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Conserved domains on  [gi|922581965|ref|NP_001300460|]
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Tropomyosin [Caenorhabditis elegans]

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 2.47e-54

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 organization 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: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 175.99  E-value: 2.47e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965   48 KKMTQTGDDLDKAQEDLSAATSKLEEKEKTVQEAEAEVASLNRRMTLLEEELERAEERLKIATEKLEEATHNVDESERSR 127
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965  128 RALSNQIDMDDDRCSDLERKLRECQSILHETENKAEEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSL 207
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 922581965  208 EVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKERYKTISEELDSTFQELS 282
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
CCDC158 super family cl37899
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 1-92 7.11e-03

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


The actual alignment was detected with superfamily member pfam15921:

Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 37.79  E-value: 7.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965     1 MDAIKKKMQAMKIEKDNALDRADAAEEKVRQITEKLERVEEELRDTQKKMTQTGDDLDKAQEDLSAATSKLEEKEKTVQE 80
Cdd:pfam15921  435 LKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEA 514

                           90
                   ....*....|..
gi 922581965    81 AEAEVASLNRRM 92
Cdd:pfam15921  515 TNAEITKLRSRV 526
 
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 2.47e-54

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 organization 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: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 175.99  E-value: 2.47e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965   48 KKMTQTGDDLDKAQEDLSAATSKLEEKEKTVQEAEAEVASLNRRMTLLEEELERAEERLKIATEKLEEATHNVDESERSR 127
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965  128 RALSNQIDMDDDRCSDLERKLRECQSILHETENKAEEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSL 207
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 922581965  208 EVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKERYKTISEELDSTFQELS 282
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 25-281 1.90e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 73.43  E-value: 1.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965  25 AEEKVRQITE---KLERVEEELRDTQKKMTQTGDDLDKAQEDLSAATSKLEEKEKTVQEAEAEVASLNRRMTLLEEELER 101
Cdd:COG1196  220 EELKELEAELlllKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965 102 AEERLKIATEKLEEATHNVDESERSRRALSNQIDMDDDRCSDLERKLRECQSILHETENKAEEVARKLAMVEADLERAEE 181
Cdd:COG1196  300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965 182 RAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELV 261
Cdd:COG1196  380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459

                        250       260
                 ....*....|....*....|
gi 922581965 262 HEKERYKTISEELDSTFQEL 281
Cdd:COG1196  460 ALLELLAELLEEAALLEAAL 479
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 28-281 5.74e-14

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: 72.01  E-value: 5.74e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965    28 KVRQITEKLERVEEELRDTQKKMTQTGDDLDKAQEDLSAATSKLEEKE-------KTVQEAEAEVASLNRRMTLLEEELE 100
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSrqisalrKDLARLEAEVEQLEERIAQLSKELT 757

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965   101 RAEERLKIATEKLEEATHNVDESERSRRALSNQIDMDDDRCSDLERKLRECQSILHETENKAEEVARKLAMVEADLERAE 180
Cdd:TIGR02168  758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965   181 ERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDEL 260
Cdd:TIGR02168  838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917

                          250       260
                   ....*....|....*....|.
gi 922581965   261 VHEKERYKTISEELDSTFQEL 281
Cdd:TIGR02168  918 EELREKLAQLELRLEGLEVRI 938
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
22-276 1.46e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 1.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965  22 ADAAEEKVRQITEKLERVEEELRDTQKKMTQTGDDLDKAQEDLSAATSKLEEKEKTVQEAEAEVASLNRRMTLLEEELER 101
Cdd:PRK02224 344 AESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDE 423

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965 102 AEERLKIATEKLEEATHNVDESERSRRAlsnqidmddDRCSDLERKLRECQ--SILHETENKAEEVARKLAMVEADLERA 179
Cdd:PRK02224 424 LREREAELEATLRTARERVEEAEALLEA---------GKCPECGQPVEGSPhvETIEEDRERVEELEAELEDLEEEVEEV 494

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965 180 EERAEAGEnKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDE 259
Cdd:PRK02224 495 EERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREE 573

                        250
                 ....*....|....*..
gi 922581965 260 LVHEKERYKTISEELDS 276
Cdd:PRK02224 574 VAELNSKLAELKERIES 590
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 1-92 7.11e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 37.79  E-value: 7.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965     1 MDAIKKKMQAMKIEKDNALDRADAAEEKVRQITEKLERVEEELRDTQKKMTQTGDDLDKAQEDLSAATSKLEEKEKTVQE 80
Cdd:pfam15921  435 LKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEA 514

                           90
                   ....*....|..
gi 922581965    81 AEAEVASLNRRM 92
Cdd:pfam15921  515 TNAEITKLRSRV 526
 
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 2.47e-54

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 organization 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: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 175.99  E-value: 2.47e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965   48 KKMTQTGDDLDKAQEDLSAATSKLEEKEKTVQEAEAEVASLNRRMTLLEEELERAEERLKIATEKLEEATHNVDESERSR 127
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965  128 RALSNQIDMDDDRCSDLERKLRECQSILHETENKAEEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSL 207
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 922581965  208 EVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKERYKTISEELDSTFQELS 282
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 25-281 1.90e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 73.43  E-value: 1.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965  25 AEEKVRQITE---KLERVEEELRDTQKKMTQTGDDLDKAQEDLSAATSKLEEKEKTVQEAEAEVASLNRRMTLLEEELER 101
Cdd:COG1196  220 EELKELEAELlllKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965 102 AEERLKIATEKLEEATHNVDESERSRRALSNQIDMDDDRCSDLERKLRECQSILHETENKAEEVARKLAMVEADLERAEE 181
Cdd:COG1196  300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965 182 RAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELV 261
Cdd:COG1196  380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459

