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Conserved domains on  [gi|1720399156|ref|XP_030107016|]
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leucine zipper putative tumor suppressor 3 isoform X3 [Mus musculus]

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 ...
 351-551 7.04e-72

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: 229.11  E-value: 7.04e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 351 TKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFGSKQASLELSEGELPPAC- 429
Cdd:pfam06818   1 TKWEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSKTLELEVCENELQRKKn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 430 ------------------LKPALTPVDLVEPQEAlasCESDEAKMRRQAGVAaaaslvsvdgeveaggeggTRALRREVG 491
Cdd:pfam06818  81 eaellrekvgkleeevsgLREALSDVSPSGYESV---YESDEAKEQRQEEAD-------------------LGSLRREVE 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 492 RLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQLERRLR 551
Cdd:pfam06818 139 RLRAELREERQRRERQASSFEQERRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
CCDC22 super family cl25503
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 255-406 4.63e-07

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.


The actual alignment was detected with superfamily member pfam05667:

Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 52.72  E-value: 4.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 255 LEQSEAAVAQVLEERQKAWERELAELRQgcsgKLQQVARRAQRAQQGLQLQVLRLqqdkKQLQEEAAQLIRQREELEDKV 334
Cdd:pfam05667 315 ATSSPPTKVETEEELQQQREEELEELQE----QLEDLESSIQELEKEIKKLESSI----KQVEEELEELKEQNEELEKQY 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 335 AVcqKEQA-DFLPRMEE--------------------TKWEVCQKA--GEISLLKQQLKDSQADVSQKLSEIVGLRSQLR 391
Cdd:pfam05667 387 KV--KKKTlDLLPDAEEniaklqalvdasaqrlvelaGQWEKHRVPliEEYRALKEAKSNKEDESQRKLEEIKELREKIK 464

                         170
                  ....*....|....*...
gi 1720399156 392 EGRASLREKEE---QLLS 406
Cdd:pfam05667 465 EVAEEAKQKEElykQLVA 482
 
Name Accession Description Interval E-value
Fez1 pfam06818
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ...
 351-551 7.04e-72

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: 229.11  E-value: 7.04e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 351 TKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFGSKQASLELSEGELPPAC- 429
Cdd:pfam06818   1 TKWEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSKTLELEVCENELQRKKn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 430 ------------------LKPALTPVDLVEPQEAlasCESDEAKMRRQAGVAaaaslvsvdgeveaggeggTRALRREVG 491
Cdd:pfam06818  81 eaellrekvgkleeevsgLREALSDVSPSGYESV---YESDEAKEQRQEEAD-------------------LGSLRREVE 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 492 RLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQLERRLR 551
Cdd:pfam06818 139 RLRAELREERQRRERQASSFEQERRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 235-534 8.88e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.96  E-value: 8.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 235 QELEERLWEKEQEVAALR-RSLEQSEAAVAQVLEERQKAWERELAELRQgCSGKLQQVARRAQRAQQGLqlqvlrlqqdk 313
Cdd:COG1196   216 RELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAE-LEAELEELRLELEELELEL----------- 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 314 KQLQEEAAQLIRQREELEDKVAVCQKEQADFLPRMEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREG 393
Cdd:COG1196   284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 394 RASLREKEEQLLSLRDSFGSKQASLELSEGELppaclkpALTPVDLVEPQEALASCESDEAKMRRQAGVAAAASLvsVDG 473
Cdd:COG1196   364 EEALLEAEAELAEAEEELEELAEELLEALRAA-------AELAAQLEELEEAEEALLERLERLEEELEELEEALA--ELE 434

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720399156 474 EVEAGGEGGTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQL 534
Cdd:COG1196   435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 231-532 3.57e-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: 56.60  E-value: 3.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  231 SALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVleerqkawERELAELRQGCSGKLQQVARRAQRAQqglqlqvlrlq 310
Cdd:TIGR02168  683 EEKIEELEEKIAELEKALAELRKELEELEEELEQL--------RKELEELSRQISALRKDLARLEAEVE----------- 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  311 qdkkQLQEEAAQLIRQREELEDKVAVCQKEQADFLPRMEETKwevcqkaGEISLLKQQLKDSQADVSQKLSEIVGLRSQL 390
Cdd:TIGR02168  744 ----QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE-------AEIEELEAQIEQLKEELKALREALDELRAEL 812

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  391 REGRASLREKEEQLLSLRDSFGSKQASLELSEGELppaclkpALTPVDLVEPQEALASCESDEAKMRRQagVAAAASLVS 470
Cdd:TIGR02168  813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQI-------EELSEDIESLAAEIEELEELIEELESE--LEALLNERA 883

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720399156  471 VDGEVEAGGEGGTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQL 532
Cdd:TIGR02168  884 SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 255-406 4.63e-07

