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Conserved domains on  [gi|1720395140|ref|XP_030106760|]
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leucine zipper putative tumor suppressor 2 isoform X2 [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 ...
 304-501 2.58e-83

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: 257.23  E-value: 2.58e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 304 TKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQ 383
Cdd:pfam06818   1 TKWEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSKTLELEVCENELQRKKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 384 EAERLREKAGHLDAEASGLRDPPVPPATTDPFLLAESDEAKVQRAAAGAGGSLRAQVERLRQELQREQRRGDEQRDSFEG 463
Cdd:pfam06818  81 EAELLREKVGKLEEEVSGLREALSDVSPSGYESVYESDEAKEQRQEEADLGSLRREVERLRAELREERQRRERQASSFEQ 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1720395140 464 ERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQ 501
Cdd:pfam06818 161 ERRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
GAS super family cl25894
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 267-336 3.98e-04

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: 41.82  E-value: 3.98e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720395140 267 RQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSG-EISLLKQQLKESQAELVQKGSEL 336
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 ...
 304-501 2.58e-83

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: 257.23  E-value: 2.58e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 304 TKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQ 383
Cdd:pfam06818   1 TKWEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSKTLELEVCENELQRKKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 384 EAERLREKAGHLDAEASGLRDPPVPPATTDPFLLAESDEAKVQRAAAGAGGSLRAQVERLRQELQREQRRGDEQRDSFEG 463
Cdd:pfam06818  81 EAELLREKVGKLEEEVSGLREALSDVSPSGYESVYESDEAKEQRQEEADLGSLRREVERLRAELREERQRRERQASSFEQ 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1720395140 464 ERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQ 501
Cdd:pfam06818 161 ERRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 265-519 1.88e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.97  E-value: 1.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 265 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALR 344
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 345 EARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASGLRdppvppATTDPFLLAESDEAK 424
Cdd:COG1196   313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE------AELAEAEEELEELAE 386

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 425 VQRAAAGAGGSLRAQVERLRQELQREQRRgdeqRDSFEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLS 504
Cdd:COG1196   387 ELLEALRAAAELAAQLEELEEAEEALLER----LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462

                         250
                  ....*....|....*
gi 1720395140 505 LELEARELADLGLAE 519
Cdd:COG1196   463 ELLAELLEEAALLEA 477
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 193-516 2.26e-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: 63.54  E-value: 2.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  193 LEGKLRDREAELQQLRDSMDESEATVCQAfgarqrrwpRERGEDCAAQAQQATQRVQRAQQLLQlqvfqlqqekrqlqdd 272
Cdd:TIGR02168  689 LEEKIAELEKALAELRKELEELEEELEQL---------RKELEELSRQISALRKDLARLEAEVE---------------- 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  273 faQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRV 352
Cdd:TIGR02168  744 --QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  353 SEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASGLRDppvppATTDpfLLAESDEAKVQRAAAGA 432
Cdd:TIGR02168  822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES-----ELEA--LLNERASLEEALALLRS 894

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  433 G-GSLRAQVERLRQELQREQRRGDEQRDSFEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEAR- 510
Cdd:TIGR02168  895 ElEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRl 974

                          330
                   ....*....|.
gi 1720395140  511 -----ELADLG 516
Cdd:TIGR02168  975 krlenKIKELG 985
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 318-387 3.23e-04

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: 41.03  E-value: 3.23e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  318 LKQQLKESQAELVQKGSELVALRVALREARATLRvsegrarglQEAARAREQELEACSQELQRYRQEAER 387
Cdd:smart00935  23 LEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS---------EAAREKKEKELQKKVQEFQRKQQKLQQ 83
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 267-336 3.98e-04

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: 41.82  E-value: 3.98e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720395140 267 RQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSG-EISLLKQQLKESQAELVQKGSEL 336
Cdd:pfam13851  95 KVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQKTGlKNLLLEKKLQALGETLEKKEAQL 165
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
265-390 6.83e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.33  E-value: 6.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 265 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALR 344
Cdd:PRK02224  259 EIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQ 338

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720395140 345 EA-------RATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLRE 390
Cdd:PRK02224  339 AHneeaeslREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEE 391
 
Name Accession Description Interval E-value
Fez1 pfam06818
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ...
 304-501 2.58e-83

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: 257.23  E-value: 2.58e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 304 TKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQ 383
Cdd:pfam06818   1 TKWEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSKTLELEVCENELQRKKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 384 EAERLREKAGHLDAEASGLRDPPVPPATTDPFLLAESDEAKVQRAAAGAGGSLRAQVERLRQELQREQRRGDEQRDSFEG 463
Cdd:pfam06818  81 EAELLREKVGKLEEEVSGLREALSDVSPSGYESVYESDEAKEQRQEEADLGSLRREVERLRAELREERQRRERQASSFEQ 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1720395140 464 ERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQ 501
Cdd:pfam06818 161 ERRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 265-519 1.88e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.97  E-value: 1.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 265 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALR 344
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 345 EARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASGLRdppvppATTDPFLLAESDEAK 424
Cdd:COG1196   313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE------AELAEAEEELEELAE 386

