          250       260
                   ....*....|....*....|....*...
gi 767938181   504 QREIQGGYM-DMYRRNQALEQELRALRE 530
Cdd:TIGR02168  895 ELEELSEELrELESKRSELRRELEELRE 922
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
284-530 2.31e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.34  E-value: 2.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181 284 QVLEERQRLWLAELKRLYVERLHEVTQKAERSERNLQLQLFMAQQEQRRLRKELraqqglapeprapgtlpeadpsarpe 363
Cdd:COG1196  216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL-------------------------- 269
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181 364 EEARWEVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVRLREAVRSLQEQAPREEApgsce 443
Cdd:COG1196  270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE----- 344
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181 444 tddcKSRGLLGEAGGSEA-RDSAEQLRAELLQERLRGQEQALRFEQERRTWQEEKERVLRYQREIQGGYMDMYRRNQALE 522
Cdd:COG1196  345 ----ELEEAEEELEEAEAeLAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420

                 ....*...
gi 767938181 523 QELRALRE 530
Cdd:COG1196  421 EELEELEE 428
PTZ00121 PTZ00121
MAEBL; Provisional
287-508 1.31e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  287 EERQRLWLAELKRLYVERLHEVTQKAERSERNLQlQLFMAQQEQRRlRKELRAQqglAPEPRAPGTLPEADPSARPEEEA 366
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD-ELKKAAAAKKK-ADEAKKK---AEEKKKADEAKKKAEEAKKADEA 1449
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  367 RWEVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVRLREAVRSLQEQAPREEAPGSCETDD 446
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK 1529
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767938181  447 CKSRGLLGEAGGSEARDSAEQLRAellQERLRGQEQALRFEQERRTwQEEKERVLRYQREIQ 508
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADELKK---AEELKKAEEKKKAEEAKKA-EEDKNMALRKAEEAK 1587
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
260-438 3.46e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 3.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181 260 AVLPETCEELKRGLGDEDGSNP---FTQVLEERQRLWLAELKRLYVERLHEVTQKAERSERNLQLQLFMAQQEQRRLRKE 336
Cdd:COG4717   45 AMLLERLEKEADELFKPQGRKPelnLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181 337 LRAQQGLAPEPRAPGTLPEADPSARPEEEARWEVCQKTAEISLLKQQLREAQAELAQKL--------AEIFSLKTQLRGS 408
Cdd:COG4717  125 LQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLeqlslateEELQDLAEELEEL 204
                        170       180       190
                 ....*....|....*....|....*....|
gi 767938181 409 RAQAQAQDAELVRLREAVRSLQEQAPREEA 438
Cdd:COG4717  205 QQRLAELEEELEEAQEELEELEEELEQLEN 234
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
286-435 9.62e-03

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 38.85  E-value: 9.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  286 LEERQRLWLAELKRLYvERLHEVTQKAERSERNLQL---QLFMAQQEQRRLRKELRAQQGLAPepRAPGTLPEAD----- 357
Cdd:pfam05667 329 LQQQREEELEELQEQL-EDLESSIQELEKEIKKLESsikQVEEELEELKEQNEELEKQYKVKK--KTLDLLPDAEeniak 405
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  358 -------PSARPEE-EARWEVCQKT--AEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVRLREAVR 427
Cdd:pfam05667 406 lqalvdaSAQRLVElAGQWEKHRVPliEEYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYE 485

                  ....*...
gi 767938181  428 SLQEQAPR 435
Cdd:pfam05667 486 RLPKDVSR 493
 
Name Accession Description Interval E-value
Fez1 pfam06818
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ...
368-526 2.61e-46

Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper region with similarity to the DNA-binding domain of the cAMP-responsive activating-transcription factor 5. There is evidence that Fez1 inhibits cancer cell growth through regulation of mitosis, and that its alterations result in abnormal cell growth. Note that some family members contain more than one copy of this region.