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: 52.72  E-value: 4.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 255 LEQSEAAVAQVLEERQKAWERELAELRQgcsgKLQQVARRAQRAQQGLQLQVLRLqqdkKQLQEEAAQLIRQREELEDKV 334
Cdd:pfam05667 315 ATSSPPTKVETEEELQQQREEELEELQE----QLEDLESSIQELEKEIKKLESSI----KQVEEELEELKEQNEELEKQY 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 335 AVcqKEQA-DFLPRMEE--------------------TKWEVCQKA--GEISLLKQQLKDSQADVSQKLSEIVGLRSQLR 391
Cdd:pfam05667 387 KV--KKKTlDLLPDAEEniaklqalvdasaqrlvelaGQWEKHRVPliEEYRALKEAKSNKEDESQRKLEEIKELREKIK 464

                         170
                  ....*....|....*...
gi 1720399156 392 EGRASLREKEE---QLLS 406
Cdd:pfam05667 465 EVAEEAKQKEElykQLVA 482
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
232-411 4.72e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.00  E-value: 4.72e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  232 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQV----------------------LEERQKAWERELAELRQGcSGKLQ 289
Cdd:COG4913    610 AKLAALEAELAELEEELAEAEERLEALEAELDALqerrealqrlaeyswdeidvasAEREIAELEAELERLDAS-SDDLA 688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  290 QVARRAQRAqqglqlqvlrlQQDKKQLQEEAAQLIRQREELEDKVAVCQKEQADFLPRMEEtkWEVCQKAGEISLLKQQL 369
Cdd:COG4913    689 ALEEQLEEL-----------EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA--AEDLARLELRALLEERF 755

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1720399156  370 KdsQADVSQKLSEIV-GLRSQLREGRASLREKEEQLLSLRDSF 411
Cdd:COG4913    756 A--AALGDAVERELReNLEERIDALRARLNRAEEELERAMRAF 796
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 234-423 5.28e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 49.68  E-value: 5.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  234 IQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQgcsgKLQQVARRAQRAQQGLqlqvlrlqqdk 313
Cdd:TIGR02169  324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAEL-KEELEDLRA----ELEEVDKEFAETRDEL----------- 387

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  314 KQLQEEAAQLIRQREEL---------------------EDKVAVCQKEQADFLPRMEETKWEVCQKAGEISLLKQQLKDS 372
Cdd:TIGR02169  388 KDYREKLEKLKREINELkreldrlqeelqrlseeladlNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY 467

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720399156  373 QADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRD-SFGSKQASLELSEG 423
Cdd:TIGR02169  468 EQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEErVRGGRAVEEVLKAS 519
PTZ00121 PTZ00121
MAEBL; Provisional
 238-556 3.85e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 3.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  238 EERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAWE-------RELAELRQGCSGKLQQVARRAQ---------RAQQG 301
Cdd:PTZ00121  1144 EARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAarkaeevRKAEELRKAEDARKAEAARKAEeerkaeearKAEDA 1223

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  302 LQLQVLRLQQDKKQLQEEAAQLIRQREELEDKvAVCQKEQADFLPRMEETKWEVCQKAGEISLLKQQLKDSQADVSQKLS 381
Cdd:PTZ00121  1224 KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIR-KFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKK 1302

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  382 EIVGLRSQLREGRAS--LREKEEQLLSLRDSFgSKQASLELSEGELPPACLKPALTPVDLVEPQEALASCESDEAKMRRQ 459
Cdd:PTZ00121  1303 KADEAKKKAEEAKKAdeAKKKAEEAKKKADAA-KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD 1381

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  460 AGVAAAASLVSVDGEVEAGGEGGTRA---LRREVGRLQAElAAERRARERQGasfAEERRVWLEEKEKVIEYQKQlqlsy 536
Cdd:PTZ00121  1382 AAKKKAEEKKKADEAKKKAEEDKKKAdelKKAAAAKKKAD-EAKKKAEEKKK---ADEAKKKAEEAKKADEAKKK----- 1452

                          330       340
                   ....*....|....*....|
gi 1720399156  537 VEMYQRNQQLERRLRERGAA 556
Cdd:PTZ00121  1453 AEEAKKAEEAKKKAEEAKKA 1472
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 227-330 1.24e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 41.86  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  227 PPSPSALIQELEerlwekeQEVAALRRSLEQ--SEAAVAQVLEERQKAWERELAELRQGCSGKLQQVARRAQRAQQGLQL 304
Cdd:PRK11448   137 PEDPENLLHALQ-------QEVLTLKQQLELqaREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAE 209

                           90       100
                   ....*....|....*....|....*.
gi 1720399156  305 QVLRLQQDKKQLQEEAAQLIRQREEL 330
Cdd:PRK11448   210 TSQERKQKRKEITDQAAKRLELSEEE 235
 
Name Accession Description Interval E-value
Fez1 pfam06818
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ...
 351-551 7.04e-72