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 425 VQRAAAGAGGSLRAQVERLRQELQREQRRgdeqRDSFEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLS 504
Cdd:COG1196   387 ELLEALRAAAELAAQLEELEEAEEALLER----LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462

                         250
                  ....*....|....*
gi 1720395140 505 LELEARELADLGLAE 519
Cdd:COG1196   463 ELLAELLEEAALLEA 477
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 265-518 8.41e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.04  E-value: 8.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 265 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWevcqksgEISLLKQQLKESQAELVQKGSELVALRVALR 344
Cdd:COG1196   282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE-------ELAELEEELEELEEELEELEEELEEAEEELE 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 345 EARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASGLRDppvppattdpfLLAESDEAK 424
Cdd:COG1196   355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE-----------RLERLEEEL 423

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 425 VQRAAAGAggSLRAQVERLRQELQREQRRGDEQRDSFEGERLAWQAEKEQVIRYQKQLQhnyiqmyRRNRQLEQELQQLS 504
Cdd:COG1196   424 EELEEALA--ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA-------ELLEELAEAAARLL 494

                         250
                  ....*....|....
gi 1720395140 505 LELEARELADLGLA 518
Cdd:COG1196   495 LLLEAEADYEGFLE 508
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 192-521 9.07e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.57  E-value: 9.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 192 VLEGKLRDREAELQQLRDSMDESEATVcQAFGARQRrwprergedcaaqaqqatqRVQRAQQLLQLQVFQLQQEKRQLQD 271
Cdd:COG1196   257 ELEAELAELEAELEELRLELEELELEL-EEAQAEEY-------------------ELLAELARLEQDIARLEERRRELEE 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 272 DFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLR 351
Cdd:COG1196   317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 352 VSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKaghldaeasglrdppvppattdpfLLAESDEAKVQRAAAG 431
Cdd:COG1196   397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE------------------------EEEEEEALEEAAEEEA 452

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 432 AGGSLRAQVERLRQELQREQRRGDEQRDSFEGERlawqAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEARE 511
Cdd:COG1196   453 ELEEEEEALLELLAELLEEAALLEAALAELLEEL----AEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV 528

                         330
                  ....*....|
gi 1720395140 512 LADLGLAESA 521
Cdd:COG1196   529 LIGVEAAYEA 538
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 193-516 2.26e-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: 63.54  E-value: 2.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  193 LEGKLRDREAELQQLRDSMDESEATVCQAfgarqrrwpRERGEDCAAQAQQATQRVQRAQQLLQlqvfqlqqekrqlqdd 272
Cdd:TIGR02168  689 LEEKIAELEKALAELRKELEELEEELEQL---------RKELEELSRQISALRKDLARLEAEVE---------------- 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  273 faQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRV 352
Cdd:TIGR02168  744 --QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  353 SEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASGLRDppvppATTDpfLLAESDEAKVQRAAAGA 432
Cdd:TIGR02168  822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES-----ELEA--LLNERASLEEALALLRS 894

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  433 G-GSLRAQVERLRQELQREQRRGDEQRDSFEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEAR- 510
Cdd:TIGR02168  895 ElEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRl 974

                          330
                   ....*....|.
gi 1720395140  511 -----ELADLG 516
Cdd:TIGR02168  975 krlenKIKELG 985
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 265-511 4.40e-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: 59.30  E-value: 4.40e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  265 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALR 344
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  345 EARATL-RVSEGRARGLQ-------EAARAREQ------ELEACSQELQRYRQEAERLREKAGHLDAEASGLRDppvppa 410
Cdd:TIGR02168  313 NLERQLeELEAQLEELESkldelaeELAELEEKleelkeELESLEAELEELEAELEELESRLEELEEQLETLRS------ 386

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  411 ttdpfllaESDEAKVQRAAAGAG-GSLRAQVERLRQELQREQRRGDEQRDSF-EGERLAWQAEKEQVIRYQKQLQHNYIQ 488
Cdd:TIGR02168  387 --------KVAQLELQIASLNNEiERLEARLERLEDRRERLQQEIEELLKKLeEAELKELQAELEELEEELEELQEELER 458

