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Conserved domains on  [gi|1040671539|ref|XP_017213163|]
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tropomyosin alpha-4 chain isoform X1 [Danio rerio]

Protein Classification

CLZ and Tropomyosin domain-containing protein( domain architecture ID 11725547)

CLZ and Tropomyosin domain-containing protein

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 4.22e-63

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: 198.33  E-value: 4.22e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  48 KKLKATEDELDKYSEALKDAQEKLELSEKKASDAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGI 127
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539 128 KVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKYEEVARKLVILEGELERAEERAEIAELKGGDLEEELKNVTNNLKSL 207
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1040671539 208 EAQSEKYSEKEDKYEDEIKVLTDKLKEVETRAEFAERTVAKLEKTIDDLEDELYAQKLRFKAISEELDHALTDMS 282
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
CLZ super family cl24932
C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the ...
 13-72 6.52e-03

C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the C-terminal leucine-zipper domain of of cyclic nucleotide-gated channel proteins. The CLZ domains form homotypic trimers in solution thus constraining the channel of the CNGs to contain three cyclic nucleotide-gated subunits, CNGA. The CLZ domains formed homotypic parallel 3-helix coiled-coil domains, consistent with their proposed role in regulating subunit assembly.


The actual alignment was detected with superfamily member pfam16526:

Pssm-ID: 465160 [Multi-domain]  Cd Length: 70  Bit Score: 34.45  E-value: 6.52e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040671539  13 LDKENAIDR-AEQAESDKKAAEDKCKQLEDELLGLQKKLKATEDELDKYSEALKDAQEKLE 72
Cdd:pfam16526   9 LLKDGLLDEaAANAGAEQKDLEEKVERLESSLDVLQTRLARLLAELESSQLKLKQRITKLE 69
 
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 4.22e-63

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: 198.33  E-value: 4.22e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  48 KKLKATEDELDKYSEALKDAQEKLELSEKKASDAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGI 127
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539 128 KVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKYEEVARKLVILEGELERAEERAEIAELKGGDLEEELKNVTNNLKSL 207
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1040671539 208 EAQSEKYSEKEDKYEDEIKVLTDKLKEVETRAEFAERTVAKLEKTIDDLEDELYAQKLRFKAISEELDHALTDMS 282
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-265 9.26e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.04  E-value: 9.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   2 EAIKKKMQMLKLDKENAIDRAEQAESDKKAAEDKCKQLEDELLGLQKKLKATEDELDKYSEALKDAQEKLELSEKKASDA 81
Cdd:COG1196   221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  82 EGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRK 161
Cdd:COG1196   301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539 162 YEEVARKLVILEGELERAEERAEIAELKGGDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEDEIKVLTDKLKEVETRAEF 241
Cdd:COG1196   381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460

                         250       260
                  ....*....|....*....|....
gi 1040671539 242 AERTVAKLEKTIDDLEDELYAQKL 265
Cdd:COG1196   461 LLELLAELLEEAALLEAALAELLE 484
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 32-260 3.37e-12

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 66.62  E-value: 3.37e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   32 AEDKCKQLEDELLGLQKKLKATEDELDKYSEALKDAQEKLELSEKKASDAEGDVAALNRRIQLVEEELDRAQERLATALQ 111
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  112 KLEEAEKAADESERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKYEEVARKLVILEGELERAEERAEIAELKGG 191
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1040671539  192 DLEEELKNVTNNLKSLEAQSEKYSEKEDKYEDEIKVLTDKLKEVETRAEFAERTVAKLEKTIDDLEDEL 260
Cdd:TIGR02168  842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 23-246 5.53e-05

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 44.15  E-value: 5.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  23 EQAESDKKAAED--KCKQLEDELLGLQKKLKATEDELDKYS-----EALKDAQEKLELSEKKASDAEGDVAALNRRIQLV 95
Cdd:PRK05771   40 LSNERLRKLRSLltKLSEALDKLRSYLPKLNPLREEKKKVSvksleELIKDVEEELEKIEKEIKELEEEISELENEIKEL 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  96 EEELDRAQerlatALQKLEEAEKAADESERgIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKY----------EEV 165
Cdd:PRK05771  120 EQEIERLE-----PWGNFDLDLSLLLGFKY-VSVFVGTVPEDKLEELKLESDVENVEYISTDKGYVYvvvvvlkelsDEV 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539 166 ARKLVILEGELERAEERAEIAELKgGDLEEELKNVTNNLKSLEAQSEKYSEkedKYEDEIKVLTDKLKEVETRAEFAERT 245
Cdd:PRK05771  194 EEELKKLGFERLELEEEGTPSELI-REIKEELEEIEKERESLLEELKELAK---KYLEELLALYEYLEIELERAEALSKF 269


                  .
gi 1040671539 246 V 246
Cdd:PRK05771  270 L 270
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
 16-220 1.29e-03

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


Pssm-ID: 467957 [Multi-domain]  Cd Length: 1848  Bit Score: 40.20  E-value: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   16 ENAIDRAEQAESDKKAAEDKCKQLEDELLGLQKKLKATE------------DELDKYSEA----LKDAQEKLELSEKKAS 79
Cdd:NF012221  1558 QNALADKERAEADRQRLEQEKQQQLAAISGSQSQLESTDqnaletngqaqrDAILEESRAvtkeLTTLAQGLDALDSQAT 1637

