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Conserved domains on  [gi|569007083|ref|XP_006527068|]
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leucine zipper putative tumor suppressor 2 isoform X3 [Mus musculus]

Protein Classification

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 ...
 220-417 2.36e-82

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: 252.23  E-value: 2.36e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083  220 TKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQ 299
Cdd:pfam06818   1 TKWEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSKTLELEVCENELQRKKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083  300 EAERLREKAGHLDAEASGLRDPPVPPATTDPFLLAESDEAKVQRAAAGAGGSLRAQVERLRQELQREQRRGDEQRDSFEG 379
Cdd:pfam06818  81 EAELLREKVGKLEEEVSGLREALSDVSPSGYESVYESDEAKEQRQEEADLGSLRREVERLRAELREERQRRERQASSFEQ 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 569007083  380 ERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQ 417
Cdd:pfam06818 161 ERRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
GAS super family cl25894
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 183-252 1.16e-03

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: 39.89  E-value: 1.16e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569007083  183 RQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSG-EISLLKQQLKESQAELVQKGSEL 252
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 ...
 220-417 2.36e-82

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: 252.23  E-value: 2.36e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083  220 TKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQ 299
Cdd:pfam06818   1 TKWEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSKTLELEVCENELQRKKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083  300 EAERLREKAGHLDAEASGLRDPPVPPATTDPFLLAESDEAKVQRAAAGAGGSLRAQVERLRQELQREQRRGDEQRDSFEG 379
Cdd:pfam06818  81 EAELLREKVGKLEEEVSGLREALSDVSPSGYESVYESDEAKEQRQEEADLGSLRREVERLRAELREERQRRERQASSFEQ 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 569007083  380 ERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQ 417
Cdd:pfam06818 161 ERRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 181-435 2.09e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.20  E-value: 2.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 181 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALR 260
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 261 EARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASGLRdppvppATTDPFLLAESDEAK 340
Cdd:COG1196  313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE------AELAEAEEELEELAE 386

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 341 VQRAAAGAGGSLRAQVERLRQELQREQRRgdeqRDSFEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLS 420
Cdd:COG1196  387 ELLEALRAAAELAAQLEELEEAEEALLER----LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462

                        250
                 ....*....|....*
gi 569007083 421 LELEARELADLGLAE 435
Cdd:COG1196  463 ELLAELLEEAALLEA 477
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 164-432 9.22e-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: 61.23  E-value: 9.22e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083   164 VQRAQQLLQLQVFQLQQEKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQA 243
Cdd:TIGR02168  717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083   244 ELVQKGSELVALRVALREARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASGLRDppv 323
Cdd:TIGR02168  797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES--- 873

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083   324 ppATTDpfLLAESDEAKVQRAAAGAG-GSLRAQVERLRQELQREQRRGDEQRDSFEGERLAWQAEKEQVIRYQKQLQHNY 402
Cdd:TIGR02168  874 --ELEA--LLNERASLEEALALLRSElEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEY 949

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 569007083   403 IQMYRRNRQLEQELQQLSLELEAR------ELADLG 432
Cdd:TIGR02168  950 SLTLEEAEALENKIEDDEEEARRRlkrlenKIKELG 985
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
181-306 8.23e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 8.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 181 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALR 260
Cdd:PRK02224 259 EIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQ 338

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 569007083 261 EA-------RATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLRE 306
Cdd:PRK02224 339 AHneeaeslREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEE 391
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 234-303 1.08e-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: 39.10  E-value: 1.08e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083   234 LKQQLKESQAELVQKGSELVALRVALREARATLRvsegrarglQEAARAREQELEACSQELQRYRQEAER 303
Cdd:smart00935  23 LEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS---------EAAREKKEKELQKKVQEFQRKQQKLQQ 83
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 183-252 1.16e-03

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: 39.89  E-value: 1.16e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569007083  183 RQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSG-EISLLKQQLKESQAELVQKGSEL 252
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 ...
 220-417 2.36e-82

