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Conserved domains on  [gi|1917203444|ref|NP_001375119|]
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leucine zipper putative tumor suppressor 3 isoform 1 [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 ...
 438-638 4.19e-74

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: 236.82  E-value: 4.19e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 438 TKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAAC- 516
Cdd:pfam06818   1 TKWEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSKTLELEVCENELQRKKn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 517 ------------------LKPALTPVDPAEPQdalATCESDEAKMRRQAgvaaaaslvsvdgeaeaggESGTRALRREVG 578
Cdd:pfam06818  81 eaellrekvgkleeevsgLREALSDVSPSGYE---SVYESDEAKEQRQE-------------------EADLGSLRREVE 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 579 RLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQLERRLR 638
Cdd:pfam06818 139 RLRAELREERQRRERQASSFEQERRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 319-552 1.46e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.14  E-value: 1.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  319 ALIQELEERLWEKEQEVAALRRSLEQSEAAVA------QVLEERQKAWERELAELrqgcSGKLQQVARRAQRAQQGLQLQ 392
Cdd:TIGR02168  267 EKLEELRLEVSELEEEIEELQKELYALANEISrleqqkQILRERLANLERQLEEL----EAQLEELESKLDELAEELAEL 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  393 VLRLQQDKKQ---LQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSE 469
Cdd:TIGR02168  343 EEKLEELKEElesLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE 422

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  470 IVGLRS-----QLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAACLKPALTPVDPAEPQDALATCES-DEAKM 543
Cdd:TIGR02168  423 IEELLKkleeaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERlQENLE 502


                   ....*....
gi 1917203444  544 RRQAGVAAA 552
Cdd:TIGR02168  503 GFSEGVKAL 511
 
Name Accession Description Interval E-value
Fez1 pfam06818
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ...
 438-638 4.19e-74

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: 236.82  E-value: 4.19e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 438 TKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAAC- 516
Cdd:pfam06818   1 TKWEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSKTLELEVCENELQRKKn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 517 ------------------LKPALTPVDPAEPQdalATCESDEAKMRRQAgvaaaaslvsvdgeaeaggESGTRALRREVG 578
Cdd:pfam06818  81 eaellrekvgkleeevsgLREALSDVSPSGYE---SVYESDEAKEQRQE-------------------EADLGSLRREVE 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 579 RLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQLERRLR 638
Cdd:pfam06818 139 RLRAELREERQRRERQASSFEQERRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 319-613 7.96e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.89  E-value: 7.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 319 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQvLEERQKAWERELAELRQGCSGKLQQVArRAQRAQQGLQLQVLRLQQ 398
Cdd:COG1196   239 AELEELEAELEELEAELEELEAELAELEAELEE-LRLELEELELELEEAQAEEYELLAELA-RLEQDIARLEERRRELEE 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 399 DKKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLR 478
Cdd:COG1196   317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 479 EGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAACLKPAltpvdpaepQDALATCESDEAKMRRQAGVAAAASLVSV 558
Cdd:COG1196   397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE---------EEEEALEEAAEEEAELEEEEEALLELLAE 467

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1917203444 559 DGEAEAGGESGTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEKEKVI 613
Cdd:COG1196   468 LLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL 522
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 318-593 1.38e-09

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: 61.61  E-value: 1.38e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  318 SALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQGCSGKLQQVARRAQRAQQGLQLQvlrlq 397
Cdd:TIGR02168  683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL-SRQISALRKDLARLEAEVEQLEERIAQLSKEL----- 756

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  398 qdkKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQL 477
Cdd:TIGR02168  757 ---TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  478 REGRASLREKEEQLLSLRDSFSSKQASLELGEgelpaaclkpaltpVDPAEPQDALAtcESDEAKMRRQAGVAAAASLVS 557
Cdd:TIGR02168  834 AATERRLEDLEEQIEELSEDIESLAAEIEELE--------------ELIEELESELE--ALLNERASLEEALALLRSELE 897

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1917203444  558 VDGEAEAGGESGTRALRREVGRLQAELAAERRARER 593
Cdd:TIGR02168  898 ELSEELRELESKRSELRRELEELREKLAQLELRLEG 933
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 319-552 1.46e-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: 58.14  E-value: 1.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  319 ALIQELEERLWEKEQEVAALRRSLEQSEAAVA------QVLEERQKAWERELAELrqgcSGKLQQVARRAQRAQQGLQLQ 392
Cdd:TIGR02168  267 EKLEELRLEVSELEEEIEELQKELYALANEISrleqqkQILRERLANLERQLEEL----EAQLEELESKLDELAEELAEL 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  393 VLRLQQDKKQ---LQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSE 469
Cdd:TIGR02168  343 EEKLEELKEElesLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE 422

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  470 IVGLRS-----QLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAACLKPALTPVDPAEPQDALATCES-DEAKM 543
Cdd:TIGR02168  423 IEELLKkleeaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERlQENLE 502


                   ....*....
gi 1917203444  544 RRQAGVAAA 552
Cdd:TIGR02168  503 GFSEGVKAL 511
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
319-498 1.16e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.31  E-value: 1.16e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  319 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQV----------------------LEERQKAWERELAELRQGcSGKLQ 376
Cdd:COG4913    610 AKLAALEAELAELEEELAEAEERLEALEAELDALqerrealqrlaeyswdeidvasAEREIAELEAELERLDAS-SDDLA 688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  377 QVARRAQRAqqglqlqvlrlQQDKKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEEtkWEVCQKAGEISLLKQQL 456
Cdd:COG4913    689 ALEEQLEEL-----------EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA--AEDLARLELRALLEERF 755

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1917203444  457 KdsQADVSQKLSEIV-GLRSQLREGRASLREKEEQLLSLRDSF 498
Cdd:COG4913    756 A--AALGDAVERELReNLEERIDALRARLNRAEEELERAMRAF 796
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 342-493 1.87e-06

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: 51.18  E-value: 1.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 342 LEQSEAAVAQVLEERQKAWERELAELRQgcsgKLQQVARRAQRAQQGLQLQVLRLqqdkKQLQEEAARLMRQREELEDKV 421
Cdd:pfam05667 315 ATSSPPTKVETEEELQQQREEELEELQE----QLEDLESSIQELEKEIKKLESSI----KQVEEELEELKEQNEELEKQY 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 422 AAcqKEQA-DFLPRIEE--------------------TKWEVCQKA--GEISLLKQQLKDSQADVSQKLSEIVGLRSQLR 478
Cdd:pfam05667 387 KV--KKKTlDLLPDAEEniaklqalvdasaqrlvelaGQWEKHRVPliEEYRALKEAKSNKEDESQRKLEEIKELREKIK 464

