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Conserved domains on  [gi|78000190|ref|NP_001029241|]
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tropomyosin alpha-1 chain isoform Tpm1.6cy [Rattus norvegicus]

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 8.24e-71

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: 217.97  E-value: 8.24e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    48 KKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 127
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   128 KVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSL 207
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 78000190   208 EAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEENLSMHQMLDQTLLELN 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 8.24e-71

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: 217.97  E-value: 8.24e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    48 KKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 127
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   128 KVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSL 207
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 78000190   208 EAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEENLSMHQMLDQTLLELN 282
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
5-266 3.14e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 75.74  E-value: 3.14e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   5 KKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEAD 84
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190  85 VASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEE 164
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190 165 VARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAER 244
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
                       250       260
                ....*....|....*....|..
gi 78000190 245 SVTKLEKSIDDLEEKVAHAKEE 266
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEE 485
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
37-266 1.81e-13

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: 70.47  E-value: 1.81e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190     37 KQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEA 116
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    117 EKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEE 196
Cdd:TIGR02168  767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    197 LKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEE 266
Cdd:TIGR02168  847 IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
2-257 1.02e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 55.82  E-value: 1.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    2 DAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDA 81
Cdd:PRK02224 324 EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA 403
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   82 EADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESER----------GMKVIES----RAQKDEEKMEIQEIQ 147
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecGQPVEGSphveTIEEDRERVEELEAE 483
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190  148 LKEAKHIAEDADRKYEEvARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKV 227
Cdd:PRK02224 484 LEDLEEEVEEVEERLER-AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAE 562
                        250       260       270
                 ....*....|....*....|....*....|
gi 78000190  228 LSDKLKEAETRAEFAERSVTKLEKSIDDLE 257
Cdd:PRK02224 563 AEEEAEEAREEVAELNSKLAELKERIESLE 592
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
16-220 5.25e-07

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: 50.99  E-value: 5.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    16 ENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTE------------DELDKYSEA----LKDAQEKLELAEKKAT 79
Cdd:NF012221 1558 QNALADKERAEADRQRLEQEKQQQLAAISGSQSQLESTDqnaletngqaqrDAILEESRAvtkeLTTLAQGLDALDSQAT 1637
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    80 DAEAdvASLNRRIQLVEEELDRAQERLATALQ----KLEEAEKAADESERGMK--VIESRA--QKDEEKMEIQEIQLKEA 151
Cdd:NF012221 1638 YAGE--SGDQWRNPFAGGLLDRVQEQLDDAKKisgkQLADAKQRHVDNQQKVKdaVAKSEAgvAQGEQNQANAEQDIDDA 1715
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 78000190   152 KhiaEDADRKYEEVARKlviiESDLERAEERAELSEGKcAELEEELKTVTNNLKSLEAQAEKYSQKEDK 220
Cdd:NF012221 1716 K---ADAEKRKDDALAK----QNEAQQAESDANAAAND-AQSRGEQDASAAENKANQAQADAKGAKQDE 1776
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
7-234 6.20e-03

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 38.07  E-value: 6.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    7 KMQMLKLDKENALDRAEQAEADKKAA----EDRS-------KQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAE 75
Cdd:NF033838 131 KKDTLEPGKKVAEATKKVEEAEKKAKdqkeEDRRnyptntyKTLELEIAESDVEVKKAELELVKEEAKEPRDEEKIKQAK 210
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   76 KKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESER------------------------------ 125
Cdd:NF033838 211 AKVESKKAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKpkrrakrgvlgepatpdkkendakssdssv 290
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190  126 GMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDAD----RKYEEVARK---LVIIESDLERAEERAEL--SEGKCAELEEE 196
Cdd:NF033838 291 GEETLPSPSLKPEKKVAEAEKKVEEAKKKAKDQKeedrRNYPTNTYKtleLEIAESDVKVKEAELELvkEEAKEPRNEEK 370
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 78000190  197 LKTVTNNLKSLEAQA---EKYSQKEDKYEEEIK---VLSDKLKE 234
Cdd:NF033838 371 IKQAKAKVESKKAEAtrlEKIKTDRKKAEEEAKrkaAEEDKVKE 414
 
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 8.24e-71

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: 217.97  E-value: 8.24e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    48 KKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 127
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   128 KVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSL 207
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 78000190   208 EAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEENLSMHQMLDQTLLELN 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 4.68e-27

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: 102.38  E-value: 4.68e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190     7 KMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEadva 86
Cdd:pfam12718   1 KMNSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNE---- 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 78000190    87 SLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAK 152
Cdd:pfam12718  77 NLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKEAK 142
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
5-266 3.14e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 75.74  E-value: 3.14e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   5 KKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEAD 84
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190  85 VASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEE 164
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190 165 VARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAER 244
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
                       250       260
                ....*....|....*....|..
gi 78000190 245 SVTKLEKSIDDLEEKVAHAKEE 266
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEE 485
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1-283 4.35e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 75.36  E-value: 4.35e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   1 MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATD 80
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190  81 AEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADR 160
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190 161 KYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAE 240
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 78000190 241 FAERSVTKLEKSIDDLEEKVAHAKEENLSMHQMLDQTLLELNN 283
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
37-266 1.81e-13

