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Conserved domains on  [gi|410060781|gb|AFV53352|]
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tropomyosin [Oreochromis mossambicus]

Protein Classification

tropomyosin( domain architecture ID 11991670)

tropomyosin binds to actin filaments in muscle and non-muscle cells and plays a central role in regulating striated and smooth muscle contraction; forms a homodimer or a heterodimer between tropomyosin alpha and beta chains

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
48-282 9.78e-73

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organisation and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


:

Pssm-ID: 425563 [Multi-domain]  Cd Length: 235  Bit Score: 222.98  E-value: 9.78e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   48 KKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGM 127
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  128 KVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKSL 207
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 410060781  208 EAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISEELDHALNDMT 282
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
 
Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
48-282 9.78e-73

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organisation and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


Pssm-ID: 425563 [Multi-domain]  Cd Length: 235  Bit Score: 222.98  E-value: 9.78e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   48 KKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGM 127
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  128 KVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKSL 207
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 410060781  208 EAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISEELDHALNDMT 282
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
21-275 4.23e-12

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 66.28  E-value: 4.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   21 RAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRIQLVEEELD 100
Cdd:COG1196   668 ELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELE 747
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  101 RAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTE 180
Cdd:COG1196   748 ELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLE 827
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  181 ERAELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSVAKLEKTIDDLEDEL 260
Cdd:COG1196   828 QEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEI 907
                         250
                  ....*....|....*
gi 410060781  261 YAQKLKYKAISEELD 275
Cdd:COG1196   908 EKLRERLEELEAKLE 922
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
37-284 5.21e-12

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: 65.85  E-value: 5.21e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781    37 KQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRIQLVEEELDRAQERLATALTKLEEA 116
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   117 EKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELSEGKCSELEEE 196
Cdd:TIGR02168  767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   197 LKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISEELDH 276
Cdd:TIGR02168  847 IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926

                   ....*...
gi 410060781   277 ALNDMTSI 284
Cdd:TIGR02168  927 LELRLEGL 934
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
2-275 7.79e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 53.12  E-value: 7.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   2 DAIKKKMQMLKLDKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDA 81
Cdd:PRK02224 324 EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA 403
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  82 EGEVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAadesergmkVIENRAMKDEEKMELQEIQLKEAKHI--AEEAD 159
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDELREREAELEATLRTARER---------VEEAEALLEAGKCPECGQPVEGSPHVetIEEDR 474
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 160 RKYEEVARKLVIIEGDLERTEERAELSEgKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRA 239
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEA 553
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 410060781 240 EFAERSVAKLEKTIDDLEDELYAQKLKYKAISEELD 275
Cdd:PRK02224 554 EEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE 589
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
16-220 2.85e-04

MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.


Pssm-ID: 380155 [Multi-domain]  Cd Length: 1848  Bit Score: 42.13  E-value: 2.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   16 ENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTE------------DELDKYSEA----LKDAQEKLELAEKIAT 79
Cdd:NF012221 1558 QNALADKERAEADRQRLEQEKQQQLAAISGSQSQLESTDqnaletngqaqrDAILEESRAvtkeLTTLAQGLDALDSQAT 1637
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   80 DAE--GEvaslNRRIQLVEEELDRAQERL-ATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAK---- 152
Cdd:NF012221 1638 YAGesGD----QWRNPFAGGLLDRVQEQLdDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGVAQGEQNQANAEqdid 1713
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 410060781  153 HIAEEADRKYEEVARKlviiEGDLERTEERAELSEGKC-SELEEELKTVTNnlKSLEAQAEKYSQKEDK 220
Cdd:NF012221 1714 DAKADAEKRKDDALAK----QNEAQQAESDANAAANDAqSRGEQDASAAEN--KANQAQADAKGAKQDE 1776
 
Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
48-282 9.78e-73

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organisation and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


Pssm-ID: 425563 [Multi-domain]  Cd Length: 235  Bit Score: 222.98  E-value: 9.78e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   48 KKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGM 127
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  128 KVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKSL 207
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 410060781  208 EAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISEELDHALNDMT 282
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
7-152 1.70e-25

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.


Pssm-ID: 403808 [Multi-domain]  Cd Length: 142  Bit Score: 98.15  E-value: 1.70e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781    7 KMQMLKLDKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEgeva 86
Cdd:pfam12718   1 KMNSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNE---- 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 410060781   87 SLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAK 152
Cdd:pfam12718  77 NLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKEAK 142
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
21-275 4.23e-12

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 66.28  E-value: 4.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   21 RAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRIQLVEEELD 100
Cdd:COG1196   668 ELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELE 747
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  101 RAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTE 180
Cdd:COG1196   748 ELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLE 827
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  181 ERAELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSVAKLEKTIDDLEDEL 260
Cdd:COG1196   828 QEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEI 907
                         250
                  ....*....|....*
gi 410060781  261 YAQKLKYKAISEELD 275
Cdd:COG1196   908 EKLRERLEELEAKLE 922
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
37-284 5.21e-12

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: 65.85  E-value: 5.21e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781    37 KQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRIQLVEEELDRAQERLATALTKLEEA 116
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   117 EKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELSEGKCSELEEE 196
Cdd:TIGR02168  767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   197 LKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISEELDH 276
Cdd:TIGR02168  847 IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926

                   ....*...
gi 410060781   277 ALNDMTSI 284
Cdd:TIGR02168  927 LELRLEGL 934
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
4-284 4.05e-11