                         170
                  ....*....|....*...
gi 1917203444 479 EGRASLREKEE---QLLS 493
Cdd:pfam05667 465 EVAEEAKQKEElykQLVA 482
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
321-611 4.42e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 50.04  E-value: 4.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 321 IQELEERLWEKEQEVAALRRSLEQSEAAvAQVLEERQKAWERELAELRQgcsgKLQQVARRAQRAQQGLQLQVLrlqqDK 400
Cdd:PRK02224  281 VRDLRERLEELEEERDDLLAEAGLDDAD-AEAVEARREELEDRDEELRD----RLEECRVAAQAHNEEAESLRE----DA 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 401 KQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEEtkwevcqkageislLKQQLKDSQA---DVSQKLSEIVGLRSQL 477
Cdd:PRK02224  352 DDLEERAEELREEAAELESELEEAREAVEDRREEIEE--------------LEEEIEELRErfgDAPVDLGNAEDFLEEL 417

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 478 REGRASLREKEEqllSLRDSFSSKQASLELGEGELPAACLKPALTPVDPAEPQDALATCESDEAKMRRQAGvAAAASLVS 557
Cdd:PRK02224  418 REERDELREREA---ELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELE-DLEEEVEE 493

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1917203444 558 VDGEAEAGGESGTRALRREVGRLQAELAAERRARERQGasfAEERRVWLEEKEK 611
Cdd:PRK02224  494 VEERLERAEDLVEAEDRIERLEERREDLEELIAERRET---IEEKRERAEELRE 544
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
320-492 4.17e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 4.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 320 LIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQkawerELAELRQGCSGKLQQVARRAQRAqqglqlqvLRLQQD 399
Cdd:PRK03918  194 LIKEKEKELEEVLREINEISSELPELREELEKLEKEVK-----ELEELKEEIEELEKELESLEGSK--------RKLEEK 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 400 KKQLQEEAARLMRQREELEDKVAACQ--KEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQL 477
Cdd:PRK03918  261 IRELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340

                         170
                  ....*....|....*
gi 1917203444 478 REgrasLREKEEQLL 492
Cdd:PRK03918  341 EE----LKKKLKELE 351
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 320-461 3.31e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 40.00  E-value: 3.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  320 LIQELEERLWEKEQEVAALRRSLEQSEAAVAQvLEERQKAWERELAELRQG---CSGKLQQVARRAQRAQQGLQLQVLRl 396
Cdd:smart00787 145 LKEGLDENLEGLKEDYKLLMKELELLNSIKPK-LRDRKDALEEELRQLKQLedeLEDCDPTELDRAKEKLKKLLQEIMI- 222

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1917203444  397 qqdKKQLQEEaarLMRQREELEDKVAACQKEQADFLPRI--EETKWEVCQK--AGEISLLKQQLKDSQA 461
Cdd:smart00787 223 ---KVKKLEE---LEEELQELESKIEDLTNKKSELNTEIaeAEKKLEQCRGftFKEIEKLKEQLKLLQS 285
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 572-640 5.97e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 37.56  E-value: 5.97e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1917203444  572 ALRREVGRLQAELAAERRARERQGASFAEERRVWLEEK--EKVIEYQKQLQLSYVEMYQRNQQLERRLRER 640
Cdd:smart00935  29 KRQAELEKLEKELQKLKEKLQKDAATLSEAAREKKEKElqKKVQEFQRKQQKLQQDLQKRQQEELQKILDK 99
 
Name Accession Description Interval E-value
Fez1 pfam06818
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ...
 438-638 4.19e-74

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: 236.82  E-value: 4.19e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 438 TKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAAC- 516
Cdd:pfam06818   1 TKWEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSKTLELEVCENELQRKKn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 517 ------------------LKPALTPVDPAEPQdalATCESDEAKMRRQAgvaaaaslvsvdgeaeaggESGTRALRREVG 578
Cdd:pfam06818  81 eaellrekvgkleeevsgLREALSDVSPSGYE---SVYESDEAKEQRQE-------------------EADLGSLRREVE 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 579 RLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQLERRLR 638
Cdd:pfam06818 139 RLRAELREERQRRERQASSFEQERRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 319-613 7.96e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.89  E-value: 7.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 319 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQvLEERQKAWERELAELRQGCSGKLQQVArRAQRAQQGLQLQVLRLQQ 398
Cdd:COG1196   239 AELEELEAELEELEAELEELEAELAELEAELEE-LRLELEELELELEEAQAEEYELLAELA-RLEQDIARLEERRRELEE 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 399 DKKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLR 478
Cdd:COG1196   317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 479 EGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAACLKPAltpvdpaepQDALATCESDEAKMRRQAGVAAAASLVSV 558
Cdd:COG1196   397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE---------EEEEALEEAAEEEAELEEEEEALLELLAE 467

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1917203444 559 DGEAEAGGESGTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEKEKVI 613
Cdd:COG1196   468 LLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL 522
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 322-643 1.33e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.04  E-value: 1.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 322 QELEERLWEKEQEVAALR-RSLEQSEAAVAQVLEERQKAWERELAELRQgCSGKLQQVARRAQRAQQGLqlqvlrlqqdk 400
Cdd:COG1196   216 RELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAE-LEAELEELRLELEELELEL----------- 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 401 KQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREG 480
Cdd:COG1196   284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 481 RASLREKEEQLLSLRDSFSSKQaslelgegelpaaclkpaltpvdpaepqdalatcesdEAKMRRQAGVAAAASLVSVDG 560
Cdd:COG1196   364 EEALLEAEAELAEAEEELEELA-------------------------------------EELLEALRAAAELAAQLEELE 406

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 561 EAEAGGESGTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQLERRLRER 640
Cdd:COG1196   407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486


                  ...
gi 1917203444 641 GAA 643
Cdd:COG1196   487 AEA 489
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 319-643 5.94e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 65.73  E-value: 5.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 319 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAWERELAELRQGCSGKLQQVARRAQRAQQGLQLQVLRLQQ 398
Cdd:COG1196   407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 399 DKKQLQEEAARLMRQREELEDKVAAcQKEQADFLPRI-----EETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGL 473
Cdd:COG1196   487 AEAAARLLLLLEAEADYEGFLEGVK-AALLLAGLRGLagavaVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEY 565