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: 252.23  E-value: 2.36e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083  220 TKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQ 299
Cdd:pfam06818   1 TKWEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSKTLELEVCENELQRKKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083  300 EAERLREKAGHLDAEASGLRDPPVPPATTDPFLLAESDEAKVQRAAAGAGGSLRAQVERLRQELQREQRRGDEQRDSFEG 379
Cdd:pfam06818  81 EAELLREKVGKLEEEVSGLREALSDVSPSGYESVYESDEAKEQRQEEADLGSLRREVERLRAELREERQRRERQASSFEQ 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 569007083  380 ERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQ 417
Cdd:pfam06818 161 ERRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 181-435 2.09e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.20  E-value: 2.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 181 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALR 260
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 261 EARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASGLRdppvppATTDPFLLAESDEAK 340
Cdd:COG1196  313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE------AELAEAEEELEELAE 386

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 341 VQRAAAGAGGSLRAQVERLRQELQREQRRgdeqRDSFEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLS 420
Cdd:COG1196  387 ELLEALRAAAELAAQLEELEEAEEALLER----LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462

                        250
                 ....*....|....*
gi 569007083 421 LELEARELADLGLAE 435
Cdd:COG1196  463 ELLAELLEEAALLEA 477
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 181-434 9.86e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 67.27  E-value: 9.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 181 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWevcqksgEISLLKQQLKESQAELVQKGSELVALRVALR 260
Cdd:COG1196  282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE-------ELAELEEELEELEEELEELEEELEEAEEELE 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 261 EARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASGLRDppvppattdpfLLAESDEAK 340
Cdd:COG1196  355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE-----------RLERLEEEL 423

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 341 VQRAAAGAggSLRAQVERLRQELQREQRRGDEQRDSFEGERLAWQAEKEQVIRYQKQLQhnyiqmyRRNRQLEQELQQLS 420
Cdd:COG1196  424 EELEEALA--ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA-------ELLEELAEAAARLL 494

                        250
                 ....*....|....
gi 569007083 421 LELEARELADLGLA 434
Cdd:COG1196  495 LLLEAEADYEGFLE 508
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 164-432 9.22e-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: 61.23  E-value: 9.22e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083   164 VQRAQQLLQLQVFQLQQEKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQA 243
Cdd:TIGR02168  717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083   244 ELVQKGSELVALRVALREARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASGLRDppv 323
Cdd:TIGR02168  797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES--- 873

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083   324 ppATTDpfLLAESDEAKVQRAAAGAG-GSLRAQVERLRQELQREQRRGDEQRDSFEGERLAWQAEKEQVIRYQKQLQHNY 402
Cdd:TIGR02168  874 --ELEA--LLNERASLEEALALLRSElEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEY 949

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 569007083   403 IQMYRRNRQLEQELQQLSLELEAR------ELADLG 432
Cdd:TIGR02168  950 SLTLEEAEALENKIEDDEEEARRRlkrlenKIKELG 985
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 181-437 1.57e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.34  E-value: 1.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 181 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALR 260
Cdd:COG1196  310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 261 EARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKaghldaeasglrdppvppattdpfLLAESDEAK 340
Cdd:COG1196  390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE------------------------EEEEEEALE 445

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 341 VQRAAAGAGGSLRAQVERLRQELQREQRRGDEQRDSFEGERlawqAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLS 420
Cdd:COG1196  446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL----AEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521

                        250
                 ....*....|....*..
gi 569007083 421 LELEARELADLGLAESA 437
Cdd:COG1196  522 LAGAVAVLIGVEAAYEA 538
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 183-436 5.20e-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: 58.53  E-value: 5.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083   183 RQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREA 262
Cdd:TIGR02168  694 AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083   263 RATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASGLRDPPVPPATTDPFLLAESDEakvq 342
Cdd:TIGR02168  774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE---- 849

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083   343 raaagaggsLRAQVERLRQELQREQRRGDEQRDSFEgerlAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLE 422
Cdd:TIGR02168  850 ---------LSEDIESLAAEIEELEELIEELESELE----ALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916

                          250
                   ....*....|....*.
gi 569007083   423 LEAR--ELADLGLAES 436
Cdd:TIGR02168  917 LEELreKLAQLELRLE 932
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 181-427 7.48e-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: 58.14  E-value: 7.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083   181 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALR 260
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083   261 EARATL-RVSEGRARGLQ-------EAARAREQ------ELEACSQELQRYRQEAERLREKAGHLDAEASGLRDppvppa 326
Cdd:TIGR02168  313 NLERQLeELEAQLEELESkldelaeELAELEEKleelkeELESLEAELEELEAELEELESRLEELEEQLETLRS------ 386