                        250       260
                 ....*....|....*....|
gi 922581965 262 HEKERYKTISEELDSTFQEL 281
Cdd:COG1196  460 ALLELLAELLEEAALLEAAL 479
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 28-281 5.74e-14

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: 72.01  E-value: 5.74e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965    28 KVRQITEKLERVEEELRDTQKKMTQTGDDLDKAQEDLSAATSKLEEKE-------KTVQEAEAEVASLNRRMTLLEEELE 100
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSrqisalrKDLARLEAEVEQLEERIAQLSKELT 757

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965   101 RAEERLKIATEKLEEATHNVDESERSRRALSNQIDMDDDRCSDLERKLRECQSILHETENKAEEVARKLAMVEADLERAE 180
Cdd:TIGR02168  758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965   181 ERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDEL 260
Cdd:TIGR02168  838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917

                          250       260
                   ....*....|....*....|.
gi 922581965   261 VHEKERYKTISEELDSTFQEL 281
Cdd:TIGR02168  918 EELREKLAQLELRLEGLEVRI 938
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 7-283 4.31e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.20  E-value: 4.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965   7 KMQAMKIEKDNALDRADAAEEKVRQITEKLERVEEELRDTQKKMTQTGDDLDKAQEDLSAATSKLEEKEKTVQEAEAEVA 86
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965  87 SLNRRMTLLEEELERAEERLKIATEKLEEATHNVDESERSRRALSNQIDMDDDRCSDLERKLRECQSILHETENKAEEVA 166
Cdd:COG1196  313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965 167 RKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSV 246
Cdd:COG1196  393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 922581965 247 QKLQKEVDRLEDELVHEKERYKTISEELDSTFQELSG 283
Cdd:COG1196  473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
 7-152 4.00e-12

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: 62.32  E-value: 4.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965    7 KMQAMKIEKDNALDRADAAEEKVRQITEKLERVEEELRDTQKKMTQTGDDLDKAQEDLSAATSKLEEKEKTVQEAEaeva 86
Cdd:pfam12718   1 KMNSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNE---- 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 922581965   87 SLNRRMTLLEEELERAEERLKIATEKLEEATHNVDESERSRRALSNQIDMDDDRCSDLERKLRECQ 152
Cdd:pfam12718  77 NLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKEAK 142
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-257 9.87e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.96  E-value: 9.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965   2 DAIKKKMQAMKIEKDNALDRADAAEEKVRQITEKLERVEEELRDTQKKMTQTGDDLDKAQEDLSAATSKLEEKEKTVQEA 81
Cdd:COG1196  242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965  82 EAEVASLNRRMTLLEEELERAEERLKIATEKLEEATHNVDESERSRRALSNQIDmdddrcsDLERKLRECQSILHETENK 161
Cdd:COG1196  322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA-------EAEEELEELAEELLEALRA 394

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965 162 AEEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEF 241
Cdd:COG1196  395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474

                        250
                 ....*....|....*.
gi 922581965 242 AERSVQKLQKEVDRLE 257
Cdd:COG1196  475 LEAALAELLEELAEAA 490
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1-266 2.81e-11

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 63.92  E-value: 2.81e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965     1 MDAIKKKMQAMKIEKDNALDRADAAEEKVRQITEKLERVEEELRDTQKKMTQTGDDLDKAQEDLSAATSKLEEKEKTVQE 80
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965    81 AEAEVASLNRRMTLLEEELERAEERLKIATEKLEEATHNVDESERSRRALSNQIDMDDDRCSDLERKLRECQSILHETEN 160
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965   161 KAEEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAE 240
Cdd:TIGR02168  839 RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918

                          250       260
                   ....*....|....*....|....*.
gi 922581965   241 FAERSVQKLQKEVDRLEDELVHEKER 266
Cdd:TIGR02168  919 ELREKLAQLELRLEGLEVRIDNLQER 944
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 7-281 2.09e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.14  E-value: 2.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965     7 KMQAMKIEKDNALDRADAAEEKVRQITEKLERVEEELRDTQKKMTQ---TGDDLDKAQEDLSA-----ATSKLEEKEKTV 78
Cdd:TIGR02168  169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERykeLKAELRELELALLVlrleeLREELEELQEEL 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965    79 QEAEAEVASLNRRMTLLEEELERAEERLKIATEKLEEATHNVDESERSRRALSNQIDMDDDRCSDLERKLRECQSILHET 158
Cdd:TIGR02168  249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965   159 ENKAEEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETR 238
Cdd:TIGR02168  329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 922581965   239 AEFAERSVQKLQKEVDRLEDELvhEKERYKTISEELDSTFQEL 281
Cdd:TIGR02168  409 LERLEDRRERLQQEIEELLKKL--EEAELKELQAELEELEEEL 449
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-252 1.19e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 1.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965   2 DAIKKKMQAMKIEKDNALDRADAAEEKVRQITEKLERVEEELRDTQKKMTQTGDDLDKAQEDLSAATSKLEEKEKTVQEA 81
Cdd:COG1196  263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965  82 EAEVASLNRRMTLLEEELERAEERLKIATEKLEEATHNVDESERSRRALSNQIDMDDDRCSDLERKLREC---QSILHET 158
Cdd:COG1196  343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALlerLERLEEE 422