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 63.19  E-value: 4.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781    4 IKKKMQMLKLDKENALDRAEQaESDKKAAEDrsKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEG 83
Cdd:COG1196   198 LEKQLEKLERQAEKAERYQEL-KAELRELEL--ALLLAKLKELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKS 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   84 EVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYE 163
Cdd:COG1196   275 ELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLA 354
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  164 EV-----------ARKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKL 232
Cdd:COG1196   355 ELeeakeeleeklSALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAEL 434
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 410060781  233 KEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISEELDHALNDMTSI 284
Cdd:COG1196   435 EELQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQRLEKELSSL 486
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
34-275 2.00e-10

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 61.24  E-value: 2.00e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781    34 DRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRIQLVEEELDRAQERLATALTKL 113
Cdd:TIGR02169  681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL 760
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   114 EEAEKAADESErgmkvienrAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELSEGKCSEL 193
Cdd:TIGR02169  761 KELEARIEELE---------EDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   194 EEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISEE 273
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ 911

                   ..
gi 410060781   274 LD 275
Cdd:TIGR02169  912 IE 913
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
44-284 1.29e-09

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 58.57  E-value: 1.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   44 VALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADES 123
Cdd:COG1196   663 LAQKRELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEEL 742
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  124 ERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNN 203
Cdd:COG1196   743 EEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQR 822
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  204 LKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISEELDHALNDMTS 283
Cdd:COG1196   823 RERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAE 902

                  .
gi 410060781  284 I 284
Cdd:COG1196   903 L 903
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
24-266 3.04e-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: 57.76  E-value: 3.04e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781    24 QAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRIQLVEEELDRAQ 103
Cdd:TIGR02168  208 QAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ 287
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   104 ERLATALTKLEEaekaadesergmkvIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERA 183
Cdd:TIGR02168  288 KELYALANEISR--------------LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   184 ELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQ 263
Cdd:TIGR02168  354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433

                   ...
gi 410060781   264 KLK 266
Cdd:TIGR02168  434 ELK 436
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
26-275 3.67e-09

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 57.42  E-value: 3.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   26 ESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKI----ATDAEGEVASLNRRIQLVEEELDR 101
Cdd:COG1196   171 KERKEEAERKLERTEENLERLEDLLEELEKQLEKLERQAEKAERYQELKAELreleLALLLAKLKELRKELEELEEELSR 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  102 AQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEE 181
Cdd:COG1196   251 LEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELKE 330
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  182 RAELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEF----AERSVAKLEKTIDDLE 257
Cdd:COG1196   331 KIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAelaeIRNELEELKREIESLE 410
                         250
                  ....*....|....*...
gi 410060781  258 DELYAQKLKYKAISEELD 275
Cdd:COG1196   411 ERLERLSERLEDLKEELK 428
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
18-259 6.83e-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: 56.60  E-value: 6.83e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781    18 ALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRIQLVEE 97
Cdd:TIGR02168  780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781    98 ELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLE 177
Cdd:TIGR02168  860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   178 RTEER--------AELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSVAKL 249
Cdd:TIGR02168  940 NLQERlseeysltLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETL 1019
                          250
                   ....*....|
gi 410060781   250 EKTIDDLEDE 259
Cdd:TIGR02168 1020 EEAIEEIDRE 1029
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
1-258 2.42e-08

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 54.72  E-value: 2.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781    1 MDAIKKKMQMLKLDKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATD 80
Cdd:COG1196   697 LRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAK 776
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   81 AEGEVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADR 160
Cdd:COG1196   777 LKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEK 856
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  161 KYEEVARKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAE 240
Cdd:COG1196   857 ELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERLEVELPELEEELE 936
                         250       260
                  ....*....|....*....|....*..
gi 410060781  241 ---------FAERSVAKLEKTIDDLED 258
Cdd:COG1196   937 eeyedtletELEREIERLEEEIEALGP 963
COG4372 COG4372
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
43-258 3.08e-08

Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 54.26  E-value: 3.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  43 LVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRIQLVEEELDRAQERLATALTKLEEA------ 116
Cdd:COG4372   62 LFLLNRNLRSGVFQLDDIRPQLRALRTELGTAQGEKRAAETEREAARSELQKARQEREAVRQELAAARQNLAKAqqelar 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 117 --EKAADESERGMKVIENRAMKDEEKMELQEiQLKEAKHIAEEADRKYEEVARKLVIIEG---DLERTEERAELSEGKCS 191
Cdd:COG4372  142 ltKQAQDLQTRLKTLAEQRRQLEAQAQSLQA-SQKQLQASATQLKSQVLDLKLRSAQIEQeaqNLATRANAAQARTEELA 220
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 410060781 192 ELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSVAKLEKTIDDLED 258
Cdd:COG4372  221 RRAAAAQQTAQAIQQRDAQISQKAQQIAARAEQIRERERQLQRLETAQARLEQEVAQLEAYYQAYVR 287
NtpI COG1269
Archaeal/vacuolar-type H+-ATPase subunit I/STV1 [Energy production and conversion];
55-278 3.92e-08

Archaeal/vacuolar-type H+-ATPase subunit I/STV1 [Energy production and conversion];