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 474 RSQLREGRASLREKEeqLLSLRDSFSSKQASLELGEGELPAACLKPALTPVDPAEPQDAL-ATCESDEAKMRRQAGVAAA 552
Cdd:COG1196   566 LKAAKAGRATFLPLD--KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLgRTLVAARLEAALRRAVTLA 643

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 553 ASLVSVDGEAEAGGESGTRALRREVGRLQAELAAERRARERQGASFAEERRvwLEEKEKVIEYQKQLQLSYVEMYQRNQQ 632
Cdd:COG1196   644 GRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELE--LEEALLAEEEEERELAEAEEERLEEEL 721

                         330
                  ....*....|.
gi 1917203444 633 LERRLRERGAA 643
Cdd:COG1196   722 EEEALEEQLEA 732
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 321-614 6.00e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 65.73  E-value: 6.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 321 IQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQGcSGKLQQVARRAQRAQQGLQLQVLRLQQDK 400
Cdd:COG1196   332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA-EAELAEAEEE-LEELAEELLEALRAAAELAAQLEELEEAE 409

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 401 KQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKwevcQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREG 480
Cdd:COG1196   410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA----EEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 481 RASLREKEEQLLSLRDSFSSKQAS--LELGEGELPAACLKPALTPVDPAEPQDALATCESD--EAKMRRQAGVAAAAslv 556
Cdd:COG1196   486 LAEAAARLLLLLEAEADYEGFLEGvkAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAalQNIVVEDDEVAAAA--- 562

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1917203444 557 sVDGEAEAGGESGTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEKEKVIE 614
Cdd:COG1196   563 -IEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLG 619
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 318-593 1.38e-09

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: 61.61  E-value: 1.38e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  318 SALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQGCSGKLQQVARRAQRAQQGLQLQvlrlq 397
Cdd:TIGR02168  683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL-SRQISALRKDLARLEAEVEQLEERIAQLSKEL----- 756

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  398 qdkKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQL 477
Cdd:TIGR02168  757 ---TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  478 REGRASLREKEEQLLSLRDSFSSKQASLELGEgelpaaclkpaltpVDPAEPQDALAtcESDEAKMRRQAGVAAAASLVS 557
Cdd:TIGR02168  834 AATERRLEDLEEQIEELSEDIESLAAEIEELE--------------ELIEELESELE--ALLNERASLEEALALLRSELE 897

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1917203444  558 VDGEAEAGGESGTRALRREVGRLQAELAAERRARER 593
Cdd:TIGR02168  898 ELSEELRELESKRSELRRELEELREKLAQLELRLEG 933
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 318-586 8.61e-09

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: 58.91  E-value: 8.61e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  318 SALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAWER------ELAELRQGcSGKLQQVARRAQRAQQGLQL 391
Cdd:TIGR02168  725 SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERleeaeeELAEAEAE-IEELEAQIEQLKEELKALRE 803

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  392 QVLRLQQDKKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIV 471
Cdd:TIGR02168  804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA 883

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  472 GLRSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAACLKPALTPVDPAEPQDALATCESDEAKMrrqagvaa 551
Cdd:TIGR02168  884 SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE-------- 955

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1917203444  552 aaslvsvDGEAEAGGESGTRALRREVGRLQAELAA 586
Cdd:TIGR02168  956 -------AEALENKIEDDEEEARRRLKRLENKIKE 983
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 319-552 1.46e-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: 58.14  E-value: 1.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  319 ALIQELEERLWEKEQEVAALRRSLEQSEAAVA------QVLEERQKAWERELAELrqgcSGKLQQVARRAQRAQQGLQLQ 392
Cdd:TIGR02168  267 EKLEELRLEVSELEEEIEELQKELYALANEISrleqqkQILRERLANLERQLEEL----EAQLEELESKLDELAEELAEL 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  393 VLRLQQDKKQ---LQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSE 469
Cdd:TIGR02168  343 EEKLEELKEElesLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE 422

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  470 IVGLRS-----QLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAACLKPALTPVDPAEPQDALATCES-DEAKM 543
Cdd:TIGR02168  423 IEELLKkleeaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERlQENLE 502


                   ....*....
gi 1917203444  544 RRQAGVAAA 552
Cdd:TIGR02168  503 GFSEGVKAL 511
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 321-643 4.35e-08

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: 56.61  E-value: 4.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  321 IQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQK-AWERELAELRQGCSGKLQQV----------ARRAQRAQQGL 389
Cdd:TIGR02169  165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERlRREREKAERYQALLKEKREYegyellkekeALERQKEAIER 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  390 QLQVLRLQQDK--KQLQEEAARLMRQREELEDKVAACQK----EQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADV 463
Cdd:TIGR02169  245 QLASLEEELEKltEEISELEKRLEEIEQLLEELNKKIKDlgeeEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERL 324

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  464 SQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAACLKPALTPVDPAEPQDAL--ATCESDEA 541
Cdd:TIGR02169  325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLekLKREINEL 404

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  542 KMRRQAGVAAAASLVSVDGEAE---AGGESGTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQK- 617
Cdd:TIGR02169  405 KRELDRLQEELQRLSEELADLNaaiAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKe 484

                          330       340
                   ....*....|....*....|....*...
gi 1917203444  618 --QLQLSYVEMYQRNQQLERRLRERGAA 643
Cdd:TIGR02169  485 lsKLQRELAEAEAQARASEERVRGGRAV 512
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
319-498 1.16e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.31  E-value: 1.16e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  319 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQV----------------------LEERQKAWERELAELRQGcSGKLQ 376
Cdd:COG4913    610 AKLAALEAELAELEEELAEAEERLEALEAELDALqerrealqrlaeyswdeidvasAEREIAELEAELERLDAS-SDDLA 688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  377 QVARRAQRAqqglqlqvlrlQQDKKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEEtkWEVCQKAGEISLLKQQL 456
Cdd:COG4913    689 ALEEQLEEL-----------EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA--AEDLARLELRALLEERF 755

