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Conserved domains on  [gi|109090301|ref|XP_001109817|]
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leucine zipper putative tumor suppressor 2 isoform X1 [Macaca mulatta]

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 ...
 439-636 4.34e-81

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: 255.31  E-value: 4.34e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301  439 TKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSEGRARGLQEAARARELELEACSQELQRHRQ 518
Cdd:pfam06818   1 TKWEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSKTLELEVCENELQRKKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301  519 EAERLREKAGQLDAEAAGLREPAVPPATADPFLLAESDEAKVQRAAAGVGGSLRAQVERLRVELQRERRRGEEQRDSFEG 598
Cdd:pfam06818  81 EAELLREKVGKLEEEVSGLREALSDVSPSGYESVYESDEAKEQRQEEADLGSLRREVERLRAELREERQRRERQASSFEQ 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 109090301  599 ERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQ 636
Cdd:pfam06818 161 ERRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
GAS super family cl25894
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 402-471 2.39e-05

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


The actual alignment was detected with superfamily member pfam13851:

Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 45.67  E-value: 2.39e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109090301  402 RQLQDDFAQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSG-EISLLKQQLKESQAELVQKGSEL 471
Cdd:pfam13851  95 KVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQKTGlKNLLLEKKLQALGETLEKKEAQL 165
 
Name Accession Description Interval E-value
Fez1 pfam06818
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ...
 439-636 4.34e-81

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: 255.31  E-value: 4.34e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301  439 TKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSEGRARGLQEAARARELELEACSQELQRHRQ 518
Cdd:pfam06818   1 TKWEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSKTLELEVCENELQRKKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301  519 EAERLREKAGQLDAEAAGLREPAVPPATADPFLLAESDEAKVQRAAAGVGGSLRAQVERLRVELQRERRRGEEQRDSFEG 598
Cdd:pfam06818  81 EAELLREKVGKLEEEVSGLREALSDVSPSGYESVYESDEAKEQRQEEADLGSLRREVERLRAELREERQRRERQASSFEQ 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 109090301  599 ERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQ 636
Cdd:pfam06818 161 ERRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 332-657 4.82e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 79.21  E-value: 4.82e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 332 KLQEREAELQQLRDSLDENEATMcQAYEERQRHWQREREALREDcaaqaqraqraqqllqlqVFQLQQEKRQLQDDFAQL 411
Cdd:COG1196  233 KLRELEAELEELEAELEELEAEL-EELEAELAELEAELEELRLE------------------LEELELELEEAQAEEYEL 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 412 LQEREQLERRCATLEREQRELGPRLEETKWevcqksgEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSEGR 491
Cdd:COG1196  294 LAELARLEQDIARLEERRRELEERLEELEE-------ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 492 ARGLQEAARARELELEACSQELQRHRQEAERLREKAGQLDAEAAGLREpavppatadpfLLAESDEAKVQRAAAgvggsl 571
Cdd:COG1196  367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE-----------RLERLEEELEELEEA------ 429

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 572 RAQVERLRVELQRErrrgeeqrdsfEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEARELAELG 651
Cdd:COG1196  430 LAELEEEEEEEEEA-----------LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498


                 ....*.
gi 109090301 652 LAEQAP 657
Cdd:COG1196  499 AEADYE 504
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 329-548 4.22e-11

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 66.62  E-value: 4.22e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301   329 LEGKLQEREAELQQLRDSLDENEATMCQAYEERQRHwQREREALREdcaaqaqraqraqqllqlQVFQLQQEKRQLQDDF 408
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL-KEELKALRE------------------ALDELRAELTLLNEEA 819

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301   409 AQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSE-------LVALRVALREA 481
Cdd:TIGR02168  820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNErasleeaLALLRSELEEL 899

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301   482 RATLRVSEGRARGLQEAARARELELEACSQELQRHRQEAERLREKA---GQLDAEAAGLREPAVPPATAD 548
Cdd:TIGR02168  900 SEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLseeYSLTLEEAEALENKIEDDEEE 969
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 402-471 2.39e-05

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 45.67  E-value: 2.39e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109090301  402 RQLQDDFAQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSG-EISLLKQQLKESQAELVQKGSEL 471
Cdd:pfam13851  95 KVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQKTGlKNLLLEKKLQALGETLEKKEAQL 165
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
329-539 8.43e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.80  E-value: 8.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 329 LEGKLQEREAELQQLRDSLDENEATMCQAYEERQRHWQReREALREdcaaqaqraqraqqllqlqvfqLQQEKRQLQDDF 408
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHEER-REELET----------------------LEAEIEDLRETI 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 409 AQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVA----------L 478
Cdd:PRK02224 268 AETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAaqahneeaesL 347

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109090301 479 REARATLrvsEGRARGLQEAARARELELEACsqelqrhRQEAERLREKAGQLDAEAAGLRE 539
Cdd:PRK02224 348 REDADDL---EERAEELREEAAELESELEEA-------REAVEDRREEIEELEEEIEELRE 398
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 453-529 4.45e-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: 37.95  E-value: 4.45e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109090301   453 LKQQLKESQAELVQKGSELVALRVALREARATLRvsegrarglQEAARARELELEACSQELQRHRQEAERLREKAGQ 529
Cdd:smart00935  23 LEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS---------EAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQ 90
 