Pssm-ID: 224188 [Multi-domain]  Cd Length: 660  Bit Score: 53.90  E-value: 3.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  55 DELDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRIQLVEEELdraqERLATALTKLEEAEKAADESERGMKVIENRA 134
Cdd:COG1269   50 KVAEVAQISLSSLLSEVLDYLRSVKGLEGRLFILPEEVEKLEAEL----KSLEEVIKPAEKFSSEVEELTRKLEERLSEL 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 135 MKDEEKMELQEIQLKEAKHIAEEADRKYEevaRKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKSLEAQAEKY 214
Cdd:COG1269  126 DEELEDLEDLLEELEPLAYLDFDLSLLRG---LKFLLVRLGLVRREKLEALVGVIEDEVALYGENVEASVVIVVAHGAED 202
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 410060781 215 SQKEDKYEEEIKALTDKLKEAEtraEFAERSVAKLEKTIDDLEDELYAQKLKYKAISEELDHAL 278
Cdd:COG1269  203 LDKVSKILNELGFELYEVPEFD---GGPSELISELEEVIAEIQDELESLRSELEALAEKIAEEL 263
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
7-260 4.13e-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: 54.30  E-value: 4.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781     7 KMQMLKLDKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVA 86
Cdd:TIGR02169  682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781    87 SLNRRIQLVEEELdrAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVA 166
Cdd:TIGR02169  762 ELEARIEELEEDL--HKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQ 839
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   167 RKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSV 246
Cdd:TIGR02169  840 EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRL 919
                          250
                   ....*....|....
gi 410060781   247 AKLEKTIDDLEDEL 260
Cdd:TIGR02169  920 SELKAKLEALEEEL 933
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1-277 4.87e-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: 53.91  E-value: 4.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781     1 MDAIKKKMQMLKLDKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATD 80
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781    81 AEGEVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADR 160
Cdd:TIGR02168  321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   161 KYEEVARKLVIIEGDLERTEERAELSEGKCSELeeELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAE 240
Cdd:TIGR02168  401 EIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 410060781   241 FAERSVAKLEKTIDDLEDELYAQKLKYKAISEELDHA 277
Cdd:TIGR02168  479 AAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQ 515
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
2-275 7.79e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 53.12  E-value: 7.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   2 DAIKKKMQMLKLDKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDA 81
Cdd:PRK02224 324 EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA 403
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  82 EGEVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAadesergmkVIENRAMKDEEKMELQEIQLKEAKHI--AEEAD 159
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDELREREAELEATLRTARER---------VEEAEALLEAGKCPECGQPVEGSPHVetIEEDR 474
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 160 RKYEEVARKLVIIEGDLERTEERAELSEgKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRA 239
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEA 553
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 410060781 240 EFAERSVAKLEKTIDDLEDELYAQKLKYKAISEELD 275
Cdd:PRK02224 554 EEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE 589
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
20-277 8.82e-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: 53.15  E-value: 8.82e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781    20 DRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLElaekiatDAEGEVASLNRRIQLVEEEL 99
Cdd:TIGR02169  660 RAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELS-------DASRKIGEIEKEIEQLEQEE 732
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   100 DRAQERLATALTKLEEAEKAADESERGMKviENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERT 179
Cdd:TIGR02169  733 EKLKERLEELEEDLSSLEQEIENVKSELK--ELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRI 810
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   180 EERAELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSVAKLEKTIDDLEDE 259
Cdd:TIGR02169  811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE 890
                          250
                   ....*....|....*...
gi 410060781   260 LYAQKLKYKAISEELDHA 277
Cdd:TIGR02169  891 RDELEAQLRELERKIEEL 908
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
68-280 9.75e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.14  E-value: 9.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781    68 QEKLELAEKIAtDAEGEVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQ 147
Cdd:TIGR02168  677 REIEELEEKIE-ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   148 LKEAKHIAEEADRKYE-------EVARKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDK 220
Cdd:TIGR02168  756 LTELEAEIEELEERLEeaeeelaEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   221 YEEEIKALTDKLKEAETRAEFAERSVAKLEKTIDDLEDELyAQKLKYKAISEELDHALND 280
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL-EALLNERASLEEALALLRS 894
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2-256 1.63e-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: 1.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781     2 DAIKKKMQMLKLDKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDA 81
Cdd:TIGR02168  729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781    82 EGEVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRK 161
Cdd:TIGR02168  809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA 888
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   162 YEEVARKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKSLEAQ-AEKYSQKEDKYEEEIKALTDKLKEAETRAE 240
Cdd:TIGR02168  889 LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRiDNLQERLSEEYSLTLEEAEALENKIEDDEE 968
                          250
                   ....*....|....*.
gi 410060781   241 FAERSVAKLEKTIDDL 256
Cdd:TIGR02168  969 EARRRLKRLENKIKEL 984
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
11-260 2.44e-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: 51.60  E-value: 2.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781    11 LKLDKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKL-ELAEKIAT---------- 79
Cdd:TIGR02168  230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELyALANEISRleqqkqilre 309
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781    80 ---DAEGEVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADEsergmkvIENRAMKDEEKMELQEIQLKEAKHIAE 156
Cdd:TIGR02168  310 rlaNLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELES-------LEAELEELEAELEELESRLEELEEQLE 382
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   157 EADRKYEEVARKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKslEAQAEKYSQKEDKYEEEIKALTDKLKEAE 236
Cdd:TIGR02168  383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQEELERLE 460
                          250       260
                   ....*....|....*....|....
gi 410060781   237 TRAEFAERSVAKLEKTIDDLEDEL 260
Cdd:TIGR02168  461 EALEELREELEEAEQALDAAEREL 484
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2-259 2.74e-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: 51.61  E-value: 2.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781     2 DAIKKKMQMLKLDKENALDRAEQAESDKKAAEDRSKQL-EDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATD 80
Cdd:TIGR02169  247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK 326
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781    81 AEGEVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADR 160
Cdd:TIGR02169  327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   161 KYEEVARKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAE 240
Cdd:TIGR02169  407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELS 486
                          250
                   ....*....|....*....
gi 410060781   241 FAERSVAKLEKTIDDLEDE 259
Cdd:TIGR02169  487 KLQRELAEAEAQARASEER 505
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
89-275 2.06e-06