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083   327 ttdpfllaESDEAKVQRAAAGAG-GSLRAQVERLRQELQREQRRGDEQRDSF-EGERLAWQAEKEQVIRYQKQLQHNYIQ 404
Cdd:TIGR02168  387 --------KVAQLELQIASLNNEiERLEARLERLEDRRERLQQEIEELLKKLeEAELKELQAELEELEEELEELQEELER 458

                          250       260
                   ....*....|....*....|...
gi 569007083   405 MYRRNRQLEQELQQLSLELEARE 427
Cdd:TIGR02168  459 LEEALEELREELEEAEQALDAAE 481
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 181-415 1.67e-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: 57.00  E-value: 1.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083   181 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALR 260
Cdd:TIGR02169  288 EQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELE 367

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083   261 EARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASGLRDppvppATTDpfllAESDEAK 340
Cdd:TIGR02169  368 DLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA-----AIAG----IEAKINE 438

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569007083   341 VQRAAAgaggSLRAQVERLRQELQREQrrgdEQRDSFEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQE 415
Cdd:TIGR02169  439 LEEEKE----DKALEIKKQEWKLEQLA----ADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
236-425 2.14e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.85  E-value: 2.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083  236 QQLKESQAELVQKGSELVALR--VALREARATLRVSEGRARGLQEAARA--REQELEACSQELQRYRQEAERLREKAGHL 311
Cdd:COG4913   235 DDLERAHEALEDAREQIELLEpiRELAERYAAARERLAELEYLRAALRLwfAQRRLELLEAELEELRAELARLEAELERL 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083  312 DAEASGLRdppvppattdpfllAESDEAKVQRAAAGAG--GSLRAQVERLRQELQREQRRGDEQ--------------RD 375
Cdd:COG4913   315 EARLDALR--------------EELDELEAQIRGNGGDrlEQLEREIERLERELEERERRRARLeallaalglplpasAE 380

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 569007083  376 SFEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEA 425
Cdd:COG4913   381 EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 181-420 3.85e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.83  E-value: 3.85e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083   181 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSEL-------V 253
Cdd:TIGR02168  275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLeelkeelE 354

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083   254 ALRVALREARATLRVSEGRARGLQEAARAR-------EQELEACSQELQRYRQEAERLREKAGHLDAEASGLRDPpvppa 326
Cdd:TIGR02168  355 SLEAELEELEAELEELESRLEELEEQLETLrskvaqlELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK----- 429

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083   327 ttdpflLAESDEAKVQRAAAGaggsLRAQVERLRQELQREQRRGDEQRDSFEGERLAWQAEKEQVIRYQ------KQLQH 400
Cdd:TIGR02168  430 ------LEEAELKELQAELEE----LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQarldslERLQE 499

                          250       260
                   ....*....|....*....|
gi 569007083   401 NYIQMYRRNRQLEQELQQLS 420
Cdd:TIGR02168  500 NLEGFSEGVKALLKNQSGLS 519
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 226-438 4.66e-08

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: 54.77  E-value: 4.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 226 QKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLR 305
Cdd:COG4942   24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 306 EKAGHLDAEA--SGLRDPPVPPATTDPFLLAESDE------AKVQRAAAGAGGSLRAQVERLRQELQREQRRGDEQRDSF 377
Cdd:COG4942  104 EELAELLRALyrLGRQPPLALLLSPEDFLDAVRRLqylkylAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569007083 378 EGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEARELADLGLAESAP 438
Cdd:COG4942  184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
181-399 9.67e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.54  E-value: 9.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083  181 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGpRLEETKWE---VCQKSGEISLLKQQLkesqAELVQKGSELVALRV 257
Cdd:COG4913   618 ELAELEEELAEAEERLEALEAELDALQERREALQ-RLAEYSWDeidVASAEREIAELEAEL----ERLDASSDDLAALEE 692