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965 159 ENKAEEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETR 238
Cdd:COG1196  423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502

                        250
                 ....*....|....
gi 922581965 239 AEFAERSVQKLQKE 252
Cdd:COG1196  503 YEGFLEGVKAALLL 516
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 69-276 1.48e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.45  E-value: 1.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965    69 SKLEEKEKTVQEAEAEVASLNRRMTLLEEELERAEERLKIATEKLEEATHNVDE-------SERSRRALSNQIDMDDDRC 141
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAlrkdlarLEAEVEQLEERIAQLSKEL 756

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965   142 SDLERKLRECQSILHETENKAEEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSY 221
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 922581965   222 EEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKERYKTISEELDS 276
Cdd:TIGR02168  837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 22-271 3.67e-08

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 53.61  E-value: 3.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965  22 ADAAEEKVRQITEKLERVEEELRDTQKKMTQTGDDLDKAQEDLSAATSKLEEKEKTVQEAEAEVASLNRRMTLLEEELER 101
Cdd:COG4942   15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965 102 AEERLKIATEKLEEAthnVDESERSRRALSNQIDMDDDRCSDLERKLRECQSILHETENKAEEVARKLAMVEADLERAEE 181
Cdd:COG4942   95 LRAELEAQKEELAEL---LRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965 182 RAEAGENKIVELEEELRvvgnNLKSLEVSEEKALQRedsyeeqirtVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELV 261
Cdd:COG4942  172 ERAELEALLAELEEERA----ALEALKAERQKLLAR----------LEKELAELAAELAELQQEAEELEALIARLEAEAA 237

                        250
                 ....*....|
gi 922581965 262 HEKERYKTIS 271
Cdd:COG4942  238 AAAERTPAAG 247
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-240 4.90e-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: 4.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965     2 DAIKKKMQAMKIEKDNALDRADAAEEKVRQITEKLERVEEELRDTQKKMTQTGDDLDKAQEDLSAATSKLEEKEKTVQEA 81
Cdd:TIGR02168  270 EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL 349

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965    82 EAEVASLNRRMTLLEEELERAEERLKIATEKLEEATHNVDESERSRRALSNQIDMDDDRCSDLERKLRECQSILHETENK 161
Cdd:TIGR02168  350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 922581965   162 AEevarklamvEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAE 240
Cdd:TIGR02168  430 LE---------EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 7-273 6.77e-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: 53.53  E-value: 6.77e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965     7 KMQAMKIEKDNALDRADAAEEKVRQITEKLERVEEELRDTQKKMTQTGDDLDKAQEDLSAATSKLEEKEKTVQEAEAEVA 86
Cdd:TIGR02169  682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965    87 SLNRRMtlLEEELERAEERLKIATEKLEEATHNVDESERSRRALSNQIDMDDDRCSDLERKLRECQSILHETENKAEEVA 166
Cdd:TIGR02169  762 ELEARI--EELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQ 839

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965   167 RKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSV 246
Cdd:TIGR02169  840 EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRL 919

                          250       260
                   ....*....|....*....|....*..
gi 922581965   247 QKLQKEVDRLEDELVHEKERYKTISEE 273
Cdd:TIGR02169  920 SELKAKLEALEEELSEIEDPKGEDEEI 946
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 26-275 6.14e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.45  E-value: 6.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965    26 EEKVRQITEKLERVEEELRDTQKKMTQTGDDLDKAQEDLSAATSKLEEKEKTVQEAEAEVASLNRRMTLLEEELERAEEr 105
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ- 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965   106 lKIATEKLEEATHNVDESERSRRALSNQIDMDDDRCSDLERKLRECQSILHETENKAEEVARKLAMVEADLERAEERAEA 185
Cdd:TIGR02169  752 -EIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEY 830

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965   186 GENKIVELEEELRVVGNNLKSLEvseekalQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKE 265
Cdd:TIGR02169  831 LEKEIQELQEQRIDLKEQIKSIE-------KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELER 903

                          250
                   ....*....|
gi 922581965   266 RYKTISEELD 275
Cdd:TIGR02169  904 KIEELEAQIE 913
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1-279 6.85e-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: 50.44  E-value: 6.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965     1 MDAIKKKMQAMKIEKDNALDRADAAEEKVRQITEKLERVEEELRDTQKKMTQTGDDLDKAQEDLSAATSKLEEKEKTVQE 80
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965    81 AEAEVASLNRRMTLLEEELERAEERLKIATEKLEEATHNVDESERSRRALSNQIDMDDDRCSDLERKLRECQSILHETEN 160
Cdd:TIGR02168  321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965   161 KAEEVARKLAMVEADLERAEERAEAGENKIVELeeELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAE 240
Cdd:TIGR02168  401 EIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 922581965   241 FAERSVQKLQKEVDRLEDELVHEKERYKTISEELDSTFQ 279
Cdd:TIGR02168  479 AAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
9-247 8.69e-07