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 48.94  E-value: 2.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   89 NRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARK 168
Cdd:COG1196   659 KRSSLAQKRELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSR 738
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  169 LVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSVAK 248
Cdd:COG1196   739 LEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELES 818
                         170       180
                  ....*....|....*....|....*..
gi 410060781  249 LEKTIDDLEDELYAQKLKYKAISEELD 275
Cdd:COG1196   819 LEQRRERLEQEIEELEEEIEELEEKLD 845
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
47-284 7.11e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 7.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781    47 QKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEgevASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERG 126
Cdd:TIGR02168  178 ERKLERTRENLDRLEDILNELERQLKSLERQAEKAE---RYKELKAELRELELALLVLRLEELREELEELQEELKEAEEE 254
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   127 MKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKS 206
Cdd:TIGR02168  255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE 334
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 410060781   207 LEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISEELDHALNDMTSI 284
Cdd:TIGR02168  335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
NtpI COG1269
Archaeal/vacuolar-type H+-ATPase subunit I/STV1 [Energy production and conversion];
13-284 8.18e-06

Archaeal/vacuolar-type H+-ATPase subunit I/STV1 [Energy production and conversion];


Pssm-ID: 224188 [Multi-domain]  Cd Length: 660  Bit Score: 46.97  E-value: 8.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  13 LDKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRI 92
Cdd:COG1269   43 LKELEKLKVAEVAQISLSSLLSEVLDYLRSVKGLEGRLFILPEEVEKLEAELKSLEEVIKPAEKFSSEVEELTRKLEERL 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  93 QLVEEELDRAQERLaTALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQeiqlkeAKHIAEEADRKYEEVARKLVII 172
Cdd:COG1269  123 SELDEELEDLEDLL-EELEPLAYLDFDLSLLRGLKFLLVRLGLVRREKLEAL------VGVIEDEVALYGENVEASVVIV 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 173 ----EGDL--------ERTEERAELSEGK------CSELEEELKTVTNNLKSLEAQAEKYSqkeDKYEEEIKALTDKLKE 234
Cdd:COG1269  196 vahgAEDLdkvskilnELGFELYEVPEFDggpselISELEEVIAEIQDELESLRSELEALA---EKIAEELLAVREILEI 272
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 410060781 235 AETRAEFAErsvaKLEKTIDDLEDELYAQKLKYKAISEELDHALNDMTSI 284
Cdd:COG1269  273 EKALGDVLS----KLARTEYTLAIEGWVPADEVEKLKKIINRATGGAAYF 318
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
28-248 1.44e-05

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


Pssm-ID: 227278 [Multi-domain]  Cd Length: 420  Bit Score: 45.87  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  28 DKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRIQLVEEELDRAQERLA 107
Cdd:COG4942   32 SAAADDKQLKQIQKEIAALEKKIREQQDQRAKLEKQLKSLETEIASLEAQLIETADDLKKLRKQIADLNARLNALEVQER 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 108 TALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELSE 187
Cdd:COG4942  112 EQRRRLAEQLAALQRSGRNPPPALLVSPEDAQRSVRLAIYYGALNPARAERIDALKATLKQLAAVRAEIAAEQAELTTLL 191
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 410060781 188 GKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSVAK 248
Cdd:COG4942  192 SEQRAQQAKLAQLLEERKKTLAQLNSELSADQKKLEELRANESRLKNEIASAEAAAAKARE 252
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
23-261 1.52e-05

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 46.07  E-value: 1.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  23 EQAESDKKAAEDRSK--QLEDDLVALQKKLKGTEDELDKYS-----EALKDAQEKLELAEKIATDAEGEVASLNRRIQLV 95
Cdd:PRK05771  40 LSNERLRKLRSLLTKlsEALDKLRSYLPKLNPLREEKKKVSvksleELIKDVEEELEKIEKEIKELEEEISELENEIKEL 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  96 EEELDRAQerlatALTKLEEAEKAADESERgMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKY----------EEV 165
Cdd:PRK05771 120 EQEIERLE-----PWGNFDLDLSLLLGFKY-VSVFVGTVPEDKLEELKLESDVENVEYISTDKGYVYvvvvvlkelsDEV 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 166 ARKLVIIEGDLERTEERAELSEgKCSELEEELKTVTNNLKSLEAQAEKYSQkedKYEEEIKALTDKL----KEAETRAEF 241
Cdd:PRK05771 194 EEELKKLGFERLELEEEGTPSE-LIREIKEELEEIEKERESLLEELKELAK---KYLEELLALYEYLeielERAEALSKF 269
                        250       260       270
                 ....*....|....*....|....*....|...
gi 410060781 242 A-------------ERSVAKLEKTIDDLEDELY 261
Cdd:PRK05771 270 LktdktfaiegwvpEDRVKKLKELIDKATGGSA 302
PTZ00121 PTZ00121
MAEBL; Provisional
2-269 1.63e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781    2 DAIKKKMQMLKLDKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQE--KLELAEKIAT 79
Cdd:PTZ00121 1119 EAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEvrKAEELRKAED 1198
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   80 DAEGEVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEAd 159
Cdd:PTZ00121 1199 ARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA- 1277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  160 RKYEEVARKLVIIEGD-LERTEERAELSEG--------KCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTD 230
Cdd:PTZ00121 1278 RKADELKKAEEKKKADeAKKAEEKKKADEAkkkaeeakKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD 1357
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 410060781  231 KLKEAETRAEFAERSVAKLEKTIDDL----EDELYAQKLKYKA 269
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKKKEEAKKKADAAkkkaEEKKKADEAKKKA 1400
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
52-260 2.26e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.42  E-value: 2.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  52 GTEDELDKYSEALKDAQEKLELAE-----KIATDAEGEVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERG 126
Cdd:PRK02224 177 GVERVLSDQRGSLDQLKAQIEEKEekdlhERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETL 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 127 MKVIENRAMK---DEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNN 203
Cdd:PRK02224 257 EAEIEDLRETiaeTEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVA 336
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 410060781 204 LKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSVAKLEKTIDDLEDEL 260
Cdd:PRK02224 337 AQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
4-218 4.47e-05