Pssm-ID: 462015 [Multi-domain]  Cd Length: 198  Bit Score: 160.93  E-value: 2.61e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  368 WEVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVRLREAVRS------------------- 428
Cdd:pfam06818   3 WEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSktlelevcenelqrkknea 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  429 --LQEQAPREEAP-----------------GSCETDDCKSRGLLGEAGGSEARDsAEQLRAELLQERLRGQEQALRFEQE 489
Cdd:pfam06818  83 elLREKVGKLEEEvsglrealsdvspsgyeSVYESDEAKEQRQEEADLGSLRRE-VERLRAELREERQRRERQASSFEQE 161
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 767938181  490 RRTWQEEKERVLRYQREIQGGYMDMYRRNQALEQELR 526
Cdd:pfam06818 162 RRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
278-530 2.83e-11

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: 66.62  E-value: 2.83e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181   278 GSNPFTQVLEERQRlwlaELkrlyvERLHEVTQKAERSERNLQLQLFMAQQEQRRLRKELRAQQGLAPEPRAPGTLPEAD 357
Cdd:TIGR02168  664 GSAKTNSSILERRR----EI-----EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181   358 PSARPEEEARW---------EVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVRLREAVRS 428
Cdd:TIGR02168  735 LARLEAEVEQLeeriaqlskELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL 814
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181   429 LQE---QAPREEAPGSCETDDCKSRGLLGEAGGSEARDSAEQLRAEL--LQERLRGQEQALRFEQERRTWQEEKERVLRY 503
Cdd:TIGR02168  815 LNEeaaNLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIeeLEELIEELESELEALLNERASLEEALALLRS 894
                          250       260
                   ....*....|....*....|....*...
gi 767938181   504 QREIQGGYM-DMYRRNQALEQELRALRE 530
Cdd:TIGR02168  895 ELEELSEELrELESKRSELRRELEELRE 922
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
284-530 2.31e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.34  E-value: 2.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181 284 QVLEERQRLWLAELKRLYVERLHEVTQKAERSERNLQLQLFMAQQEQRRLRKELraqqglapeprapgtlpeadpsarpe 363
Cdd:COG1196  216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL-------------------------- 269
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181 364 EEARWEVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVRLREAVRSLQEQAPREEApgsce 443
Cdd:COG1196  270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE----- 344
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181 444 tddcKSRGLLGEAGGSEA-RDSAEQLRAELLQERLRGQEQALRFEQERRTWQEEKERVLRYQREIQGGYMDMYRRNQALE 522
Cdd:COG1196  345 ----ELEEAEEELEEAEAeLAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420

                 ....*...
gi 767938181 523 QELRALRE 530
Cdd:COG1196  421 EELEELEE 428
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
284-530 6.05e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.79  E-value: 6.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181 284 QVLEERQRLWLAELkrlyvERLHEVTQKAERSERNLQLQLFMAQQEQRRLRKELRAQQGLAPEprapgtlpeadpSARPE 363
Cdd:COG1196  256 EELEAELAELEAEL-----EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE------------LEERL 318
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181 364 EEARWEVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVRLREAVRSLQEQAPREEApgscE 443
Cdd:COG1196  319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR----A 394
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181 444 TDDCKSRgllgEAGGSEARDSAEQLRAELLQERLRGQEQALRFEQERRTWQEEKERVLRYQREIQggymdmyRRNQALEQ 523
Cdd:COG1196  395 AAELAAQ----LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE-------EEEEALLE 463

                 ....*..
gi 767938181 524 ELRALRE 530
Cdd:COG1196  464 LLAELLE 470
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
287-529 1.68e-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: 1.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  287 EERQRLWLAELKRLYVERLHEVTQKAERSERNLQLQLFMAQQEQRRLRKELRAQQGLApeprapgtlpeadpsARPEEEA 366
Cdd:COG4913   247 AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAEL---------------ARLEAEL 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  367 RwevcQKTAEISLLKQQLREAQAELAQ-KLAEIFSLKTQLRGSRAQAQAQDAELVRLREAVRSLQEQAPreeapgscetd 445
Cdd:COG4913   312 E----RLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLP----------- 376
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  446 dcksrglLGEAGGSEARDSAEQLRAELlqERLRGQEQALRFEQERRTWQEEKERvlryqreiqggymdmyrrnQALEQEL 525
Cdd:COG4913   377 -------ASAEEFAALRAEAAALLEAL--EEELEALEEALAEAEAALRDLRREL-------------------RELEAEI 428

