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Conserved domains on  [gi|2038132594|ref|XP_041428860|]
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tropomyosin 4 S homeolog isoform X3 [Xenopus laevis]

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 1.13e-66

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: 207.57  E-value: 1.13e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  48 KKLKGTEDELDKYSEALKDAQEKLEQAEKKATDAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 127
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594 128 KVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKCSDLEEELKNVTNNLKSL 207
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2038132594 208 EAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDELYTQKLKYKAISEELDHALNDMT 282
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
 
Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 48-282 1.13e-66

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: 207.57  E-value: 1.13e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  48 KKLKGTEDELDKYSEALKDAQEKLEQAEKKATDAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 127
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594 128 KVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKCSDLEEELKNVTNNLKSL 207
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2038132594 208 EAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDELYTQKLKYKAISEELDHALNDMT 282
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-279 9.36e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.12  E-value: 9.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   2 EAIKKKMQMLKLDKENAIDRAEQAEADKKAAEDKFKQVEDELVALQKKLKGTEDELDKYSEALKDAQEKLEQAEKKATDA 81
Cdd:COG1196   221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  82 EGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRK 161
Cdd:COG1196   301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594 162 YEEVARKLVILEGELERAEERAEVSELKCSDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEF 241
Cdd:COG1196   381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2038132594 242 AERTVTKLEKAIDDLEDELYTQKLKYKAISEELDHALN 279
Cdd:COG1196   461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 32-260 9.34e-12

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 65.08  E-value: 9.34e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   32 AEDKFKQVEDELVALQKKLKGTEDELDKYSEALKDAQEKLEQAEKKATDAEGDVAALNRRIQLVEEELDRAQERLATALQ 111
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  112 KLEEAEKAADESERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKCS 191
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038132594  192 DLEEELKNVTNNLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDEL 260
Cdd:TIGR02168  842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
2-275 8.99e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.96  E-value: 8.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   2 EAIKKKMQMLKLDKENAIDRAEQAEADKKAAEDKFKQVEDELVALQKKLKGTEDELDKYSEALKDAQEKLEQAEKKATDA 81
Cdd:PRK02224  324 EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA 403

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  82 EGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAadesergmkVIENRAMKDEEKMDVQEMQLKEAKHI--AEEAD 159
Cdd:PRK02224  404 PVDLGNAEDFLEELREERDELREREAELEATLRTARER---------VEEAEALLEAGKCPECGQPVEGSPHVetIEEDR 474

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594 160 RKYEEVARKLVILEGELERAEERAEVSElKCSDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRA 239
Cdd:PRK02224  475 ERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEA 553

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2038132594 240 EFAERTVTKLEKAIDDLEDELYTQKLKYKAISEELD 275
Cdd:PRK02224  554 EEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE 589
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
 16-220 1.92e-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: 39.82  E-value: 1.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   16 ENAIDRAEQAEADKKAAEDKFKQVEDELVALQKKLKGTE------------DELDKYSEA----LKDAQEKLEQAEKKAT 79
Cdd:NF012221  1558 QNALADKERAEADRQRLEQEKQQQLAAISGSQSQLESTDqnaletngqaqrDAILEESRAvtkeLTTLAQGLDALDSQAT 1637

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   80 DAE--GD------VAALNRRIQ--------LVEEELDRAQERLATALQKLEEAEKaadESERGMkvienraMKDEEKMDV 143
Cdd:NF012221  1638 YAGesGDqwrnpfAGGLLDRVQeqlddakkISGKQLADAKQRHVDNQQKVKDAVA---KSEAGV-------AQGEQNQAN 1707

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038132594  144 QEMQLKEAKHIAEEadRKYEEVARKlviLEGELERAEERAEVSELKcSDLEEELKNVTNnlKSLEAQSEKYSEKEDK 220
Cdd:NF012221  1708 AEQDIDDAKADAEK--RKDDALAKQ---NEAQQAESDANAAANDAQ-SRGEQDASAAEN--KANQAQADAKGAKQDE 1776
 
Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 48-282 1.13e-66

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: 207.57  E-value: 1.13e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  48 KKLKGTEDELDKYSEALKDAQEKLEQAEKKATDAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 127
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594 128 KVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKCSDLEEELKNVTNNLKSL 207
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2038132594 208 EAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDELYTQKLKYKAISEELDHALNDMT 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 1.91e-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: 1.91e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   7 KMQMLKLDKENAIDRAEQAEADKKAAEDKFKQVEDELVALQKKLKGTEDELDKYSEALKDAQEKLEQAEKKATDAEgdva 86
Cdd:pfam12718   1 KMNSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNE---- 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038132594  87 ALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMDVQEMQLKEAK 152
Cdd:pfam12718  77 NLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKEAK 142
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-279 9.36e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.12  E-value: 9.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   2 EAIKKKMQMLKLDKENAIDRAEQAEADKKAAEDKFKQVEDELVALQKKLKGTEDELDKYSEALKDAQEKLEQAEKKATDA 81
Cdd:COG1196   221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  82 EGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRK 161
Cdd:COG1196   301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594 162 YEEVARKLVILEGELERAEERAEVSELKCSDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEF 241
Cdd:COG1196   381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2038132594 242 AERTVTKLEKAIDDLEDELYTQKLKYKAISEELDHALN 279
Cdd:COG1196   461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 32-260 9.34e-12