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 44.71  E-value: 4.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781    4 IKKKMQMLKLDKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEG 83
Cdd:COG1196   293 LKEEIEELEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLE 372
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   84 EVASlnrRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYE 163
Cdd:COG1196   373 ELEE---LFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELE 449
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 410060781  164 EVARKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKE 218
Cdd:COG1196   450 ELEEQLEELRDRLKELERELAELQEELQRLEKELSSLEARLDRLEAEQRASQGVR 504
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
14-258 6.35e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.26  E-value: 6.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  14 DKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRIQ 93
Cdd:PRK02224 273 EREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDAD 352
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  94 LVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIE 173
Cdd:PRK02224 353 DLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELE 432
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 174 GDLERTEERAE-----LSEGKCSELEEELK--TVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEfAERSV 246
Cdd:PRK02224 433 ATLRTARERVEeaealLEAGKCPECGQPVEgsPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVE-AEDRI 511
                        250
                 ....*....|..
gi 410060781 247 AKLEKTIDDLED 258
Cdd:PRK02224 512 ERLEERREDLEE 523
PTZ00121 PTZ00121
MAEBL; Provisional
5-269 8.35e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 8.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781    5 KKKMQMLKLDKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKlkgtEDELDKYSEALKDAQEKLELAEKIATDAEGE 84
Cdd:PTZ00121 1342 KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK----AEEKKKADEAKKKAEEDKKKADELKKAAAAK 1417
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   85 VASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGmkviENRAMKDEEKMELQEIQLK--------EAKHIAE 156
Cdd:PTZ00121 1418 KKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKA----EEAKKKAEEAKKADEAKKKaeeakkadEAKKKAE 1493
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  157 EADRKYEEVARKlviiegdLERTEERAELSEGKCSELEEELKTVTNNLKSLEAQA--EKYSQKEDKYEEEIKALTDKLKE 234
Cdd:PTZ00121 1494 EAKKKADEAKKA-------AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKaeEKKKADELKKAEELKKAEEKKKA 1566
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 410060781  235 AETRAEFAERSVA--------KLEKTIDDLEDELYAQKLKYKA 269
Cdd:PTZ00121 1567 EEAKKAEEDKNMAlrkaeeakKAEEARIEEVMKLYEEEKKMKA 1609
PTZ00121 PTZ00121
MAEBL; Provisional
6-269 9.04e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 9.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781    6 KKMQMLKLDKENA--LDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKySEALKDAQEKLELAEKIATDAEG 83
Cdd:PTZ00121 1230 KKAEEAKKDAEEAkkAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK-AEEKKKADEAKKAEEKKKADEAK 1308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   84 EVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYE 163
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE 1388
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  164 EVARKlviiegdlERTEERAELSEGKCSELE--EELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEF 241
Cdd:PTZ00121 1389 EKKKA--------DEAKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAE 1460
                         250       260       270
                  ....*....|....*....|....*....|..
gi 410060781  242 AERSVAKLEKTIDDL----EDELYAQKLKYKA 269
Cdd:PTZ00121 1461 EAKKKAEEAKKADEAkkkaEEAKKADEAKKKA 1492
PTZ00121 PTZ00121
MAEBL; Provisional
14-238 1.02e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   14 DKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRIQ 93
Cdd:PTZ00121 1575 DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK 1654
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   94 LVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIE 173
Cdd:PTZ00121 1655 AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE 1734
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 410060781  174 GDLERTEERAELSEGKCSElEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETR 238
Cdd:PTZ00121 1735 AKKEAEEDKKKAEEAKKDE-EEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
mukB PRK04863
chromosome partition protein MukB;
57-260 1.13e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.41  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   57 LDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIEN---- 132
Cdd:PRK04863  350 IERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERakql 429
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  133 -----------RAMKDEEKMELQEI--QLKEAKH---IAEEADRKYEEVARKLVIIEGDLERtEERAELSEGKCSELEEE 196
Cdd:PRK04863  430 cglpdltadnaEDWLEEFQAKEQEAteELLSLEQklsVAQAAHSQFEQAYQLVRKIAGEVSR-SEAWDVARELLRRLREQ 508
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 410060781  197 lKTVTNNLKSLEAQ---AEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSVAKLEKTIDDLEDEL 260
Cdd:PRK04863  509 -RHLAEQLQQLRMRlseLEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESV 574
GumC COG3206
Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane ...
18-243 1.43e-04

Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 225747 [Multi-domain]  Cd Length: 458  Bit Score: 42.82  E-value: 1.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  18 ALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYsealkDAQEKLELAEKIATDAEGEVASLNRRIQLVEE 97
Cdd:COG3206  179 QAYLADQLEAQLEAFRRASDSLDERLEELRARLQEAEAQVEDF-----RAQHGLTDAARGQLLSEQQLSALNTQLQSARA 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  98 ELDRAQERLATALTKLEEAEKAADESErgmkVIENRAMkdeEKMELQEIQLKeakhiAEEADRKYEEVARKLVIIEGDLE 177
Cdd:COG3206  254 RLAQAEARLASLLQLLPLGREAAALRE----VLESPTI---QDLRQQYAQVR-----QQIADLSTELGAKHPQLVALEAQ 321
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 410060781 178 RTEERAELSEgkcsELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTD---KLKEAETRAEFAE 243
Cdd:COG3206  322 LAELRQQIAA----ELRQILASLPNELALLEQQEAALEKELAQLKGRLSKLPKlqvQLRELEREAEAAR 386
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
4-284 1.79e-04