                  ....
gi 767938181  526 RALR 529
Cdd:COG4913   429 ASLE 432
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
283-543 1.72e-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: 47.76  E-value: 1.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181   283 TQVLEERQRLWLAELKRLY--VERLHEVTQKAER--SERNLQLQLFMA--QQEQRRLRKELRAQQglapeprapgtlPEA 356
Cdd:TIGR02169  250 EEELEKLTEEISELEKRLEeiEQLLEELNKKIKDlgEEEQLRVKEKIGelEAEIASLERSIAEKE------------REL 317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181   357 DPSARPEEEARWEVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVRLREAVRSLQ---EQA 433
Cdd:TIGR02169  318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYReklEKL 397
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181   434 PREEAPGSCETDDCKSRGLLGEAGGSEARDSAEQLRAELLQERLRGQEQALRFEQERRTWQEEKERVLRYQREI---QGG 510
Cdd:TIGR02169  398 KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELydlKEE 477
                          250       260       270
                   ....*....|....*....|....*....|...
gi 767938181   511 YMDMYRRNQALEQELRALREPPTPWSPRLESSK 543
Cdd:TIGR02169  478 YDRVEKELSKLQRELAEAEAQARASEERVRGGR 510
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
288-530 5.33e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 5.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181   288 ERQRLWLAELKRLYVERLHEV-TQKAERSERNLQLQ--LFMAQQEQRRLRKELRAQQglapeprapgtlpeadpsaRPEE 364
Cdd:TIGR02168  252 EEELEELTAELQELEEKLEELrLEVSELEEEIEELQkeLYALANEISRLEQQKQILR-------------------ERLA 312
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181   365 EARWEVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVRLREAVRSLQEQAPREEApgscET 444
Cdd:TIGR02168  313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS----KV 388
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181   445 DDCKSRGLLGEAGGSEARDSAEQL--RAELLQERLRGQEQALRfEQERRTWQEEKERVLRYQREIQGGYMDMYRRNQALE 522
Cdd:TIGR02168  389 AQLELQIASLNNEIERLEARLERLedRRERLQQEIEELLKKLE-EAELKELQAELEELEEELEELQEELERLEEALEELR 467