Name Accession Description Interval E-value
Fez1 pfam06818
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ...
 439-636 4.34e-81

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: 255.31  E-value: 4.34e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301  439 TKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSEGRARGLQEAARARELELEACSQELQRHRQ 518
Cdd:pfam06818   1 TKWEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSKTLELEVCENELQRKKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301  519 EAERLREKAGQLDAEAAGLREPAVPPATADPFLLAESDEAKVQRAAAGVGGSLRAQVERLRVELQRERRRGEEQRDSFEG 598
Cdd:pfam06818  81 EAELLREKVGKLEEEVSGLREALSDVSPSGYESVYESDEAKEQRQEEADLGSLRREVERLRAELREERQRRERQASSFEQ 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 109090301  599 ERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQ 636
Cdd:pfam06818 161 ERRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 332-657 4.82e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 79.21  E-value: 4.82e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 332 KLQEREAELQQLRDSLDENEATMcQAYEERQRHWQREREALREDcaaqaqraqraqqllqlqVFQLQQEKRQLQDDFAQL 411
Cdd:COG1196  233 KLRELEAELEELEAELEELEAEL-EELEAELAELEAELEELRLE------------------LEELELELEEAQAEEYEL 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 412 LQEREQLERRCATLEREQRELGPRLEETKWevcqksgEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSEGR 491
Cdd:COG1196  294 LAELARLEQDIARLEERRRELEERLEELEE-------ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 492 ARGLQEAARARELELEACSQELQRHRQEAERLREKAGQLDAEAAGLREpavppatadpfLLAESDEAKVQRAAAgvggsl 571
Cdd:COG1196  367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE-----------RLERLEEELEELEEA------ 429

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 572 RAQVERLRVELQRErrrgeeqrdsfEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEARELAELG 651
Cdd:COG1196  430 LAELEEEEEEEEEA-----------LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498


                 ....*.
gi 109090301 652 LAEQAP 657
Cdd:COG1196  499 AEADYE 504
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 329-548 4.22e-11

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 66.62  E-value: 4.22e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301   329 LEGKLQEREAELQQLRDSLDENEATMCQAYEERQRHwQREREALREdcaaqaqraqraqqllqlQVFQLQQEKRQLQDDF 408
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL-KEELKALRE------------------ALDELRAELTLLNEEA 819

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301   409 AQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSE-------LVALRVALREA 481
Cdd:TIGR02168  820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNErasleeaLALLRSELEEL 899

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301   482 RATLRVSEGRARGLQEAARARELELEACSQELQRHRQEAERLREKA---GQLDAEAAGLREPAVPPATAD 548
Cdd:TIGR02168  900 SEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLseeYSLTLEEAEALENKIEDDEEE 969
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 329-634 2.02e-10

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: 64.32  E-value: 2.02e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301   329 LEGKLQEREAELQQLRDSLDENEATMCQAyEERQRHWQREREALREDcaaqaqraqraqqllqlqvfqlqqEKRQLQDDF 408
Cdd:TIGR02169  242 IERQLASLEEELEKLTEEISELEKRLEEI-EQLLEELNKKIKDLGEE------------------------EQLRVKEKI 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301   409 AQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVS 488
Cdd:TIGR02169  297 GELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEV 376

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301   489 EGRARGLQEAARARELELEACSQELQRHRQEAERLREKAGQLDAEAAGLREpAVPPATADpflLAESDEAKVQRAAAgvg 568
Cdd:TIGR02169  377 DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA-AIAGIEAK---INELEEEKEDKALE--- 449

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109090301   569 gsLRAQVERLrvelqrerRRGEEQRDSFEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQE 634
Cdd:TIGR02169  450 --IKKQEWKL--------EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 403-652 5.22e-10

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: 62.77  E-value: 5.22e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301   403 QLQDDFAQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREAR 482
Cdd:TIGR02168  702 ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE 781

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301   483 ATLRVSEGRARGLQEAARARELELEACSQELQRHRQEAERLREKAGQLDAEAAGLREPAVppatadpFLLAESDEAKVQR 562
Cdd:TIGR02168  782 AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE-------DLEEQIEELSEDI 854

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301   563 AaagvggSLRAQVERLRVELqrerrrgeeqrDSFEGERLAWQAEKEQVIRYQKQLQHNYIQMY-------RRNRQLEQEL 635
Cdd:TIGR02168  855 E------SLAAEIEELEELI-----------EELESELEALLNERASLEEALALLRSELEELSeelreleSKRSELRREL 917

                          250
                   ....*....|....*..
gi 109090301   636 QQLSLELEARELAELGL 652
Cdd:TIGR02168  918 EELREKLAQLELRLEGL 934
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 402-655 5.31e-10