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   80 DAE--GDvaalNRRIQLVEEELDRAQERLATALQKLEEA-EKAADESERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAE 156
Cdd:NF012221  1638 YAGesGD----QWRNPFAGGLLDRVQEQLDDAKKISGKQlADAKQRHVDNQQKVKDAVAKSEAGVAQGEQNQANAEQDID 1713

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1040671539  157 D----SDRKYEEVARKLVILEGELERAEERAEIAELKGgdlEEELKNVTNnlKSLEAQSEKYSEKEDK 220
Cdd:NF012221  1714 DakadAEKRKDDALAKQNEAQQAESDANAAANDAQSRG---EQDASAAEN--KANQAQADAKGAKQDE 1776
CLZ pfam16526
C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the ...
 13-72 6.52e-03

C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the C-terminal leucine-zipper domain of of cyclic nucleotide-gated channel proteins. The CLZ domains form homotypic trimers in solution thus constraining the channel of the CNGs to contain three cyclic nucleotide-gated subunits, CNGA. The CLZ domains formed homotypic parallel 3-helix coiled-coil domains, consistent with their proposed role in regulating subunit assembly.


Pssm-ID: 465160 [Multi-domain]  Cd Length: 70  Bit Score: 34.45  E-value: 6.52e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040671539  13 LDKENAIDR-AEQAESDKKAAEDKCKQLEDELLGLQKKLKATEDELDKYSEALKDAQEKLE 72
Cdd:pfam16526   9 LLKDGLLDEaAANAGAEQKDLEEKVERLESSLDVLQTRLARLLAELESSQLKLKQRITKLE 69
 
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 4.22e-63

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: 198.33  E-value: 4.22e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  48 KKLKATEDELDKYSEALKDAQEKLELSEKKASDAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGI 127
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539 128 KVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKYEEVARKLVILEGELERAEERAEIAELKGGDLEEELKNVTNNLKSL 207
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1040671539 208 EAQSEKYSEKEDKYEDEIKVLTDKLKEVETRAEFAERTVAKLEKTIDDLEDELYAQKLRFKAISEELDHALTDMS 282
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
 7-152 1.99e-25

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


Pssm-ID: 403808 [Multi-domain]  Cd Length: 142  Bit Score: 98.15  E-value: 1.99e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   7 KMQMLKLDKENAIDRAEQAESDKKAAEDKCKQLEDELLGLQKKLKATEDELDKYSEALKDAQEKLELSEKKASDAEgdva 86
Cdd:pfam12718   1 KMNSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNE---- 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1040671539  87 ALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGIKVIENRAMKDEEKMEIQEIQLKEAK 152
Cdd:pfam12718  77 NLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKEAK 142
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-265 9.26e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.04  E-value: 9.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   2 EAIKKKMQMLKLDKENAIDRAEQAESDKKAAEDKCKQLEDELLGLQKKLKATEDELDKYSEALKDAQEKLELSEKKASDA 81
Cdd:COG1196   221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  82 EGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRK 161
Cdd:COG1196   301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539 162 YEEVARKLVILEGELERAEERAEIAELKGGDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEDEIKVLTDKLKEVETRAEF 241
Cdd:COG1196   381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460

                         250       260
                  ....*....|....*....|....
gi 1040671539 242 AERTVAKLEKTIDDLEDELYAQKL 265
Cdd:COG1196   461 LLELLAELLEEAALLEAALAELLE 484
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1-264 2.85e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.88  E-value: 2.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   1 MEAIKKKMQMLKLDKENAIDRAEQAESDKKAAEDKCKQLEDELLGLQKKLKATEDELDKYSEALKDAQEKLELSEKKASD 80
Cdd:COG1196   234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  81 AEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDR 160
Cdd:COG1196   314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539 161 KYEEVARKLVILEGELERAEERAEIAELKGGDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEDEIKVLTDKLKEVETRAE 240
Cdd:COG1196   394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473

                         250       260
                  ....*....|....*....|....
gi 1040671539 241 FAERTVAKLEKTIDDLEDELYAQK 264
Cdd:COG1196   474 LLEAALAELLEELAEAAARLLLLL 497
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 32-260 3.37e-12

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 66.62  E-value: 3.37e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   32 AEDKCKQLEDELLGLQKKLKATEDELDKYSEALKDAQEKLELSEKKASDAEGDVAALNRRIQLVEEELDRAQERLATALQ 111
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  112 KLEEAEKAADESERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKYEEVARKLVILEGELERAEERAEIAELKGG 191
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1040671539  192 DLEEELKNVTNNLKSLEAQSEKYSEKEDKYEDEIKVLTDKLKEVETRAEFAERTVAKLEKTIDDLEDEL 260
Cdd:TIGR02168  842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 22-274 1.79e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 1.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  22 AEQAESDKKAAEDKCKQLEDELLGLQKKLKATEDELDKYSEALKDAQEKLELSEKKASDAEGDVAALNRRIQLVEEELDR 101
Cdd:COG1196   206 ERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539 102 AQERLATALQKLEEAEKA--------------ADESERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKYEEVAR 167
Cdd:COG1196   286 AQAEEYELLAELARLEQDiarleerrreleerLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539 168 KLVILEGELERAEERAEIAELKGGDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEDEIKVLTDKLKEVETRAEFAERTVA 247
Cdd:COG1196   366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445