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1917203444  457 KdsQADVSQKLSEIV-GLRSQLREGRASLREKEEQLLSLRDSF 498
Cdd:COG4913    756 A--AALGDAVERELReNLEERIDALRARLNRAEEELERAMRAF 796
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
319-455 4.90e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.38  E-value: 4.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  319 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAWERELAELRQgcsgKLQQVARRAQRAQQGLQLQVLRLQQ 398
Cdd:COG4913    302 AELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLER----ELEERERRRARLEALLAALGLPLPA 377

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1917203444  399 DKKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQKAGEISLLKQQ 455
Cdd:COG4913    378 SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 342-493 1.87e-06

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: 51.18  E-value: 1.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 342 LEQSEAAVAQVLEERQKAWERELAELRQgcsgKLQQVARRAQRAQQGLQLQVLRLqqdkKQLQEEAARLMRQREELEDKV 421
Cdd:pfam05667 315 ATSSPPTKVETEEELQQQREEELEELQE----QLEDLESSIQELEKEIKKLESSI----KQVEEELEELKEQNEELEKQY 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 422 AAcqKEQA-DFLPRIEE--------------------TKWEVCQKA--GEISLLKQQLKDSQADVSQKLSEIVGLRSQLR 478
Cdd:pfam05667 387 KV--KKKTlDLLPDAEEniaklqalvdasaqrlvelaGQWEKHRVPliEEYRALKEAKSNKEDESQRKLEEIKELREKIK 464

                         170
                  ....*....|....*...
gi 1917203444 479 EGRASLREKEE---QLLS 493
Cdd:pfam05667 465 EVAEEAKQKEElykQLVA 482
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
321-611 4.42e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 50.04  E-value: 4.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 321 IQELEERLWEKEQEVAALRRSLEQSEAAvAQVLEERQKAWERELAELRQgcsgKLQQVARRAQRAQQGLQLQVLrlqqDK 400
Cdd:PRK02224  281 VRDLRERLEELEEERDDLLAEAGLDDAD-AEAVEARREELEDRDEELRD----RLEECRVAAQAHNEEAESLRE----DA 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 401 KQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEEtkwevcqkageislLKQQLKDSQA---DVSQKLSEIVGLRSQL 477
Cdd:PRK02224  352 DDLEERAEELREEAAELESELEEAREAVEDRREEIEE--------------LEEEIEELRErfgDAPVDLGNAEDFLEEL 417

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 478 REGRASLREKEEqllSLRDSFSSKQASLELGEGELPAACLKPALTPVDPAEPQDALATCESDEAKMRRQAGvAAAASLVS 557
Cdd:PRK02224  418 REERDELREREA---ELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELE-DLEEEVEE 493

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1917203444 558 VDGEAEAGGESGTRALRREVGRLQAELAAERRARERQGasfAEERRVWLEEKEK 611
Cdd:PRK02224  494 VEERLERAEDLVEAEDRIERLEERREDLEELIAERRET---IEEKRERAEELRE 544
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 321-501 7.33e-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: 47.61  E-value: 7.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 321 IQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQgcsgKLQQVARRAQRaqqglqlqvlrlqqDK 400
Cdd:COG1579    19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDL-EKEIKRLEL----EIEEVEARIKK--------------YE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 401 KQL-----QEEAARLMRQREELEDKVAACQKEQADFLPRIEEtkwevcqkageislLKQQLKDSQADVSQKLSEIVGLRS 475
Cdd:COG1579    80 EQLgnvrnNKEYEALQKEIESLKRRISDLEDEILELMERIEE--------------LEEELAELEAELAELEAELEEKKA 145

                         170       180
                  ....*....|....*....|....*.
gi 1917203444 476 QLREGRASLREKEEQLLSLRDSFSSK 501
Cdd:COG1579   146 ELDEELAELEAELEELEAEREELAAK 171
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
322-639 9.83e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 9.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 322 QELEERLWEKEQEVAALRRSLEQSEAAVAQV--LEERQKAWERELAELRQGCSGKLQQVARRAQRAQQGLQLQVLRLQQD 399
Cdd:COG4717   135 EALEAELAELPERLEELEERLEELRELEEELeeLEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 400 KKQLQEEAARLMRQREELEDKVAACQKEQadflpRIEETKWEVCQKAG--EISLLKQQLKDSQADVSQKLSEIVGL---- 473
Cdd:COG4717   215 LEEAQEELEELEEELEQLENELEAAALEE-----RLKEARLLLLIAAAllALLGLGGSLLSLILTIAGVLFLVLGLlall 289

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 474 ----------------RSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAACLKPALTPVDPAEPQDALATCE 537
Cdd:COG4717   290 flllarekaslgkeaeELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELE 369

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 538 SDEAKMRRQAGVAAAASLVSVDGEAEAGgesgtRALRREVGRLQAELAAERRARERQGASFAEERrvWLEEKEKVIEYQK 617
Cdd:COG4717   370 QEIAALLAEAGVEDEEELRAALEQAEEY-----QELKEELEELEEQLEELLGELEELLEALDEEE--LEEELEELEEELE 442

                         330       340
                  ....*....|....*....|..
gi 1917203444 618 QLQLSYVEMYQRNQQLERRLRE 639
Cdd:COG4717   443 ELEEELEELREELAELEAELEQ 464
PTZ00121 PTZ00121
MAEBL; Provisional
 325-658 1.27e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 1.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  325 EERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAWE-------RELAELRQGCSGKLQQVARRAQ---------RAQQG 388
Cdd:PTZ00121  1144 EARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAarkaeevRKAEELRKAEDARKAEAARKAEeerkaeearKAEDA 1223

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  389 LQLQVLRLQQDKKQLQEEAARLMRQREELEDKVAAcQKEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLS 468
Cdd:PTZ00121  1224 KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFE-EARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKK 1302

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  469 EIVGLRSQLREGRAS--LREKEEQLLSLRDSfSSKQASLELGEGELPAACLKPALTPVDPAEPQDALATCESDEAKMRRQ 546
Cdd:PTZ00121  1303 KADEAKKKAEEAKKAdeAKKKAEEAKKKADA-AKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD 1381

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  547 AGVAAAASLVSVD---GEAEAGGESGTRALRREVGRLQAElAAERRARERQGasfAEERRVWLEEKEKVIEYQKQlqlsy 623
Cdd:PTZ00121  1382 AAKKKAEEKKKADeakKKAEEDKKKADELKKAAAAKKKAD-EAKKKAEEKKK---ADEAKKKAEEAKKADEAKKK----- 1452