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 50.02  E-value: 8.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965   9 QAMKIEKDNALDRADAAEEKVRQITEKLERVEEELRD--TQKKMTQTGDDLDKAQEDLSAATSKLEEKEKTVQEAEAEVA 86
Cdd:COG3206  164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965  87 SLNRRMTLLEEELERAEERLKIATEKLEEATHNVDESERSRRALSNQIDMDddrcsDLERKLRECQSILhetenkAEEVA 166
Cdd:COG3206  244 ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVI-----ALRAQIAALRAQL------QQEAQ 312

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965 167 RKLAMVEADLERAEERAEAGENKIVELEEELRvvgnNLKSLEVsEEKALQRE-DSYEEQIRTVSSRLKEAETRAEFAERS 245
Cdd:COG3206  313 RILASLEAELEALQAREASLQAQLAQLEARLA----ELPELEA-ELRRLEREvEVARELYESLLQRLEEARLAEALTVGN 387


                 ..
gi 922581965 246 VQ 247
Cdd:COG3206  388 VR 389
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 24-282 1.19e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 49.68  E-value: 1.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965    24 AAEEKVRQITEKLERVEEELRDTQKKMTQTGDDLDKAQEDLSAATSKLEEK--------EKTVQEAEAEVASLNRRMTLL 95
Cdd:TIGR02169  234 ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAEIASLERSIAEK 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965    96 EEELERAEERLKIATEKLEEATHNVDESERSRRALSNQIDMDDDRCSDLERKLRECQSilhetenKAEEVARKLAMVEAD 175
Cdd:TIGR02169  314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRA-------ELEEVDKEFAETRDE 386

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965   176 LERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDR 255
Cdd:TIGR02169  387 LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSK 466

                          250       260
                   ....*....|....*....|....*..
gi 922581965   256 LEDELVHEKERYKTISEELDSTFQELS 282
Cdd:TIGR02169  467 YEQELYDLKEEYDRVEKELSKLQRELA 493
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 25-276 2.82e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 2.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965  25 AEEKVRQITEKLERVEEELRDTQKKMTQTGDDLDKAQEdlsAATSKLEEKEKTVQEAEAEVASLNRRMTLLEEELERAEE 104
Cdd:COG1196  177 AERKLEATEENLERLEDILGELERQLEPLERQAEKAER---YRELKEELKELEAELLLLKLRELEAELEELEAELEELEA 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965 105 RLKIATEKLEEATHNVDESERSRRALSNQIDMDDDRCSDLERKLRECQSILHETENKAEEVARKLAMVEADLERAEERAE 184
Cdd:COG1196  254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965 185 AGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEK 264
Cdd:COG1196  334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413

                        250
                 ....*....|..
gi 922581965 265 ERYKTISEELDS 276
Cdd:COG1196  414 ERLERLEEELEE 425
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 4-260 4.26e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.14  E-value: 4.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965     4 IKKKMQAMKIEKDNALDRADAAEEKVRQITEKLERVEEELRDTQKKMTQTGDDLDKAQEDLSAATSKLEEKEKTVQEAEA 83
Cdd:TIGR02169  700 IENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEE 779

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965    84 EVASLNRRMTLL-------------------EEELERAEERLKIATEKLEEATHNVDESERSRRALSNQIDMDDDRCSDL 144
Cdd:TIGR02169  780 ALNDLEARLSHSripeiqaelskleeevsriEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENL 859

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965   145 ERKLRECQSILHETENKAEEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQ 224
Cdd:TIGR02169  860 NGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDP 939

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 922581965   225 IRTVSSRLKEaetraefaERSVQKLQKEVDRLEDEL 260
Cdd:TIGR02169  940 KGEDEEIPEE--------ELSLEDVQAELQRVEEEI 967
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 14-274 8.93e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.98  E-value: 8.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965    14 EKDNALDRADAAEEKVRQITEKLERVEEELRDTQKKMTQTGDDLDKAQE--------DLSAATSKLEEKEKTVQEAEAEV 85
Cdd:TIGR02169  167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQAllkekreyEGYELLKEKEALERQKEAIERQL 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965    86 ASLNRRMTLLEEELERAEERLKIATEKLEEATHNV-DESERSRRALSNQIdmdddrcSDLERKLRECQSILHETENKAEE 164
Cdd:TIGR02169  247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkDLGEEEQLRVKEKI-------GELEAEIASLERSIAEKERELED 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965   165 VARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAER 244
Cdd:TIGR02169  320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKR 399

                          250       260       270
                   ....*....|....*....|....*....|
gi 922581965   245 SVQKLQKEVDRLEDELVHEKERYKTISEEL 274
Cdd:TIGR02169  400 EINELKRELDRLQEELQRLSEELADLNAAI 429
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1-193 1.20e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 1.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965     1 MDAIKKKMQAMKIEKDNALDRADAAEEKVRQITEKLERVEEELRDTQKKMTQTGDDLDKAQEDLSAATSKLEEKEKTVQE 80
Cdd:TIGR02168  791 IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965    81 AEAEVASLNRRMTLLEEELERAEERLKIATEKLEEATHNVDESERSRRALSNQIDMDDDRCSDLERKLRECQSILHETEN 160
Cdd:TIGR02168  871 LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYS 950