                         250       260
                  ....*....|....*....|....*..
gi 1040671539 248 KLEKTIDDLEDELYAQKLRFKAISEEL 274
Cdd:COG1196   446 EAAEEEAELEEEEEALLELLAELLEEA 472
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 18-247 3.64e-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: 3.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  18 AIDRAEQAESDKKAAEDKCKQLEDELLGLQKKLKATEDELDKYSEALKDAQEKLELSEKKASDAEGDVAALNRRIQLVEE 97
Cdd:COG4942    18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  98 ELDRAQERLATALQKleeAEKAADESERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKYEEVARKLVILEGELE 177
Cdd:COG4942    98 ELEAQKEELAELLRA---LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539 178 RAEERAEIAELKGGDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEDEIKVLTDKLKEVETRAEFAERTVA 247
Cdd:COG4942   175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 48-275 4.81e-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: 4.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   48 KKLKATEDELDKYSEA--LKDAQEKLELSEKKASDAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESER 125
Cdd:TIGR02168  216 KELKAELRELELALLVlrLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  126 GIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKYEEVARKLVILEGELERAEERAEIAELKGGDLEEELKNVTNNLK 205
Cdd:TIGR02168  296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  206 SLEAQSEKYSEKEDKYEDEIKVLTDKLKEVETRAEFAERTVAKLEKTIDDLEDELyaQKLRFKAISEELD 275
Cdd:TIGR02168  376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL--EEAELKELQAELE 443
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-250 1.89e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 1.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   2 EAIKKKMQMLKLDKENAIDRAEQAESDKKAAEDKCKQLEDELLGLQKKLKATEDELDKYSEALKDAQEKLELSEKKASDA 81
Cdd:COG1196   256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  82 EGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRK 161
Cdd:COG1196   336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539 162 YEEVARKLVILEGELERAEERAEIAELKGGDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEDEIKVLTDKLKEVETRAEF 241
Cdd:COG1196   416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495


                  ....*....
gi 1040671539 242 AERTVAKLE 250
Cdd:COG1196   496 LLEAEADYE 504
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 15-259 4.45e-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: 50.83  E-value: 4.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   15 KENAIDRAEQAESDKKAAEDKCKQLEDELLGLQKKLKATEDELDKYSEALKDAQEKLELSEKKASDAEGDVAALNRRIQL 94
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   95 VEEELDRAQERLATALQKLEEAEKAADESERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKYEEVARKLVILEG 174
Cdd:TIGR02168  843 LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELRE 922

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  175 ELERAEERAEIAELKGGDLEEELKNVTN-NLKSLEAQSEKYSEKEDKYEDEIKVLTDKLK--------------EVETRA 239
Cdd:TIGR02168  923 KLAQLELRLEGLEVRIDNLQERLSEEYSlTLEEAEALENKIEDDEEEARRRLKRLENKIKelgpvnlaaieeyeELKERY 1002

                          250       260
                   ....*....|....*....|....*..
gi 1040671539  240 EF-------AERTVAKLEKTIDDLEDE 259
Cdd:TIGR02168 1003 DFltaqkedLTEAKETLEEAIEEIDRE 1029
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 37-284 1.08e-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: 1.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   37 KQLEDELLGLQKKLKATEDELDKYSEALKDAQEKLELSEKKASDAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEA 116
Cdd:TIGR02169  670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  117 EKAADESERGIKVIENR-----AMKDEEKMEIQEIQLKEAKHIAEDSDRKYEEVARKLVILEGELERAEERAEIAELKGG 191
Cdd:TIGR02169  750 EQEIENVKSELKELEARieeleEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE 829

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  192 DLEEELKNVTNNLKSLEAQSEKYSEKEDKYEDEIKVLTDKLKEVETRAEFAERTVAKLEKTIDDLEDELYAQKLRFKAIS 271
Cdd:TIGR02169  830 YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909

                          250
                   ....*....|...
gi 1040671539  272 EELDHALTDMSSL 284
Cdd:TIGR02169  910 AQIEKKRKRLSEL 922
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1-270 2.60e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.51  E-value: 2.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539    1 MEAIKKKMQMLKLDKENAIDRAEQAESDKKAAEDKCKQLEDELLGLQKKLKATEDELdkysealkdaqeklelsekkaSD 80
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI---------------------SR 299

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   81 AEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDR 160
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  161 KYEEVARKLVILEGELERAEERAEIAELKGGDLEEELKNVTNNLKSL-----EAQSEKYSEKEDKYEDEIKVLTDKLKEV 235
Cdd:TIGR02168  380 QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELlkkleEAELKELQAELEELEEELEELQEELERL 459

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1040671539  236 ETRAEFAERTVAKLEKTIDDLEDELYAQKLRFKAI 270
Cdd:TIGR02168  460 EEALEELREELEEAEQALDAAERELAQLQARLDSL 494
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 47-284 4.87e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.74  E-value: 4.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   47 QKKLKATEDELDKYSEALKDAQEKLELSEKKASDAEG-----------DVAALNRRIQLVEEELDRAQERLATALQKLEE 115
Cdd:TIGR02168  178 ERKLERTRENLDRLEDILNELERQLKSLERQAEKAERykelkaelrelELALLVLRLEELREELEELQEELKEAEEELEE 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  116 AEKAADESERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKYEEVARKLVILEGELERAEERAEIAELKGGDLEE 195
Cdd:TIGR02168  258 LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  196 ELKNVTNNLKSLEAQSEKYSEKEDKYEDEIKVLTDKLKEVETRAEFAERTVAKLEKTIDDLEDELYAQKLRFKAISEELD 275
Cdd:TIGR02168  338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRE 417