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1917203444  624 VEMYQRNQQLERRLRERGAAGGAStptpQHGEEKK 658
Cdd:PTZ00121  1453 AEEAKKAEEAKKKAEEAKKADEAK----KKAEEAK 1483
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
314-643 1.90e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.84  E-value: 1.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 314 PPSPSALIQELEERLWEKEQEVAALRRSLEQSEAAVAQV--LEERQKAWERELAELRQGCS-GKLQQVARRAQRAQQGLQ 390
Cdd:COG4717    66 PELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELeeLEAELEELREELEKLEKLLQlLPLYQELEALEAELAELP 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 391 LQVLRLQQDKKQLQEEAARLMRQREELEDKVAACQKEQADFLP----RIEETKWEVCQKAGEISLLKQQLKDSQADVSQK 466
Cdd:COG4717   146 ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLateeELQDLAEELEELQQRLAELEEELEEAQEELEEL 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 467 LSEIVGLRSQLREGRASLREKEEQ----LLSLRDSFSSKQASLELGEGELPA---------ACLKPALTPVDPAEPQDAL 533
Cdd:COG4717   226 EEELEQLENELEAAALEERLKEARllllIAAALLALLGLGGSLLSLILTIAGvlflvlgllALLFLLLAREKASLGKEAE 305

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 534 ATCESDEAKMRRQAGVAAAASLVSVDGEAEAGGESG-------TRALRREVGRLQAELAAERRARERQ------GASFAE 600
Cdd:COG4717   306 ELQALPALEELEEEELEELLAALGLPPDLSPEELLElldrieeLQELLREAEELEEELQLEELEQEIAallaeaGVEDEE 385

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1917203444 601 ERRVWLEEKEKVIEYQKQLQlsyvemyQRNQQLERRLRERGAA 643
Cdd:COG4717   386 ELRAALEQAEEYQELKEELE-------ELEEQLEELLGELEEL 421
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 321-515 2.14e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.45  E-value: 2.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 321 IQELEERLWEKEQEVAALRRSLEQSEAAVAQvLEERQKAWERELAELRQgcsgKLQQVARRAQRAQQGLQLQVLRLQQDK 400
Cdd:COG4942    57 LAALERRIAALARRIRALEQELAALEAELAE-LEKEIAELRAELEAQKE----ELAELLRALYRLGRQPPLALLLSPEDF 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 401 KQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREG 480
Cdd:COG4942   132 LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL 211

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1917203444 481 RASLREKEEQLLSLRDSFSSKQASLELGEGELPAA 515
Cdd:COG4942   212 AAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 319-494 3.56e-05

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: 45.69  E-value: 3.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 319 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQ---GCSGKLQQVarRAQRAQQGLQLQVLR 395
Cdd:COG1579    24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRL-ELEIEEVEArikKYEEQLGNV--RNNKEYEALQKEIES 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 396 LQQDKKQLQEEAARLMRQREELEDKVAACQKEQADflprieetkwevcqkageislLKQQLKDSQADVSQKLSEIVGLRS 475
Cdd:COG1579   101 LKRRISDLEDEILELMERIEELEEELAELEAELAE---------------------LEAELEEKKAELDEELAELEAELE 159

                         170       180
                  ....*....|....*....|
gi 1917203444 476 QLREGRASLREK-EEQLLSL 494
Cdd:COG1579   160 ELEAEREELAAKiPPELLAL 179
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 317-637 3.69e-05

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: 46.81  E-value: 3.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 317 PSALIqeLEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKA---WERELAELRQGCsGKLQQVARRAQRAQQGLQLQV 393
Cdd:pfam07888  27 PRAEL--LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDreqWERQRRELESRV-AELKEELRQSREKHEELEEKY 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 394 LRLQQDKKQLQEEAARLMRQRE-------ELEDKVAACQKEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADVSQK 466
Cdd:pfam07888 104 KELSASSEELSEEKDALLAQRAahearirELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQT 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 467 LSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQasLELGEGELPAACLKPALTPVDPAepQDALATCESDEAKMRRQ 546
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLT--QKLTTAHRKEAENEALLEELRSL--QERLNASERKVEGLGEE 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 547 AGVAAA-------------------------ASLVSVDGEAEAGGESGT------------RALRREVGRLQAELAAERR 589
Cdd:pfam07888 260 LSSMAAqrdrtqaelhqarlqaaqltlqladASLALREGRARWAQERETlqqsaeadkdriEKLSAELQRLEERLQEERM 339

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1917203444 590 ARERQGASFAEER---RVWLEEKEKVIEYQK-----------QLQLSYVEMYQRNQQLERRL 637
Cdd:pfam07888 340 EREKLEVELGREKdcnRVQLSESRRELQELKaslrvaqkekeQLQAEKQELLEYIRQLEQRL 401
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 321-639 5.98e-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: 46.59  E-value: 5.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  321 IQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRqgcsGKLQQVARRAQRAQQglqlqvlrlqqDK 400
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL-EEEIEELQ----KELYALANEISRLEQ-----------QK 304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  401 KQLQEEAARLMRQREELEDkvaacqkEQADFLPRIEETKWEVCQKAGEISLLKQQLkdsqADVSQKLSEivgLRSQLREG 480
Cdd:TIGR02168  305 QILRERLANLERQLEELEA-------QLEELESKLDELAEELAELEEKLEELKEEL----ESLEAELEE---LEAELEEL 370

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  481 RASLREKEEQLLSLRDSFSSKQASLELGEGELpaaclkpaltpvdpaEPQDALATCESDEAKMRRQAGVAAAASLVSVDG 560
Cdd:TIGR02168  371 ESRLEELEEQLETLRSKVAQLELQIASLNNEI---------------ERLEARLERLEDRRERLQQEIEELLKKLEEAEL 435

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1917203444  561 EAEAGGESGTRALRREvgrLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQlSYVEMYQRNQQLERRLRE 639
Cdd:TIGR02168  436 KELQAELEELEEELEE---LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD-SLERLQENLEGFSEGVKA 510
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 309-515 8.21e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.53  E-value: 8.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 309 FAACSPPSPSALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQgcsgKLQQVARRAQRAQQG 388
Cdd:COG4942    10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL-ERRIAALAR----RIRALEQELAALEAE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 389 LQLQvlrlqqdKKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQKAGEISLLKQ----------QLKD 458
Cdd:COG4942    85 LAEL-------EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYlaparreqaeELRA 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1917203444 459 SQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAA 515
Cdd:COG4942   158 DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE 214
PTZ00121 PTZ00121
MAEBL; Provisional
 322-633 1.29e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 1.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  322 QELEERLWEKEQEVAALRRSLEQSEAA--VAQVLEERQKAWE-RELAELRQGCSGKLQQVARRAQRAQQGLQLQVLRLQQ 398
Cdd:PTZ00121  1473 DEAKKKAEEAKKADEAKKKAEEAKKKAdeAKKAAEAKKKADEaKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELK 1552