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: 62.77  E-value: 5.31e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301   402 RQLQDDFAQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREA 481
Cdd:TIGR02168  694 AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301   482 RATLRVSEGRARGLQEAARARELELEACSQELQRHRQEAERLREKAGQLDAEAAGLREPAVPPATADPFLLAESDEAKVQ 561
Cdd:TIGR02168  774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED 853

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301   562 RAaagvggSLRAQVERLRVelqrerrrgeeQRDSFEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLE 641
Cdd:TIGR02168  854 IE------SLAAEIEELEE-----------LIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916

                          250
                   ....*....|....*.
gi 109090301   642 LEAR--ELAELGLAEQ 655
Cdd:TIGR02168  917 LEELreKLAQLELRLE 932
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
332-654 6.61e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 59.01  E-value: 6.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 332 KLQEREAELQQLRDSLDEneatmCQAYEERQRHWQREREALREDcaaqaqraqraqqllqlqvfqlQQEKRQLQDDFAQL 411
Cdd:COG4717   72 ELKELEEELKEAEEKEEE-----YAELQEELEELEEELEELEAE----------------------LEELREELEKLEKL 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 412 LQEREQLERRCAtLEREQRELGPRLEETKWEVCqksgEISLLKQQLKESQAELVQKGSELVALRVALR-EARATLRVSEG 490
Cdd:COG4717  125 LQLLPLYQELEA-LEAELAELPERLEELEERLE----ELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAE 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 491 RARGLQEAARARELELEACSQELQRHRQEAERLrEKAGQLDAEAAGLREPAVPP----------ATADPFLLAESDEAKV 560
Cdd:COG4717  200 ELEELQQRLAELEEELEEAQEELEELEEELEQL-ENELEAAALEERLKEARLLLliaaallallGLGGSLLSLILTIAGV 278

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 561 QRAAAGVGGSLRAQVERLRVELQRERRRGEEQRDSFEGERLAWQAEKEQV----------IRYQKQLQHNYIQMYRRNRQ 630
Cdd:COG4717  279 LFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALglppdlspeeLLELLDRIEELQELLREAEE 358

                        330       340
                 ....*....|....*....|....
gi 109090301 631 LEQELQQLSLELEARELAELGLAE 654
Cdd:COG4717  359 LEEELQLEELEQEIAALLAEAGVE 382
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
400-579 1.91e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 57.62  E-value: 1.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301  400 EKRQLQDDFAQLLQEREQLERRCATLEREQRELGpRLEETKWE---VCQKSGEISLLKQQLkesqAELVQKGSELVALRV 476
Cdd:COG4913   618 ELAELEEELAEAEERLEALEAELDALQERREALQ-RLAEYSWDeidVASAEREIAELEAEL----ERLDASSDDLAALEE 692

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301  477 ALREARATLRVSEGRARGLQEAARARELELEACSQELQRHRQEAERLREKAGQLDAEAaglrepavppatADPFLLAESD 556
Cdd:COG4913   693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL------------LEERFAAALG 760

                         170       180
                  ....*....|....*....|...
gi 109090301  557 EAKVQRAAAGVGGSLRAQVERLR 579
Cdd:COG4913   761 DAVERELRENLEERIDALRARLN 783
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 329-651 2.75e-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: 57.37  E-value: 2.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301   329 LEGKLQEREAELQQLRDSLDENEatmcQAYEERQRHWQREREALREDcAAQAQRAQRAQQLLQLQVFQLQQEKRQLQDDF 408
Cdd:TIGR02168  689 LEEKIAELEKALAELRKELEELE----EELEQLRKELEELSRQISAL-RKDLARLEAEVEQLEERIAQLSKELTELEAEI 763

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301   409 AQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVS 488
Cdd:TIGR02168  764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301   489 EGRARGLQEAARARELELEACSQELQRHRQEAERLREKAGQLDAEAAGLREpavppatadpfllAESDEAKVQRAAAGVG 568
Cdd:TIGR02168  844 EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS-------------ELEELSEELRELESKR 910

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301   569 GSLRAQVERLRvelqrerrrgeeqrDSFEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEAR--- 645
Cdd:TIGR02168  911 SELRRELEELR--------------EKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRlkr 976


                   ....*....
gi 109090301   646 ---ELAELG 651
Cdd:TIGR02168  977 lenKIKELG 985
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 322-639 4.11e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.60  E-value: 4.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301   322 EALLHCVLEGKLQEREAELQQLRDSLDENEaTMCQAYEERQRHWQREREALRedcaaqaqraqraqqllqLQVFQLQQEK 401
Cdd:TIGR02168  223 RELELALLVLRLEELREELEELQEELKEAE-EELEELTAELQELEEKLEELR------------------LEVSELEEEI 283

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301   402 RQLQDDFAQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREA 481
Cdd:TIGR02168  284 EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL 363

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301   482 RATLRVSEGRARGLQEAARARELELEACSQELQRHRQEAERLREKAGQLDAEAAGLREPAvppatadPFLLAESDEAKVQ 561
Cdd:TIGR02168  364 EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI-------EELLKKLEEAELK 436