                   ....*....
gi 1040671539  276 HALTDMSSL 284
Cdd:TIGR02168  418 RLQQEIEEL 426
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 7-259 5.61e-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: 47.76  E-value: 5.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539    7 KMQMLKLDKENAIDRAEQAESDKKAAEDKCKQLEDELLGLQKKLKATEDELDKYSEALKDAQEKLELSEKKASDAEGDVA 86
Cdd:TIGR02169  682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   87 ALNRRIQLVEEEL------------DRAQERLATALQKLEEAEKAADESERGIKVIENRAMKDEEKMEIQEIQLKEAKHI 154
Cdd:TIGR02169  762 ELEARIEELEEDLhkleealndleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ 841

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  155 AEDSDRKYEEVARKLVILEGELERAEERAEIAELKGGDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEDEIKVLTDKLKE 234
Cdd:TIGR02169  842 RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921

                          250       260
                   ....*....|....*....|....*
gi 1040671539  235 VETRAEFAERTVAKLEKTIDDLEDE 259
Cdd:TIGR02169  922 LKAKLEALEEELSEIEDPKGEDEEI 946
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2-125 8.67e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 8.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539    2 EAIKKKMQMLKLDKENAIDRAEQAESDKKAAEDKCKQL---------EDELLGLQKKLKATEDELDKYSEA---LKDAQE 69
Cdd:COG4913    613 AALEAELAELEEELAEAEERLEALEAELDALQERREALqrlaeyswdEIDVASAEREIAELEAELERLDASsddLAALEE 692

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1040671539   70 KLELSEKKASDAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESER 125
Cdd:COG4913    693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 39-246 8.78e-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: 8.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   39 LEDELLGLQKKLKATEDELDKYSEALKDAQEKLELSEKKASDAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEK 118
Cdd:TIGR02169  299 LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDK 378

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  119 AADESERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKYEEVARKLVILEGELERAEERAEIAELKGGDLEEELK 198
Cdd:TIGR02169  379 EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1040671539  199 NVTNNLKSLEAQSEKYSEKEDKYEDEIKVLTDKLKEVETRAEFAERTV 246
Cdd:TIGR02169  459 QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 5-275 8.94e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.97  E-value: 8.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539    5 KKKMQMLKLDKENAIDRAEQAESDKKAAEDKCKQLEDELLGLQKKLKATEDELDKYSEALKDAQEKLELSEKKASDAEGD 84
Cdd:TIGR02168  732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE 811

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   85 VAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKYEE 164
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  165 VARKLVILEGELERAEERAEIAELKGGDLEEELKNVTNNLKSLEAQSEKYSEK-EDKYEDEIKVLTDKLKEVETRAEFAE 243
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEAR 971

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1040671539  244 RTVAKLEKTIDDL-------EDELYAQKLRFKAISEELD 275
Cdd:TIGR02168  972 RRLKRLENKIKELgpvnlaaIEEYEELKERYDFLTAQKE 1010
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
32-167 1.44e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 1.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   32 AEDKCKQLEDELLGLQKKLKATEDELDKYSEALKDAQEKLELSEK--KASDAEGDVAALNRRIQLVEEELDRAQE---RL 106
Cdd:COG4913    608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAELEAELERLDAssdDL 687

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040671539  107 ATALQKLEEAEKAADESERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKYEEVAR 167
Cdd:COG4913    688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 2-259 1.92e-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: 45.83  E-value: 1.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539    2 EAIKKKMQMLKLDKENAIDRAEQAESDKKAAEDKCKQL-EDELLGLQKKLKATEDELDKYSEALKDAQEKLELSEKKASD 80
Cdd:TIGR02169  247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK 326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   81 AEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDR 160
Cdd:TIGR02169  327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  161 KYEEVARKLVILEGELERAEERAEIAELKGGDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEDEIKVLTDKLKEVETRAE 240
Cdd:TIGR02169  407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELS 486

                          250
                   ....*....|....*....
gi 1040671539  241 FAERTVAKLEKTIDDLEDE 259
Cdd:TIGR02169  487 KLQRELAEAEAQARASEER 505
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 24-224 4.90e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.44  E-value: 4.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  24 QAESDKKAAEDKCKQLEDELLGLQKKLKATEDELDKYSEALKDAQEKLELSEKKASDAEGDVAALNRRIQLVEEELDRA- 102
Cdd:COG3883    13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERa 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539 103 -----QERLATALQKLEEAEKAADESERgIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKYEEVARKLVILEGELE 177
Cdd:COG3883    93 ralyrSGGSVSYLDVLLGSESFSDFLDR-LSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1040671539 178 RAEERAEIAELKGGDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEDE 224
Cdd:COG3883   172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-215 5.36e-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: 44.66  E-value: 5.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539    2 EAIKKKMQMLKLDKENAIDRAEQAESDKKAAEDKCKQLEDELLGLQKKLKATEDELDKYSE-------ALKDAQEKLELS 74
Cdd:TIGR02168  305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAeleelesRLEELEEQLETL 384

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   75 EKKASDAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGikviENRAMKDEEKMEIQEIQLKEAKHI 154
Cdd:TIGR02168  385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK----ELQAELEELEEELEELQEELERLE 460