                          250       260
                   ....*....|....*....|...
gi 1720395140  489 MYRRNRQLEQELQQLSLELEARE 511
Cdd:TIGR02168  459 LEEALEELREELEEAEQALDAAE 481
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 265-511 1.28e-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: 57.77  E-value: 1.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  265 EKRQLQDdfaQLLQEREQLER----RCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALR 340
Cdd:TIGR02169  195 EKRQQLE---RLRREREKAERyqalLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIE 271

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  341 VALREARATLR-VSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASGLRdppvppATTDPFLLAE 419
Cdd:TIGR02169  272 QLLEELNKKIKdLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLL------AEIEELEREI 345

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  420 SDEAKVQRAAAGAGGSLRAQVERLRQELQREQRRGDEQRDsfegERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQE 499
Cdd:TIGR02169  346 EEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD----ELKDYREKLEKLKREINELKRELDRLQEELQRLSEE 421

                          250
                   ....*....|..
gi 1720395140  500 LQQLSLELEARE 511
Cdd:TIGR02169  422 LADLNAAIAGIE 433
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
320-509 1.31e-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: 1.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  320 QQLKESQAELVQKGSELVALR--VALREARATLRVSEGRARGLQEAARA--REQELEACSQELQRYRQEAERLREKAGHL 395
Cdd:COG4913    235 DDLERAHEALEDAREQIELLEpiRELAERYAAARERLAELEYLRAALRLwfAQRRLELLEAELEELRAELARLEAELERL 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  396 DAEASGLRdppvppattdpfllAESDEAKVQRAAAGAG--GSLRAQVERLRQELQREQRRGDEQ--------------RD 459
Cdd:COG4913    315 EARLDALR--------------EELDELEAQIRGNGGDrlEQLEREIERLERELEERERRRARLeallaalglplpasAE 380

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720395140  460 SFEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEA 509
Cdd:COG4913    381 EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 265-504 1.98e-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: 1.98e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  265 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSEL-------V 337
Cdd:TIGR02168  275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLeelkeelE 354

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  338 ALRVALREARATLRVSEGRARGLQEAARAR-------EQELEACSQELQRYRQEAERLREKAGHLDAEASGLRDPpvppa 410
Cdd:TIGR02168  355 SLEAELEELEAELEELESRLEELEEQLETLrskvaqlELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK----- 429

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  411 ttdpflLAESDEAKVQRAAAGaggsLRAQVERLRQELQREQRRGDEQRDSFEGERLAWQAEKEQVIRYQ------KQLQH 484
Cdd:TIGR02168  430 ------LEEAELKELQAELEE----LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQarldslERLQE 499

                          250       260
                   ....*....|....*....|
gi 1720395140  485 NYIQMYRRNRQLEQELQQLS 504
Cdd:TIGR02168  500 NLEGFSEGVKALLKNQSGLS 519
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 310-522 5.19e-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: 55.16  E-value: 5.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 310 QKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLR 389
Cdd:COG4942    24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 390 EKAGHLDAEA--SGLRDPPVPPATTDPFLLAESDE------AKVQRAAAGAGGSLRAQVERLRQELQREQRRGDEQRDSF 461
Cdd:COG4942   104 EELAELLRALyrLGRQPPLALLLSPEDFLDAVRRLqylkylAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720395140 462 EGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEARELADLGLAESAP 522
Cdd:COG4942   184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
265-483 6.08e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.69  E-value: 6.08e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  265 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGpRLEETKWE---VCQKSGEISLLKQQLkesqAELVQKGSELVALRV 341
Cdd:COG4913    618 ELAELEEELAEAEERLEALEAELDALQERREALQ-RLAEYSWDeidVASAEREIAELEAEL----ERLDASSDDLAALEE 692

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  342 ALREARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAG-HLDAEASGLRDPpvppattdpfLLAES 420
Cdd:COG4913    693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlELRALLEERFAA----------ALGDA 762

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720395140  421 DEAKVQRAAAGAGGSLRAQVERLRQELQREQRRGDEQrdsFEGERLAWQAEKEQVIRYQKQLQ 483
Cdd:COG4913    763 VERELRENLEERIDALRARLNRAEEELERAMRAFNRE---WPAETADLDADLESLPEYLALLD 822
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 196-448 1.14e-07

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: 54.69  E-value: 1.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  196 KLRDREAELQQLRDSMDESEATVCQAfGARQRRWPRERGedcaaqaqqatqRVQRAQQLLQLQVFQLQQEKRQLQDDFAQ 275
Cdd:TIGR02169  295 KIGELEAEIASLERSIAEKERELEDA-EERLAKLEAEID------------KLLAEIEELEREIEEERKRRDKLTEEYAE 361

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  276 LLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSEG 355
Cdd:TIGR02169  362 LKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEE 441

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  356 RARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASGLRdppvppattdpfllAESDEAKVQRAAAG-AGG 434
Cdd:TIGR02169  442 EKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ--------------RELAEAEAQARASEeRVR 507