                   ....*...
gi 767938181   523 QELRALRE 530
Cdd:TIGR02168  468 EELEEAEQ 475
PTZ00121 PTZ00121
MAEBL; Provisional
287-508 1.31e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  287 EERQRLWLAELKRLYVERLHEVTQKAERSERNLQlQLFMAQQEQRRlRKELRAQqglAPEPRAPGTLPEADPSARPEEEA 366
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD-ELKKAAAAKKK-ADEAKKK---AEEKKKADEAKKKAEEAKKADEA 1449
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  367 RWEVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVRLREAVRSLQEQAPREEAPGSCETDD 446
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK 1529
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767938181  447 CKSRGLLGEAGGSEARDSAEQLRAellQERLRGQEQALRFEQERRTwQEEKERVLRYQREIQ 508
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADELKK---AEELKKAEEKKKAEEAKKA-EEDKNMALRKAEEAK 1587
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
284-530 3.58e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 43.57  E-value: 3.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  284 QVLEERQRLWLAELKRLYVERLHEV-----TQKAERSERNLQLQLFMAQQEQRRL-RKELRAQQglaPEPRAPGTLPEAD 357
Cdd:pfam17380 326 QAEMDRQAAIYAEQERMAMERERELerirqEERKRELERIRQEEIAMEISRMRELeRLQMERQQ---KNERVRQELEAAR 402
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  358 PSARPEEEARWEVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVRLREAVRSLQEQAPREE 437
Cdd:pfam17380 403 KVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKE 482
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  438 APGSCETDDCKSRGLLGEAGGSEARDSAEQLRAELLQERLRGQEQALRFEQERRTWQEE--KERVLRYQREIQGGYM--- 512
Cdd:pfam17380 483 KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEErrKQQEMEERRRIQEQMRkat 562
                         250
                  ....*....|....*...
gi 767938181  513 DMYRRNQALEQELRALRE 530
Cdd:pfam17380 563 EERSRLEAMEREREMMRQ 580
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
312-530 4.57e-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: 42.83  E-value: 4.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181 312 AERSERNLQLQLFMAQQEQRRLRKELRAQQglapeprapgtlpeadpsaRPEEEARWEVCQKTAEISLLKQQLREAQAEL 391
Cdd:COG4942   18 QADAAAEAEAELEQLQQEIAELEKELAALK-------------------KEEKALLKQLAALERRIAALARRIRALEQEL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181 392 AQKLAEIFSLKTQLRGSRAQAQAQDAELVRLREAVRSLQEQAPREEAPGSCETDDCKSRGLLGEAGGSEARDSAEQLRA- 470
Cdd:COG4942   79 AALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAd 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767938181 471 --ELLQERLRGQEQALRFEQERRTWQEEKERVLRYQREIQGGYMDMYRRNQALEQELRALRE 530
Cdd:COG4942  159 laELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
301-529 5.56e-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: 42.74  E-value: 5.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181   301 YVERLHEVTQKAERSERNL------------QLQLFMAQQEQ----RRLRKELRAqqglapeprapgtlpeadpsarpee 364
Cdd:TIGR02168  170 YKERRKETERKLERTRENLdrledilnelerQLKSLERQAEKaeryKELKAELRE------------------------- 224
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181   365 earwevcqktAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVRLREAVRSLQEQAprEEAPG---- 440
Cdd:TIGR02168  225 ----------LELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEI--EELQKelya 292
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181   441 -SCETDDCKSRGLLGEAGGSEARDSAEQL---RAELLQERLRGQEQALRFEQERRTWQEEKERVLRYQREIQGGYMDMYR 516
Cdd:TIGR02168  293 lANEISRLEQQKQILRERLANLERQLEELeaqLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
                          250
                   ....*....|...
gi 767938181   517 RNQALEQELRALR 529
Cdd:TIGR02168  373 RLEELEEQLETLR 385
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
250-508 6.32e-04