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 42.83  E-value: 1.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   4 IKKKMQMLKLDKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKG----TEDELDKYSEALKDAQEKLELAEKIAT 79
Cdd:COG0419  166 LEKYEKLSELLKEVIKEAKAKIEELEGQLSELLEDIEDLLEALEEELKElkklEEIQEEQEEEELEQEIEALEERLAELE 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  80 DAEGEVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEAD 159
Cdd:COG0419  246 EEKERLEELKARLLEIESLELEALKIREEELRELERLLEELEEKIERLEELEREIEELEEELEGLRALLEELEELLEKLK 325
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 160 RKYEEVARKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRA 239
Cdd:COG0419  326 SLEERLEKLEEKLEKLESELEELAEEKNELAKLLEERLKELEERLEELEKELEKALERLKQLEEAIQELKEELAELSAAL 405
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 410060781 240 EFAERSVAKLEKTIDDLEDELYAQKLKYKAISEELDHALNDMTSI 284
Cdd:COG0419  406 EEIQEELEELEKELEELERELEELEEEIKKLEEQINQLESKELMI 450
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
85-264 1.88e-04

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 42.78  E-value: 1.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   85 VASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKeakhiaeeadRKYEE 164
Cdd:COG1196   167 VSKYKERKEEAERKLERTEENLERLEDLLEELEKQLEKLERQAEKAERYQELKAELRELELALLL----------AKLKE 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  165 VARKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAER 244
Cdd:COG1196   237 LRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELEN 316
                         170       180
                  ....*....|....*....|
gi 410060781  245 SVAKLEKTIDDLEDELYAQK 264
Cdd:COG1196   317 ELEELEERLEELKEKIEALK 336
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
23-233 2.50e-04

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 42.35  E-value: 2.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   23 EQAESDKKAAE-DRSKQLEDDLVALQKKlKGTEDELDKYSEALKD--------AQEKLELAEKIATDAEG-EVASLNRRI 92
Cdd:PRK10929   33 EQAKAAKTPAQaEIVEALQSALNWLEER-KGSLERAKQYQQVIDNfpklsaelRQQLNNERDEPRSVPPNmSTDALEQEI 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   93 -----QLVEE------ELDRAQErLATALTKL----EEAEKAADESERGMKVIENRAMKDEEkmelqeiqlkeakhiAEE 157
Cdd:PRK10929  112 lqvssQLLEKsrqaqqEQDRARE-ISDSLSQLpqqqTEARRQLNEIERRLQTLGTPNTPLAQ---------------AQL 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  158 ADRKYEEVARKLVIIEGDLE------RTE---ERAELSEGKCSELEEELKTVTNNLKSLEAQ-AEKYSQKEDKYEEEI-- 225
Cdd:PRK10929  176 TALQAESAALKALVDELELAqlsannRQElarLRSELAKKRSQQLDAYLQALRNQLNSQRQReAERALESTELLAEQSgd 255
                         250
                  ....*....|
gi 410060781  226 --KALTDKLK 233
Cdd:PRK10929  256 lpKSIVAQFK 265
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
13-278 2.59e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.33  E-value: 2.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  13 LDKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRI 92
Cdd:PRK02224 307 ADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEI 386
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  93 QLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVII 172
Cdd:PRK02224 387 EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPH 466
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 173 EGDLERTEERAELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKyEEEIKALTDKLKEAETRAEFAERSVAKLEKT 252
Cdd:PRK02224 467 VETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERL-EERREDLEELIAERRETIEEKRERAEELRER 545
                        250       260
                 ....*....|....*....|....*.
gi 410060781 253 IDDLEDELYAQKLKYKAISEELDHAL 278
Cdd:PRK02224 546 AAELEAEAEEKREAAAEAEEEAEEAR 571
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
16-220 2.85e-04

MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.


Pssm-ID: 380155 [Multi-domain]  Cd Length: 1848  Bit Score: 42.13  E-value: 2.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   16 ENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTE------------DELDKYSEA----LKDAQEKLELAEKIAT 79
Cdd:NF012221 1558 QNALADKERAEADRQRLEQEKQQQLAAISGSQSQLESTDqnaletngqaqrDAILEESRAvtkeLTTLAQGLDALDSQAT 1637
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   80 DAE--GEvaslNRRIQLVEEELDRAQERL-ATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAK---- 152
Cdd:NF012221 1638 YAGesGD----QWRNPFAGGLLDRVQEQLdDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGVAQGEQNQANAEqdid 1713
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 410060781  153 HIAEEADRKYEEVARKlviiEGDLERTEERAELSEGKC-SELEEELKTVTNnlKSLEAQAEKYSQKEDK 220
Cdd:NF012221 1714 DAKADAEKRKDDALAK----QNEAQQAESDANAAANDAqSRGEQDASAAEN--KANQAQADAKGAKQDE 1776
PTZ00121 PTZ00121
MAEBL; Provisional
2-259 3.15e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 3.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781    2 DAIKKKMQMLKLDKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDA 81
Cdd:PTZ00121 1543 EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   82 EGEvaslnRRIQLVEEELDRAQERLATALTKLEEAEKAadESERGMKVIENRAMKDEEKMELQEI-QLKEAKHIAEEADR 160
Cdd:PTZ00121 1623 EEL-----KKAEEEKKKVEQLKKKEAEEKKKAEELKKA--EEENKIKAAEEAKKAEEDKKKAEEAkKAEEDEKKAAEALK 1695
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  161 KYEEVARKLVIIEGDLERTEERAElsegKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAE 240
Cdd:PTZ00121 1696 KEAEEAKKAEELKKKEAEEKKKAE----ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAE 1771
                         250
                  ....*....|....*....
gi 410060781  241 FAERSVAKLEKTIDDLEDE 259
Cdd:PTZ00121 1772 EIRKEKEAVIEEELDEEDE 1790
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
16-260 7.83e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 7.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  16 ENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAE--KIATDAEGE-----VASL 88
Cdd:PRK02224 394 EELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpECGQPVEGSphvetIEED 473
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  89 NRRIQLVEEELDRAQERLATALTKLEEAEKAAdESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARK 168
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAE 552
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 169 LVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDkYEEEIKALTDKLKEAETRAEFAERSVAK 248
Cdd:PRK02224 553 AEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIAD-AEDEIERLREKREALAELNDERRERLAE 631
                        250
                 ....*....|..
gi 410060781 249 LEKTIDDLEDEL 260
Cdd:PRK02224 632 KRERKRELEAEF 643
PTZ00121 PTZ00121
MAEBL; Provisional
20-258 7.87e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 7.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   20 DRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTE---DELDKYSEALKDAQEK-----LELAEKIATDAEGEVASLNRR 91
Cdd:PTZ00121 1480 EEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEakkAEEAKKADEAKKAEEAkkadeAKKAEEKKKADELKKAEELKK 1559
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   92 IQLVE--EELDRAQERLATALTKLEEAEKAadesERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKL 169
Cdd:PTZ00121 1560 AEEKKkaEEAKKAEEDKNMALRKAEEAKKA----EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV 1635
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  170 VIIEGDLERTEERAElsegKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSVAKL 249
Cdd:PTZ00121 1636 EQLKKKEAEEKKKAE----ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711