                          250
                   ....*....|....
gi 1720395140  435 SLRAQVERLRQELQ 448
Cdd:TIGR02169  508 GGRAVEEVLKASIQ 521
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 250-521 5.36e-07

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: 52.76  E-value: 5.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  250 RAQQLLQLQVFQLQQEKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAEL 329
Cdd:TIGR02169  660 RAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL 739

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  330 VQKGSELVALRVALREARATLRVSEGRARGLQEAARAREQELEACSQELQRyrQEAERLREKAGHLDAEASGLRdppvpp 409
Cdd:TIGR02169  740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIE------ 811

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  410 attdpfLLAESDEAKVQRAAAgaggsLRAQVERLRQELQREQRRGDEQRDSFEGERLAWQAEKE----QVIRYQKQL--- 482
Cdd:TIGR02169  812 ------ARLREIEQKLNRLTL-----EKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEeleeELEELEAALrdl 880

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1720395140  483 --QHNYIQMYRRN-----RQLEQELQQLSLELEARELADLGLAESA 521
Cdd:TIGR02169  881 esRLGDLKKERDEleaqlRELERKIEELEAQIEKKRKRLSELKAKL 926
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 278-519 7.01e-07

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: 52.37  E-value: 7.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  278 QEREQLERRCATFEREQRELGPRLEETKwevcqksGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSEGRA 357
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELR-------KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  358 RGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASGLrdppvppattdpfllaeSDEAKVQRAAAGAggsLR 437
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL-----------------KEELKALREALDE---LR 809

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  438 AQVERLRQE-------LQREQRRGDEQRDSFEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEAR 510
Cdd:TIGR02168  810 AELTLLNEEaanlrerLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889


                   ....*....
gi 1720395140  511 ELADLGLAE 519
Cdd:TIGR02168  890 ALLRSELEE 898
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
265-520 2.39e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.15  E-value: 2.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 265 EKRQLQDDFAQLLQEREQLERRCATfEREQRELGPRLEETKWEVCqksgEISLLKQQLKESQAELVQKGSELVALRVALR 344
Cdd:COG4717   113 ELREELEKLEKLLQLLPLYQELEAL-EAELAELPERLEELEERLE----ELRELEEELEELEAELAELQEELEELLEQLS 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 345 -EARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASgLRDPPVPP----------ATTD 413
Cdd:COG4717   188 lATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER-LKEARLLLliaaallallGLGG 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 414 PFLLAESDEAKVQRAAAGAGGSLRAQVERLRQELQREQRRGDEQRDSFEGERLAWQAEKEQV----------IRYQKQLQ 483
Cdd:COG4717   267 SLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALglppdlspeeLLELLDRI 346

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1720395140 484 HNYIQMYRRNRQLEQELQQLSLELEARELADLGLAES 520
Cdd:COG4717   347 EELQELLREAEELEEELQLEELEQEIAALLAEAGVED 383
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
265-403 1.91e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 1.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  265 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKwEVCQKSG--EISLLKQQLKESQAELVQKGSELVALRVA 342
Cdd:COG4913    289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELE-AQIRGNGgdRLEQLEREIERLERELEERERRRARLEAL 367

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720395140  343 LREARATLRVSEGRARGLQEAARAR----EQELEACSQELQRYRQEAERLREKAGHLDAEASGLR 403
Cdd:COG4913    368 LAALGLPLPASAEEFAALRAEAAALlealEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 319-519 7.96e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 7.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  319 KQQLKESQAELVQKGSELVALRVALREARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAE 398
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  399 ASGLRDppvppattdpfllaesdEAKVQRAAAGAGGSLRAQVERLRQELQREQRRGDEQRDSFEGERLAWQAEKEQV-IR 477
Cdd:TIGR02168  756 LTELEA-----------------EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLnEE 818

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720395140  478 YQKQ------LQHNYIQMYRRNRQLEQELQQLSLELE--ARELADLGLAE 519
Cdd:TIGR02168  819 AANLrerlesLERRIAATERRLEDLEEQIEELSEDIEslAAEIEELEELI 868
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 318-387 1.62e-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: 42.52  E-value: 1.62e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 318 LKQQLKESQAELVQKGSELVALRVALREARATLRvsegrarglQEAARAREQELEACSQELQRYRQEAER 387
Cdd:COG2825    48 LEKEFKKRQAELQKLEKELQALQEKLQKEAATLS---------EEERQKKERELQKKQQELQRKQQEAQQ 108
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 274-508 1.95e-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: 44.19  E-value: 1.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  274 AQLLQEREQLE--RRCATFEREQRelgpRLEETKWEVCQKsgEISLLKQQLKESQAELVQKGSELVALRVALREARATLR 351
Cdd:TIGR00618  166 KELLMNLFPLDqyTQLALMEFAKK----KSLHGKAELLTL--RSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQ 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  352 VSEGRARGLQEAARAREQELEACSQ---ELQRYRQEAERLREKAGHLDAEASGLRDPPVPPATTDPFLLAESDEAKVQRA 428
Cdd:TIGR00618  240 QSHAYLTQKREAQEEQLKKQQLLKQlraRIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSK 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  429 AAGAGGSLRAQVERLRQELQREQRRGDEQRDSFEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQ----LEQELQQLS 504
Cdd:TIGR00618  320 MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQqkttLTQKLQSLC 399


                   ....
gi 1720395140  505 LELE 508
Cdd:TIGR00618  400 KELD 403
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 265-483 2.12e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.60  E-value: 2.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 265 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQkgsELVALRVALR 344
Cdd:COG4942    42 ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE---LLRALYRLGR 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 345 EARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASGLRdppvppattdpfllaesdeak 424
Cdd:COG4942   119 QPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE--------------------- 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720395140 425 vqraaagaggSLRAQVERLRQELQREQRRGDEQRDSFEGERLAWQAEKEQVIRYQKQLQ 483
Cdd:COG4942   178 ----------ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 370-519 2.76e-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: 43.21  E-value: 2.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 370 ELEACSQELQRYRQEAERLREKAGHLDA---EASGLRDPPVPPATTdpfllAESDEAKVQRAAAGAG-GSLRAQVERLRQ 445
Cdd:pfam09787   1 NLESAKQELADYKQKAARILQSKEKLIAslkEGSGVEGLDSSTALT-----LELEELRQERDLLREEiQKLRGQIQQLRT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 446 ELQREQRRGDEQRDS-----------FEGERLAWQAEKEQVIRYQKQLQHNYIQMYR-------RNRQLEQELQQLSLEL 507
Cdd:pfam09787  76 ELQELEAQQQEEAESsreqlqeleeqLATERSARREAEAELERLQEELRYLEEELRRskatlqsRIKDREAEIEKLRNQL 155

                         170
                  ....*....|..
gi 1720395140 508 EARELADLGLAE 519
Cdd:pfam09787 156 TSKSQSSSSQSE 167
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
318-511 3.19e-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: 3.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 318 LKQQLKESQAELVQKGSELVALRvalreARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDA 397
Cdd:COG3206   180 LEEQLPELRKELEEAEAALEEFR-----QKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPD 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 398 EASGLRDPPVPPAttdpfLLAESDEAKVQRAAAGAGG--------SLRAQVERLRQELQREQRRGdeqRDSFEGERLAWQ 469
Cdd:COG3206   255 ALPELLQSPVIQQ-----LRAQLAELEAELAELSARYtpnhpdviALRAQIAALRAQLQQEAQRI---LASLEAELEALQ 326

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1720395140 470 AEKEQVIRYQKQLQhnyiQMYRRNRQLEQELQQLSLELEARE 511
Cdd:COG3206   327 AREASLQAQLAQLE----ARLAELPELEAELRRLEREVEVAR 364
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 318-387 3.23e-04

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: 41.03  E-value: 3.23e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  318 LKQQLKESQAELVQKGSELVALRVALREARATLRvsegrarglQEAARAREQELEACSQELQRYRQEAER 387
Cdd:smart00935  23 LEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS---------EAAREKKEKELQKKVQEFQRKQQKLQQ 83
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 267-336 3.98e-04

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: 41.82  E-value: 3.98e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720395140 267 RQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSG-EISLLKQQLKESQAELVQKGSEL 336
Cdd:pfam13851  95 KVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQKTGlKNLLLEKKLQALGETLEKKEAQL 165
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
265-400 6.60e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 6.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 265 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALR 344
Cdd:COG4372    46 ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ 125

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720395140 345 EARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEAS 400
Cdd:COG4372   126 DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
265-390 6.83e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.33  E-value: 6.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 265 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALR 344
Cdd:PRK02224  259 EIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQ 338

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720395140 345 EA-------RATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLRE 390
Cdd:PRK02224  339 AHneeaeslREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEE 391
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
279-515 9.97e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 9.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 279 EREQLER---RCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELvqkgSELVALRVALREARATLRVSEG 355
Cdd:PRK03918  177 RIERLEKfikRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKELESLEG 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 356 RARGLQEAARARE---QELEACSQELQRYRQEAERLREKAghldAEASGLRDppvppattdpfLLAESDEAKVQraaaga 432
Cdd:PRK03918  253 SKRKLEEKIRELEeriEELKKEIEELEEKVKELKELKEKA----EEYIKLSE-----------FYEEYLDELRE------ 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 433 ggsLRAQVERLRQELQREQRRGDEQRDsfEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEAREL 512
Cdd:PRK03918  312 ---IEKRLSRLEEEINGIEERIKELEE--KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTP 386