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 65.08  E-value: 9.34e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   32 AEDKFKQVEDELVALQKKLKGTEDELDKYSEALKDAQEKLEQAEKKATDAEGDVAALNRRIQLVEEELDRAQERLATALQ 111
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  112 KLEEAEKAADESERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKCS 191
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038132594  192 DLEEELKNVTNNLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDEL 260
Cdd:TIGR02168  842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 22-278 1.01e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.26  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  22 AEQAEADKKAAEDKFKQVEDELVALQKKLKGTEDELDKYSEALKDAQEKLEQAEKKATDAEGDVAALNRRIQLVEEELDR 101
Cdd:COG1196   206 ERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594 102 AQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEE 181
Cdd:COG1196   286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594 182 RAEVSELKCSDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDELY 261
Cdd:COG1196   366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445

                         250
                  ....*....|....*..
gi 2038132594 262 TQKLKYKAISEELDHAL 278
Cdd:COG1196   446 EAAEEEAELEEEEEALL 462
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 11-277 2.80e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.76  E-value: 2.80e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   11 LKLDKENAIDRAEQAEADKKAAEDKFKQVEDELVALQKKLKGTEDELDKYSEALKDAQEKLEQAEKKATDAEGDVAALNR 90
Cdd:TIGR02168  230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   91 RIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARK-- 168
Cdd:TIGR02168  310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKva 389

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  169 ------------LVILEGELE-----RAEERAEVSELKCSDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEEEIKILTDK 231
Cdd:TIGR02168  390 qlelqiaslnneIERLEARLErledrRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 2038132594  232 LKEAETRAEFAERTVTKLEKAIDDLEDELYTQKLKYKAISEELDHA 277
Cdd:TIGR02168  470 LEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQ 515
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 18-239 1.04e-08

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 55.54  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  18 AIDRAEQAEADKKAAEDKFKQVEDELVALQKKLKGTEDELDKYSEALKDAQEKLEQAEKKATDAEGDVAALNRRIQLVEE 97
Cdd:COG4942    18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  98 ELDRAQERLATALQKLEEAEKAADE----SERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILE 173
Cdd:COG4942    98 ELEAQKEELAELLRALYRLGRQPPLalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038132594 174 GELERAEERAEVSELKCSDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRA 239
Cdd:COG4942   178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 34-275 7.02e-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: 7.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   34 DKFKQVEDELVALQKKLKGTEDELDKYSEALKDAQEKLEQAEKKATDAEGDVAALNRRIQLVEEELDRAQERLATALQKL 113
Cdd:TIGR02169  681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL 760

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  114 EEAEKAADESErgmkvienrAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKCSDL 193
Cdd:TIGR02169  761 KELEARIEELE---------EDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  194 EEELKNVTNNLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDELYTQKLKYKAISEE 273
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ 911


                   ..
gi 2038132594  274 LD 275
Cdd:TIGR02169  912 IE 913
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2-125 4.51e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.07  E-value: 4.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594    2 EAIKKKMQMLKLDKENAIDRAEQAEADKKAAEDKF----------------KQVEDELVALQKKLkgteDELDKYSEALK 65
Cdd:COG4913    613 AALEAELAELEEELAEAEERLEALEAELDALQERRealqrlaeyswdeidvASAEREIAELEAEL----ERLDASSDDLA 688

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   66 DAQEKLEQAEKKATDAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESER 125
Cdd:COG4913    689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 16-246 4.82e-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: 50.84  E-value: 4.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   16 ENAIDRAEQAEADKKAAEDKFKQVEDELVALQKKLKGTEDELDKYSEALKDAQEKLEQAE-------KKATDAEGDVAAL 88
Cdd:TIGR02169  269 EIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEaeidkllAEIEELEREIEEE 348

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   89 NRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARK 168
Cdd:TIGR02169  349 RKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAA 428

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038132594  169 LVILEGELERAEERAEVSELKCSDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTV 246
Cdd:TIGR02169  429 IAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 7-259 1.42e-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: 49.30  E-value: 1.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594    7 KMQMLKLDKENAIDRAEQAEADKKAAEDKFKQVEDELVALQKKLKGTEDELDKYSEALKDAQEKLEQAEKKATDAEGDVA 86
Cdd:TIGR02169  682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   87 ALNRRIQLVEEEL------------DRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMDVQEMQLKEAKHI 154
Cdd:TIGR02169  762 ELEARIEELEEDLhkleealndleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ 841

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  155 AEEADRKYEEVARKLVILEGELERAEERAEVSELKCSDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEEEIKILTDKLKE 234
Cdd:TIGR02169  842 RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921

                          250       260
                   ....*....|....*....|....*
gi 2038132594  235 AETRAEFAERTVTKLEKAIDDLEDE 259
Cdd:TIGR02169  922 LKAKLEALEEELSEIEDPKGEDEEI 946
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 43-260 5.12e-06