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301   562 RAAAGVGGsLRAQVERLRVELQRERRRGEEQRDSFEGERLAWQAEKEQVIRYQ------KQLQHNYIQMYRRNRQLEQEL 635
Cdd:TIGR02168  437 ELQAELEE-LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQarldslERLQENLEGFSEGVKALLKNQ 515


                   ....
gi 109090301   636 QQLS 639
Cdd:TIGR02168  516 SGLS 519
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
333-572 1.35e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.92  E-value: 1.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301  333 LQEREAELQQLRDSLDENEA--TMCQAYEERQRH--WQREREALREDcaaqaqraqraqqllqlqVFQLQQEKRQLQDDF 408
Cdd:COG4913   257 IRELAERYAAARERLAELEYlrAALRLWFAQRRLelLEAELEELRAE------------------LARLEAELERLEARL 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301  409 AQLLQEREQLERRCAT-----LEREQRELGpRLEETKWEVCQKSGEislLKQQLKESQAELVQKGSELVALRvalREARA 483
Cdd:COG4913   319 DALREELDELEAQIRGnggdrLEQLEREIE-RLERELEERERRRAR---LEALLAALGLPLPASAEEFAALR---AEAAA 391

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301  484 TLRVSEGRARGLQEAARARELELEACSQELQRHRQEAERLREKAGQLDAEAAGLRE---PAVPPATADPFLLAE-----S 555
Cdd:COG4913   392 LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDalaEALGLDEAELPFVGElievrP 471

                         250
                  ....*....|....*..
gi 109090301  556 DEAKVQRAAAGVGGSLR 572
Cdd:COG4913   472 EEERWRGAIERVLGGFA 488
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 328-577 3.90e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 3.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 328 VLEGKLQEREAELQQLRDSLDENEATMcQAYEERQRHWQREREAL---REDCAAQAQRAQRAQQLLQLQVFQLQQEKRQL 404
Cdd:COG1196  306 RLEERRRELEERLEELEEELAELEEEL-EELEEELEELEEELEEAeeeLEEAEAELAEAEEALLEAEAELAEAEEELEEL 384

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 405 QDDFAQLLQEREQLERRCATLEREQRELGPRLEETKWEvcqksgEISLLKQQLKESQAELVQKGSELVALRVALREARAT 484
Cdd:COG1196  385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE------LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 485 LRVSEGRARGLQEAARARELELEAcSQELQRHRQEAERLREKAGQLDAEAAGLREPAVPPATAD---PFLLAESDEAKVQ 561
Cdd:COG1196  459 EALLELLAELLEEAALLEAALAEL-LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlagAVAVLIGVEAAYE 537

                        250
                 ....*....|....*.
gi 109090301 562 RAAAGVGGSLRAQVER 577
Cdd:COG1196  538 AALEAALAAALQNIVV 553
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 329-656 5.08e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 5.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 329 LEGKLQEREAELQQLRDSLDENEATMCQAYEERQRHWQREREALREdcaaqaqraqraqqllqlqVFQLQQEKRQLQDDF 408
Cdd:COG1196  349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA-------------------AAELAAQLEELEEAE 409

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 409 AQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVS 488
Cdd:COG1196  410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 489 EGRARGLQEAARARE-----------------------------------LELEACSQELQRHRQEAERL--------RE 525
Cdd:COG1196  490 AARLLLLLEAEADYEgflegvkaalllaglrglagavavligveaayeaaLEAALAAALQNIVVEDDEVAaaaieylkAA 569

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 526 KAGQldAEAAGLREPAVPPATADPFLLAESDEAKVQRAAAGVGGSLRAQVERL----RVELQRERRRGEEQRDSFEGERL 601
Cdd:COG1196  570 KAGR--ATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDtllgRTLVAARLEAALRRAVTLAGRLR 647

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 109090301 602 AWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEARELAELGLAEQA 656
Cdd:COG1196  648 EVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
455-644 5.47e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.00  E-value: 5.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301  455 QQLKESQAELVQKGSELVALR--VALREARATLRVSEGRARGLQEAARA--RELELEACSQELQRHRQEAERLREKAGQL 530
Cdd:COG4913   235 DDLERAHEALEDAREQIELLEpiRELAERYAAARERLAELEYLRAALRLwfAQRRLELLEAELEELRAELARLEAELERL 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301  531 DAEAAGLREpavppatadpfllaESDEAKVQRAAAGVG--GSLRAQVERLRVELQRERR--------------RGEEQRD 594
Cdd:COG4913   315 EARLDALRE--------------ELDELEAQIRGNGGDrlEQLEREIERLERELEERERrrarleallaalglPLPASAE 380

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 109090301  595 SFEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEA 644
Cdd:COG4913   381 EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 332-549 5.93e-07