                  ...
gi 1720395140 513 ADL 515
Cdd:PRK03918  387 EKL 389
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 193-484 1.97e-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: 41.26  E-value: 1.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  193 LEGKLRDREAELQQLRDSMDESEATVcqafgarqrrwpRErgedcaaqaqqATQRVQRAQQLLQLQVFQLQQEKRQLQDd 272
Cdd:pfam15921  595 LEKEINDRRLELQEFKILKDKKDAKI------------RE-----------LEARVSDLELEKVKLVNAGSERLRAVKD- 650

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  273 faqLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISL----LKQQLKESQAELVQkgselvalrvalreARA 348
Cdd:pfam15921  651 ---IKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETttnkLKMQLKSAQSELEQ--------------TRN 713

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  349 TLRVSEGR-------ARGLQEAARAREQELEACSQELQrYRQEAERLREKAGH-LDAEASGLRDPPVPPATTdpfllaes 420
Cdd:pfam15921  714 TLKSMEGSdghamkvAMGMQKQITAKRGQIDALQSKIQ-FLEEAMTNANKEKHfLKEEKNKLSQELSTVATE-------- 784

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  421 deakvQRAAAGAGGSLRAQVERLRQELQREQRRGDEQRDSFegerlawqAEKEQVIRYQKQ------LQH 484
Cdd:pfam15921  785 -----KNKMAGELEVLRSQERRLKEKVANMEVALDKASLQF--------AECQDIIQRQEQesvrlkLQH 841
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
269-511 2.31e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 269 LQDDFAQLLQEREQLERRCATFEREQRELGPRLEETkwEVCQKSGEISLLKQQLKESQ-----AELVQKGSELVALRVAL 343
Cdd:PRK02224  410 AEDFLEELREERDELREREAELEATLRTARERVEEA--EALLEAGKCPECGQPVEGSPhvetiEEDRERVEELEAELEDL 487

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 344 REARATLRVSEGRARGLQEAARARE----------QELEACSQELQRYRQEAERLREKAGHLDAEASGLRdppvppattd 413
Cdd:PRK02224  488 EEEVEEVEERLERAEDLVEAEDRIErleerredleELIAERRETIEEKRERAEELRERAAELEAEAEEKR---------- 557

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 414 pfllaesDEAKVQRAAAGAGGSLRAQVERLRQELQREQRRGDEQRDSFE-----GERLAWQAEKEQVIRYQKQLQHNYIQ 488
Cdd:PRK02224  558 -------EAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAaiadaEDEIERLREKREALAELNDERRERLA 630

                         250       260
                  ....*....|....*....|....
gi 1720395140 489 MYR-RNRQLEQELQQLSLElEARE 511
Cdd:PRK02224  631 EKReRKRELEAEFDEARIE-EARE 653
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 270-351 2.41e-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: 39.52  E-value: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 270 QDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARAT 349
Cdd:COG1579    88 NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167


                  ..
gi 1720395140 350 LR 351
Cdd:COG1579   168 LA 169
PRK12704 PRK12704
phosphodiesterase; Provisional
 266-387 3.06e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 266 KRQLQDDFAQLLQEREQLERRCATFEREQRElgprLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVAlrE 345
Cdd:PRK12704   81 RNELQKLEKRLLQKEENLDRKLELLEKREEE----LEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE--E 154

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1720395140 346 ARATL--RVsEGRARgLQEAARAREQELEAcsqelqryRQEAER 387
Cdd:PRK12704  155 AKEILleKV-EEEAR-HEAAVLIKEIEEEA--------KEEADK 188
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 265-468 3.13e-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: 40.13  E-value: 3.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 265 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALR 344
Cdd:COG4942    21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 345 EARATLRV-------------------------SEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEA 399
Cdd:COG4942   101 AQKEELAEllralyrlgrqpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 400 SGL-------------RDPPVPPATTDPFLLAESDEAKVQRAAagaggSLRAQVERLRQELQREQRRGDEQRDSFEGERL 466
Cdd:COG4942   181 AELeeeraalealkaeRQKLLARLEKELAELAAELAELQQEAE-----ELEALIARLEAEAAAAAERTPAAGFAALKGKL 255


                  ..
gi 1720395140 467 AW 468
Cdd:COG4942   256 PW 257
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
275-517 3.24e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 3.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 275 QLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSE 354
Cdd:COG4372    14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 355 GRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASglrdppvppattdpfLLAESDEAKVQRAAagagg 434
Cdd:COG4372    94 AELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIA---------------ELQSEIAEREEELK----- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 435 SLRAQVERLRQELQR---EQRRGDEQRDSFEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEARE 511
Cdd:COG4372   154 ELEEQLESLQEELAAleqELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233