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083  258 ALREARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAG-HLDAEASGLRDPpvppattdpfLLAES 336
Cdd:COG4913   693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlELRALLEERFAA----------ALGDA 762

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569007083  337 DEAKVQRAAAGAGGSLRAQVERLRQELQREQRRGDEQrdsFEGERLAWQAEKEQVIRYQKQLQ 399
Cdd:COG4913   763 VERELRENLEERIDALRARLNRAEEELERAMRAFNRE---WPAETADLDADLESLPEYLALLD 822
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 166-437 1.36e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.84  E-value: 1.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083   166 RAQQLLQLQVFQLQQEKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAEL 245
Cdd:TIGR02169  660 RAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL 739

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083   246 VQKGSELVALRVALREARATLRVSEGRARGLQEAARAREQELEACSQELQRyrQEAERLREKAGHLDAEASGLRdppvpp 325
Cdd:TIGR02169  740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIE------ 811

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083   326 attdpfLLAESDEAKVQRAAAgaggsLRAQVERLRQELQREQRRGDEQRDSFEGERLAWQAEKE----QVIRYQKQL--- 398
Cdd:TIGR02169  812 ------ARLREIEQKLNRLTL-----EKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEeleeELEELEAALrdl 880

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 569007083   399 --QHNYIQMYRRN-----RQLEQELQQLSLELEARELADLGLAESA 437
Cdd:TIGR02169  881 esRLGDLKKERDEleaqlRELERKIEELEAQIEKKRKRLSELKAKL 926
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 181-364 2.03e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.45  E-value: 2.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083   181 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALR 260
Cdd:TIGR02169  351 RRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIA 430

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083   261 EARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASGLRdppvppattdpfllAESDEAK 340
Cdd:TIGR02169  431 GIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ--------------RELAEAE 496

                          170       180
                   ....*....|....*....|....*
gi 569007083   341 VQRAAAG-AGGSLRAQVERLRQELQ 364
Cdd:TIGR02169  497 AQARASEeRVRGGRAVEEVLKASIQ 521
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
181-436 9.63e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.84  E-value: 9.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 181 EKRQLQDDFAQLLQEREQLERRCATfEREQRELGPRLEETKWEVCqksgEISLLKQQLKESQAELVQKGSELVALRVALR 260
Cdd:COG4717  113 ELREELEKLEKLLQLLPLYQELEAL-EAELAELPERLEELEERLE----ELRELEEELEELEAELAELQEELEELLEQLS 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 261 -EARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASgLRDPPVPP----------ATTD 329
Cdd:COG4717  188 lATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER-LKEARLLLliaaallallGLGG 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 330 PFLLAESDEAKVQRAAAGAGGSLRAQVERLRQELQREQRRGDEQRDSFEGERLAWQAEKEQV----------IRYQKQLQ 399
Cdd:COG4717  267 SLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALglppdlspeeLLELLDRI 346

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 569007083 400 HNYIQMYRRNRQLEQELQQLSLELEARELADLGLAES 436
Cdd:COG4717  347 EELQELLREAEELEEELQLEELEQEIAALLAEAGVED 383
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
181-319 2.42e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 2.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083  181 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKwEVCQKSG--EISLLKQQLKESQAELVQKGSELVALRVA 258
Cdd:COG4913   289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELE-AQIRGNGgdRLEQLEREIERLERELEERERRRARLEAL 367

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569007083  259 LREARATLRVSEGRARGLQEAARAR----EQELEACSQELQRYRQEAERLREKAGHLDAEASGLR 319
Cdd:COG4913   368 LAALGLPLPASAEEFAALRAEAAALlealEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 181-399 1.93e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.60  E-value: 1.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 181 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQkgsELVALRVALR 260
Cdd:COG4942   42 ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE---LLRALYRLGR 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 261 EARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASGLRdppvppattdpfllaesdeak 340
Cdd:COG4942  119 QPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE--------------------- 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 569007083 341 vqraaagaggSLRAQVERLRQELQREQRRGDEQRDSFEGERLAWQAEKEQVIRYQKQLQ 399
Cdd:COG4942  178 ----------ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
234-427 2.27e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.47  E-value: 2.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 234 LKQQLKESQAELVQKGSELVALRvalreARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDA 313
Cdd:COG3206  180 LEEQLPELRKELEEAEAALEEFR-----QKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPD 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 314 EASGLRDPPVPPAttdpfLLAESDEAKVQRAAAGAGG--------SLRAQVERLRQELQREQRRGdeqRDSFEGERLAWQ 385
Cdd:COG3206  255 ALPELLQSPVIQQ-----LRAQLAELEAELAELSARYtpnhpdviALRAQIAALRAQLQQEAQRI---LASLEAELEALQ 326