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: 52.07  E-value: 5.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 332 KLQEREAELQQLRDSLDENEATMcQAYEERQRHWQREREALREDcaaqaqraqraQQLLQLQVFQLQQEKRQLQDDFAQL 411
Cdd:COG4942   21 AAAEAEAELEQLQQEIAELEKEL-AALKKEEKALLKQLAALERR-----------IAALARRIRALEQELAALEAELAEL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 412 LQEREQLERRcatLEREQRELGPRLEETkwevcQKSGEISLLK----------------------QQLKESQAELVQKGS 469
Cdd:COG4942   89 EKEIAELRAE---LEAQKEELAELLRAL-----YRLGRQPPLAlllspedfldavrrlqylkylaPARREQAEELRADLA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 470 ELVALRVALREARATLRVS----EGRARGLQEAARARELELEACSQELQRHRQEAERLREKAGQLDAEAAGLREPAVPPA 545
Cdd:COG4942  161 ELAALRAELEAERAELEALlaelEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240


                 ....
gi 109090301 546 TADP 549
Cdd:COG4942  241 ERTP 244
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 400-657 1.57e-06

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: 50.92  E-value: 1.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 400 EKRQLQDDFAQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALR 479
Cdd:COG4942   21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 480 EARATLRvseGRARGLQEAARARELELEACSQELQRHRQEAERLREKAGQLDAEAAGLREpavppatadpfllaesdeak 559
Cdd:COG4942  101 AQKEELA---ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRA-------------------- 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 560 vqraaagvggsLRAQVERLRVELQRERRRGEEQRDSFEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLS 639
Cdd:COG4942  158 -----------DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226

                        250
                 ....*....|....*...
gi 109090301 640 LELEARELAELGLAEQAP 657
Cdd:COG4942  227 ALIARLEAEAAAAAERTP 244
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 400-651 1.82e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.60  E-value: 1.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301   400 EKRQLQDDFAQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALR 479
Cdd:TIGR02168  254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301   480 EARATLRVSEGRARGLQEaararelELEACSQELQRHRQEAERLREKAGQLDAEAAGLREpavppATADPFLLAESDEAK 559
Cdd:TIGR02168  334 ELAEELAELEEKLEELKE-------ELESLEAELEELEAELEELESRLEELEEQLETLRS-----KVAQLELQIASLNNE 401

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301   560 VQRaaagvggsLRAQVERLRVELQRERRRGEEQRDSF-EGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQL 638
Cdd:TIGR02168  402 IER--------LEARLERLEDRRERLQQEIEELLKKLeEAELKELQAELEELEEELEELQEELERLEEALEELREELEEA 473

                          250
                   ....*....|....*
gi 109090301   639 SLELEA--RELAELG 651
Cdd:TIGR02168  474 EQALDAaeRELAQLQ 488
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 402-471 2.39e-05

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 45.67  E-value: 2.39e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109090301  402 RQLQDDFAQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSG-EISLLKQQLKESQAELVQKGSEL 471
Cdd:pfam13851  95 KVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQKTGlKNLLLEKKLQALGETLEKKEAQL 165
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
400-535 3.03e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.82  E-value: 3.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 400 EKRQLQDDFAQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALR 479
Cdd:COG4372   46 ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ 125

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 109090301 480 EARATLRVSEGRARGLQEAARARELELEACSQELQRHRQEAERLREKAGQLDAEAA 535
Cdd:COG4372  126 DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 400-579 3.95e-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: 3.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 400 EKRQLQDDFAQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAEL--VQKGSELVALRVA 477
Cdd:COG1579   18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnVRNNKEYEALQKE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 478 LREARATLRVSEGRARGLQEAARARELELEACSQELQrhrQEAERLREKAGQLDAEAAGLREpavppatadpflLAESDE 557
Cdd:COG1579   98 IESLKRRISDLEDEILELMERIEELEEELAELEAELA---ELEAELEEKKAELDEELAELEA------------ELEELE 162

                        170       180
                 ....*....|....*....|..
gi 109090301 558 AKVQRAAAGVGGSLRAQVERLR 579
Cdd:COG1579  163 AEREELAAKIPPELLALYERIR 184
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 329-486 8.03e-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: 44.53  E-value: 8.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 329 LEGKLQEREAELQQLRDSLDENEATMcQAYEERQRHWQREREALREDcaaqaqraqraqqLLQLQVFQLQQEKRQLQ--- 405
Cdd:COG1579   22 LEHRLKELPAELAELEDELAALEARL-EAAKTELEDLEKEIKRLELE-------------IEEVEARIKKYEEQLGNvrn 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 406 -DDFAQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARAT 484
Cdd:COG1579   88 nKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167


                 ..
gi 109090301 485 LR 486
Cdd:COG1579  168 LA 169
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
329-576 8.06e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.28  E-value: 8.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 329 LEGKLQEREAELQQLRDSLDENEATMCQAYEERQRHWQREREALREdcaaqAQRAQRAQQLLQLQVFQLQQEKRQLQDDF 408
Cdd:COG4372   43 LQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ-----LQAAQAELAQAQEELESLQEEAEELQEEL 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 409 AQLLQEREQLERRCATLEREQRELgprleetKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVS 488
Cdd:COG4372  118 EELQKERQDLEQQRKQLEAQIAEL-------QSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 489 EGRARGLQEAARARELELEACSQELQRHRQEAERLREKAGQLDAEAAGLREPAVPPATADPFLLAESDEAKVQRAAAGVG 568
Cdd:COG4372  191 EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVE 270