                  ....*.
gi 1720395140 512 LADLGL 517
Cdd:COG4372   234 ALSALL 239
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 193-476 4.44e-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: 40.05  E-value: 4.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  193 LEGKLRDREAELQQLRDSMDESEATVcqafgaRQRRWPRERGE-----DCAAQAQQATQRVQRAQQLLQLQVFQLQQEKR 267
Cdd:TIGR02169  763 LEARIEELEEDLHKLEEALNDLEARL------SHSRIPEIQAElskleEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ 836

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  268 QLQddfaqllQEREQLERRCATFEREQRELGPRLEEtkwevcqksgeislLKQQLKESQAELVQKGSELVALRVALREAR 347
Cdd:TIGR02169  837 ELQ-------EQRIDLKEQIKSIEKEIENLNGKKEE--------------LEEELEELEAALRDLESRLGDLKKERDELE 895

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  348 ATLRvsegrarglqeAARAREQELEAcsqELQRYRQEAERLREKAGHLDAEASGLRDPPVPPATTDPFLLAESDEAKVQR 427
Cdd:TIGR02169  896 AQLR-----------ELERKIEELEA---QIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQ 961

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1720395140  428 AAAGAGGSLRAQVERLRQELQREQRRgdeqRDSFEGERLAWQAEKEQVI 476
Cdd:TIGR02169  962 RVEEEIRALEPVNMLAIQEYEEVLKR----LDELKEKRAKLEEERKAIL 1006
PTZ00121 PTZ00121
MAEBL; Provisional
 248-514 4.95e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 4.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  248 VQRAQQLLQLQVFQLQQEKRQLQDDFAQLLQ--EREQLERRCATFEREQRELGPRL-----EETKWEVCQKSGEISLLKQ 320
Cdd:PTZ00121  1557 LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKkaEEARIEEVMKLYEEEKKMKAEEAkkaeeAKIKAEELKKAEEEKKKVE 1636

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  321 QLKESQAELVQKGSELvalrvalREARatlrvSEGRARGLQEAARAREQELEAcsqelQRYRQEAERLREKAGHLDAEAS 400
Cdd:PTZ00121  1637 QLKKKEAEEKKKAEEL-------KKAE-----EENKIKAAEEAKKAEEDKKKA-----EEAKKAEEDEKKAAEALKKEAE 1699

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140  401 GLRdppvppaTTDPFLLAESDEAKVQRAAAGAGGSLRAQVERLRQELQREQRRGDEQRDSfEGERLAWQAEKEQVIRYQK 480
Cdd:PTZ00121  1700 EAK-------KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD-EEEKKKIAHLKKEEEKKAE 1771

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1720395140  481 QLQHNYIQMYRRNRQLEQELQQLSLELEARELAD 514
Cdd:PTZ00121  1772 EIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFD 1805
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
266-513 5.13e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 5.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 266 KRQLQDDFAQLLQEREQLErrcatfEREQRELGPRLEETKWEVCQKSGEISLLKQQlKESQAELVQKGSELVAlrvALRE 345
Cdd:PRK02224  179 ERVLSDQRGSLDQLKAQIE------EKEEKDLHERLNGLESELAELDEEIERYEEQ-REQARETRDEADEVLE---EHEE 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 346 ARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEAsGLRDPpvppattdpfllaeSDEAkv 425
Cdd:PRK02224  249 RREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA-GLDDA--------------DAEA-- 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 426 qraaagaggslraqVERLRQELQReqrRGDEQRDSFEGERLAWQAEKEQVIRYQKqlqhNYIQMYRRNRQLEQELQQLSL 505
Cdd:PRK02224  312 --------------VEARREELED---RDEELRDRLEECRVAAQAHNEEAESLRE----DADDLEERAEELREEAAELES 370