                  ....*....
gi 410060781  250 EKTIDDLED 258
Cdd:PTZ00121 1712 AEEKKKAEE 1720
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
2-201 1.23e-03

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 40.08  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781    2 DAIKKKMQMLKLDKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDA----QEKLELAEKI 77
Cdd:COG1196   312 EELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELfealREELAELEAE 391
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   78 ATDAEGEVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEE 157
Cdd:COG1196   392 LAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAE 471
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 410060781  158 ADRKYEEVARKLVIIEGDLERTEERAELSEGKCSELEEELKTVT 201
Cdd:COG1196   472 LQEELQRLEKELSSLEARLDRLEAEQRASQGVRAVLEALESGLP 515
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1-211 1.41e-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: 1.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781     1 MDAIKKKMQMLKLDKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATD 80
Cdd:TIGR02169  289 QLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELED 368
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781    81 AEGEVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADR 160
Cdd:TIGR02169  369 LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL 448
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 410060781   161 KYEEVARKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKSLEAQA 211
Cdd:TIGR02169  449 EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQA 499
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
15-260 1.96e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 1.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  15 KENALDRAEQAESDKKAAEDRSKQLED---DLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVA----- 86
Cdd:PRK02224 229 REQARETRDEADEVLEEHEERREELETleaEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlddad 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  87 --SLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEE 164
Cdd:PRK02224 309 aeAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEE 388
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 165 VARKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKA--------------LTD 230
Cdd:PRK02224 389 LEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegspHVE 468
                        250       260       270
                 ....*....|....*....|....*....|
gi 410060781 231 KLKEAETRAEFAERSVAKLEKTIDDLEDEL 260
Cdd:PRK02224 469 TIEEDRERVEELEAELEDLEEEVEEVEERL 498
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
20-261 2.09e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 2.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  20 DRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRIQLVEEEL 99
Cdd:PRK02224 509 DRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERI 588
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 100 DRAqERLATALTKLEEAEKAADE------------SERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVAR 167
Cdd:PRK02224 589 ESL-ERIRTLLAAIADAEDEIERlrekrealaelnDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEE 667
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 168 KLVIIEGDLERTEERAELSEGKCSELE---EELKTVTNNLKSLEAQAEKYSQKEDKYeeeikaltdklkeAETRAEFAER 244
Cdd:PRK02224 668 KLDELREERDDLQAEIGAVENELEELEelrERREALENRVEALEALYDEAEELESMY-------------GDLRAELRQR 734
                        250
                 ....*....|....*..
gi 410060781 245 SVAKLEKTIDDLEDELY 261
Cdd:PRK02224 735 NVETLERMLNETFDLVY 751
PRK11281 PRK11281
mechanosensitive channel MscK;
11-278 2.89e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 39.12  E-value: 2.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   11 LKLDKENALDRAEQAESDKKAAEDRSKQLEDdlvaLQKKLKGTEDELDKYSEALKDAQ----EKLELAEkiatdAEGEVA 86
Cdd:PRK11281   61 VQQDLEQTLALLDKIDRQKEETEQLKQQLAQ----APAKLRQAQAELEALKDDNDEETretlSTLSLRQ-----LESRLA 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   87 SLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENR---------AMKDEEKMELQ-EIQLKEAKHiae 156
Cdd:PRK11281  132 QTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLlkggkvggkALRPSQRVLLQaEQALLNAQN--- 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  157 EADRKYEEVARKLViiegDLErTEERAELSEgKCSELEEELKTVTN--NLKSLEaQAEKYSQKEDKYEEEIKALTDKL-- 232
Cdd:PRK11281  209 DLQRKSLEGNTQLQ----DLL-QKQRDYLTA-RIQRLEHQLQLLQEaiNSKRLT-LSEKTVQEAQSQDEAARIQANPLva 281
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 410060781  233 KEAETRAEFAERSVAKLEKTiddleDELYAQKLKYKAIseeLDHAL 278
Cdd:PRK11281  282 QELEINLQLSQRLLKATEKL-----NTLTQQNLRVKNW---LDRLT 319
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
58-235 3.36e-03