                 ....*...
gi 109090301 569 GSLRAQVE 576
Cdd:COG4372  271 KDTEEEEL 278
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
329-539 8.43e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.80  E-value: 8.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 329 LEGKLQEREAELQQLRDSLDENEATMCQAYEERQRHWQReREALREdcaaqaqraqraqqllqlqvfqLQQEKRQLQDDF 408
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHEER-REELET----------------------LEAEIEDLRETI 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 409 AQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVA----------L 478
Cdd:PRK02224 268 AETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAaqahneeaesL 347

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109090301 479 REARATLrvsEGRARGLQEAARARELELEACsqelqrhRQEAERLREKAGQLDAEAAGLRE 539
Cdd:PRK02224 348 REDADDL---EERAEELREEAAELESELEEA-------REAVEDRREEIEELEEEIEELRE 398
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
410-539 1.68e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 1.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 410 QLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSE 489
Cdd:COG4372   14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQ 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 109090301 490 GRARGLQEAARARELELEACSQELQRHRQEAERLREKAGQLDAEAAGLRE 539
Cdd:COG4372   94 AELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQS 143
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 328-576 1.87e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 1.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 328 VLEGKLQEREAELQQLRDSLDENEATMCQAYEERQRHWQREREALREDCAAQAQRAQRAQQLLQLQVFQLQQEKRQLQD- 406
Cdd:COG1196  535 AYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADAr 614

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 407 --DFAQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARAT 484
Cdd:COG1196  615 yyVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELE 694

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 485 LRVSEGRARGLQEAARARELELEACSQELQRHRQEAERLREKAGQLDAEAAGLREPAVPPATADPFLLAEsdeakvqraa 564
Cdd:COG1196  695 LEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE---------- 764

                        250
                 ....*....|..
gi 109090301 565 agvggsLRAQVE 576
Cdd:COG1196  765 ------LERELE 770
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
404-541 2.50e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.26  E-value: 2.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 404 LQDDFAQLLQEREQLERRCATLEREQRELGPRLEETkwEVCQKSGEISLLKQQLKESQ-----AELVQKGSELVALRVAL 478
Cdd:PRK02224 410 AEDFLEELREERDELREREAELEATLRTARERVEEA--EALLEAGKCPECGQPVEGSPhvetiEEDRERVEELEAELEDL 487

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109090301 479 REARATLRVSEGRARGLQEAARARELELEACS----------QELQRHRQEAERLREKAGQLDAEAAGLREPA 541
Cdd:PRK02224 488 EEEVEEVEERLERAEDLVEAEDRIERLEERREdleeliaerrETIEEKRERAEELRERAAELEAEAEEKREAA 560
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 324-563 5.51e-04

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 42.96  E-value: 5.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301  324 LLHCVLEGKLQEReAELQQLRDSLDENEATMCQAYEERQRHWQREREALREDCAAQAQRAQRAQQLLQLQVFQLQQEKR- 402
Cdd:pfam07888  31 LLQNRLEECLQER-AELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAs 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301  403 --QLQDDFAQLLQEREQLERRCATLEREQRELGPRLEEtkwevcqKSGEISLLKQQLKE--------------SQAELVQ 466
Cdd:pfam07888 110 seELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLE-------RETELERMKERAKKagaqrkeeeaerkqLQAKLQQ 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301  467 KGSELVALRVALREARATLRVSEGRARGLQE----------AARARELELEACSQELQrhrqeaeRLREKAGQLDAEAAG 536
Cdd:pfam07888 183 TEEELRSLSKEFQELRNSLAQRDTQVLQLQDtittltqkltTAHRKEAENEALLEELR-------SLQERLNASERKVEG 255

                         250       260
                  ....*....|....*....|....*..
gi 109090301  537 LREPAVPPATADPFLLAESDEAKVQRA 563
Cdd:pfam07888 256 LGEELSSMAAQRDRTQAELHQARLQAA 282
PTZ00121 PTZ00121
MAEBL; Provisional
 330-656 5.84e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 5.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301  330 EGKLQEREAELQQLRDSLDENEATMCQAYEERQRHWQREREA--LREDCAAQAQRAQRAQQLLQLQVFQLQQEKRQlQDD 407
Cdd:PTZ00121 1204 AARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAeeERNNEEIRKFEEARMAHFARRQAAIKAEEARK-ADE 1282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301  408 FAQLLQEREQLERRCATLEREQRELGPRLEET-KWEVCQKSGEISLLKQQLKESQAELVQKGSElvalrVALREARATLR 486
Cdd:PTZ00121 1283 LKKAEEKKKADEAKKAEEKKKADEAKKKAEEAkKADEAKKKAEEAKKKADAAKKKAEEAKKAAE-----AAKAEAEAAAD 1357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301  487 VSEgRARGLQEAARARELELEACSQELQRHRQE---AERLREKAGQLDAEAAGLREPAVPPATADPFL-----LAESDEA 558
Cdd:PTZ00121 1358 EAE-AAEEKAEAAEKKKEEAKKKADAAKKKAEEkkkADEAKKKAEEDKKKADELKKAAAAKKKADEAKkkaeeKKKADEA 1436