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 42.57  E-value: 6.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  250 FSCSSAEEMGAVLPETCEELKRGLGDEDGSNPFTQVLEERQrlwlAELKRL--YVERLHEVTQKAERSERNLQLQLFMAQ 327
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERE----TELERMkeRAKKAGAQRKEEEAERKQLQAKLQQTE 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  328 QEQRRLRKELRAqqglapeprAPGTLPEADPSArpeeearwevcqktaeisllkQQLREAQAELAQKLAeifslktqlrg 407
Cdd:pfam07888 185 EELRSLSKEFQE---------LRNSLAQRDTQV---------------------LQLQDTITTLTQKLT----------- 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  408 sraQAQAQDAELVRLREAVRSLQEQAPREEAPGSCETDDCKSRGLLGEAGGSE---ARDSAEQLRAELLQERLRGQEQAL 484
Cdd:pfam07888 224 ---TAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAElhqARLQAAQLTLQLADASLALREGRA 300
                         250       260
                  ....*....|....*....|....*...
gi 767938181  485 RFEQERRTWQE----EKERVLRYQREIQ 508
Cdd:pfam07888 301 RWAQERETLQQsaeaDKDRIEKLSAELQ 328
mukB PRK04863
chromosome partition protein MukB;
286-535 7.68e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 42.64  E-value: 7.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  286 LEERQRLwlAELKRLYVERLHEVTQKAERSERNLQLQLFMAQQ----EQRRLRKELRAQQGLApEPRAPGTLPEADPSAR 361
Cdd:PRK04863  364 LEEQNEV--VEEADEQQEENEARAEAAEEEVDELKSQLADYQQaldvQQTRAIQYQQAVQALE-RAKQLCGLPDLTADNA 440
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  362 PE--EEARWEVCQKTAEISLLKQQLREAQAELAQkLAEIFSLKTQLRGSRAQAQAQDAELVRLREAvRSLQEQAPREEAp 439
Cdd:PRK04863  441 EDwlEEFQAKEQEATEELLSLEQKLSVAQAAHSQ-FEQAYQLVRKIAGEVSRSEAWDVARELLRRL-REQRHLAEQLQQ- 517
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  440 gscetddckSRGLLGEAGGS-EARDSAEQLRAELLQERLRGQEQALRFEQERRTWQEEKERVLRYQREIQGGYMDMYRRN 518
Cdd:PRK04863  518 ---------LRMRLSELEQRlRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQL 588
                         250
                  ....*....|....*..
gi 767938181  519 QALEQELRALREPPTPW 535
Cdd:PRK04863  589 EQLQARIQRLAARAPAW 605
PTZ00121 PTZ00121
MAEBL; Provisional
296-499 1.01e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  296 ELKRLYVERLHEVTQKAERSERNLQLQLFMAQQ-EQRRLRKELRAQQGL--APEPRAPGTLPEADPSARPEEEAR-WEVC 371
Cdd:PTZ00121 1241 EAKKAEEERNNEEIRKFEEARMAHFARRQAAIKaEEARKADELKKAEEKkkADEAKKAEEKKKADEAKKKAEEAKkADEA 1320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  372 QKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVRLR---------EAVRSLQEQAPREEAPGSC 442
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKkeeakkkadAAKKKAEEKKKADEAKKKA 1400
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767938181  443 ETDDCKSRGLLGEAggsEARDSAEQLRAEllQERLRGQEQALRFEQERRTWQEEKER 499
Cdd:PTZ00121 1401 EEDKKKADELKKAA---AAKKKADEAKKK--AEEKKKADEAKKKAEEAKKADEAKKK 1452
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
302-496 1.47e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  302 VERLHEVTQKAERSERNLQLQLFMAQQEQRRLRKELRAQQGLAPEPRAPGTLPEADpsarpEEEARWEVcQKTA------ 375
Cdd:COG4913   612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE-----REIAELEA-ELERldassd 685
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  376 EISLLKQQLREAQAELAQKLAEIfslkTQLRGSRAQAQAQDAELVRLREAVRSLQEQAPREEAPGSCETDDCKSRGLLGE 455
Cdd:COG4913   686 DLAALEEQLEELEAELEELEEEL----DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGD 761
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 767938181  456 AGGSEARDSAEQLRAElLQERLRGQEQALR--FEQERRTWQEE 496
Cdd:COG4913   762 AVERELRENLEERIDA-LRARLNRAEEELEraMRAFNREWPAE 803
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
283-539 1.48e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 41.48  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  283 TQVLEERQRLWLAELKRLYVERLHEVTQKA----ERSErnlqlqlfmAQQEQRRLRKELRAQQGLAP-EPRAPGTLPEAD 357
Cdd:COG3096   455 EEVLELEQKLSVADAARRQFEKAYELVCKIagevERSQ---------AWQTARELLRRYRSQQALAQrLQQLRAQLAELE 525
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  358 PSARPEEEARW---EVCQKTA-------EISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVRLREAVR 427
Cdd:COG3096   526 QRLRQQQNAERlleEFCQRIGqqldaaeELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWL 605
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  428 SLQEQAPReeapgscetddcksrglLGEAGGSEARDSAE--QLRAELLqerlrgqeqalrfEQERRTWQEEKERVlryqr 505
Cdd:COG3096   606 AAQDALER-----------------LREQSGEALADSQEvtAAMQQLL-------------EREREATVERDELA----- 650
                         250       260       270
                  ....*....|....*....|....*....|....
gi 767938181  506 eiqggymdmyRRNQALEQELRALREPPTPWSPRL 539
Cdd:COG3096   651 ----------ARKQALESQIERLSQPGGAEDPRL 674
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