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  399 DKKQLQ--EEAARLMRQREELEDKVAACQKeqADFLPRIEETKWEvcqkagEISLLKQQLKDSQADVSQKLSEIVGLRSQ 476
Cdd:PTZ00121  1553 KAEELKkaEEKKKAEEAKKAEEDKNMALRK--AEEAKKAEEARIE------EVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  477 LREGRaSLREKEEQLLSLRDSFSSKQASLELGEGELPAACLKPALTPVDPAEPQDALATCESDEAK----MRRQAGVAAA 552
Cdd:PTZ00121  1625 LKKAE-EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKaaeaLKKEAEEAKK 1703

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  553 ASLVSVDGEAEAGGESGTRAlRREVGRLQAELAAERRARERQGAsfaEERRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQ 632
Cdd:PTZ00121  1704 AEELKKKEAEEKKKAEELKK-AEEENKIKAEEAKKEAEEDKKKA---EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEA 1779


                   .
gi 1917203444  633 L 633
Cdd:PTZ00121  1780 V 1780
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 399-642 1.38e-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: 45.43  E-value: 1.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  399 DKK---QLQEEAARLMRQREELEDKVAACQ--------------KEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQA 461
Cdd:TIGR02168  237 LREeleELQEELKEAEEELEELTAELQELEekleelrlevseleEEIEELQKELYALANEISRLEQQKQILRERLANLER 316

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  462 DVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAACLKpaltpvdPAEPQDALATCESDEA 541
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR-------LEELEEQLETLRSKVA 389

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  542 KMRRQAGvAAAASLVSVDGEAEAGGESGTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQL 621
Cdd:TIGR02168  390 QLELQIA-SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELRE 468

                          250       260
                   ....*....|....*....|.
gi 1917203444  622 SYVEMYQRNQQLERRLRERGA 642
Cdd:TIGR02168  469 ELEEAEQALDAAERELAQLQA 489
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 399-654 1.59e-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: 44.37  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 399 DKKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLR 478
Cdd:COG4942    21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 479 EGRASLREkeeqllSLRDSFSSKQASLelgegelpaacLKPALTPVDPAEPQDALATCESDEAKMRRQAG--VAAAASLV 556
Cdd:COG4942   101 AQKEELAE------LLRALYRLGRQPP-----------LALLLSPEDFLDAVRRLQYLKYLAPARREQAEelRADLAELA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 557 SVDGEAEAGGESgTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQlsyvemyQRNQQLERR 636
Cdd:COG4942   164 ALRAELEAERAE-LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE-------ALIARLEAE 235

                         250
                  ....*....|....*...
gi 1917203444 637 LRERGAAGGASTPTPQHG 654
Cdd:COG4942   236 AAAAAERTPAAGFAALKG 253
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
326-639 3.82e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.88  E-value: 3.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 326 ERLWEKEQEVAALRRSLEQseaavaqvLEERQKAWERELAELRQgcsgkLQQVARRAQRAQQGLQLQVLRLQQDKKQLQE 405
Cdd:PRK02224  468 ETIEEDRERVEELEAELED--------LEEEVEEVEERLERAED-----LVEAEDRIERLEERREDLEELIAERRETIEE 534

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 406 E---AARLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQKAGEISLLKQQLkDSQADVSQKLSEIVGLRSQ---LRE 479
Cdd:PRK02224  535 KrerAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERI-ESLERIRTLLAAIADAEDEierLRE 613

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 480 GRASLREKEEQllsLRDSFSSKQASLELGEGELPAACLkpaltpvdpaepqdalatcesDEAKMRRQagvAAAASLVSVD 559
Cdd:PRK02224  614 KREALAELNDE---RRERLAEKRERKRELEAEFDEARI---------------------EEAREDKE---RAEEYLEQVE 666

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 560 GEAEAGGESGTRaLRREVGRLQAELAAERRARERQGAsfAEERRVWLEEkekVIEYQKQLQLSY----VEMYQRN-QQLE 634
Cdd:PRK02224  667 EKLDELREERDD-LQAEIGAVENELEELEELRERREA--LENRVEALEA---LYDEAEELESMYgdlrAELRQRNvETLE 740


                  ....*
gi 1917203444 635 RRLRE 639
Cdd:PRK02224  741 RMLNE 745
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
320-492 4.17e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 4.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 320 LIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQkawerELAELRQGCSGKLQQVARRAQRAqqglqlqvLRLQQD 399
Cdd:PRK03918  194 LIKEKEKELEEVLREINEISSELPELREELEKLEKEVK-----ELEELKEEIEELEKELESLEGSK--------RKLEEK 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 400 KKQLQEEAARLMRQREELEDKVAACQ--KEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQL 477
Cdd:PRK03918  261 IRELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340

                         170
                  ....*....|....*
gi 1917203444 478 REgrasLREKEEQLL 492
Cdd:PRK03918  341 EE----LKKKLKELE 351
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 434-643 4.32e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 4.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  434 RIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELP 513
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  514 AACLKPALTPVDPAEPQDALATCESDEAKmrRQAGVAAAASLVSVDGEAEAGGESGTRALRREVGRLQAELAAERRARER 593
Cdd:TIGR02168  758 ELEAEIEELEERLEEAEEELAEAEAEIEE--LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1917203444  594 QGASFAEERRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQLERRLRERGAA 643
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL 885
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 321-507 7.08e-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: 43.02  E-value: 7.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  321 IQELEERLWEKEQEVAALRRSLEQ----SEAAVAQ---VLE---------ERQKAWERELAELRQGCSgkLQQVARRAQ- 383
Cdd:COG3096    439 AEDYLAAFRAKEQQATEEVLELEQklsvADAARRQfekAYElvckiagevERSQAWQTARELLRRYRS--QQALAQRLQq 516