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040671539  155 AEDSDRKYEEVARKLVILEGELERAEERAEIAELKggDLEEELKNVTNNLKSLEAQSEKYS 215
Cdd:TIGR02168  461 EALEELREELEEAEQALDAAERELAQLQARLDSLE--RLQENLEGFSEGVKALLKNQSGLS 519
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 23-246 5.53e-05

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 44.15  E-value: 5.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  23 EQAESDKKAAED--KCKQLEDELLGLQKKLKATEDELDKYS-----EALKDAQEKLELSEKKASDAEGDVAALNRRIQLV 95
Cdd:PRK05771   40 LSNERLRKLRSLltKLSEALDKLRSYLPKLNPLREEKKKVSvksleELIKDVEEELEKIEKEIKELEEEISELENEIKEL 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  96 EEELDRAQerlatALQKLEEAEKAADESERgIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKY----------EEV 165
Cdd:PRK05771  120 EQEIERLE-----PWGNFDLDLSLLLGFKY-VSVFVGTVPEDKLEELKLESDVENVEYISTDKGYVYvvvvvlkelsDEV 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539 166 ARKLVILEGELERAEERAEIAELKgGDLEEELKNVTNNLKSLEAQSEKYSEkedKYEDEIKVLTDKLKEVETRAEFAERT 245
Cdd:PRK05771  194 EEELKKLGFERLELEEEGTPSELI-REIKEELEEIEKERESLLEELKELAK---KYLEELLALYEYLEIELERAEALSKF 269


                  .
gi 1040671539 246 V 246
Cdd:PRK05771  270 L 270
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
2-275 5.80e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.26  E-value: 5.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   2 EAIKKKMQMLKLDKENAIDRAEQAESDKKAAEDKCKQLEDELLGLQKKLKATEDELDKYSEALKDAQEKLELSEKKASDA 81
Cdd:PRK02224  324 EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA 403

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  82 EGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAadesergikVIENRAMKDEEKMEIQEIQLKEAKHI--AEDSD 159
Cdd:PRK02224  404 PVDLGNAEDFLEELREERDELREREAELEATLRTARER---------VEEAEALLEAGKCPECGQPVEGSPHVetIEEDR 474

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539 160 RKYEEVARKLVILEGELERAEERAEIAElKGGDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEDEIKVLTDKLKEVETRA 239
Cdd:PRK02224  475 ERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEA 553

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1040671539 240 EFAERTVAKLEKTIDDLEDELYAQKLRFKAISEELD 275
Cdd:PRK02224  554 EEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE 589
PTZ00121 PTZ00121
MAEBL; Provisional
 2-247 1.22e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539    2 EAIKKKMQMLKLDKENAIDRAEQAESDKKAAEDKCKQLEDELLGLQKKlkatEDELDKYSEALKDAQEKLELSEKKASDA 81
Cdd:PTZ00121  1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK----AEEKKKADEAKKKAEEDKKKADELKKAA 1414

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   82 EGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGikviENRAMKDEEKMEIQEIQLK-EAKHIAEDSDR 160
Cdd:PTZ00121  1415 AAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKA----EEAKKKAEEAKKADEAKKKaEEAKKADEAKK 1490

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  161 KYEEVARKLVILEGELERAEERAEIAELKGGDLEEELKNVTNNLKSLEAQ--SEKYSEKEDKYEDEIKVLTDKLKEVETR 238
Cdd:PTZ00121  1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKkaEEKKKADELKKAEELKKAEEKKKAEEAK 1570


                   ....*....
gi 1040671539  239 AEFAERTVA 247
Cdd:PTZ00121  1571 KAEEDKNMA 1579
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
11-152 1.79e-04

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 42.34  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  11 LKLDKENAIDRAEQAESDKKAAEDKCKQLEDElLGLQKKLKATEDELDKYSEALKDAQEKLELSEKKAsdAEGDVAAlnr 90
Cdd:COG1566    74 ARLDPTDLQAALAQAEAQLAAAEAQLARLEAE-LGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALY--KKGAVSQ--- 147

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1040671539  91 riqlveEELDRAQERLATALQKLEEAEKAADESERGIKVIENRAMKDEEKMEIQEiQLKEAK 152
Cdd:COG1566   148 ------QELDEARAALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEA-ALAQAE 202
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
2-132 1.81e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 42.54  E-value: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   2 EAIKKKMQMLKLDKENAIDRAEQAESDKKAAED-KCKQLE---DELLGLQKKLKATEDELDKYSEALKDAQEKLELSEKK 77
Cdd:COG2433   380 EALEELIEKELPEEEPEAEREKEHEERELTEEEeEIRRLEeqvERLEAEVEELEAELEEKDERIERLERELSEARSEERR 459

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1040671539  78 ASDAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERG----IKVIEN 132
Cdd:COG2433   460 EIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSGelvpVKVVEK 518
outer_NodT TIGR01845
efflux transporter, outer membrane factor (OMF) lipoprotein, NodT family; Members of this ...
 23-112 3.39e-04

efflux transporter, outer membrane factor (OMF) lipoprotein, NodT family; Members of this model comprise a subfamily of the Outer Membrane Factor (TCDB 1.B.17) porins. OMF proteins operate in conjunction with a primary transporter of the RND, MFS, ABC, or PET systems, and a MFP (membrane fusion protein) to tranport substrates across membranes. The complex thus formed allows transport (export) of various solutes (heavy metal cations; drugs, oligosaccharides, proteins, etc.) across the two envelopes of the Gram-negative bacterial cell envelope in a single energy-coupled step. Current data suggest that the OMF (and not the MFP) is largely responsible for the formation of both the trans-outer membrane and trans-periplasmic channels. The roles played by the MFP have yet to be determined. [Cellular processes, Detoxification, Transport and binding proteins, Porins]