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301  559 KVQRAAAGVGGSLRAQVERLRvELQRERRRGEEQRDSFEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQL 638
Cdd:PTZ00121 1437 KKKAEEAKKADEAKKKAEEAK-KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEA 1515

                         330
                  ....*....|....*...
gi 109090301  639 SLELEARELAELGLAEQA 656
Cdd:PTZ00121 1516 KKAEEAKKADEAKKAEEA 1533
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
332-486 8.98e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 8.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 332 KLQEREAELQQLrdsLDENEATMCQAYEERQRHWQREREALREdcaAQAQRAQRAQQLLQLQVFQLQQEKRQLQDDFAQL 411
Cdd:COG4717  364 QLEELEQEIAAL---LAEAGVEDEEELRAALEQAEEYQELKEE---LEELEEQLEELLGELEELLEALDEEELEEELEEL 437

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109090301 412 LQEREQLERRCATLEREQRELGPRLEETKwevcqKSGEISLLKQQ---LKESQAELVQKGSELVALRVALREARATLR 486
Cdd:COG4717  438 EEELEELEEELEELREELAELEAELEQLE-----EDGELAELLQEleeLKAELRELAEEWAALKLALELLEEAREEYR 510
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 337-539 1.04e-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: 42.36  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301   337 EAELQQLRDSLDENEATMCQAYEERQRHWQREREALREdcaaqaqraqraQQLLQLQVFQLQQEKRQLQDDFAQLLQERE 416
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQE------------LSDASRKIGEIEKEIEQLEQEEEKLKERLE 740

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301   417 QLERRCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQkgSELVALRVALREARATLRVSEGRARGLQ 496
Cdd:TIGR02169  741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIE 818

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 109090301   497 EAARARELE---LEACSQELQRHRQEAE-RLREKAGQLDAEAAGLRE 539
Cdd:TIGR02169  819 QKLNRLTLEkeyLEKEIQELQEQRIDLKeQIKSIEKEIENLNGKKEE 865
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 400-656 1.48e-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: 41.98  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301   400 EKRQLQDDFAQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALR 479
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301   480 EARATLRVSEGRARGLQEAARARELELEACSQELQRHR-----QEAERLREKAGQLDAEAAGLrepavppatadpfllaE 554
Cdd:TIGR02169  755 NVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipeiqAELSKLEEEVSRIEARLREI----------------E 818

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301   555 SDEAKVQRaaagvggsLRAQVERLRVELQRERRRGEEQRDSFEGERLAWQAEKE----QVIRYQKQL-----QHNYIQMY 625
Cdd:TIGR02169  819 QKLNRLTL--------EKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEeleeELEELEAALrdlesRLGDLKKE 890

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 109090301   626 RRN-----RQLEQELQQLSLELEARELAELGLAEQA 656
Cdd:TIGR02169  891 RDEleaqlRELERKIEELEAQIEKKRKRLSELKAKL 926
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 453-656 3.10e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 3.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 453 LKQQLK--ESQAELVQKgseLVALRVALREARATLRVS-----EGRARGLQEAARARELELEACSQELQRHRQEAERLRE 525
Cdd:COG1196  198 LERQLEplERQAEKAER---YRELKEELKELEAELLLLklrelEAELEELEAELEELEAELEELEAELAELEAELEELRL 274

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 526 KAGQLDAEAAGLREpavppatadPFLLAESDEAKVQRAAAgVGGSLRAQVERLRVELQRERRRGEEQRDSFEGERLAWQA 605
Cdd:COG1196  275 ELEELELELEEAQA---------EEYELLAELARLEQDIA-RLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 109090301 606 EKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEARELAELGLAEQA 656
Cdd:COG1196  345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
329-647 3.48e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 3.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 329 LEGKLQEREAELQQLRDSLDENEATMCQAYEERQRHWQREREALREdcaaqaqraqraqqllqlqvfqlqqEKRQLQDDF 408
Cdd:COG4717  161 LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ-------------------------RLAELEEEL 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 409 AQLLQEREQLERRCATLEREQRELGP--RLEETKWEVCQKSGEISLLkqQLKESQAELVQKGSELVALRVAL-------- 478
Cdd:COG4717  216 EEAQEELEELEEELEQLENELEAAALeeRLKEARLLLLIAAALLALL--GLGGSLLSLILTIAGVLFLVLGLlallflll 293

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 479 -----------REARATLRVSEGRARGLQEAARARELELEACSQELQRHRQEAERLREKAGQLDAEAAGLREPAVPPATA 547
Cdd:COG4717  294 arekaslgkeaEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIA 373

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 548 DPFLLAESD-----EAKVQRAAAGVggSLRAQVERLRVELQRERRRGEEQRDSFEGERLawQAEKEQVIRYQKQLQHNYI 622
Cdd:COG4717  374 ALLAEAGVEdeeelRAALEQAEEYQ--ELKEELEELEEQLEELLGELEELLEALDEEEL--EEELEELEEELEELEEELE 449