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  384 -RAQQGLQLQVLRLQQDKKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQKAGEislLKQQLKDSQAD 462
Cdd:COG3096    517 lRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSE---LRQQLEQLRAR 593

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1917203444  463 VSQ----------------KLSEIVGL----RSQLREGRASLREKEEQLLSLRDSFSSKQASLEL 507
Cdd:COG3096    594 IKElaarapawlaaqdaleRLREQSGEaladSQEVTAAMQQLLEREREATVERDELAARKQALES 658
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
315-646 8.95e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 8.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 315 PSPSALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQgcsgKLQQVARRAQRAqqglqlqvl 394
Cdd:COG4372    20 PKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQL-EEELEQARS----ELEQLEEELEEL--------- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 395 rlqqdKKQLQEEAARLMRQREELEDKvaacQKEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLR 474
Cdd:COG4372    86 -----NEQLQAAQAELAQAQEELESL----QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 475 SQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAACLKPALTPVDPAEPQDALATCESDEAKMRRQAGVAAAAS 554
Cdd:COG4372   157 EQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALS 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 555 LVSVDGEAEAGGESGTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEK--EKVIEYQKQLQLSYVEMYQRNQQ 632
Cdd:COG4372   237 ALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAalELKLLALLLNLAALSLIGALEDA 316

                         330
                  ....*....|....
gi 1917203444 633 LERRLRERGAAGGA 646
Cdd:COG4372   317 LLAALLELAKKLEL 330
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 321-649 2.74e-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: 41.09  E-value: 2.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  321 IQELEERLWEKEQEVAALRRSLEQSEAAvAQVLEERQKAWERELAELRQGC------SGKLQQVARRAQRAQQ------- 387
Cdd:COG3096    356 LEELTERLEEQEEVVEEAAEQLAEAEAR-LEAAEEEVDSLKSQLADYQQALdvqqtrAIQYQQAVQALEKARAlcglpdl 434

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  388 --GLQLQVLRLQQDKKQLQEEAARLMRQREELEDkVAACQKEQADFLprieetkweVCQKAGEISLL------KQQLKD- 458
Cdd:COG3096    435 tpENAEDYLAAFRAKEQQATEEVLELEQKLSVAD-AARRQFEKAYEL---------VCKIAGEVERSqawqtaRELLRRy 504

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  459 -SQADVSQKLSeivGLRSQLREGRASLREKEEqLLSLRDSFSsKQASLELGEGELPAACLKPALTPVDpaEPQDALATCE 537
Cdd:COG3096    505 rSQQALAQRLQ---QLRAQLAELEQRLRQQQN-AERLLEEFC-QRIGQQLDAAEELEELLAELEAQLE--ELEEQAAEAV 577

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  538 SDEAKMRRQagvaaaaslvsvdgeaeaggESGTRALRREVGR-----LQAELAAERrARERQGASFAEERRVwLEEKEKV 612
Cdd:COG3096    578 EQRSELRQQ--------------------LEQLRARIKELAArapawLAAQDALER-LREQSGEALADSQEV-TAAMQQL 635

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1917203444  613 IEYQKQLQLSYVEMYQRNQQLERRLRERGAAGGASTP 649
Cdd:COG3096    636 LEREREATVERDELAARKQALESQIERLSQPGGAEDP 672
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
332-529 2.99e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.77  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 332 EQEVAALRRSLEQSEAAV---------------AQVLEERQKAWERELAELRQGCSGKLQQVAR-RAQRAQQGLQLQVLR 395
Cdd:COG3206   181 EEQLPELRKELEEAEAALeefrqknglvdlseeAKLLLQQLSELESQLAEARAELAEAEARLAAlRAQLGSGPDALPELL 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 396 LQQDKKQLQEEAARLMRQREELEDK-------VAACQKEQADFLPRIEETKWEVCQKAG-EISLLKQQ---LKDSQADVS 464
Cdd:COG3206   261 QSPVIQQLRAQLAELEAELAELSARytpnhpdVIALRAQIAALRAQLQQEAQRILASLEaELEALQAReasLQAQLAQLE 340

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1917203444 465 QKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFssKQASLELGEGELPAACLKPALTPVDPAEP 529
Cdd:COG3206   341 ARLAELPELEAELRRLEREVEVARELYESLLQRL--EEARLAEALTVGNVRVIDPAVVPLKPVSP 403
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 320-461 3.31e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 40.00  E-value: 3.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  320 LIQELEERLWEKEQEVAALRRSLEQSEAAVAQvLEERQKAWERELAELRQG---CSGKLQQVARRAQRAQQGLQLQVLRl 396
Cdd:smart00787 145 LKEGLDENLEGLKEDYKLLMKELELLNSIKPK-LRDRKDALEEELRQLKQLedeLEDCDPTELDRAKEKLKKLLQEIMI- 222

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1917203444  397 qqdKKQLQEEaarLMRQREELEDKVAACQKEQADFLPRI--EETKWEVCQK--AGEISLLKQQLKDSQA 461
Cdd:smart00787 223 ---KVKKLEE---LEEELQELESKIEDLTNKKSELNTEIaeAEKKLEQCRGftFKEIEKLKEQLKLLQS 285
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
402-640 4.27e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 4.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  402 QLQEEAARLMRQREELEDKVAACQK-EQADFlpriEETKWEVCQKagEISLLKQQLKDSQADvSQKLSEivgLRSQLREG 480
Cdd:COG4913    628 EAEERLEALEAELDALQERREALQRlAEYSW----DEIDVASAER--EIAELEAELERLDAS-SDDLAA---LEEQLEEL 697

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  481 RASLREKEEQLLSLRDSFSSKQASLELGEGELPAAclKPALTPVDPAEPQDALATCEsdeaKMRRQAGVAAAASLVSVDG 560
Cdd:COG4913    698 EAELEELEEELDELKGEIGRLEKELEQAEEELDEL--QDRLEAAEDLARLELRALLE----ERFAAALGDAVERELRENL 771

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  561 EAEaggesgTRALRREVGRLQAELaaeRRARERQGASFAEERRVWLEEKEKVIEYQKQL-QLSYVEMYQRNQQLERRLRE 639
Cdd:COG4913    772 EER------IDALRARLNRAEEEL---ERAMRAFNREWPAETADLDADLESLPEYLALLdRLEEDGLPEYEERFKELLNE 842