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: 229.11  E-value: 7.04e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 351 TKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFGSKQASLELSEGELPPAC- 429
Cdd:pfam06818   1 TKWEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSKTLELEVCENELQRKKn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 430 ------------------LKPALTPVDLVEPQEAlasCESDEAKMRRQAGVAaaaslvsvdgeveaggeggTRALRREVG 491
Cdd:pfam06818  81 eaellrekvgkleeevsgLREALSDVSPSGYESV---YESDEAKEQRQEEAD-------------------LGSLRREVE 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 492 RLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQLERRLR 551
Cdd:pfam06818 139 RLRAELREERQRRERQASSFEQERRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 235-534 8.88e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.96  E-value: 8.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 235 QELEERLWEKEQEVAALR-RSLEQSEAAVAQVLEERQKAWERELAELRQgCSGKLQQVARRAQRAQQGLqlqvlrlqqdk 313
Cdd:COG1196   216 RELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAE-LEAELEELRLELEELELEL----------- 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 314 KQLQEEAAQLIRQREELEDKVAVCQKEQADFLPRMEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREG 393
Cdd:COG1196   284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 394 RASLREKEEQLLSLRDSFGSKQASLELSEGELppaclkpALTPVDLVEPQEALASCESDEAKMRRQAGVAAAASLvsVDG 473
Cdd:COG1196   364 EEALLEAEAELAEAEEELEELAEELLEALRAA-------AELAAQLEELEEAEEALLERLERLEEELEELEEALA--ELE 434

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720399156 474 EVEAGGEGGTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQL 534
Cdd:COG1196   435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 232-526 2.15e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.80  E-value: 2.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 232 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQvLEERQKAWERELAELRQGCSGKLQQVArRAQRAQQGLQLQVLRLQQ 311
Cdd:COG1196   239 AELEELEAELEELEAELEELEAELAELEAELEE-LRLELEELELELEEAQAEEYELLAELA-RLEQDIARLEERRRELEE 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 312 DKKQLQEEAAQLIRQREELEDKVAVCQKEQADFLPRMEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLR 391
Cdd:COG1196   317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 392 EGRA---SLREKEEQLLSLRDSFGSKQASLELSEGELppaclkpaltpvDLVEPQEALASCESDEAKMRRQAGVAAAASL 468
Cdd:COG1196   397 ELAAqleELEEAEEALLERLERLEEELEELEEALAEL------------EEEEEEEEEALEEAAEEEAELEEEEEALLEL 464

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720399156 469 VSVDGEVEAGGEGGTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEKEKVI 526
Cdd:COG1196   465 LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL 522
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 234-527 8.38e-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: 8.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 234 IQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAElrqgcsgkLQQVARRAQRAQQGLQLQVLRLQQDK 313
Cdd:COG1196   332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA-EAELAE--------AEEELEELAEELLEALRAAAELAAQL 402

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 314 KQLQEEAAQLIRQREELEDKVAVCQKEQADFLPRMEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREG 393
Cdd:COG1196   403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 394 RASLREKEEQLLSLrdsfgskQASLELSEGELPPAclKPALTPVDLVEPQEALASCESDEAKMRRQAGVAAAASLVSVDG 473
Cdd:COG1196   483 LEELAEAAARLLLL-------LEAEADYEGFLEGV--KAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVV 553

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720399156 474 EVEAGGEGGTRALRRE------------VGRLQAELAAERRARERQGASFAEERRVWLEEKEKVIE 527
Cdd:COG1196   554 EDDEVAAAAIEYLKAAkagratflpldkIRARAALAAALARGAIGAAVDLVASDLREADARYYVLG 619
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 231-532 3.57e-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: 56.60  E-value: 3.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  231 SALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVleerqkawERELAELRQGCSGKLQQVARRAQRAQqglqlqvlrlq 310
Cdd:TIGR02168  683 EEKIEELEEKIAELEKALAELRKELEELEEELEQL--------RKELEELSRQISALRKDLARLEAEVE----------- 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  311 qdkkQLQEEAAQLIRQREELEDKVAVCQKEQADFLPRMEETKwevcqkaGEISLLKQQLKDSQADVSQKLSEIVGLRSQL 390
Cdd:TIGR02168  744 ----QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE-------AEIEELEAQIEQLKEELKALREALDELRAEL 812

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  391 REGRASLREKEEQLLSLRDSFGSKQASLELSEGELppaclkpALTPVDLVEPQEALASCESDEAKMRRQagVAAAASLVS 470
Cdd:TIGR02168  813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQI-------EELSEDIESLAAEIEELEELIEELESE--LEALLNERA 883