                          170       180       190
                   ....*....|....*....|....*....|....
gi 922581965   161 -KAEEVARKLAMVEADLERAEERAEAGENKIVEL 193
Cdd:TIGR02168  951 lTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 146-282 1.42e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965 146 RKLRECQSILHETENKAEEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQI 225
Cdd:COG1196  232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 922581965 226 RTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKERYKTISEELDSTFQELS 282
Cdd:COG1196  312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1-226 1.47e-05

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: 46.21  E-value: 1.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965     1 MDAIKKKMQAMKIEKDNALDRADAAEEKVRQITEKLERVEEELRDTQKKMtqtgDDLDKAQEDLSAATSKLEEKektVQE 80
Cdd:TIGR02169  289 QLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEI----EELEREIEEERKRRDKLTEE---YAE 361

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965    81 AEAEVASLNRRMTLLEEELERAEERLKIATEKLEEATHNVDESERSRRALSNQIDMDDDRCSDLERKLRECQSILHETEN 160
Cdd:TIGR02169  362 LKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEE 441

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 922581965   161 KAEEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIR 226
Cdd:TIGR02169  442 EKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVR 507
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 2-247 1.58e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.59  E-value: 1.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965   2 DAIKKKMQAMKIEKDNALDRADAAEEKVRQITEKLERVEEELRDTQKKMTQTGDDLDKAQEDLSAATSKLEEKEKTVQEA 81
Cdd:COG3883   19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965  82 EAEVASLNRRMTLLE-----EELERAEERLKIATEKLEEATHNVDESERSRRALSNQIDMDDDRCSDLERKLRECQSILH 156
Cdd:COG3883   99 GGSVSYLDVLLGSESfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965 157 ETENKAEEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAE 236
Cdd:COG3883  179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAA 258

                        250
                 ....*....|.
gi 922581965 237 TRAEFAERSVQ 247
Cdd:COG3883  259 AGSAGAAGAAA 269
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
40-284 3.02e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 3.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965   40 EEELRDTQKKMTQTG-----------DDLDKAQEDL---SAATSKLEEKEKTVQEAEAEVASLNRRMTLLEEELERAEER 105
Cdd:COG4913   567 PEELRRHPRAITRAGqvkgngtrhekDDRRRIRSRYvlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQER 646

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965  106 LKIAT--EKLEEATHNVDESERSRRALSNQIDM---DDDRCSDLERKLRECQSILHETENKAEEVARKLAMVEADLERAE 180
Cdd:COG4913   647 REALQrlAEYSWDEIDVASAEREIAELEAELERldaSSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE 726

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965  181 ERAEagenkivELEEELRvvgnnlkslEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERsVQKLQKEVDRLEDEL 260
Cdd:COG4913   727 EELD-------ELQDRLE---------AAEDLARLELRALLEERFAAALGDAVERELRENLEER-IDALRARLNRAEEEL 789

                         250       260
                  ....*....|....*....|....*...
gi 922581965  261 VHE----KERYKTISEELDSTFQELSGY 284
Cdd:COG4913   790 ERAmrafNREWPAETADLDADLESLPEY 817
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1-259 1.44e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965   1 MDAIKKKMQAMKIEKDNALDRADAAEEKVRQITEKLERVEEELRDTQKKMTQTGDDLDKAQEDLSAATSKLEEKEKTVQE 80
Cdd:COG4372   40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965  81 AEAEVASLNRRMTLLEEELERAEERLKIATEKLEEATHNVDESERSRRALSNQIdmdddRCSDLERKLRECQSILHETEN 160
Cdd:COG4372  120 LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL-----QALSEAEAEQALDELLKEANR 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965 161 KAEEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAE 240
Cdd:COG4372  195 NAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTE 274

                        250
                 ....*....|....*....
gi 922581965 241 FAERSVQKLQKEVDRLEDE 259
Cdd:COG4372  275 EEELEIAALELEALEEAAL 293
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
22-276 1.46e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 1.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965  22 ADAAEEKVRQITEKLERVEEELRDTQKKMTQTGDDLDKAQEDLSAATSKLEEKEKTVQEAEAEVASLNRRMTLLEEELER 101
Cdd:PRK02224 344 AESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDE 423

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965 102 AEERLKIATEKLEEATHNVDESERSRRAlsnqidmddDRCSDLERKLRECQ--SILHETENKAEEVARKLAMVEADLERA 179
Cdd:PRK02224 424 LREREAELEATLRTARERVEEAEALLEA---------GKCPECGQPVEGSPhvETIEEDRERVEELEAELEDLEEEVEEV 494

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965 180 EERAEAGEnKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDE 259
Cdd:PRK02224 495 EERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREE 573

                        250
                 ....*....|....*..
gi 922581965 260 LVHEKERYKTISEELDS 276
Cdd:PRK02224 574 VAELNSKLAELKERIES 590
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
14-231 2.13e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965   14 EKDNALDRADAAEEKVRQitekLERVEEELRDTQKKMTQTGDdLDKAQEDLSAATSKLEEKEK-----TVQEAEAEVASL 88
Cdd:COG4913   219 EEPDTFEAADALVEHFDD----LERAHEALEDAREQIELLEP-IRELAERYAAARERLAELEYlraalRLWFAQRRLELL 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965   89 NRRMTLLEEELERAEERLKIATEKLEEATHNVDESERSRRALsnqidmDDDRCSDLERKLRECQSILHETENKAEEVARK 168
Cdd:COG4913   294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGN------GGDRLEQLEREIERLERELEERERRRARLEAL 367