Pssm-ID: 273830 [Multi-domain]  Cd Length: 460  Bit Score: 41.63  E-value: 3.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  23 EQAESDKKAAEDkckQLEDELLGLQK-------KLKATEDELDKYSEALKDAQEKLELSEKK-------ASD---AEGDV 85
Cdd:TIGR01845 147 ESALAQLEAAEA---DSQAARLTLSAsianayvQLAALRAQLDVYHAALASRRKTLELTQKRyaagvaaASDvrqAEAAV 223

                          90       100
                  ....*....|....*....|....*..
gi 1040671539  86 AALNRRIQLVEEELDRAQERLATALQK 112
Cdd:TIGR01845 224 ASAEAELPSLDVQIAQARNALAALLGK 250
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1-251 5.28e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 5.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   1 MEAIKKKMQMLKLDKENAIDRAEQAESDKKAAEDKCKQLEDELLGLQKKLKATEDELDKYSEALKDAQEKLELSEKKASD 80
Cdd:COG4372    40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  81 AEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGIKVIENRAMKDEEKMEIQEIQ--LKEAKHIAEDS 158
Cdd:COG4372   120 LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDelLKEANRNAEKE 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539 159 DRKYEEVARKLVILEGELERAEERAEIAELKGGDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEDEIKVLTDKLKEVETR 238
Cdd:COG4372   200 EELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELE 279

                         250
                  ....*....|...
gi 1040671539 239 AEFAERTVAKLEK 251
Cdd:COG4372   280 IAALELEALEEAA 292
PTZ00121 PTZ00121
MAEBL; Provisional
 2-251 6.36e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 6.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539    2 EAIKKKMQMLKLDKE--NAIDRAEQAESDKKAAEDKCKQLEDELLGLQKKLKATEDELDKYSEALKDAQEKLELSEKKAS 79
Cdd:PTZ00121  1493 EEAKKKADEAKKAAEakKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKA 1572

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   80 DAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGIKVIENRAmKDEEKMEIQEIQLKEAKHIAEDSD 159
Cdd:PTZ00121  1573 EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK-AEEEKKKVEQLKKKEAEEKKKAEE 1651

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  160 RKYEEVARKLVILEGELERAEERAEIAELKGGdlEEELKNVTNNLKSLEAQSEKYSEKEDKYEDEIKVLTDKLKEVETRA 239
Cdd:PTZ00121  1652 LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA--EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENK 1729

                          250
                   ....*....|..
gi 1040671539  240 EFAERTVAKLEK 251
Cdd:PTZ00121  1730 IKAEEAKKEAEE 1741
PTZ00121 PTZ00121
MAEBL; Provisional
 14-218 6.53e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 6.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   14 DKENAIDRAEQAESDKKAAEDKCKQLEDELLGLQKKLKATEDELDKYSEALKDAQEKLELSEKKASDAEGDVAALNRRIQ 93
Cdd:PTZ00121  1575 DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK 1654

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   94 LVEEELDRAQERLATALQKLEEAEKAADESERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKYEEVARKLVILE 173
Cdd:PTZ00121  1655 AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE 1734

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1040671539  174 GELERAEERAEIAELKggdLEEELKNVTNNLKSLEAQSEKYSEKE 218
Cdd:PTZ00121  1735 AKKEAEEDKKKAEEAK---KDEEEKKKIAHLKKEEEKKAEEIRKE 1776
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
12-147 8.49e-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: 8.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   12 KLDKENAIDRAEQAESDKKAAEDKCKQLEDELLGLQKKLKATEDELDKYSEA---------------LKDAQEKLELSEK 76
Cdd:COG4913    280 ALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgnggdrleqlereIERLERELEERER 359

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040671539   77 KASDAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGIKVIENRAMKDEEKMEiQEIQ 147
Cdd:COG4913    360 RRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE-AEIA 429
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
38-243 9.75e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.39  E-value: 9.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  38 QLEDELLGLQKKLKATEDELDKYSEALKDAQEKLE--LSEKKASDAEGDVAALNRRIQLVEEELDRAQERLATALQKLEE 115
Cdd:COG3206   165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539 116 AEKAADESERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDR--KYEEVARKLVILEGELERAEERAEI-AELKGGD 192
Cdd:COG3206   245 LRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNhpDVIALRAQIAALRAQLQQEAQRILAsLEAELEA 324

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1040671539 193 LEEELKNVTNNLKSLEAQSEKYSEKEDKYED---EIKVLTDKLKEVETRAEFAE 243
Cdd:COG3206   325 LQAREASLQAQLAQLEARLAELPELEAELRRlerEVEVARELYESLLQRLEEAR 378
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
37-275 1.06e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   37 KQLEDELLGLQKKLKATEDELDKYSEAlkdAQEKLELSEKKASDAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEA 116
Cdd:COG4913    238 ERAHEALEDAREQIELLEPIRELAERY---AAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERL 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  117 EKAADESERGIKVIENRamkdeekmeIQEIQLKEAKHIAEDSDRkyeevarklvilegeleraeeraeiaelkggdLEEE 196
Cdd:COG4913    315 EARLDALREELDELEAQ---------IRGNGGDRLEQLEREIER--------------------------------LERE 353