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720399156  471 VDGEVEAGGEGGTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQL 532
Cdd:TIGR02168  884 SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 231-523 7.33e-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: 55.83  E-value: 7.33e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  231 SALIQELEERLWEKEQEVAALRRSLEQSEAAVaQVLEERQKAWERELAELRQgcsgKLQQVARraqraqqglqlqvlrlq 310
Cdd:TIGR02168  259 TAELQELEEKLEELRLEVSELEEEIEELQKEL-YALANEISRLEQQKQILRE----RLANLER----------------- 316

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  311 qDKKQLQEEAAQLIRQREELEDKVAVCQKEQADFLPRMEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQL 390
Cdd:TIGR02168  317 -QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  391 REGRASLREKEEQLLSLRDSFGSKQASLELSEGELPPACLKPALTPVDLVEPQEAlascesdEAKMRRQAGVAAAASLvs 470
Cdd:TIGR02168  396 ASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELE-------ELQEELERLEEALEEL-- 466

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720399156  471 vdGEVEAGGEGGTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEKE 523
Cdd:TIGR02168  467 --REELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 255-406 4.63e-07

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: 52.72  E-value: 4.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 255 LEQSEAAVAQVLEERQKAWERELAELRQgcsgKLQQVARRAQRAQQGLQLQVLRLqqdkKQLQEEAAQLIRQREELEDKV 334
Cdd:pfam05667 315 ATSSPPTKVETEEELQQQREEELEELQE----QLEDLESSIQELEKEIKKLESSI----KQVEEELEELKEQNEELEKQY 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 335 AVcqKEQA-DFLPRMEE--------------------TKWEVCQKA--GEISLLKQQLKDSQADVSQKLSEIVGLRSQLR 391
Cdd:pfam05667 387 KV--KKKTlDLLPDAEEniaklqalvdasaqrlvelaGQWEKHRVPliEEYRALKEAKSNKEDESQRKLEEIKELREKIK 464

                         170
                  ....*....|....*...
gi 1720399156 392 EGRASLREKEE---QLLS 406
Cdd:pfam05667 465 EVAEEAKQKEElykQLVA 482
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
232-411 4.72e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.00  E-value: 4.72e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  232 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQV----------------------LEERQKAWERELAELRQGcSGKLQ 289
Cdd:COG4913    610 AKLAALEAELAELEEELAEAEERLEALEAELDALqerrealqrlaeyswdeidvasAEREIAELEAELERLDAS-SDDLA 688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  290 QVARRAQRAqqglqlqvlrlQQDKKQLQEEAAQLIRQREELEDKVAVCQKEQADFLPRMEEtkWEVCQKAGEISLLKQQL 369
Cdd:COG4913    689 ALEEQLEEL-----------EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA--AEDLARLELRALLEERF 755

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1720399156  370 KdsQADVSQKLSEIV-GLRSQLREGRASLREKEEQLLSLRDSF 411
Cdd:COG4913    756 A--AALGDAVERELReNLEERIDALRARLNRAEEELERAMRAF 796
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 234-407 2.74e-06

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 48.77  E-value: 2.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 234 IQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQgcsgKLQQVARRAQRaqqglqlqvlrlqqDK 313
Cdd:COG1579    19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDL-EKEIKRLEL----EIEEVEARIKK--------------YE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 314 KQL-----QEEAAQLIRQREELEDKVAVCQKEQADFLPRMEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRS 388
Cdd:COG1579    80 EQLgnvrnNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159

                         170       180
                  ....*....|....*....|
gi 1720399156 389 QLREGRASLREK-EEQLLSL 407
Cdd:COG1579   160 ELEAEREELAAKiPPELLAL 179
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 234-423 5.28e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 49.68  E-value: 5.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  234 IQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQgcsgKLQQVARRAQRAQQGLqlqvlrlqqdk 313
Cdd:TIGR02169  324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAEL-KEELEDLRA----ELEEVDKEFAETRDEL----------- 387

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  314 KQLQEEAAQLIRQREEL---------------------EDKVAVCQKEQADFLPRMEETKWEVCQKAGEISLLKQQLKDS 372
Cdd:TIGR02169  388 KDYREKLEKLKREINELkreldrlqeelqrlseeladlNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY 467

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720399156  373 QADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRD-SFGSKQASLELSEG 423
Cdd:TIGR02169  468 EQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEErVRGGRAVEEVLKAS 519
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 290-556 7.09e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 7.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 290 QVARRAQR-AQQGLQLQVLRLQQDKKQLQEEAAQLIRQREELEDKVAVCQKEQADFLPRMEETKWEVCQKAGEISLLKQQ 368
Cdd:COG1196   210 EKAERYRElKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 369 LKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFGSKQASLELSEGElppacLKPALTPVDLVEPQEALAS 448
Cdd:COG1196   290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE-----LEEAEEELEEAEAELAEAE 364

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 449 CESDEAKMRRQAGVAAAASLVSvDGEVEAGGEGGTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEKEKVIEY 528
Cdd:COG1196   365 EALLEAEAELAEAEEELEELAE-ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443