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 922581965  169 LAMVE----ADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSR 231
Cdd:COG4913   368 LAALGlplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 40-245 2.87e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 2.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965  40 EEELRDTQKKMTQTGDDLDKAQEDLSAATSKLEEKEKTVQEAEAEVASLNRRMTLLEEELERAEERLKIATEKLEEATHN 119
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965 120 VDESERSRRALSNQIDMDD-----DRCSDLERKLRECQSILHETENKAEEVARKLAMVEADLERAEERAEAGENKIVELE 194
Cdd:COG3883   95 LYRSGGSVSYLDVLLGSESfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 922581965 195 EELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERS 245
Cdd:COG3883  175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
PTZ00121 PTZ00121
MAEBL; Provisional
 2-268 3.28e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 3.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965    2 DAIKKKMQAMKIEKDNALDRADAAEEKVRQITEKLERVEEELRDTQKKmtQTGDDLDKAQEDLSAATSKLEEKEKTVQEA 81
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEA--KKADEAKKAEEKKKADELKKAEELKKAEEK 1563

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965   82 ----EAEVASLNRRMTLLEEELERAEERLKIATEKLEEATHNVDESERSRRALSNQIDMDDDRCSDLERKLRECQSILHE 157
Cdd:PTZ00121 1564 kkaeEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA 1643

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965  158 TENKAEEVARK----LAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLK 233
Cdd:PTZ00121 1644 EEKKKAEELKKaeeeNKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK 1723

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 922581965  234 EAETRAEFAERSVQKLQKEVDRLEDELVHEKERYK 268
Cdd:PTZ00121 1724 AEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKK 1758
MutS2 COG1193
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
164-282 4.19e-04

dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];


Pssm-ID: 440806 [Multi-domain]  Cd Length: 784  Bit Score: 41.67  E-value: 4.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965 164 EVARKLAMVEADLERAEERAEAGENK----IVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRA 239
Cdd:COG1193  490 EIARRLGLPEEIIERARELLGEESIDveklIEELERERRELEEEREEAERLREELEKLREELEEKLEELEEEKEEILEKA 569

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 922581965 240 EF-AERSVQKLQKEVDRLEDEL---VHEKERYKTISEELDSTFQELS 282
Cdd:COG1193  570 REeAEEILREARKEAEELIRELreaQAEEEELKEARKKLEELKQELE 616
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 121-284 5.54e-04

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 41.07  E-value: 5.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965 121 DESERSRRALSNQIDMDddRCSDLERKLRECQSILHETENKAEEVARK--LAMVEADLERAEERAEAGENKIVELEEELR 198
Cdd:PRK05771  40 LSNERLRKLRSLLTKLS--EALDKLRSYLPKLNPLREEKKKVSVKSLEelIKDVEEELEKIEKEIKELEEEISELENEIK 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965 199 VVGNNLKSLE------------------------VSEEKA----LQREDSYEEQIRT---------VSSRLKEAETRAEF 241
Cdd:PRK05771 118 ELEQEIERLEpwgnfdldlslllgfkyvsvfvgtVPEDKLeelkLESDVENVEYISTdkgyvyvvvVVLKELSDEVEEEL 197

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 922581965 242 AERSVQKLQKEVDRLEDELVHE-KERYKTISEELDSTFQELSGY 284
Cdd:PRK05771 198 KKLGFERLELEEEGTPSELIREiKEELEEIEKERESLLEELKEL 241
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
10-273 6.15e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 6.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965  10 AMKIEKDNALDRADAAEEKVRQITEKLERVEEELRDTQKKMTQTGDDLDKAQEDLSAATSKLEEKEKTVQEAEAEVASLN 89
Cdd:COG4372   28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965  90 RRMTLLEEELERAEERLKIATEKLEEATHNVDESERSRRALSNQIDMDDDRCSDLERKLRECQSILHETENkaEEVARKL 169
Cdd:COG4372  108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE--AEAEQAL 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965 170 AMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKL 249
Cdd:COG4372  186 DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265

                        250       260
                 ....*....|....*....|....
gi 922581965 250 QKEVDRLEDELVHEKERYKTISEE 273
Cdd:COG4372  266 AILVEKDTEEEELEIAALELEALE 289
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1-235 6.58e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.90  E-value: 6.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965   1 MDAIKKKMQAMKIEKDNALDRADAAEEKVRQITEKLERVEEELRDTQKKMTQTGDDLDKAQEDLSAatskLEEKEKTVQE 80
Cdd:COG4942   29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE----LRAELEAQKE 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965  81 AEAEVASLNRRMtlleeeleraeerLKIATEKLEEATHNVDESERSRRALSNQIDMDDDRCSDLERKLRECQSILHETEN 160
Cdd:COG4942  105 ELAELLRALYRL-------------GRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 922581965 161 KAEEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEA 235
Cdd:COG4942  172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
6-179 9.28e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 9.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965    6 KKMQAMKIEKDNALDRADAAEEKVRQITEKLERVEEELRDTQKKMTQT-GDDLDKAQEDLSAATSKLEEKEKTVQEAEAE 84
Cdd:COG4913   288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEAL 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965   85 VASLNrrmtlleeelERAEERLKIATEKLEEATHNVDESERSRRALSNQIDMDDDRCSDLERKLRECQSILHETENKAEE 164
Cdd:COG4913   368 LAALG----------LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSN 437