287-495 1.72e-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: 1.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181   287 EERQRLWLAELKRLYVERLHEVTQKAERSERNL-QLQLFMAQQEQRR--LRKELRAQQGLAPEPRApgtlpEADPSARPE 363
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIeELEAQIEQLKEELkaLREALDELRAELTLLNE-----EAANLRERL 826
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181   364 EEARWEVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVRLREAVRSLQEQApreeapgscE 443
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL---------E 897
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 767938181   444 TDDCKSRGLLGEAggSEARDSAEQLRAELLQERLRGQEqalrFEQERRTWQE 495
Cdd:TIGR02168  898 ELSEELRELESKR--SELRRELEELREKLAQLELRLEG----LEVRIDNLQE 943
PTZ00121 PTZ00121
MAEBL; Provisional
296-524 1.99e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  296 ELKRLYVERLHEVTQKAERSERNLQLQlFMAQQEQRRLRKELRAQQGLAPEPRAPGTLPEADpSARPEEEARW--EVCQK 373
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEDK-NMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE-EAKKAEEAKIkaEELKK 1627
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  374 TAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVRLREAVRSLQEQAPREEAPGSCETDDCKSRGLL 453
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEEL 1707
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767938181  454 GEAGGSEARdSAEQLRAELlQERLRGQEQALRFEQE--------RRTwQEEKERVLRYQREIQGGYMDMYRRNQALEQE 524
Cdd:PTZ00121 1708 KKKEAEEKK-KAEELKKAE-EENKIKAEEAKKEAEEdkkkaeeaKKD-EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
296-529 2.09e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 40.98  E-value: 2.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181   296 ELKRLYVERLHEVTQ----KAERSERNLQLQLFMAQQEQRRL---RKELRAQQglAPEPRAPGTLPEADPSARP---EEE 365
Cdd:pfam12128  586 DLKRIDVPEWAASEEelreRLDKAEEALQSAREKQAAAEEQLvqaNGELEKAS--REETFARTALKNARLDLRRlfdEKQ 663
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181   366 ARWEVCQK--TAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQ------------DAELVRLREAVRSLQE 431
Cdd:pfam12128  664 SEKDKKNKalAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEkqaywqvvegalDAQLALLKAAIAARRS 743
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181   432 QAPREEApgSCETD---DCKSRGLLGEAGGSEARDSAEqLRAELLQERLRGQE-------QALRFEQERRTWQEEKERVL 501
Cdd:pfam12128  744 GAKAELK--ALETWykrDLASLGVDPDVIAKLKREIRT-LERKIERIAVRRQEvlryfdwYQETWLQRRPRLATQLSNIE 820
                          250       260       270
                   ....*....|....*....|....*....|..
gi 767938181   502 RYQREIQGGY----MDMYRRNQALEQELRALR 529
Cdd:pfam12128  821 RAISELQQQLarliADTKLRRAKLEMERKASE 852
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
411-530 2.15e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  411 QAQAQDAELVRLREAVRSLQEQAPR-EEAPGSCET-DDCKSRGLLGEAGGSEARDSAEQLRAELLQERLRGQEQAL---- 484
Cdd:COG4913   229 ALVEHFDDLERAHEALEDAREQIELlEPIRELAERyAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELarle 308
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 767938181  485 ----RFEQERRTwQEEKERVLRYQREIQGGymdmyRRNQALEQELRALRE 530
Cdd:COG4913   309 aeleRLEARLDA-LREELDELEAQIRGNGG-----DRLEQLEREIERLER 352
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
284-509 2.48e-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: 2.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181   284 QVLEERQRLWLAELKRLYVERlhevtQKAERSERNLQLQLFMAQQEQRRLRKELRAQQGLAPEPRApgtlpeadpsARPE 363
Cdd:TIGR02168  305 QILRERLANLERQLEELEAQL-----EELESKLDELAEELAELEEKLEELKEELESLEAELEELEA----------ELEE 369
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181   364 EEARWEVCQKTAEisllkqQLREAQAELAQKLAeifSLKTQLRGSRAQAQAQDAELVRLREAVRSLQEQAPREEAPGSCE 443
Cdd:TIGR02168  370 LESRLEELEEQLE------TLRSKVAQLELQIA---SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQA 440
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767938181   444 TDDCKSRGLLgeagGSEARDSAEQLRAELLQERLRGQEQALR-FEQERRTWQEEKERVLRYQREIQG 509
Cdd:TIGR02168  441 ELEELEEELE----ELQEELERLEEALEELREELEEAEQALDaAERELAQLQARLDSLERLQENLEG 503
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
260-438 3.46e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 3.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181 260 AVLPETCEELKRGLGDEDGSNP---FTQVLEERQRLWLAELKRLYVERLHEVTQKAERSERNLQLQLFMAQQEQRRLRKE 336
Cdd:COG4717   45 AMLLERLEKEADELFKPQGRKPelnLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181 337 LRAQQGLAPEPRAPGTLPEADPSARPEEEARWEVCQKTAEISLLKQQLREAQAELAQKL--------AEIFSLKTQLRGS 408
Cdd:COG4717  125 LQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLeqlslateEELQDLAEELEEL 204
                        170       180       190
                 ....*....|....*....|....*....|
gi 767938181 409 RAQAQAQDAELVRLREAVRSLQEQAPREEA 438
Cdd:COG4717  205 QQRLAELEEELEEAQEELEELEEELEQLEN 234
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
284-432 3.92e-03