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: 47.07  E-value: 5.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  43 LVALQKKLKGTEDELDKYSEALKDAQEKLEQAEKKATDAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 122
Cdd:COG4942    15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594 123 SERGMKVIENRAmkdEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKCSDLEEELKNVTN 202
Cdd:COG4942    95 LRAELEAQKEEL---AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2038132594 203 NLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDEL 260
Cdd:COG4942   172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1-208 8.25e-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: 8.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594    1 MEAIKKKMQMLKLDKENAIDRAEQAEADKKAAEDKFKQVEDELVALQKKLKGTEDELDKYSEALKDAQEKLEQAEKKATD 80
Cdd:TIGR02168  311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   81 AEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERgMKVIENRAMKDEEKMDVQEmQLKEAKHIAEEADR 160
Cdd:TIGR02168  391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL-KELQAELEELEEELEELQE-ELERLEEALEELRE 468

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2038132594  161 KYEEVARKLVILEGELERAEERAEVSELKCSDLEEELKNVTNNLKSLE 208
Cdd:TIGR02168  469 ELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQS 516
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 24-224 8.32e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.75  E-value: 8.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  24 QAEADKKAAEDKFKQVEDELVALQKKLKGTEDELDKYSEALKDAQEKLEQAEKKATDAEGDVAALNRRIQLVEEELDRA- 102
Cdd:COG3883    13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERa 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594 103 -----QERLATALQKLEEAEKAADESERgMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELE 177
Cdd:COG3883    93 ralyrSGGSVSYLDVLLGSESFSDFLDR-LSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2038132594 178 RAEERAEVSELKCSDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEEE 224
Cdd:COG3883   172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
2-275 8.99e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.96  E-value: 8.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   2 EAIKKKMQMLKLDKENAIDRAEQAEADKKAAEDKFKQVEDELVALQKKLKGTEDELDKYSEALKDAQEKLEQAEKKATDA 81
Cdd:PRK02224  324 EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA 403

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  82 EGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAadesergmkVIENRAMKDEEKMDVQEMQLKEAKHI--AEEAD 159
Cdd:PRK02224  404 PVDLGNAEDFLEELREERDELREREAELEATLRTARER---------VEEAEALLEAGKCPECGQPVEGSPHVetIEEDR 474

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594 160 RKYEEVARKLVILEGELERAEERAEVSElKCSDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRA 239
Cdd:PRK02224  475 ERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEA 553

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2038132594 240 EFAERTVTKLEKAIDDLEDELYTQKLKYKAISEELD 275
Cdd:PRK02224  554 EEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE 589
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 34-261 9.94e-06

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 46.46  E-value: 9.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  34 DKFKQVEDELVALQKKLKGTEDEldKYSEALKDAQEKLEQAEKKATDAEGDVAALNRRIQLVEEELDRAQ---------- 103
Cdd:PRK05771   60 DKLRSYLPKLNPLREEKKKVSVK--SLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwgnfdldls 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594 104 -----ERLATALQKLEEAEKAADESERGMKVIENRAmKDEEKMDVQEMQLKEAKHIAEEADRKYEevARKLVILEGELER 178
Cdd:PRK05771  138 lllgfKYVSVFVGTVPEDKLEELKLESDVENVEYIS-TDKGYVYVVVVVLKELSDEVEEELKKLG--FERLELEEEGTPS 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594 179 AEERAEVSELKcsDLEEELKNVtnnLKSLEAQSEKYSEKEDKYEEEIKILTDK----LKEAETRAEFA------ERTVTK 248
Cdd:PRK05771  215 ELIREIKEELE--EIEKERESL---LEELKELAKKYLEELLALYEYLEIELERaealSKFLKTDKTFAiegwvpEDRVKK 289

                         250
                  ....*....|...
gi 2038132594 249 LEKAIDDLEDELY 261
Cdd:PRK05771  290 LKELIDKATGGSA 302
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 5-256 3.23e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 3.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594    5 KKKMQMLKLDKENAIDRAEQAEADKKAAEDKFKQVEDELVALQKKLKGTEDELDKYSEALKDAQEKLEQAEKKATDAEGD 84
Cdd:TIGR02168  732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE 811

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   85 VAALN--------------RRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMDVQEMQLKE 150
Cdd:TIGR02168  812 LTLLNeeaanlrerlesleRRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  151 AKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKCSDLEEELKNVtnnlksLEAQSEKYSEKEDKYEEEIKILTD 230
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL------QERLSEEYSLTLEEAEALENKIED 965

                          250       260
                   ....*....|....*....|....*.
gi 2038132594  231 KLKEAETRaefaertVTKLEKAIDDL 256
Cdd:TIGR02168  966 DEEEARRR-------LKRLENKIKEL 984
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
40-210 3.49e-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: 3.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   40 EDELVALQKKLKGTEDELDKYSEALKDAQEKLEQAEKKATDAEG---------DVAALNRRIQLVEEELDRAQE---RLA 107
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeiDVASAEREIAELEAELERLDAssdDLA 688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  108 TALQKLEEAEKAADESERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLviLEGELERAEERAEVSE 187
Cdd:COG4913    689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL--LEERFAAALGDAVERE 766