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 38.45  E-value: 3.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   58 DKYSEALKDAQEK-LELAEKIATDAEGEVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMK 136
Cdd:pfam05262 180 KKVVEALREDNEKgVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKN 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  137 DEEKMELQEIqlKEAKHIAEEADRKYEEVARKLViiegdlERTEERAELSEGKCSELEEElktvtnnLKSLEAQAEKYSQ 216
Cdd:pfam05262 260 LPKPADTSSP--KEDKQVAENQKREIEKAQIEIK------KNDEEALKAKDHKAFDLKQE-------SKASEKEAEDKEL 324
                         170
                  ....*....|....*....
gi 410060781  217 KEDKYEEEIKALTDKLKEA 235
Cdd:pfam05262 325 EAQKKREPVAEDLQKTKPQ 343
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2-275 3.95e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.51  E-value: 3.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   2 DAIKKKMQMLKLDKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKK---LKGTEDELDKYSEALKDAQEKLELAEKIA 78
Cdd:PRK03918 366 EAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARigeLKKEIKELKKAIEELKKAKGKCPVCGREL 445
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  79 TDAEGE--VASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAkhiaE 156
Cdd:PRK03918 446 TEEHRKelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEEL----E 521
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 157 EADRKYEEVARKLVIIEGDLERTE---ERAELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQK-EDKYEEEIKALTD-- 230
Cdd:PRK03918 522 KKAEEYEKLKEKLIKLKGEIKSLKkelEKLEELKKKLAELEKKLDELEEELAELLKELEELGFEsVEELEERLKELEPfy 601
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 410060781 231 ----KLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISEELD 275
Cdd:PRK03918 602 neylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE 650
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
23-240 4.41e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 38.44  E-value: 4.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781    23 EQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAqEKLELAEKIATDAEGEVASLNRRIQL-VEEELDR 101
Cdd:TIGR00927  679 NESEGEIPAERKGEQEGEGEIEAKEADHKGETEAEEVEHEGETEA-EGTEDEGEIETGEEGEEVEDEGEGEAeGKHEVET 757
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   102 AQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEkmelQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEE 181
Cdd:TIGR00927  758 EGDRKETEHEGETEAEGKEDEDEGEIQAGEDGEMKGDE----GAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETG 833
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 410060781   182 RAELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAE 240
Cdd:TIGR00927  834 EQELNAENQGEAKQDEKGVDGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEE 892
PLN03223 PLN03223
Polycystin cation channel protein; Provisional
3-152 4.81e-03

Polycystin cation channel protein; Provisional


Pssm-ID: 215637 [Multi-domain]  Cd Length: 1634  Bit Score: 38.39  E-value: 4.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781    3 AIKKKMQMLKLDKENALDRAEQAESDKkAAEDRSKQLEDDLVALQKKLKGTEDE-LDKYSEALKDAQEKLELAEKIATDA 81
Cdd:PLN03223  796 SLDTQIETLKTQQDRANQEAEAHHADN-SLETLINAGFTDIKAGQAALEAKLDEiLGKQQQALAAAQESLAIQQRTNGLA 874
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 410060781   82 EGEVAslnrriqlveeeldrAQERLATALTKLEEAEKAADESERGMKV-----IENRAMKDeekmelQEIQLKEAK 152
Cdd:PLN03223  875 ERQAA---------------AIEKLAKAVEKQLSSIKSAYTYGAFISLtqylaIQERARRT------RELTAKANF 929
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
85-275 7.51e-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: 37.74  E-value: 7.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781    85 VASLNRRIQLVEEELDRAQERLATALTKLEEAEkaaDESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEE 164
Cdd:TIGR02169  165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKR---QQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEA 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   165 VARKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKSL-EAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAE 243
Cdd:TIGR02169  242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 410060781   244 RSVAKLE-------KTIDDLEDELYAQKLKYKAISEELD 275
Cdd:TIGR02169  322 ERLAKLEaeidkllAEIEELEREIEEERKRRDKLTEEYA 360
EmrA COG1566
Multidrug resistance efflux pump [Defense mechanisms];
38-183 8.28e-03

Multidrug resistance efflux pump [Defense mechanisms];


Pssm-ID: 224482 [Multi-domain]  Cd Length: 352  Bit Score: 37.31  E-value: 8.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781  38 QLEDDLVALQKKLKGTEDELDKYSEALkdAQEKLELAEKIATDAEgEVASLNRRIQLVEEELDRAQerlaTALTKLEEAE 117
Cdd:COG1566   95 QAEAALAAAEAQLRNLRAQLASAQALI--AQAEAQDLDQAQNELE-RRAELAQRGVVSREELDRAR----AALQAAEAAL 167
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 410060781 118 KAADESERgmkviENRAMKDEEKMELQEiQLKEAKHIAEEAdrkyeevarklviiEGDLERTEERA 183
Cdd:COG1566  168 AAAQAAQK-----QNLALLESEVSGAQA-QVASAEAALDQA--------------KLDLERTVIRA 213
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
33-284 8.70e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 37.72  E-value: 8.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781    33 EDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRIQLVEEELDRAQERLATALTK 112
Cdd:TIGR00606  701 QSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPE 780
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   113 LEEAEKAADE----SERGMKVIENRAMKDEEKMELQEIQL----KEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAE 184
Cdd:TIGR00606  781 EESAKVCLTDvtimERFQMELKDVERKIAQQAAKLQGSDLdrtvQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQ 860
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781   185 LSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQK 264
Cdd:TIGR00606  861 HLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQ 940
                          250       260
                   ....*....|....*....|
gi 410060781   265 LKYKAISEELDHALNDMTSI 284
Cdd:TIGR00606  941 DKVNDIKEKVKNIHGYMKDI 960
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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