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1040671539  197 LKNVTNNLKSLEAQSEKYSEkedKYEDEIKVLTDKLKEVETRAEFAERTVAKLEKTIDDLEDELYAQKLRFKAISEELD 275
Cdd:COG4913    354 LEERERRRARLEALLAALGL---PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
PTZ00121 PTZ00121
MAEBL; Provisional
 2-257 1.10e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 1.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539    2 EAIKKKMQMLKLDKENAIDRAEQAESDKKAAEDKCKQLEDELLGLQKKLKATEDELDKYSEALKDAQEKLELSE-KKASD 80
Cdd:PTZ00121  1119 EAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEElRKAED 1198

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   81 AEGDVAALNRRIQLVEEELDRAQE-RLATALQKLEEAEKAADESERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAE--- 156
Cdd:PTZ00121  1199 ARKAEAARKAEEERKAEEARKAEDaKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEear 1278

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  157 --DSDRKYEEVARKLVILEGELERAEERAEIAELKGGDLEEELKNVTNNLKSLEAQSEKYSEKEDKYE---DEIKVLTDK 231
Cdd:PTZ00121  1279 kaDELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEaakAEAEAAADE 1358

                          250       260
                   ....*....|....*....|....*.
gi 1040671539  232 LKEVETRAEFAERTVAKLEKTIDDLE 257
Cdd:PTZ00121  1359 AEAAEEKAEAAEKKKEEAKKKADAAK 1384
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
 16-220 1.29e-03

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


Pssm-ID: 467957 [Multi-domain]  Cd Length: 1848  Bit Score: 40.20  E-value: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   16 ENAIDRAEQAESDKKAAEDKCKQLEDELLGLQKKLKATE------------DELDKYSEA----LKDAQEKLELSEKKAS 79
Cdd:NF012221  1558 QNALADKERAEADRQRLEQEKQQQLAAISGSQSQLESTDqnaletngqaqrDAILEESRAvtkeLTTLAQGLDALDSQAT 1637

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   80 DAE--GDvaalNRRIQLVEEELDRAQERLATALQKLEEA-EKAADESERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAE 156
Cdd:NF012221  1638 YAGesGD----QWRNPFAGGLLDRVQEQLDDAKKISGKQlADAKQRHVDNQQKVKDAVAKSEAGVAQGEQNQANAEQDID 1713

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1040671539  157 D----SDRKYEEVARKLVILEGELERAEERAEIAELKGgdlEEELKNVTNnlKSLEAQSEKYSEKEDK 220
Cdd:NF012221  1714 DakadAEKRKDDALAKQNEAQQAESDANAAANDAQSRG---EQDASAAEN--KANQAQADAKGAKQDE 1776
PTZ00121 PTZ00121
MAEBL; Provisional
 1-277 1.85e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 1.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539    1 MEAIKKKMQMLKLDKENAIDRAEQAESDKKAAEDKCKQLEDELLGLQKKL--KATEDELDKYSEalkDAQEKLELSEKKA 78
Cdd:PTZ00121  1262 MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAeeAKKADEAKKKAE---EAKKKADAAKKKA 1338

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   79 SDAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADE----SERGIKVIENRAMKDEEKMEIQEIQLK-EAKH 153
Cdd:PTZ00121  1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAakkkAEEKKKADEAKKKAEEDKKKADELKKAaAAKK 1418

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  154 IAEDSDRKYEEVARKLVILEGELERAEERAEIAELKGGDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEDEIKVLTDKLK 233
Cdd:PTZ00121  1419 KADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKK 1498

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1040671539  234 EVETRAEFAERTVAKLEKTIDDLEDELYAQKLRFKAISEELDHA 277
Cdd:PTZ00121  1499 ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKA 1542
mukB PRK04863
chromosome partition protein MukB;
41-152 3.79e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 38.78  E-value: 3.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   41 DELLGLQKKLKATEDELDKYSEALKDAQEKLELSEKKASDAEGDVAALNRRIQLVEEELdRAQERLATALQKLEEAEKAA 120
Cdd:PRK04863   286 EEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTAL-RQQEKIERYQADLEELEERL 364

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1040671539  121 DESERGIKVIENRAMKDEEKMEIQEIQLKEAK 152
Cdd:PRK04863   365 EEQNEVVEEADEQQEENEARAEAAEEEVDELK 396
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
16-260 3.80e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 3.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  16 ENAIDRAEQAESDKKAAEDKCKQLEDELLGLQKKLKATEDELDKYSEALKDAQEKLELSE--------KKASDAEGdVAA 87
Cdd:PRK02224  394 EELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpvEGSPHVET-IEE 472

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  88 LNRRIQLVEEELDRAQERLATALQKLEEAEKAAdESERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKYEEVAR 167
Cdd:PRK02224  473 DRERVEELEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEA 551

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539 168 KLVILEGELERAEERAEIAELKGGDLEEELKNVTNNLKSLEAQSEKYSEKEDkYEDEIKVLTDKLKEVETRAEFAERTVA 247
Cdd:PRK02224  552 EAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIAD-AEDEIERLREKREALAELNDERRERLA 630