                          170       180
                   ....*....|....*....|...
gi 2038132594  188 LKcSDLEEELKNVTNNLKSLEAQ 210
Cdd:COG4913    767 LR-ENLEERIDALRARLNRAEEE 788
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
11-125 3.69e-05

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 44.65  E-value: 3.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  11 LKLDKENAIDRAEQAEADKKAAEDKF-------------KQVEDELVALQKKLKGTEDELDKYSEALKD---AQEKLEQA 74
Cdd:COG1566    74 ARLDPTDLQAALAQAEAQLAAAEAQLarleaelgaeaeiAAAEAQLAAAQAQLDLAQRELERYQALYKKgavSQQELDEA 153

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2038132594  75 EKKATDAEGDVAALNRRIQLVEEELdRAQERLATALQKLEEAEKAADESER 125
Cdd:COG1566   154 RAALDAAQAQLEAAQAQLAQAQAGL-REEEELAAAQAQVAQAEAALAQAEL 203
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 20-284 1.15e-04

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: 43.40  E-value: 1.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   20 DRAEQAEADKKAAEDKFKQVEdELVALQKKLkgtedelDKYSEALKDAQEKLEQAEKKATDAEGDVAALNRRIQLVEEEL 99
Cdd:COG3096    320 ARESDLEQDYQAASDHLNLVQ-TALRQQEKI-------ERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEV 391

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  100 DRAQERLA-----------------TALQKLEEAEKAADESERGMKVIENRAMKDEEKMDVQEMQLKEAKH---IAEEAD 159
Cdd:COG3096    392 DSLKSQLAdyqqaldvqqtraiqyqQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQklsVADAAR 471

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  160 RKYEEVARKLVILEGELERAEERAEVSELkcsdLEE--ELKNVTNNLKSLEAQ---SEKYSEKEDKYEEEIKILTDKLKE 234
Cdd:COG3096    472 RQFEKAYELVCKIAGEVERSQAWQTAREL----LRRyrSQQALAQRLQQLRAQlaeLEQRLRQQQNAERLLEEFCQRIGQ 547

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 2038132594  235 AETRAEFAERTVTKLEKAIDDLEDELYTQKLKYKAISEELDHALNDMTSL 284
Cdd:COG3096    548 QLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKEL 597
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 29-277 1.71e-04

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: 43.13  E-value: 1.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   29 KKAAEDKFKQVEDELVALQKKLKGTEDELDKYSEALKDAQEKLEQAEKKATDA---------------EGDVAALNRRIQ 93
Cdd:TIGR02169  232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvkekigelEAEIASLERSIA 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   94 LVEEELDRAQERLATALQKLEEAEKAADESER--GMKVIENRAMKDEEKMDVQEMQLKEAKhiAEEADRKYEEVARKLVI 171
Cdd:TIGR02169  312 EKERELEDAEERLAKLEAEIDKLLAEIEELEReiEEERKRRDKLTEEYAELKEELEDLRAE--LEEVDKEFAETRDELKD 389

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  172 LEGELERAEERAEVSELKCSDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEK 251
Cdd:TIGR02169  390 YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ 469

                          250       260
                   ....*....|....*....|....*.
gi 2038132594  252 AIDDLEDELYTQKLKYKAISEELDHA 277
Cdd:TIGR02169  470 ELYDLKEEYDRVEKELSKLQRELAEA 495
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
23-280 1.80e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 1.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  23 EQAEADKKAAEDKFKQVEDELVALQKKLKGTEDELDKYSEALKDAQEKLEQAEKKATDAEGDVAALNRRIQLVEEELDRA 102
Cdd:COG4372    55 EQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQL 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594 103 QERLATALQKLEEAEKAADESERGMKVIEN---RAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERA 179
Cdd:COG4372   135 EAQIAELQSEIAEREEELKELEEQLESLQEelaALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594 180 EERAEVSELKCSDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDE 259
Cdd:COG4372   215 ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALE 294

                         250       260
                  ....*....|....*....|.
gi 2038132594 260 LYTQKLKYKAISEELDHALND 280
Cdd:COG4372   295 LKLLALLLNLAALSLIGALED 315
PTZ00121 PTZ00121
MAEBL; Provisional
 2-269 1.86e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 1.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594    2 EAIKKKMQMLKLDKENAIDRAEQAEADKKAAEDKFKQVEDELVALQKKLKGTEDELDKYSEALKDAQEKLEQAE-KKATD 80
Cdd:PTZ00121  1119 EAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEElRKAED 1198

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   81 AEGDVAALNRRIQLVEEELDRAQE-RLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEAd 159
Cdd:PTZ00121  1199 ARKAEAARKAEEERKAEEARKAEDaKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA- 1277

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  160 RKYEEVARKLVILEGELERAEERAEVSelkcsdleEELKNVTNNLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRA 239
Cdd:PTZ00121  1278 RKADELKKAEEKKKADEAKKAEEKKKA--------DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAK 1349

                          250       260       270
                   ....*....|....*....|....*....|.
gi 2038132594  240 EFAERTVTKLEKAIDDLE-DELYTQKLKYKA 269
Cdd:PTZ00121  1350 AEAEAAADEAEAAEEKAEaAEKKKEEAKKKA 1380
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 97-284 2.18e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  97 EELDRAQERLAtaLQKLEEAEKAADESERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGEL 176
Cdd:COG1196   220 EELKELEAELL--LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594 177 ERAEERAEVSELKCSDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDL 256
Cdd:COG1196   298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377