                         170
                  ....*....|....*
gi 922581965  165 VARKLAMVEADLERA 179
Cdd:COG4913   438 IPARLLALRDALAEA 452
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 62-281 1.14e-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: 40.44  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965    62 EDLSAATSKLEEKEKTVQEAEAEVASLNRRMTLLEEELERAEERLKIATEKLE----EATHNVDESERSRRALSNQIDmd 137
Cdd:TIGR02169  170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREyegyELLKEKEALERQKEAIERQLA-- 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965   138 ddrcsDLERKLRECQSILHETENKAEEVARKLAMVEADLERaeeraeAGENKIVELEEELRVVGNNLKSLEVSEEKALQR 217
Cdd:TIGR02169  248 -----SLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKD------LGEEEQLRVKEKIGELEAEIASLERSIAEKERE 316

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 922581965   218 EDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKERYKTI---SEELDSTFQEL 281
Cdd:TIGR02169  317 LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLraeLEEVDKEFAET 383
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
39-276 1.36e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965  39 VEEELRDTQKKMTQTGDDLDKAQEDLSAATSKLEEKEKTVQEAEAEVASLNRRMTLLEEELERAEERLKIATEKLEEATH 118
Cdd:COG4372   29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965 119 NVDESERSRRALSNQIDMDDDRCSDLERKLRECQSILHETENKAEEVARKLAMVEADLERAEERAEAGENKIV--ELEEE 196
Cdd:COG4372  109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAeqALDEL 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965 197 LRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKERYKTISEELDS 276
Cdd:COG4372  189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
14-250 1.40e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965  14 EKDNALDRADAAEEKVRQITEKLERVEEELRDTQKKMTQTGDDLDKAQEDLSAATSKLEEKEKTVQEAEAEVASLNrrmt 93
Cdd:PRK02224 217 ELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELE---- 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965  94 lleeeleraeerlkiatEKLEEATHNVDESERSRRALSNQIDMDDDRCSDLERKLRECQSILHETENKAE---------- 163
Cdd:PRK02224 293 -----------------EERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAEslredaddle 355

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965 164 ----EVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRA 239
Cdd:PRK02224 356 eraeELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATL 435

                        250
                 ....*....|.
gi 922581965 240 EFAERSVQKLQ 250
Cdd:PRK02224 436 RTARERVEEAE 446
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
111-281 2.47e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965  111 EKLEEATHNVDESERSRRALSnQIDMDDDRCSDLERKLRECQSILHETEnkAEEVARKLAMVEADLERAEERAEAGENKI 190
Cdd:COG4913   235 DDLERAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALR--LWFAQRRLELLEAELEELRAELARLEAEL 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965  191 VELEEELRVVGNNLKSLEVSEEKA-LQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKERYKT 269
Cdd:COG4913   312 ERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAA 391

                         170
                  ....*....|..
gi 922581965  270 ISEELDSTFQEL 281
Cdd:COG4913   392 LLEALEEELEAL 403
46 PHA02562
endonuclease subunit; Provisional
 184-284 2.76e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 38.84  E-value: 2.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965 184 EAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTV---SSRLKEAETRAEFAERSVQKLQKEVDRLEDEL 260
Cdd:PHA02562 295 SEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLlelKNKISTNKQSLITLVDKAKKVKAAIEELQAEF 374

                         90       100
                 ....*....|....*....|....
gi 922581965 261 VHEKERYKTISEELDSTFQELSGY 284
Cdd:PHA02562 375 VDNAEELAKLQDELDKIVKTKSEL 398
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
25-217 2.98e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 2.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965   25 AEEKVRQITEKLERVEEELRDTQKKMTQTGDDLDKAQEDLSAAT--SKLEEKEKTVQEAEAEVASLNRRMTLLEEELERA 102
Cdd:COG4913   608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLDASSDDL 687

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965  103 EErlkiATEKLEEATHNVDESERSRRALSNQIDMDDDRCSDLERKLRECQSILHETENKAEEVARKlamvEADLERAEER 182
Cdd:COG4913   688 AA----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA----LLEERFAAAL 759

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 922581965  183 AEAGENKIVE-LEEELRVVGNNLKSLEVSEEKALQR 217
Cdd:COG4913   760 GDAVERELREnLEERIDALRARLNRAEEELERAMRA 795
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
2-237 3.83e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 3.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965   2 DAIKKKMQAMKIEKDNALDRADAAEEKVRQITEKLERVEEELRDTQKKMTQTGDDLDKAQEDLSAATSKLEEKEKTVQEA 81
Cdd:PRK02224 219 DEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDL 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965  82 EAEVAslnrrmtLLEEELERAEERLKIATEKLEEATHNVDESERSRRALSNQIDMDDDRCSDLERKLRECQSILHETENK 161
Cdd:PRK02224 299 LAEAG-------LDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE 371