                         250
                  ....*....|...
gi 1040671539 248 KLEKTIDDLEDEL 260
Cdd:PRK02224  631 EKRERKRELEAEF 643
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
 12-121 4.73e-03

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 38.17  E-value: 4.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  12 KLDKENAIDRAEQAESDKKA---AEDKCKQLEDELLGLQKKLKATEDELDKYSEALKDAQEKLE-LSEKKASDAEGDVAA 87
Cdd:TIGR04320 243 KFDKTPIPNPPNSLAALQAKlatAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELAnAQAQALQTAQNNLAT 322

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1040671539  88 LNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 121
Cdd:TIGR04320 323 AQAALANAEARLAKAKEALANLNADLAKKQAALD 356
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 40-284 4.99e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 38.39  E-value: 4.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   40 EDELLGLQKKLKATEdELDKYSEALKDAQEKLELSEKKASDAEGDVAALNRRIQLVEEELDRAQERLA------------ 107
Cdd:COG3096    333 SDHLNLVQTALRQQE-KIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAdyqqaldvqqtr 411

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  108 -----TALQKLEEAEKAADESERGIKVIENRAMKDEEKMEIQEIQLKEAKH---IAEDSDRKYEEVARKLVILEGELERA 179
Cdd:COG3096    412 aiqyqQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQklsVADAARRQFEKAYELVCKIAGEVERS 491

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  180 EERAEIAELkggdLEE--ELKNVTNNLKSLEAQ---SEKYSEKEDKYEDEIKVLTDKLKEVETRAEFAERTVAKLEKTID 254
Cdd:COG3096    492 QAWQTAREL----LRRyrSQQALAQRLQQLRAQlaeLEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLE 567

                          250       260       270
                   ....*....|....*....|....*....|
gi 1040671539  255 DLEDELYAQKLRFKAISEELDHALTDMSSL 284
Cdd:COG3096    568 ELEEQAAEAVEQRSELRQQLEQLRARIKEL 597
PTZ00121 PTZ00121
MAEBL; Provisional
 2-251 5.30e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.20  E-value: 5.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539    2 EAIKKKMQMLKLDKENAIDRAEQAESDKKAAEDKCKQLEDELLGLQKKLKATEDELDKYSEALKDAQEKLELSEKKASDA 81
Cdd:PTZ00121  1227 EAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADE 1306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   82 EGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRK 161
Cdd:PTZ00121  1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK 1386

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  162 YEEVARKlviLEGELERAEERAEIAELKGgdlEEELKNVTNNLKSLEAQSEKYSEKEDKYEDEIKvlTDKLKEVETRAEF 241
Cdd:PTZ00121  1387 AEEKKKA---DEAKKKAEEDKKKADELKK---AAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK--ADEAKKKAEEAKK 1458

                          250
                   ....*....|
gi 1040671539  242 AERTVAKLEK 251
Cdd:PTZ00121  1459 AEEAKKKAEE 1468
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 84-284 5.31e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.38  E-value: 5.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  84 DVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKYE 163
Cdd:COG1196   226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539 164 EVARKLVILEGELERAEERAEIAELKGGDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEDEIKVLTDKLKEVETRAEFAE 243
Cdd:COG1196   306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1040671539 244 RTVAKLEKTIDDLEDELYAQKLRFKAISEELDHALTDMSSL 284
Cdd:COG1196   386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
CLZ pfam16526
C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the ...
 13-72 6.52e-03

C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the C-terminal leucine-zipper domain of of cyclic nucleotide-gated channel proteins. The CLZ domains form homotypic trimers in solution thus constraining the channel of the CNGs to contain three cyclic nucleotide-gated subunits, CNGA. The CLZ domains formed homotypic parallel 3-helix coiled-coil domains, consistent with their proposed role in regulating subunit assembly.


Pssm-ID: 465160 [Multi-domain]  Cd Length: 70  Bit Score: 34.45  E-value: 6.52e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040671539  13 LDKENAIDR-AEQAESDKKAAEDKCKQLEDELLGLQKKLKATEDELDKYSEALKDAQEKLE 72
Cdd:pfam16526   9 LLKDGLLDEaAANAGAEQKDLEEKVERLESSLDVLQTRLARLLAELESSQLKLKQRITKLE 69
PTZ00121 PTZ00121
MAEBL; Provisional
 2-259 7.02e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.81  E-value: 7.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539    2 EAIKKKMQMLKLDKENAIDRAEQAESDKKAAEDKCKQLEDELLGLQKKLKATEDELDKYSEALKDAQEKLELSEKKASDA 81
Cdd:PTZ00121  1543 EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539   82 EGDVAALNRRIQLVEEELDRAQE-RLATALQKLEEAEKAADESERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDR 160
Cdd:PTZ00121  1623 EELKKAEEEKKKVEQLKKKEAEEkKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040671539  161 KYEEVARKlvilegeleRAEERAEIAELKGGdlEEELKNVTNNLKSLEAQSEKYSEKEDKYEDEIKVLTDKLKEVETRAE 240
Cdd:PTZ00121  1703 KAEELKKK---------EAEEKKKAEELKKA--EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAE 1771

                          250
                   ....*....|....*....
gi 1040671539  241 FAERTVAKLEKTIDDLEDE 259
Cdd:PTZ00121  1772 EIRKEKEAVIEEELDEEDE 1790
 
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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