                         170       180
                  ....*....|....*....|....*...
gi 2038132594 257 EDELYTQKLKYKAISEELDHALNDMTSL 284
Cdd:COG1196   378 EEELEELAEELLEALRAAAELAAQLEEL 405
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
25-274 2.23e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 2.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  25 AEADKKAAEDKFKQVEDELVALQKKLKGTEDELDKYSEALKDAQEKLEQAEKKATDAEGDVAALNRRIQLVEEELDRAQE 104
Cdd:COG4372    29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594 105 RLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAE 184
Cdd:COG4372   109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594 185 VSELKCS-DLEEELKNVTNNLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDELYTQ 263
Cdd:COG4372   189 LKEANRNaEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268

                         250
                  ....*....|.
gi 2038132594 264 KLKYKAISEEL 274
Cdd:COG4372   269 VEKDTEEEELE 279
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 47-284 2.99e-04

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: 42.35  E-value: 2.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   47 QKKLKGTEDELDKYSEALKDAQEKLEQAEKKATDAEgdvAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERG 126
Cdd:TIGR02168  178 ERKLERTRENLDRLEDILNELERQLKSLERQAEKAE---RYKELKAELRELELALLVLRLEELREELEELQEELKEAEEE 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  127 MKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKCSDLEEELKNVTNNLKS 206
Cdd:TIGR02168  255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE 334

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038132594  207 LEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDELYTQKLKYKAISEELDHALNDMTSL 284
Cdd:TIGR02168  335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
PTZ00121 PTZ00121
MAEBL; Provisional
 14-246 3.34e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 3.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   14 DKENAIDRAEQA-EADKKAAEDKFKQVEDELVALQKKLKGTEDELDKySEALKDAQEKLEQAEKKATDAEGDVAALNRRI 92
Cdd:PTZ00121  1575 DKNMALRKAEEAkKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK-AEELKKAEEEKKKVEQLKKKEAEEKKKAEELK 1653

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   93 QLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVIL 172
Cdd:PTZ00121  1654 KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAE 1733

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2038132594  173 EGELERAEERAEVSELKCSdlEEELKNVTNNLKSLEAQSEKY-SEKEDKYEEEIKiltdklKEAETRAEFAERTV 246
Cdd:PTZ00121  1734 EAKKEAEEDKKKAEEAKKD--EEEKKKIAHLKKEEEKKAEEIrKEKEAVIEEELD------EEDEKRRMEVDKKI 1800
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1-133 4.22e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 4.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594    1 MEAIKKKMQMLKLDKENAIDRAEQAEADKKAAEDKFKQVE--------DELVALQKKLKGTEDELDKYSEALKDAQEKLE 72
Cdd:COG4913    290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEaqirgnggDRLEQLEREIERLERELEERERRRARLEALLA 369

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2038132594   73 QAEKKATDAEGDVAALNRRIQL----VEEELDRAQERLATALQKLEEAEKAADESERGMKVIENR 133
Cdd:COG4913    370 ALGLPLPASAEEFAALRAEAAAlleaLEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
PTZ00121 PTZ00121
MAEBL; Provisional
 6-252 5.01e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 5.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594    6 KKMQMLKLDKENA--IDRAEQAEADKKAAEDKFKQVEDELVALQKKLKGTEDELDKySEALKDAQEKLEQAEKKATDAEG 83
Cdd:PTZ00121  1230 KKAEEAKKDAEEAkkAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK-AEEKKKADEAKKAEEKKKADEAK 1308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   84 DVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYE 163
Cdd:PTZ00121  1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE 1388

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  164 EVARKlviLEGELERAEERAEVSELKcsdLEEELKNVTNNLKSLEAQSEKYSEKEDKYEEEIKilTDKLKEAETRAEFAE 243
Cdd:PTZ00121  1389 EKKKA---DEAKKKAEEDKKKADELK---KAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK--ADEAKKKAEEAKKAE 1460


                   ....*....
gi 2038132594  244 RTVTKLEKA 252
Cdd:PTZ00121  1461 EAKKKAEEA 1469
PTZ00121 PTZ00121
MAEBL; Provisional
 5-244 5.01e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 5.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594    5 KKKMQMLKLDKENAIDRAEQ---AEADKKAAEDKFKQVEDELVALQKKLKGTE----DELDKYSEALKDAQEKLEQAEKK 77
Cdd:PTZ00121  1390 KKKADEAKKKAEEDKKKADElkkAAAAKKKADEAKKKAEEKKKADEAKKKAEEakkaDEAKKKAEEAKKAEEAKKKAEEA 1469

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   78 ATDAEGDVAALNRRiqlveeELDRAQERLATALQKLEEAEKAADESERGmkvieNRAMKDEEKMDVQEMQLKEAKHIAEE 157
Cdd:PTZ00121  1470 KKADEAKKKAEEAK------KADEAKKKAEEAKKKADEAKKAAEAKKKA-----DEAKKAEEAKKADEAKKAEEAKKADE 1538