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 569007083 386 AEKEQVIRYQKQLQhnyiQMYRRNRQLEQELQQLSLELEARE 427
Cdd:COG3206  327 AREASLQAQLAQLE----ARLAELPELEAELRRLEREVEVAR 364
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
235-419 2.77e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083  235 KQQLKESQAELVQKGSELVALRVALREARATLRVSEGRARGLQEAARAREQEL--EACSQELQRYRQEAERLREKAGHLD 312
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDASSDDLA 688

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083  313 AEASGLRDppvppattdpfLLAESDEAKVQRAAA-GAGGSLRAQVERLRQELQREQRR--------GDEQRDSFEgERLA 383
Cdd:COG4913   689 ALEEQLEE-----------LEAELEELEEELDELkGEIGRLEKELEQAEEELDELQDRleaaedlaRLELRALLE-ERFA 756

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 569007083  384 WQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQL 419
Cdd:COG4913   757 AALGDAVERELRENLEERIDALRARLNRAEEELERA 792
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 286-435 3.51e-04

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 42.44  E-value: 3.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083  286 ELEACSQELQRYRQEAERLREKAGHLDA---EASGLRDPPVPPATTdpfllAESDEAKVQRAAAGAG-GSLRAQVERLRQ 361
Cdd:pfam09787   1 NLESAKQELADYKQKAARILQSKEKLIAslkEGSGVEGLDSSTALT-----LELEELRQERDLLREEiQKLRGQIQQLRT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083  362 ELQREQRRGDEQRDS-----------FEGERLAWQAEKEQVIRYQKQLQHNYIQMYR-------RNRQLEQELQQLSLEL 423
Cdd:pfam09787  76 ELQELEAQQQEEAESsreqlqeleeqLATERSARREAEAELERLQEELRYLEEELRRskatlqsRIKDREAEIEKLRNQL 155

                         170
                  ....*....|..
gi 569007083  424 EARELADLGLAE 435
Cdd:pfam09787 156 TSKSQSSSSQSE 167
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 234-303 4.41e-04

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: 40.97  E-value: 4.41e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 234 LKQQLKESQAELVQKGSELVALRVALREARATLRvsegrarglQEAARAREQELEACSQELQRYRQEAER 303
Cdd:COG2825   48 LEKEFKKRQAELQKLEKELQALQEKLQKEAATLS---------EEERQKKERELQKKQQELQRKQQEAQQ 108
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
181-306 8.23e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 8.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 181 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALR 260
Cdd:PRK02224 259 EIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQ 338

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 569007083 261 EA-------RATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLRE 306
Cdd:PRK02224 339 AHneeaeslREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEE 391
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 190-424 9.39e-04

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: 41.88  E-value: 9.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083   190 AQLLQEREQLE--RRCATFEREQRelgpRLEETKWEVCQKsgEISLLKQQLKESQAELVQKGSELVALRVALREARATLR 267
Cdd:TIGR00618  166 KELLMNLFPLDqyTQLALMEFAKK----KSLHGKAELLTL--RSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQ 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083   268 VSEGRARGLQEAARAREQELEACSQ---ELQRYRQEAERLREKAGHLDAEASGLRDPPVPPATTDPFLLAESDEAKVQRA 344
Cdd:TIGR00618  240 QSHAYLTQKREAQEEQLKKQQLLKQlraRIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSK 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083   345 AAGAGGSLRAQVERLRQELQREQRRGDEQRDSFEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQ----LEQELQQLS 420
Cdd:TIGR00618  320 MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQqkttLTQKLQSLC 399


                   ....
gi 569007083   421 LELE 424
Cdd:TIGR00618  400 KELD 403
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 234-303 1.08e-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: 39.10  E-value: 1.08e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083   234 LKQQLKESQAELVQKGSELVALRVALREARATLRvsegrarglQEAARAREQELEACSQELQRYRQEAER 303
Cdd:smart00935  23 LEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS---------EAAREKKEKELQKKVQEFQRKQQKLQQ 83
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 183-252 1.16e-03

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: 39.89  E-value: 1.16e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569007083  183 RQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSG-EISLLKQQLKESQAELVQKGSEL 252
Cdd:pfam13851  95 KVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQKTGlKNLLLEKKLQALGETLEKKEAQL 165
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 223-438 2.27e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.20  E-value: 2.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 223 EVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSEGRARGLQEAARAREQELEACSQELqryrqeAE 302
Cdd:COG3883   17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL------GE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 303 RLRekaghlDAEASGLRDPPVppattDPFLLAESDEAKVQRAAA-----GAGGSLRAQVERLRQELQREQRRGDEQRDSF 377
Cdd:COG3883   91 RAR------ALYRSGGSVSYL-----DVLLGSESFSDFLDRLSAlskiaDADADLLEELKADKAELEAKKAELEAKLAEL 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569007083 378 EGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEARELADLGLAESAP 438
Cdd:COG3883  160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
181-316 2.30e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 2.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 181 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALR 260
Cdd:COG4372   46 ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ 125

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 569007083 261 EARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEAS 316
Cdd:COG4372  126 DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
181-326 2.98e-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: 2.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083  181 EKRQLQDDFAQLLQEREQLERRCAT--------FEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSEL 252
Cdd:COG4913   310 ELERLEARLDALREELDELEAQIRGnggdrleqLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEA 389

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569007083  253 VALRVALREARATLRVSEGRARGLQEAARAREQELEACSQELQR----YRQEAERLREKAghldAEASGLRDPPVPPA 326
Cdd:COG4913   390 AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERrksnIPARLLALRDAL----AEALGLDEAELPFV 463
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 181-384 3.15e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 3.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 181 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALR 260
Cdd:COG4942   21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 261 EARATLRV-------------------------SEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEA 315
Cdd:COG4942  101 AQKEELAEllralyrlgrqpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 316 SGL-------------RDPPVPPATTDPFLLAESDEAKVQRAAagaggSLRAQVERLRQELQREQRRGDEQRDSFEGERL 382
Cdd:COG4942  181 AELeeeraalealkaeRQKLLARLEKELAELAAELAELQQEAE-----ELEALIARLEAEAAAAAERTPAAGFAALKGKL 255


                 ..
gi 569007083 383 AW 384
Cdd:COG4942  256 PW 257
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
195-431 3.50e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 3.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 195 EREQLER---RCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELvqkgSELVALRVALREARATLRVSEG 271
Cdd:PRK03918 177 RIERLEKfikRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKELESLEG 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 272 RARGLQEAARARE---QELEACSQELQRYRQEAERLREKAghldAEASGLRDppvppattdpfLLAESDEAKVQraaaga 348
Cdd:PRK03918 253 SKRKLEEKIRELEeriEELKKEIEELEEKVKELKELKEKA----EEYIKLSE-----------FYEEYLDELRE------ 311

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 349 ggsLRAQVERLRQELQREQRRGDEQRDsfEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEAREL 428
Cdd:PRK03918 312 ---IEKRLSRLEEEINGIEERIKELEE--KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTP 386


                 ...
gi 569007083 429 ADL 431
Cdd:PRK03918 387 EKL 389
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
185-427 4.19e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 4.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 185 LQDDFAQLLQEREQLERRCATFEREQRELGPRLEETkwEVCQKSGEISLLKQQLKESQ-----AELVQKGSELVALRVAL 259
Cdd:PRK02224 410 AEDFLEELREERDELREREAELEATLRTARERVEEA--EALLEAGKCPECGQPVEGSPhvetiEEDRERVEELEAELEDL 487

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 260 REARATLRVSEGRARGLQEAARARE----------QELEACSQELQRYRQEAERLREKAGHLDAEASGLRdppvppattd 329
Cdd:PRK02224 488 EEEVEEVEERLERAEDLVEAEDRIErleerredleELIAERRETIEEKRERAEELRERAAELEAEAEEKR---------- 557