                  ....*...
gi 1720395140 506 ELEARELA 513
Cdd:PRK02224  371 ELEEAREA 378
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 196-403 5.96e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.98  E-value: 5.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 196 KLRDREAELQQLRDSMDESEATVCQAFGARQRrwprergedcaaqAQQATQRVQRAQQLLQLQVFQLQQEKRQLQDDFAQ 275
Cdd:COG4942    21 AAAEAEAELEQLQQEIAELEKELAALKKEEKA-------------LLKQLAALERRIAALARRIRALEQELAALEAELAE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 276 LLQEREQLERRcatFEREQRELGPRLEETkwevcQKSGEISLLK-----------------------------QQLKESQ 326
Cdd:COG4942    88 LEKEIAELRAE---LEAQKEELAELLRAL-----YRLGRQPPLAlllspedfldavrrlqylkylaparreqaEELRADL 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720395140 327 AELVQKGSELVALRVALREARATLrvsEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASGLR 403
Cdd:COG4942   160 AELAALRAELEAERAELEALLAEL---EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 307-522 6.04e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.04  E-value: 6.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 307 EVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSEGRARGLQEAARAREQELEACSQELqryrqeAE 386
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL------GE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 387 RLRekaghlDAEASGLRDPPVppattDPFLLAESDEAKVQRAAA-----GAGGSLRAQVERLRQELQREQRRGDEQRDSF 461
Cdd:COG3883    91 RAR------ALYRSGGSVSYL-----DVLLGSESFSDFLDRLSAlskiaDADADLLEELKADKAELEAKKAELEAKLAEL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720395140 462 EGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEARELADLGLAESAP 522
Cdd:COG3883   160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 318-387 6.68e-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: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 37.17  E-value: 6.68e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 318 LKQQLKESQAELVQKGSELVALRVALREARATLrvsegrarglQEAARAREQELEACSQELQRYRQEAER 387
Cdd:pfam03938  24 LEKKFKKRQAELEAKQKELQKLYEELQKDGALL----------EEEREEKEQELQKKEQELQQLQQKAQQ 83
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 265-445 6.99e-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: 6.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 265 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAEL--VQKGSELVALRVA 342
Cdd:COG1579    18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnVRNNKEYEALQKE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 343 LREARATLRVSEGRARGLQEAARAREQELEACSQELQryrQEAERLREKAGHLDAEASGLRdppvppattdpfllAESDE 422
Cdd:COG1579    98 IESLKRRISDLEDEILELMERIEELEEELAELEAELA---ELEAELEEKKAELDEELAELE--------------AELEE 160

                         170       180
                  ....*....|....*....|....*
gi 1720395140 423 AKVQRAAAGAG--GSLRAQVERLRQ 445
Cdd:COG1579   161 LEAEREELAAKipPELLALYERIRK 185
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 268-385 7.02e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 38.90  E-value: 7.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 268 QLQDDFAQLLQEREQLERRCATFEREQR-------ELGPRLEE---TKWEVCQKSGEISLLKQQLKESQAELVQKGSELV 337
Cdd:pfam05622 301 SYRERLTELQQLLEDANRRKNELETQNRlanqrilELQQQVEElqkALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQ 380

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1720395140 338 ALRVALREARATLRVSEGR-ARGLQEAARAREQELEACSQELQRYRQEA 385
Cdd:pfam05622 381 KKKEQIEELEPKQDSNLAQkIDELQEALRKKDEDMKAMEERYKKYVEKA 429
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 194-509 7.58e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 7.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 194 EGKLRDREAELQQLRDSMDESEATVcqafGARQRRWPRERGEDCAAQAQQATQRVQRAQQLLQLQVFQLQQEKRQLQDDF 273
Cdd:COG1196   486 LAEAAARLLLLLEAEADYEGFLEGV----KAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAA 561

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 274 AQLLQEREQLERrcATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVS 353
Cdd:COG1196   562 AIEYLKAAKAGR--ATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRA 639

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 354 EGRARGLQEAARAREQELEACSQELQRYRQEAERLREKaghldaeasglrdppvppattdpfllAESDEAKVQRAAAGAG 433
Cdd:COG1196   640 VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEA--------------------------EAELEELAERLAEEEL 693

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 434 GSLRAQVERLRQELQREQRRGDEQRDSFEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNR---------QLEQELQQLS 504
Cdd:COG1196   694 ELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEelpeppdleELERELERLE 773


                  ....*
gi 1720395140 505 LELEA 509
Cdd:COG1196   774 REIEA 778
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 266-502 9.29e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 38.95  E-value: 9.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 266 KRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALRE 345
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERI 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 346 ARATLRVSEGRARGLQEAARAREQELEACSQELQRYR----QEAERLReKAGHLDAEASGLRDPPVPPATTDPFLLAESD 421
Cdd:pfam17380 366 RQEEIAMEISRMRELERLQMERQQKNERVRQELEAARkvkiLEEERQR-KIQQQKVEMEQIRAEQEEARQREVRRLEEER 444

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395140 422 EAKVQRAAAGAGgSLRAQVERLRQElQREQRRGDEQRDSFEGERLAWQAEKEQVIRYQ-KQLQHNYIQMYRRNRQLEQEL 500
Cdd:pfam17380 445 AREMERVRLEEQ-ERQQQVERLRQQ-EEERKRKKLELEKEKRDRKRAEEQRRKILEKElEERKQAMIEEERKRKLLEKEM 522


                  ..
gi 1720395140 501 QQ 502
Cdd:pfam17380 523 EE 524
 
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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