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  158 AdRKYEEVARKLVILEGELERAEERAEVSELKCSDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAET 237
Cdd:PTZ00121  1539 A-KKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617


                   ....*..
gi 2038132594  238 RAEFAER 244
Cdd:PTZ00121  1618 AKIKAEE 1624
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
22-253 5.01e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 5.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  22 AEQAEADKKAAEDKFKQVEDELVALQKKLKGTEDELDKY---------SEALKDAQEKLEQAEKKATDAEGDVAALNRRI 92
Cdd:COG3206   163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFrqknglvdlSEEAKLLLQQLSELESQLAEARAELAEAEARL 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  93 QLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMDVQEMQLKEA---KHIAEEADRKYEEVARKL 169
Cdd:COG3206   243 AALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAalrAQLQQEAQRILASLEAEL 322

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594 170 VILEGELEraeeraevselkcsDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEEEIKILTD---KLKEAETRAEFAERTV 246
Cdd:COG3206   323 EALQAREA--------------SLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESllqRLEEARLAEALTVGNV 388


                  ....*..
gi 2038132594 247 TKLEKAI 253
Cdd:COG3206   389 RVIDPAV 395
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
41-260 6.40e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 6.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   41 DELVALQKKLKGTEDELDKYSE------ALKDAQEKLEQAEKKATDAEGDVAALN-----RRIQLVEEELDRAQERLATA 109
Cdd:COG4913    228 DALVEHFDDLERAHEALEDAREqiellePIRELAERYAAARERLAELEYLRAALRlwfaqRRLELLEAELEELRAELARL 307

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  110 LQKLEEAEKAADESERgmKVIENRAMKDEEKMDvqemQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSElk 189
Cdd:COG4913    308 EAELERLEARLDALRE--ELDELEAQIRGNGGD----RLEQLEREIERLERELEERERRRARLEALLAALGLPLPASA-- 379

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038132594  190 cSDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDEL 260
Cdd:COG4913    380 -EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 33-260 7.51e-04

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: 40.82  E-value: 7.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   33 EDKFKQVEDELVALQKKLKGTEDELDKYsEALKDAQEKLEQAE--KKATDAEGDVAALNRRIQLVEEELDRAQERLATAL 110
Cdd:TIGR02169  186 IERLDLIIDEKRQQLERLRREREKAERY-QALLKEKREYEGYEllKEKEALERQKEAIERQLASLEEELEKLTEEISELE 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  111 QKLEEAEKAADE-SERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELK 189
Cdd:TIGR02169  265 KRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE 344

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038132594  190 CSDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDEL 260
Cdd:TIGR02169  345 IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEEL 415
PTZ00121 PTZ00121
MAEBL; Provisional
 2-259 7.72e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 7.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594    2 EAIKKKMQMLKLDKENAIDRAEQAEADKKAAEDKFKQVEDELVALQKKLKGTEDELDKYSEALKDAQEKLEQAEKKATDA 81
Cdd:PTZ00121  1543 EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   82 EGDVAALNRRIQLVEEELDRAQE-RLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADR 160
Cdd:PTZ00121  1623 EELKKAEEEKKKVEQLKKKEAEEkKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  161 KYEEVARKlvilegeleRAEERAEVSELKCSdlEEELKNVTNNLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAE 240
Cdd:PTZ00121  1703 KAEELKKK---------EAEEKKKAEELKKA--EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAE 1771

                          250
                   ....*....|....*....
gi 2038132594  241 FAERTVTKLEKAIDDLEDE 259
Cdd:PTZ00121  1772 EIRKEKEAVIEEELDEEDE 1790
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2-116 8.65e-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: 8.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594    2 EAIKKKMQMLKLDKENAIDRAEQAEADKKAAEDKFKQVEDELVALQKKLKGT----EDELDKYSEALKDAQEKLEQAEKK 77
Cdd:COG4913    341 EQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALlealEEELEALEEALAEAEAALRDLRRE 420

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2038132594   78 ATDAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEA 116
Cdd:COG4913    421 LRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAE 459
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
3-274 9.20e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 9.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   3 AIKKKMQMLKLDKENAIDRAEQAEADKKAAEDKFKQVEDELVALQKKLKGTEDELDKYSEALKDAQEKLEQAEKKATDAE 82
Cdd:COG4372    28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  83 GDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKY 162
Cdd:COG4372   108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDE 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594 163 EEVARKLVILEGELERAEERAEVSELKCSDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFA 242
Cdd:COG4372   188 LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2038132594 243 ERTVTKLEKAIDDLEDELYTQKLKYKAISEEL 274
Cdd:COG4372   268 LVEKDTEEEELEIAALELEALEEAALELKLLA 299
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
66-269 1.14e-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: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   66 DAQEKLEQAEKKATDAEGDVAALNRRIQLVEEELDRAQERLAtALQKLEEaekaADESERGMKVIENRAMKDEEKMDvqe 145
Cdd:COG4913    607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERRE-ALQRLAE----YSWDEIDVASAEREIAELEAELE--- 678