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 330 pfllaesDEAKVQRAAAGAGGSLRAQVERLRQELQREQRRGDEQRDSFE-----GERLAWQAEKEQVIRYQKQLQHNYIQ 404
Cdd:PRK02224 558 -------EAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAaiadaEDEIERLREKREALAELNDERRERLA 630

                        250       260
                 ....*....|....*....|....
gi 569007083 405 MYR-RNRQLEQELQQLSLElEARE 427
Cdd:PRK02224 631 EKReRKRELEAEFDEARIE-EARE 653
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 186-267 4.63e-03

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: 38.37  E-value: 4.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 186 QDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARAT 265
Cdd:COG1579   88 NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167


                 ..
gi 569007083 266 LR 267
Cdd:COG1579  168 LA 169
PRK12704 PRK12704
phosphodiesterase; Provisional
 182-303 6.13e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.99  E-value: 6.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 182 KRQLQDDFAQLLQEREQLERRCATFEREQRElgprLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVAlrE 261
Cdd:PRK12704  81 RNELQKLEKRLLQKEENLDRKLELLEKREEE----LEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE--E 154

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 569007083 262 ARATLRVS-EGRARgLQEAARAREQELEAcsqelqryRQEAER 303
Cdd:PRK12704 155 AKEILLEKvEEEAR-HEAAVLIKEIEEEA--------KEEADK 188
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 194-400 6.18e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 39.33  E-value: 6.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083   194 QEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISL----LKQQLKESQAELVQkgselvalrvalreARATLRVS 269
Cdd:pfam15921  653 QERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETttnkLKMQLKSAQSELEQ--------------TRNTLKSM 718

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083   270 EGR-------ARGLQEAARAREQELEACSQELQrYRQEAERLREKAGH-LDAEASGLRDPPVPPATTdpfllaesdeakv 341
Cdd:pfam15921  719 EGSdghamkvAMGMQKQITAKRGQIDALQSKIQ-FLEEAMTNANKEKHfLKEEKNKLSQELSTVATE------------- 784

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569007083   342 QRAAAGAGGSLRAQVERLRQELQREQRRGDEQRDSFegerlawqAEKEQVIRYQKQ------LQH 400
Cdd:pfam15921  785 KNKMAGELEVLRSQERRLKEKVANMEVALDKASLQF--------AECQDIIQRQEQesvrlkLQH 841
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 186-324 7.18e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.59  E-value: 7.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083 186 QDDFAQLLQEREQLERrcatFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARAT 265
Cdd:COG4942  128 PEDFLDAVRRLQYLKY----LAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLAR 203

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 569007083 266 LRVSEGRARGLQEAARAREQELEACSQELQryRQEAERLREKAGHLDAEASGLRDPPVP 324
Cdd:COG4942  204 LEKELAELAAELAELQQEAEELEALIARLE--AEAAAAAERTPAAGFAALKGKLPWPVS 260
PTZ00121 PTZ00121
MAEBL; Provisional
 133-430 8.74e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.58  E-value: 8.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083  133 KLEKAFGARQRRWPRERGEDCAAQAQQATQRVQRAQQLLQLQVFQLQQEKRQLQDDFAQLLQ--EREQLERRCATFEREQ 210
Cdd:PTZ00121 1526 EAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKkaEEARIEEVMKLYEEEK 1605

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083  211 RELGPRL-----EETKWEVCQKSGEISLLKQQLKESQAELVQKGSELvalrvalREARatlrvSEGRARGLQEAARAREQ 285
Cdd:PTZ00121 1606 KMKAEEAkkaeeAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEEL-------KKAE-----EENKIKAAEEAKKAEED 1673

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007083  286 ELEAcsqelQRYRQEAERLREKAGHLDAEASGLRdppvppaTTDPFLLAESDEAKVQRAAAGAGGSLRAQVERLRQELQR 365
Cdd:PTZ00121 1674 KKKA-----EEAKKAEEDEKKAAEALKKEAEEAK-------KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE 1741

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569007083  366 EQRRGDEQRDSfEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEARELAD 430
Cdd:PTZ00121 1742 DKKKAEEAKKD-EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFD 1805
 
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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