                   .
gi 1917203444  640 R 640
Cdd:COG4913    843 N 843
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 322-490 4.48e-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: 4.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  322 QELEERlweKEQEVAALRRSLE-QSEAAVAQVLEERQK---AWERELAELRQGCSGK--LQQVARRAQRAQQGLQLQVLR 395
Cdd:pfam01576  319 QELRSK---REQEVTELKKALEeETRSHEAQLQEMRQKhtqALEELTEQLEQAKRNKanLEKAKQALESENAELQAELRT 395

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  396 LQQDKK-----------QLQEEAARLM---RQREELEDKVAACQKEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQA 461
Cdd:pfam01576  396 LQQAKQdsehkrkklegQLQELQARLSeseRQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQE 475

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1917203444  462 ----DVSQKLSEIVGLRsQLREGRASLREKEEQ 490
Cdd:pfam01576  476 llqeETRQKLNLSTRLR-QLEDERNSLQEQLEE 507
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 572-640 5.97e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 37.56  E-value: 5.97e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1917203444  572 ALRREVGRLQAELAAERRARERQGASFAEERRVWLEEK--EKVIEYQKQLQLSYVEMYQRNQQLERRLRER 640
Cdd:smart00935  29 KRQAELEKLEKELQKLKEKLQKDAATLSEAAREKKEKElqKKVQEFQRKQQKLQQDLQKRQQEELQKILDK 99
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
326-506 6.18e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 6.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 326 ERLWEKEQEVAALRRSLEQSEAAVAQV----LEERQKAWE--RELAELRQGCSGKLQQVARRAQRAQQGLQLQVLRLQQd 399
Cdd:PRK03918  486 EKVLKKESELIKLKELAEQLKELEEKLkkynLEELEKKAEeyEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKK- 564

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444 400 KKQLQEEAARLMRQ--------REELEDKVAACQKEQADFLpRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIV 471
Cdd:PRK03918  565 LDELEEELAELLKEleelgfesVEELEERLKELEPFYNEYL-ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE 643

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1917203444 472 GLRSQLREGRASL-----REKEEQLLSLRDSFSSKQASLE 506
Cdd:PRK03918  644 ELRKELEELEKKYseeeyEELREEYLELSRELAGLRAELE 683
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 314-417 6.46e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 39.93  E-value: 6.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  314 PPSPSALIQELEerlwekeQEVAALRRSLEQ--SEAAVAQVLEERQKAWERELAELRQGCSGKLQQVARRAQRAQQGLQL 391
Cdd:PRK11448   137 PEDPENLLHALQ-------QEVLTLKQQLELqaREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAE 209

                           90       100
                   ....*....|....*....|....*.
gi 1917203444  392 QVLRLQQDKKQLQEEAARLMRQREEL 417
Cdd:PRK11448   210 TSQERKQKRKEITDQAAKRLELSEEE 235
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
316-427 6.59e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 6.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  316 SPSALIQELEERLWEKEQEVAALRRSLEQSEAAVAQvLEERQKAWERELAELRQgcsgKLQQVARRAQRAQQGLQLQVLR 395
Cdd:COG4913    682 ASSDDLAALEEQLEELEAELEELEEELDELKGEIGR-LEKELEQAEEELDELQD----RLEAAEDLARLELRALLEERFA 756

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1917203444  396 LQQDKKQLQEEAARLMRQREELEDKVAACQKE 427
Cdd:COG4913    757 AALGDAVERELRENLEERIDALRARLNRAEEE 788
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
402-623 7.11e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 7.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  402 QLQEEAARLMRQREELEDkvaacQKEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIvgLRSQLREGR 481
Cdd:COG4913    229 ALVEHFDDLERAHEALED-----AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL--LEAELEELR 301

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  482 ASLREKEEQLLSLRDSFSSKQASLElgegELPAACLKPALTPVDPAEPQDALATCESDEAKMRRQAGVAAAASLvsvdGE 561
Cdd:COG4913    302 AELARLEAELERLEARLDALREELD----ELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAL----GL 373

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1917203444  562 AEAGGESGTRALRREVGRLQAELAAER-RARERQGASFAEERRVW--LEEKEKVIEYQKQLQLSY 623
Cdd:COG4913    374 PLPASAEEFAALRAEAAALLEALEEELeALEEALAEAEAALRDLRreLRELEAEIASLERRKSNI 438
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 345-638 7.34e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.67  E-value: 7.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  345 SEAAVAQVLEERQKAWERELAELRQgcsgklqQVARRAQRAqqglqlqvlrlqqdkKQLQEEAARLMRQREELEDKVAAC 424
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQS-------ELRRIENRL---------------DELSQELSDASRKIGEIEKEIEQL 728

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  425 QKEQADFLPRIEEtkwevcqKAGEISLLKQ-------QLKDSQADVSQKLSEIVGLRSQL-----REGRASLREKEEQLL 492
Cdd:TIGR02169  729 EQEEEKLKERLEE-------LEEDLSSLEQeienvksELKELEARIEELEEDLHKLEEALndleaRLSHSRIPEIQAELS 801

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  493 SLRDSFSSKQASLELGEGELPAACLKPALTPVDPAEPQDALATCESDEAKMRRQ--AGVAAAASLVSVDGEAEAGG---E 567
Cdd:TIGR02169  802 KLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEieNLNGKKEELEEELEELEAALrdlE 881

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  568 SGTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQL----------------QLSYVEMYQRNQ 631
Cdd:TIGR02169  882 SRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELseiedpkgedeeipeeELSLEDVQAELQ 961


                   ....*..
gi 1917203444  632 QLERRLR 638
Cdd:TIGR02169  962 RVEEEIR 968
PTZ00121 PTZ00121
MAEBL; Provisional
 321-511 8.61e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 8.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  321 IQELEERLWEKEQEVAALRRSLEQSEAAVAQVLE-----ERQKAWERELAELRQGCSGKLQQVaRRAQRAQQGLQLQVLR 395
Cdd:PTZ00121  1563 KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEvmklyEEEKKMKAEEAKKAEEAKIKAEEL-KKAEEEKKKVEQLKKK 1641

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203444  396 LQQDKKQLQE--EAARLMRQREELEDKVAACQKEQADFLPRIEETKwevcQKAGEISLLKQQLKDSQADVSQKLSEIVGL 473
Cdd:PTZ00121  1642 EAEEKKKAEElkKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE----KKAAEALKKEAEEAKKAEELKKKEAEEKKK 1717

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1917203444  474 RSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGE 511
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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