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 39.65  E-value: 3.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181 284 QVLEERQRLWLAELKrlyVERLhEVTQKAERSERNLQLQLFMAQQEQRRLRKELRAQQGLAPEprapGTLPEADpsarpE 363
Cdd:COG1566   84 ALAQAEAQLAAAEAQ---LARL-EAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKK----GAVSQQE-----L 150
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767938181 364 EEARwevcqktaeisllkQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQdAELVRLREAVRSLQEQ 432
Cdd:COG1566  151 DEAR--------------AALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQ-AQVAQAEAALAQAELN 204
PTZ00121 PTZ00121
MAEBL; Provisional
271-498 4.43e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 4.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  271 RGLGDEDGSNPFTQVLEERQRLWLAELKRLYVERLHEVTQKAE----------RSERNLQLQLFMAQQEQRRLRKELRAQ 340
Cdd:PTZ00121 1070 EGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEearkaeeakkKAEDARKAEEARKAEDARKAEEARKAE 1149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  341 QGLAPE-PRAPGTLPEADPSARPEEEARWEVCQKTAEISLlKQQLREAQ----AELAQKLAEIfslkTQLRGSRAQAQAQ 415
Cdd:PTZ00121 1150 DAKRVEiARKAEDARKAEEARKAEDAKKAEAARKAEEVRK-AEELRKAEdarkAEAARKAEEE----RKAEEARKAEDAK 1224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  416 DAELVRLREAVRSLQEQAPR-------EEAPGSCETDDCKSRGLLGEAGGSEARDSAEQLRAELLQ--ERLRGQEQALRF 486
Cdd:PTZ00121 1225 KAEAVKKAEEAKKDAEEAKKaeeernnEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKkaDEAKKAEEKKKA 1304
                         250
                  ....*....|..
gi 767938181  487 EQERRTWQEEKE 498
Cdd:PTZ00121 1305 DEAKKKAEEAKK 1316
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
347-543 4.87e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 39.95  E-value: 4.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181   347 PRAPGTLPEADPSARPEEEARWEVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRgsraQAQAQDAELVRLREAV 426
Cdd:TIGR00618  211 PCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIE----ELRAQEAVLEETQERI 286
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181   427 RSLQEQAPREEAPGSCETDDCKSRGLLGEAggsearDSAEQLRAELLQERLRGQEQALRFEQERR---TWQEEKERvLRY 503
Cdd:TIGR00618  287 NRARKAAPLAAHIKAVTQIEQQAQRIHTEL------QSKMRSRAKLLMKRAAHVKQQSSIEEQRRllqTLHSQEIH-IRD 359
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 767938181   504 QREIQGGYMDMYRRNQALEQELRALREPPTPWSPRLESSK 543
Cdd:TIGR00618  360 AHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLC 399
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
380-530 6.32e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.23  E-value: 6.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181 380 LKQQLREAQAELAQKLAEI--FSLKTQLRGSRAQAQAQDAELVRLREAVRSLQEQ-----APREEAPGSCETDDCKSRGL 452
Cdd:COG3206  180 LEEQLPELRKELEEAEAALeeFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAElaeaeARLAALRAQLGSGPDALPEL 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181 453 LGEAGGSEARDSAEQLRAELLQERLRGQE-----QALRfEQERRTWQEEKERVLRYQREIQGGYMDMYRRNQALEQELRA 527
Cdd:COG3206  260 LQSPVIQQLRAQLAELEAELAELSARYTPnhpdvIALR-AQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQ 338