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  146 mQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKCSDLEEELKNVTNNLKSLEAQSEkySEKEDKYEEEI 225
Cdd:COG4913    679 -RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR--LELRALLEERF 755

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2038132594  226 KILTDKLKEAETRAEFAERtVTKLEKAIDDLEDELYTQKLKYKA 269
Cdd:COG4913    756 AAALGDAVERELRENLEER-IDALRARLNRAEEELERAMRAFNR 798
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
2-129 1.14e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 40.23  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   2 EAIKKKMQMLKLDKENAIDRAEQAEADKKAAEDKF-----KQVEdELVALQKKLKGTEDELDKYSEALKDAQEKLEQAEK 76
Cdd:COG2433   380 EALEELIEKELPEEEPEAEREKEHEERELTEEEEEirrleEQVE-RLEAEVEELEAELEEKDERIERLERELSEARSEER 458

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2038132594  77 KATDAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKV 129
Cdd:COG2433   459 REIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSGELV 511
PTZ00121 PTZ00121
MAEBL; Provisional
 2-251 1.21e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594    2 EAIKKKMQMLKLDKE--NAIDRAEQAEADKKAAEDKFKQVEDELVALQKKLKGTEDELDKYSEALKDAQEKLEQAEKKAT 79
Cdd:PTZ00121  1493 EEAKKKADEAKKAAEakKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKA 1572

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   80 DAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAmKDEEKMDVQEMQLKEAKHIAEEAD 159
Cdd:PTZ00121  1573 EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK-AEEEKKKVEQLKKKEAEEKKKAEE 1651

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  160 RKYEEVARKLVILEGELERAEERAEVSELKCSdlEEELKNVTNNLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRA 239
Cdd:PTZ00121  1652 LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA--EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENK 1729

                          250
                   ....*....|..
gi 2038132594  240 EFAERTVTKLEK 251
Cdd:PTZ00121  1730 IKAEEAKKEAEE 1741
PRK12704 PRK12704
phosphodiesterase; Provisional
 1-172 1.39e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   1 MEAIKKKMQMLKldKENAIDRAEQAEADKKAAEDKFKQVEDELVALQKKLKGTEDELDKYSEALKDAQEKLEQAEKKatd 80
Cdd:PRK12704   44 LEEAKKEAEAIK--KEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKE--- 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  81 aegdvaaLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMkVIENraMKDEEKMDVQEMQLKEAKHIAEEADR 160
Cdd:PRK12704  119 -------LEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEI-LLEK--VEEEARHEAAVLIKEIEEEAKEEADK 188

                         170
                  ....*....|..
gi 2038132594 161 KyeevARKLVIL 172
Cdd:PRK12704  189 K----AKEILAQ 196
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
14-260 1.69e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 1.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  14 DKENAIDRAEQAEADKKAAEdkfkqVEDELVALQKKLKGTEDELDKYSEALKDAQEKLEQAEKKATDAEGDVAalnrRIQ 93
Cdd:PRK02224  184 DQRGSLDQLKAQIEEKEEKD-----LHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE----ELE 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  94 LVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILE 173
Cdd:PRK02224  255 TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECR 334

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594 174 GELERAEERAEVSELKCSDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAI 253
Cdd:PRK02224  335 VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL 414


                  ....*..
gi 2038132594 254 DDLEDEL 260
Cdd:PRK02224  415 EELREER 421
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
 16-220 1.92e-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: 39.82  E-value: 1.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   16 ENAIDRAEQAEADKKAAEDKFKQVEDELVALQKKLKGTE------------DELDKYSEA----LKDAQEKLEQAEKKAT 79
Cdd:NF012221  1558 QNALADKERAEADRQRLEQEKQQQLAAISGSQSQLESTDqnaletngqaqrDAILEESRAvtkeLTTLAQGLDALDSQAT 1637

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   80 DAE--GD------VAALNRRIQ--------LVEEELDRAQERLATALQKLEEAEKaadESERGMkvienraMKDEEKMDV 143
Cdd:NF012221  1638 YAGesGDqwrnpfAGGLLDRVQeqlddakkISGKQLADAKQRHVDNQQKVKDAVA---KSEAGV-------AQGEQNQAN 1707

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038132594  144 QEMQLKEAKHIAEEadRKYEEVARKlviLEGELERAEERAEVSELKcSDLEEELKNVTNnlKSLEAQSEKYSEKEDK 220
Cdd:NF012221  1708 AEQDIDDAKADAEK--RKDDALAKQ---NEAQQAESDANAAANDAQ-SRGEQDASAAEN--KANQAQADAKGAKQDE 1776
PTZ00121 PTZ00121
MAEBL; Provisional
 2-252 2.40e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 2.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594    2 EAIKKKMQMLKLDKENAIDRAEQAEADKKAAEDKFKQveDELVALQKKLKGTEDELDKYSEALKDAQEKLEQAEKKATDA 81
Cdd:PTZ00121  1281 DELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKA--DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADE 1358

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   82 EGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMDVQEMQLK--------EAKH 153
Cdd:PTZ00121  1359 AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKaeekkkadEAKK 1438