                         250       260
                  ....*....|....*....|....*...
gi 1720399156 529 QKQLQLSYVEMYQRNQQLERRLRERGAA 556
Cdd:COG1196   444 LEEAAEEEAELEEEEEALLELLAELLEE 471
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 251-555 8.37e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.82  E-value: 8.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  251 LRRSLE----QSEAAvaqvleERQKAWERELAELRQGCSGKLQQVARRAQRAQQGlqlqvlrlqqDKKQLQEEAAQLIRQ 326
Cdd:TIGR02168  198 LERQLKslerQAEKA------ERYKELKAELRELELALLVLRLEELREELEELQE----------ELKEAEEELEELTAE 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  327 R-------EELEDKVAVCQKEQADFLPRMEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLRE 399
Cdd:TIGR02168  262 LqeleeklEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE 341

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  400 KEEQLLSLRDSFGSKQASLELSEGELPPACLKpaltpvdLVEPQEALASCESDEAKMRRQAGvAAAASLVSVDGEVEAGG 479
Cdd:TIGR02168  342 LEEKLEELKEELESLEAELEELEAELEELESR-------LEELEEQLETLRSKVAQLELQIA-SLNNEIERLEARLERLE 413

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720399156  480 EGGTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQLERRLRERGA 555
Cdd:TIGR02168  414 DRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
235-556 1.46e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.76  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 235 QELEERLWEKEQEVAALRRSLEQSEAAVAQvLEERQKAWE--RELAELRQgcsgKLQQVARRAQRAQQGLQLQvlrlqqd 312
Cdd:COG4717    91 AELQEELEELEEELEELEAELEELREELEK-LEKLLQLLPlyQELEALEA----ELAELPERLEELEERLEEL------- 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 313 kKQLQEEAAQLIRQREELEDKVA-VCQKEQADFLPRMEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLR 391
Cdd:COG4717   159 -RELEEELEELEAELAELQEELEeLLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 392 EGRASLREKEEQ----LLSLRDSFGSKQASLELSEGELPP---------ACLKPALTPVDLVEPQEALASCESDEAKMRR 458
Cdd:COG4717   238 AAALEERLKEARllllIAAALLALLGLGGSLLSLILTIAGvlflvlgllALLFLLLAREKASLGKEAEELQALPALEELE 317

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 459 QAGVAAAASLVSVDGEVEAGGEGG-------TRALRREVGRLQAELAAERRARERQ------GASFAEERRVWLEEKEKV 525
Cdd:COG4717   318 EEELEELLAALGLPPDLSPEELLElldrieeLQELLREAEELEEELQLEELEQEIAallaeaGVEDEEELRAALEQAEEY 397

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1720399156 526 IEYQKQLQlsyvemyQRNQQLERRLRERGAA 556
Cdd:COG4717   398 QELKEELE-------ELEEQLEELLGELEEL 421
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 227-551 1.98e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 44.67  E-value: 1.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  227 PPSPSALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRqgcsgklqqvarraqraqqglqlqv 306
Cdd:TIGR02169  669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDA-SRKIGEIE------------------------- 722

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  307 lrlqQDKKQLQEEAAQLIRQREELEDKVAVCQKEQADFLPRMEETKWEVCQKAGEISLLKQQLKDSQADVSQklSEIVGL 386
Cdd:TIGR02169  723 ----KEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEI 796

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  387 RSQLREGRASLREKEEQLLSLRDSFGSKQASLELSEGELPPACLKPALTPVDLVEPQEALASCESDEAKMRRQAGVAAAA 466
Cdd:TIGR02169  797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA 876

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  467 slvsvdgevEAGGEGGTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQL-------------- 532
Cdd:TIGR02169  877 ---------LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELseiedpkgedeeip 947

                          330       340
                   ....*....|....*....|.
gi 1720399156  533 --QLSYVEMYQRNQQLERRLR 551
Cdd:TIGR02169  948 eeELSLEDVQAELQRVEEEIR 968
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 234-395 2.22e-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: 43.60  E-value: 2.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 234 IQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAWERELAELRQGcSGKLQQVARRA---QRAQQGLQLQVLRLQ 310
Cdd:COG4942    78 LAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLS-PEDFLDAVRRLqylKYLAPARREQAEELR 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 311 QDKKQLQEEAAQLIRQREELEDKVAVCQKEQADFLPRMEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQL 390
Cdd:COG4942   157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236


                  ....*
gi 1720399156 391 REGRA 395
Cdd:COG4942   237 AAAAE 241
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 222-426 2.32e-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: 43.60  E-value: 2.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 222 FAACSPPSPSALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQgcsgKLQQVARRAQRAQQG 301
Cdd:COG4942    10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL-ERRIAALAR----RIRALEQELAALEAE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 302 LQLQvlrlqqdKKQLQEEAAQLIRQREELEDKVAVCQK--------------EQADFLPRMEETKWEVCQKAGEIsllkQ 367
Cdd:COG4942    85 LAEL-------EKEIAELRAELEAQKEELAELLRALYRlgrqpplalllspeDFLDAVRRLQYLKYLAPARREQA----E 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720399156 368 QLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFGSKQASLELSEGELP 426
Cdd:COG4942   154 ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA 212
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 234-562 2.97e-04