                 ...
gi 767938181 528 LRE 530
Cdd:COG3206  339 LEA 341
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
377-530 6.45e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 6.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181 377 ISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVRLREAVRSLQEQAPREEApgscETDDCKSRGLLGEA 456
Cdd:COG4372   26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNE----QLQAAQAELAQAQE 101
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767938181 457 GGSEARDSAEQLRAELlqERLRGQEQALrfeqerrtwQEEKERVLRYQREIQGGYMDMYRRNQALEQELRALRE 530
Cdd:COG4372  102 ELESLQEEAEELQEEL--EELQKERQDL---------EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
286-438 7.09e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.98  E-value: 7.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181 286 LEERQRLWLAELKRL--YVERLHEVTQKAERSERNLQLQLFMAQQEQRRLRKELRAQQG-LAPEPRAPGTLPEADP---- 358
Cdd:COG4942   46 LKKEEKALLKQLAALerRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEeLAELLRALYRLGRQPPlall 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181 359 --SARPEEEARWEVCQKTAEISLLKQ--QLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVRLREAVRSLQEQAP 434
Cdd:COG4942  126 lsPEDFLDAVRRLQYLKYLAPARREQaeELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLE 205

                 ....
gi 767938181 435 REEA 438
Cdd:COG4942  206 KELA 209
PTZ00121 PTZ00121
MAEBL; Provisional
302-499 7.98e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 7.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  302 VERLHEVTQK---AERSERNLQLQLFMAQQEQRRLRKELRAQQGLAPEPRAPGTLPEADPSARPEEEARWEVCQKTAEis 378
Cdd:PTZ00121 1229 VKKAEEAKKDaeeAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADE-- 1306
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  379 lLKQQLREA-QAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVRLREAVRSLQEQAPREEApgscETDDCKSrgllgeag 457
Cdd:PTZ00121 1307 -AKKKAEEAkKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA----EAAEKKK-------- 1373
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 767938181  458 gSEARDSAEQLRAElLQERLRGQEQALRFEQERRTWQEEKER 499
Cdd:PTZ00121 1374 -EEAKKKADAAKKK-AEEKKKADEAKKKAEEDKKKADELKKA 1413
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
286-435 9.62e-03

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 38.85  E-value: 9.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  286 LEERQRLWLAELKRLYvERLHEVTQKAERSERNLQL---QLFMAQQEQRRLRKELRAQQGLAPepRAPGTLPEAD----- 357
Cdd:pfam05667 329 LQQQREEELEELQEQL-EDLESSIQELEKEIKKLESsikQVEEELEELKEQNEELEKQYKVKK--KTLDLLPDAEeniak 405
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938181  358 -------PSARPEE-EARWEVCQKT--AEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVRLREAVR 427
Cdd:pfam05667 406 lqalvdaSAQRLVElAGQWEKHRVPliEEYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYE 485

                  ....*...
gi 767938181  428 SLQEQAPR 435
Cdd:pfam05667 486 RLPKDVSR 493
 
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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