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  154 IAEEAdRKYEEVARKlviLEGELERAEERAEVSELKCSDleeELKNVTNNLKSLEAQSEKYSEKEDKYEEEIKILTDKLK 233
Cdd:PTZ00121  1439 KAEEA-KKADEAKKK---AEEAKKAEEAKKKAEEAKKAD---EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK 1511

                          250
                   ....*....|....*....
gi 2038132594  234 EAETRAEFAERTVTKLEKA 252
Cdd:PTZ00121  1512 ADEAKKAEEAKKADEAKKA 1530
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-160 2.94e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 2.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   2 EAIKKKMQMLKLDKENAIDRAEQAEADKKAAEDKFKQVEDELVALQKKLKGTEDELDKYSEALKDAQEKLEQAEKKATDA 81
Cdd:COG1196   350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038132594  82 EGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADR 160
Cdd:COG1196   430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
 14-121 3.22e-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: 38.55  E-value: 3.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  14 DKENAIDRAEQAEADKKAAEDKFKQVEDELvalQKKLKGTEDELDKYSEALKDAQEKLEQAEKKATD-AEGDVAALNRRI 92
Cdd:TIGR04320 251 NPPNSLAALQAKLATAQADLAAAQTALNTA---QAALTSAQTAYAAAQAALATAQKELANAQAQALQtAQNNLATAQAAL 327

                          90       100
                  ....*....|....*....|....*....
gi 2038132594  93 QLVEEELDRAQERLATALQKLEEAEKAAD 121
Cdd:TIGR04320 328 ANAEARLAKAKEALANLNADLAKKQAALD 356
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
 23-123 5.44e-03

Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.


Pssm-ID: 310534 [Multi-domain]  Cd Length: 258  Bit Score: 37.39  E-value: 5.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  23 EQAEADKKAAEDKFKQVEDELVALQKKLKG----TEDELDKYSEALKDAQEKLEQAEKKATDAEGdvaaLNRRIQLVEEE 98
Cdd:pfam06008 144 QNAEAELKAAQDLLSRIQTWFQSPQEENKAlanaLRDSLAEYEAKLSDLRELLREAAAKTRDANR----LNLANQANLRE 219

                          90       100
                  ....*....|....*....|....*
gi 2038132594  99 LDRAQERLATALQKLEEAEKAADES 123
Cdd:pfam06008 220 FQRKKEEVSEQKNQLEETLKTARDS 244
PTZ00121 PTZ00121
MAEBL; Provisional
 2-277 5.68e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.20  E-value: 5.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594    2 EAIKKKMQMLKLDKENAIDRAEQAEADKKAAEDKFKQVEDELVALQKKL---KGTEDELDKYSEALKDAQEKLEQAEKKA 78
Cdd:PTZ00121  1325 EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKeeaKKKADAAKKKAEEKKKADEAKKKAEEDK 1404

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   79 TDAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM---KVIENRAMKDEEKMDVQEMQLK-EAKHI 154
Cdd:PTZ00121  1405 KKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAeeaKKAEEAKKKAEEAKKADEAKKKaEEAKK 1484

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  155 AEEADRKYEEVARKLVILEGELERAEE---------------------RAEVSELKCSDLEEELKNVTNNLKSLEAQSEK 213
Cdd:PTZ00121  1485 ADEAKKKAEEAKKKADEAKKAAEAKKKadeakkaeeakkadeakkaeeAKKADEAKKAEEKKKADELKKAEELKKAEEKK 1564

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038132594  214 YSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDELYTQKLKYKAISEELDHA 277
Cdd:PTZ00121  1565 KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA 1628
mukB PRK04863
chromosome partition protein MukB;
57-275 6.49e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 38.01  E-value: 6.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   57 LDKYSEALKDAQEKLEQAEKKATDAEGDVAALNRRIQLVEEELDRAQERLA-----------------TALQKLEEAEK- 118
Cdd:PRK04863   350 IERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLAdyqqaldvqqtraiqyqQAVQALERAKQl 429

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  119 --AADESERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELkCSDLEEE 196
Cdd:PRK04863   430 cgLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVAREL-LRRLREQ 508

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594  197 lKNVTNNLKSLEAQ---SEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDELYTQKLKYKAISEE 273
Cdd:PRK04863   509 -RHLAEQLQQLRMRlseLEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQ 587


                   ..
gi 2038132594  274 LD 275
Cdd:PRK04863   588 LE 589
PTZ00121 PTZ00121
MAEBL; Provisional
 12-236 7.93e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.81  E-value: 7.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   12 KLDKENAIDRAEQAEADKKAAEDKFKQVEDELVALQKKLKGTE----DELDKYSEALKDAQEKLEQAEKKATDAEGDVAA 87
Cdd:PTZ00121  1439 KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEakkaDEAKKKAEEAKKKADEAKKAAEAKKKADEAKKA 1518

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038132594   88 LNRR----IQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEeadRKYE 163
Cdd:PTZ00121  1519 EEAKkadeAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE---ARIE 1595

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2038132594  164 EVARKLVILEGELERAEERAEVSELKCSDL--EEELKNVTNNLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAE 236
Cdd:PTZ00121  1596 EVMKLYEEEKKMKAEEAKKAEEAKIKAEELkkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA 1670
 
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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