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: 44.17  E-value: 2.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  234 IQELEERLWEKEQEVAALRRSLEQSEAAvAQVLEERQKAWERELAELRQGC------SGKLQQVARRAQRAQQGLQLQVL 307
Cdd:COG3096    356 LEELTERLEEQEEVVEEAAEQLAEAEAR-LEAAEEEVDSLKSQLADYQQALdvqqtrAIQYQQAVQALEKARALCGLPDL 434

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  308 RLQQDKK---QLQEEAAQLIRQREELEDKVAVCQKEQADFlprmEETKWEVCQKAGEISLL------KQQLKD--SQADV 376
Cdd:COG3096    435 TPENAEDylaAFRAKEQQATEEVLELEQKLSVADAARRQF----EKAYELVCKIAGEVERSqawqtaRELLRRyrSQQAL 510

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  377 SQKLSeivGLRSQLREGRASLREKEEqLLSLRDSFgSKQASLELSEGELPPACLKPALTPVDlvEPQEALASCESDEAKM 456
Cdd:COG3096    511 AQRLQ---QLRAQLAELEQRLRQQQN-AERLLEEF-CQRIGQQLDAAEELEELLAELEAQLE--ELEEQAAEAVEQRSEL 583

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  457 RRQagvaaaaslvsvdgeveaggEGGTRALRREVGR-----LQAELAAERrARERQGASFAEERRVwLEEKEKVIEYQKQ 531
Cdd:COG3096    584 RQQ--------------------LEQLRARIKELAArapawLAAQDALER-LREQSGEALADSQEV-TAAMQQLLERERE 641

                          330       340       350
                   ....*....|....*....|....*....|.
gi 1720399156  532 LQLSYVEMYQRNQQLERRLRERGAAGGSSTP 562
Cdd:COG3096    642 ATVERDELAARKQALESQIERLSQPGGAEDP 672
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
232-429 3.06e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 3.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  232 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAWERELAELRQGCSGKLQQVARRAQRAQQGLQLQVL---R 308
Cdd:COG4913    295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAlglP 374

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  309 LQQDKKQLQEEAAQLIRQREELEDKVAVCQKEQADflprmeetkwevcqkageislLKQQLKDSQADVSQKLSEIvglrS 388
Cdd:COG4913    375 LPASAEEFAALRAEAAALLEALEEELEALEEALAE---------------------AEAALRDLRRELRELEAEI----A 429

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1720399156  389 QLREGRASLrekEEQLLSLRDSFgskQASLELSEGELPPAC 429
Cdd:COG4913    430 SLERRKSNI---PARLLALRDAL---AEALGLDEAELPFVG 464
PTZ00121 PTZ00121
MAEBL; Provisional
 238-556 3.85e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 3.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  238 EERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAWE-------RELAELRQGCSGKLQQVARRAQ---------RAQQG 301
Cdd:PTZ00121  1144 EARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAarkaeevRKAEELRKAEDARKAEAARKAEeerkaeearKAEDA 1223

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  302 LQLQVLRLQQDKKQLQEEAAQLIRQREELEDKvAVCQKEQADFLPRMEETKWEVCQKAGEISLLKQQLKDSQADVSQKLS 381
Cdd:PTZ00121  1224 KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIR-KFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKK 1302

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  382 EIVGLRSQLREGRAS--LREKEEQLLSLRDSFgSKQASLELSEGELPPACLKPALTPVDLVEPQEALASCESDEAKMRRQ 459
Cdd:PTZ00121  1303 KADEAKKKAEEAKKAdeAKKKAEEAKKKADAA-KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD 1381

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  460 AGVAAAASLVSVDGEVEAGGEGGTRA---LRREVGRLQAElAAERRARERQGasfAEERRVWLEEKEKVIEYQKQlqlsy 536
Cdd:PTZ00121  1382 AAKKKAEEKKKADEAKKKAEEDKKKAdelKKAAAAKKKAD-EAKKKAEEKKK---ADEAKKKAEEAKKADEAKKK----- 1452