                        330       340
                 ....*....|....*....|....*
gi 109090301 623 QMYRRNRQLEQELQQLSLELEAREL 647
Cdd:COG4717  450 ELREELAELEAELEQLEEDGELAEL 474
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 453-529 4.45e-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: 37.95  E-value: 4.45e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109090301   453 LKQQLKESQAELVQKGSELVALRVALREARATLRvsegrarglQEAARARELELEACSQELQRHRQEAERLREKAGQ 529
Cdd:smart00935  23 LEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS---------EAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQ 90
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 453-529 4.80e-03

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 38.28  E-value: 4.80e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109090301 453 LKQQLKESQAELVQKGSELVALRVALREARATLRvsegrarglQEAARARELELEACSQELQRHRQEAERLREKAGQ 529
Cdd:COG2825   48 LEKEFKKRQAELQKLEKELQALQEKLQKEAATLS---------EEERQKKERELQKKQQELQRKQQEAQQDLQKRQQ 115
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
400-530 5.39e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 5.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 400 EKRQLQDDFAQLLQEREQLERRCATLEREQRELGPRLEETKWEvcqksGEISLLKQQLKESQAELVQKGSELVALRVALR 479
Cdd:COG4717  389 AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE-----EELEELEEELEELEEELEELREELAELEAELE 463

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109090301 480 EARATLRVSEGRARGLQEAARARELELEACS---------QELQRHRQE-AERLREKAGQL 530
Cdd:COG4717  464 QLEEDGELAELLQELEELKAELRELAEEWAAlklalelleEAREEYREErLPPVLERASEY 524
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
414-527 7.53e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 7.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301 414 EREQLER---RCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELvqkgSELVALRVALREARATLRVSEG 490
Cdd:PRK03918 177 RIERLEKfikRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKELESLEG 252

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 109090301 491 RARGLQEAARARE---LELEACSQELQRHRQEAERLREKA 527
Cdd:PRK03918 253 SKRKLEEKIRELEeriEELKKEIEELEEKVKELKELKEKA 292
mukB PRK04863
chromosome partition protein MukB;
403-646 8.68e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.56  E-value: 8.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301  403 QLQDDFAQLLQE----REQLERRCATLEreqrELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELV----AL 474
Cdd:PRK04863  331 QAASDHLNLVQTalrqQEKIERYQADLE----ELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLAdyqqAL 406

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301  475 RV-------------ALREARATLRVSE---GRARGLQEAARARE----LELEACSQELQRHrQEAERLREKAGQLDAEA 534
Cdd:PRK04863  407 DVqqtraiqyqqavqALERAKQLCGLPDltaDNAEDWLEEFQAKEqeatEELLSLEQKLSVA-QAAHSQFEQAYQLVRKI 485

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301  535 AGlrepAVPPATADPFLLAESDEAKVQRAAAGVGGSLRAQ-------------VERLRVELQRERRRGEEQRDSFEGERL 601
Cdd:PRK04863  486 AG----EVSRSEAWDVARELLRRLREQRHLAEQLQQLRMRlseleqrlrqqqrAERLLAEFCKRLGKNLDDEDELEQLQE 561

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 109090301  602 AWQAEKEQVIRYQKQLQHNYIQMyrrnRQLEQELQQLSLELEARE 646
Cdd:PRK04863  562 ELEARLESLSESVSEARERRMAL----RQQLEQLQARIQRLAARA 602
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 332-647 9.23e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 39.18  E-value: 9.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301   332 KLQEREAELQQLRDSLDENEATMCQAYEERQ--RHWQREREALREdcaaqAQRAQRAQQLLQLQVFQLQQEKRQLQDDFA 409
Cdd:TIGR00618  315 ELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRllQTLHSQEIHIRD-----AHEVATSIREISCQQHTLTQHIHTLQQQKT 389

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301   410 QLLQEREQLERRCATLEREQRELGPRLEETkwevcqksgeiSLLKQQLKESQAELVQKGSELVALRVALREARATLRVSE 489
Cdd:TIGR00618  390 TLTQKLQSLCKELDILQREQATIDTRTSAF-----------RDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEK 458

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301   490 GRARGLQEAARARELELEA----CSQELQRHRQEAERLREKAGQLDAEAAGLREPAV-------PPATADPFLLAESDEA 558
Cdd:TIGR00618  459 IHLQESAQSLKEREQQLQTkeqiHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNParqdidnPGPLTRRMQRGEQTYA 538

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109090301   559 KVQRAAAGVGG----------SLRAQVERLRVELQRERRRGEEQRDSFEGER---------LAWQAEKEQVIR------- 612
Cdd:TIGR00618  539 QLETSEEDVYHqltserkqraSLKEQMQEIQQSFSILTQCDNRSKEDIPNLQnitvrlqdlTEKLSEAEDMLAceqhall 618

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 109090301   613 YQKQLQHNYIQMYRRNRQLEQELQQLSLELEAREL 647
Cdd:TIGR00618  619 RKLQPEQDLQDVRLHLQQCSQELALKLTALHALQL 653
 
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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