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 922581965 162 AEEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAET 237
Cdd:PRK02224 372 LEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA 447
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 76-283 6.84e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 37.44  E-value: 6.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965  76 KTVQEAEAEVASLNRRMTLLEEELERAEERLKIATEKLEEATHNVDESERSRRALSNQIDMDDDRCSDLERKLRECQSIL 155
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965 156 HETENKAEEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEA 235
Cdd:COG4942  100 EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 922581965 236 ETRAEFAERSVQKLQKEVDRLEDELVHEKERYKTISEELDSTFQELSG 283
Cdd:COG4942  180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
PRK12704 PRK12704
phosphodiesterase; Provisional
 149-273 6.87e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 37.84  E-value: 6.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965 149 RECQSILHETENKAEEVaRKLAMVEADLERAEERAEagenkiveLEEELRVVGNNLKSLEvseEKALQREDSYEEQIRTV 228
Cdd:PRK12704  38 EEAKRILEEAKKEAEAI-KKEALLEAKEEIHKLRNE--------FEKELRERRNELQKLE---KRLLQKEENLDRKLELL 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 922581965 229 SSR---LKEAETRAEFAERSVQKLQKEVDRLEDELVHEKERYKTISEE 273
Cdd:PRK12704 106 EKReeeLEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE 153
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 1-92 7.11e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 37.79  E-value: 7.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965     1 MDAIKKKMQAMKIEKDNALDRADAAEEKVRQITEKLERVEEELRDTQKKMTQTGDDLDKAQEDLSAATSKLEEKEKTVQE 80
Cdd:pfam15921  435 LKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEA 514

                           90
                   ....*....|..
gi 922581965    81 AEAEVASLNRRM 92
Cdd:pfam15921  515 TNAEITKLRSRV 526
PTZ00121 PTZ00121
MAEBL; Provisional
 5-280 7.73e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.81  E-value: 7.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965    5 KKKMQAMKIEKDNALDRADAAEEKVRqiTEKLERVEEELRDTQKKMTQtgdDLDKAQEDLSAATSKLEEKEKTVQEAEAE 84
Cdd:PTZ00121 1522 KKADEAKKAEEAKKADEAKKAEEKKK--ADELKKAEELKKAEEKKKAE---EAKKAEEDKNMALRKAEEAKKAEEARIEE 1596

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965   85 VASLNRRMTLLEEELERAEERLKIATEKLEEAthnvdESERSRRALSNQIDMDDDRCSDLERKLRECQSILHETENKAEE 164
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-----EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE 1671

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965  165 VARKLAmveADLERAEERAEAGENKIVELEEELRVVgNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAER 244
Cdd:PTZ00121 1672 EDKKKA---EEAKKAEEDEKKAAEALKKEAEEAKKA-EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE 1747

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 922581965  245 SVQKLQKEVDRLEDELVHEKERYKTISEELDSTFQE 280
Cdd:PTZ00121 1748 EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
V_ATPase_I pfam01496
V-type ATPase 116kDa subunit family; This family consists of the 116kDa V-type ATPase ...
 140-208 9.17e-03

V-type ATPase 116kDa subunit family; This family consists of the 116kDa V-type ATPase (vacuolar (H+)-ATPases) subunits, as well as V-type ATP synthase subunit i. The V-type ATPases family are proton pumps that acidify intracellular compartments in eukaryotic cells for example yeast central vacuoles, clathrin-coated and synaptic vesicles. They have important roles in membrane trafficking processes. The 116kDa subunit (subunit a) in the V-type ATPase is part of the V0 functional domain responsible for proton transport. The a subunit is a transmembrane glycoprotein with multiple putative transmembrane helices it has a hydrophilic amino terminal and a hydrophobic carboxy terminal. It has roles in proton transport and assembly of the V-type ATPase complex. This subunit is encoded by two homologous gene in yeast VPH1 and STV1.


Pssm-ID: 460232 [Multi-domain]  Cd Length: 748  Bit Score: 37.46  E-value: 9.17e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965  140 RCSDLERKLRecqsILHETENKAEEVARKLAMVEADLERAEERA-EAGENKIVELEEELRVVGNNLKSLE 208
Cdd:pfam01496  31 RCDEMERKLR----FFEEEIEKLDIIPIKDTLDLETPEAPSPREiDELEEKLEKLENELRELNENYETLK 96
PTZ00121 PTZ00121
MAEBL; Provisional
 2-274 9.21e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.81  E-value: 9.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965    2 DAIKKKMQAMKIEKDNALDRADAAEEKVRQITEKLERVEEELRDTQKKMTQTGDDLDKAQEDLSAATSKLEEKEKTVQEA 81
Cdd:PTZ00121 1332 DAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELK 1411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965   82 EAEVASLNRRMTLLEEELERAEERLKIATEKLEEATHNVDESERSRRALSNQIDMDDDRCSDLERKLRECQSILHETENK 161
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581965  162 AEEVARK---LAMVEADLERAEERAEAGENKIVE---LEEELRVVGNNLKSLEVSEEKALQREDSYE--EQIRTVSSRLK 233
Cdd:PTZ00121 1492 AEEAKKKadeAKKAAEAKKKADEAKKAEEAKKADeakKAEEAKKADEAKKAEEKKKADELKKAEELKkaEEKKKAEEAKK 1571

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 922581965  234 EAETRAEFAERSVQKLQKEVDRLEDELVHEKERYKTISEEL 274
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA 1612
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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