                          330       340
                   ....*....|....*....|
gi 1720399156  537 VEMYQRNQQLERRLRERGAA 556
Cdd:PTZ00121  1453 AEEAKKAEEAKKKAEEAKKA 1472
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 312-567 8.91e-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: 42.06  E-value: 8.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 312 DKKQLQEEAAQLIRQREELEDKVAVCQKEQADFLPRMEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLR 391
Cdd:COG4942    21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 392 EGRASLREkeeqllSLRDSFGSKQASlelsegelPPACLKPALTPVDLVEPQEALASCEsdEAKMRRQAGVAAAASLVSV 471
Cdd:COG4942   101 AQKEELAE------LLRALYRLGRQP--------PLALLLSPEDFLDAVRRLQYLKYLA--PARREQAEELRADLAELAA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 472 DGEVEAGGEGGTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQlsyvemyQRNQQLERRLR 551
Cdd:COG4942   165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE-------ALIARLEAEAA 237

                         250
                  ....*....|....*.
gi 1720399156 552 ERGAAGGSSTPTPQHG 567
Cdd:COG4942   238 AAAERTPAAGFAALKG 253
PTZ00121 PTZ00121
MAEBL; Provisional
 235-546 9.24e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 9.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  235 QELEERLWEKEQEVAALRRSLEQSEAA-VAQVLEERQKAWE-RELAELRQGCSGKLQQVARRA---QRAQQGLQLQVLRL 309
Cdd:PTZ00121  1486 DEAKKKAEEAKKKADEAKKAAEAKKKAdEAKKAEEAKKADEaKKAEEAKKADEAKKAEEKKKAdelKKAEELKKAEEKKK 1565

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  310 QQDKKQLQEEAAQLIRQREELEdkvavcQKEQADFLPRMEETKWEVCQKAGEisLLKQQLKDSQADVSQKLSEIVGLRSQ 389
Cdd:PTZ00121  1566 AEEAKKAEEDKNMALRKAEEAK------KAEEARIEEVMKLYEEEKKMKAEE--AKKAEEAKIKAEELKKAEEEKKKVEQ 1637

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  390 LREGRASLREKEEQLLSLRDSFGSKQASLELSEGELPpaclkpaltpvdlvEPQEALASCESDEAK----MRRQAGVAAA 465
Cdd:PTZ00121  1638 LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK--------------KKAEEAKKAEEDEKKaaeaLKKEAEEAKK 1703

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  466 ASLVSVDGEVEAGGEGGTRAlRREVGRLQAELAAERRARERQGAsfaEERRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQ 545
Cdd:PTZ00121  1704 AEELKKKEAEEKKKAEELKK-AEEENKIKAEEAKKEAEEDKKKA---EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEA 1779


                   .
gi 1720399156  546 L 546
Cdd:PTZ00121  1780 V 1780
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 227-330 1.24e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 41.86  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  227 PPSPSALIQELEerlwekeQEVAALRRSLEQ--SEAAVAQVLEERQKAWERELAELRQGCSGKLQQVARRAQRAQQGLQL 304
Cdd:PRK11448   137 PEDPENLLHALQ-------QEVLTLKQQLELqaREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAE 209

                           90       100
                   ....*....|....*....|....*.
gi 1720399156  305 QVLRLQQDKKQLQEEAAQLIRQREEL 330
Cdd:PRK11448   210 TSQERKQKRKEITDQAAKRLELSEEE 235
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
235-552 1.50e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 235 QELEERLWEKEQEVAALRRSLEQSEAAVAQV--LEERQKAWERELAELRQGCSGKLQQVARRAQRAQQGLQLQVLRLQQD 312
Cdd:COG4717   128 LPLYQELEALEAELAELPERLEELEERLEELreLEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 313 KKQLQEEAAQLIRQREELEDKVAVCQKEQADFLPRMEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQL-- 390
Cdd:COG4717   208 LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLla 287

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 391 ------REGRASLREKEEQLLSLRDSFGSKQASLE--LSEGELPPACLKPALTPV--DLVEPQEALASCESDEAKMRRQA 460
Cdd:COG4717   288 llflllAREKASLGKEAEELQALPALEELEEEELEelLAALGLPPDLSPEELLELldRIEELQELLREAEELEEELQLEE 367

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 461 GVAAAASL------VSVDGEVEAGGEGGTR-ALRREVGRLQAELAAERRARERQGASFAEERrvWLEEKEKVIEYQKQLQ 533
Cdd:COG4717   368 LEQEIAALlaeagvEDEEELRAALEQAEEYqELKEELEELEEQLEELLGELEELLEALDEEE--LEEELEELEEELEELE 445

                         330
                  ....*....|....*....
gi 1720399156 534 LSYVEMYQRNQQLERRLRE 552
Cdd:COG4717   446 EELEELREELAELEAELEQ 464
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
233-405 2.21e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 233 LIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQkawerELAELRQGCSGKLQQVARRAQRAqqglqlqvLRLQQD 312
Cdd:PRK03918  194 LIKEKEKELEEVLREINEISSELPELREELEKLEKEVK-----ELEELKEEIEELEKELESLEGSK--------RKLEEK 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 313 KKQLQEEAAQLIRQREELEDKVAVCQ--KEQADFLPRMEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQL 390
Cdd:PRK03918  261 IRELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340

                         170
                  ....*....|....*
gi 1720399156 391 REgrasLREKEEQLL 405
Cdd:PRK03918  341 EE----LKKKLKELE 351
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 232-552 2.95e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 2.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 232 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAWERELAELRQGCSGKLQQVARRAQRAQQGLQLQVLRLQQ 311
Cdd:COG1196   407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 312 DKKQLQEEAAQLIRQREELEDKVAVCQKEQADFLPRM----EETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLR 387
Cdd:COG1196   487 AEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAgavaVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYL 566

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 388 SQLREGRASL----REKEEQLLSLRDSFGSKQASLELSEGELPPACLKPALTPVDLVEPQEALASCESDEAKMRRQAGVA 463
Cdd:COG1196   567 KAAKAGRATFlpldKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRL 646

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 464 AAASL---------------VSVDGEVEAGGEGGTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEKEKVIEY 528
Cdd:COG1196   647 REVTLegeggsaggsltggsRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEAL 726

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1720399156 529 QKQLQLSYVEMYQRNQ---------------------QLERRLRE 552
Cdd:COG1196   727 EEQLEAEREELLEELLeeeelleeealeelpeppdleELERELER 771
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 235-403 3.02e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.54  E-value: 3.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  235 QELEERlweKEQEVAALRRSLE-QSEAAVAQVLEERQK---AWERELAELRQGCSGK----------------LQQVARR 294
Cdd:pfam01576  319 QELRSK---REQEVTELKKALEeETRSHEAQLQEMRQKhtqALEELTEQLEQAKRNKanlekakqalesenaeLQAELRT 395

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  295 AQRAQQGLQLQVLRLQQDKKQLQEEAAQLIRQREELEDKVAVCQKEQADFLPRMEETKWEVCQKAGEISLLKQQLKDSQA 374
Cdd:pfam01576  396 LQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQE 475

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1720399156  375 ----DVSQKLSEIVGLRsQLREGRASLREKEEQ 403
Cdd:pfam01576  476 llqeETRQKLNLSTRLR-QLEDERNSLQEQLEE 507
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 237-582 7.48e-03

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: 39.11  E-value: 7.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 237 LEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKA---WERELAELRQGCsGKLQQVARRAQRAQQGLQLQVLRLQQDK 313
Cdd:pfam07888  32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDreqWERQRRELESRV-AELKEELRQSREKHEELEEKYKELSASS 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 314 KQLQEEAAQLIRQRE-------ELEDKVAVCQKEQADFLPRMEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGL 386
Cdd:pfam07888 111 EELSEEKDALLAQRAahearirELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSL 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 387 RSQLREGRASLREKEEQLLSLRDSFGSKQasLELSEGELPPACLKPALTpvDLVEPQEALASCESDEAKMRRQAGVAAA- 465
Cdd:pfam07888 191 SKEFQELRNSLAQRDTQVLQLQDTITTLT--QKLTTAHRKEAENEALLE--ELRSLQERLNASERKVEGLGEELSSMAAq 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 466 --------------ASLVSVDGEVEAGGEGGTRA----------------------LRREVGRLQAELAAERRARERQGA 509
Cdd:pfam07888 267 rdrtqaelhqarlqAAQLTLQLADASLALREGRArwaqeretlqqsaeadkdriekLSAELQRLEERLQEERMEREKLEV 346

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156 510 SFAEER---RVWLEEKEKVIEYQK-----------QLQLSYVEMYQRNQQLERRLRERGAAGGSSTPTPQHGEEKKAWTP 575
Cdd:pfam07888 347 ELGREKdcnRVQLSESRRELQELKaslrvaqkekeQLQAEKQELLEYIRQLEQRLETVADAKWSEAALTSTERPDSPLSD 426


                  ....*..
gi 1720399156 576 SRLERIE 582
Cdd:pfam07888 427 SEDENPE 433
PTZ00121 PTZ00121
MAEBL; Provisional
 234-424 8.23e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 8.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  234 IQELEERLWEKEQEVAALRRSLEQSEAAVAQVLE-----ERQKAWERELAELRQGCSGKLQQVaRRAQRAQQGLQLQVLR 308
Cdd:PTZ00121  1563 KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEvmklyEEEKKMKAEEAKKAEEAKIKAEEL-KKAEEEKKKVEQLKKK 1641

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720399156  309 LQQDKKQLQE--EAAQLIRQREELEDKVAVCQKEQADFLPRMEETKwevcQKAGEISLLKQQLKDSQADVSQKLSEIVGL 386
Cdd:PTZ00121  1642 EAEEKKKAEElkKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE----KKAAEALKKEAEEAKKAEELKKKEAEEKKK 1717

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1720399156  387 RSQLREGRASLREKEEQLLSLRDSFGSKQASLELSEGE 424
Cdd:PTZ00121  1718 AEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE 1755
 
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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