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: 70.47  E-value: 1.81e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190     37 KQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEA 116
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    117 EKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEE 196
Cdd:TIGR02168  767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    197 LKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEE 266
Cdd:TIGR02168  847 IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
21-282 3.68e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.58  E-value: 3.68e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190  21 RAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELD 100
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190 101 RAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAE 180
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190 181 ERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKV 260
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
                       250       260
                ....*....|....*....|..
gi 78000190 261 AHAKEENLSMHQMLDQTLLELN 282
Cdd:COG1196 466 AELLEEAALLEAALAELLEELA 487
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
22-268 5.23e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.11  E-value: 5.23e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190  22 AEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDR 101
Cdd:COG1196 206 ERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE 285
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190 102 AQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEE 181
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190 182 RAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVA 261
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445

                ....*..
gi 78000190 262 HAKEENL 268
Cdd:COG1196 446 EAAEEEA 452
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
21-261 8.67e-11

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 62.38  E-value: 8.67e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190     21 RAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELD 100
Cdd:TIGR02168  734 DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    101 RAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAE 180
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    181 ERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKE--------AETRAEFAERSVTKLEKS 252
Cdd:TIGR02168  894 SELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEeysltleeAEALENKIEDDEEEARRR 973

                   ....*....
gi 78000190    253 IDDLEEKVA 261
Cdd:TIGR02168  974 LKRLENKIK 982
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
18-239 2.39e-10

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: 60.55  E-value: 2.39e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190  18 ALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEE 97
Cdd:COG4942  18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190  98 ELDRAQERLATALQKLEEAEKA-----------ADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVA 166
Cdd:COG4942  98 ELEAQKEELAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 78000190 167 RKLViiesdlERAEERAELSEGKcAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRA 239
Cdd:COG4942 178 ALLA------ELEEERAALEALK-AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
5-281 3.95e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.46  E-value: 3.95e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190      5 KKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEAD 84
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190     85 VASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIES-----RAQKDEEKMEIQEIQLKEAKHIAEDAD 159
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREaldelRAELTLLNEEAANLRERLESLERRIAA 835
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    160 --RKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAET 237
Cdd:TIGR02168  836 teRRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 78000190    238 RAEFAERSVTKLEKSIDDLEEKVAHAKEENLSMHQMLDQTLLEL 281
Cdd:TIGR02168  916 ELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEAL 959
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
48-283 5.49e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.95  E-value: 5.49e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190  48 KKLKGTEDELDKYSEALKD--AQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESER 125
Cdd:COG1196 216 RELKEELKELEAELLLLKLreLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190 126 GMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLK 205
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 78000190 206 SLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEENLSMHQMLDQTLLELNN 283
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4-282 8.73e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 59.30  E-value: 8.73e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190      4 IKKKMQMLKLDKENALD----RAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKAT 79
Cdd:TIGR02168  198 LERQLKSLERQAEKAERykelKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS 277
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190     80 DAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDAD 159
Cdd:TIGR02168  278 ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    160 RKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRA 239
Cdd:TIGR02168  358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE 437
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 78000190    240 efAERSVTKLEKSIDDLEEKVAHAKEENLSMHQMLDQTLLELN 282
Cdd:TIGR02168  438 --LQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
31-269 9.07e-10

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: 58.62  E-value: 9.07e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190  31 AAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATAL 110
Cdd:COG4942  17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190 111 QKLEEAEkaaDESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAelsegkc 190
Cdd:COG4942  97 AELEAQK---EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR------- 166
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 78000190 191 AELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEENLS 269
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
34-266 4.73e-09

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 57.00  E-value: 4.73e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190     34 DRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKL 113
Cdd:TIGR02169  681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL 760
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    114 EEAEKAADESErgmkviesrAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAEL 193
Cdd:TIGR02169  761 KELEARIEELE---------EDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 78000190    194 EEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEE 266
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK 904
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
63-284 9.26e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.22  E-value: 9.26e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190     63 ALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKME 142
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    143 IQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYE 222
Cdd:TIGR02168  758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 78000190    223 EEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEENLSMHQMLDQTLLELNNM 284
Cdd:TIGR02168  838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
2-257 1.02e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 55.82  E-value: 1.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    2 DAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDA 81
Cdd:PRK02224 324 EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA 403
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   82 EADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESER----------GMKVIES----RAQKDEEKMEIQEIQ 147
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecGQPVEGSphveTIEEDRERVEELEAE 483
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190  148 LKEAKHIAEDADRKYEEvARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKV 227
Cdd:PRK02224 484 LEDLEEEVEEVEERLER-AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAE 562
                        250       260       270
                 ....*....|....*....|....*....|
gi 78000190  228 LSDKLKEAETRAEFAERSVTKLEKSIDDLE 257
Cdd:PRK02224 563 AEEEAEEAREEVAELNSKLAELKERIESLE 592
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
6-256 1.30e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.83  E-value: 1.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190      6 KKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEADV 85
Cdd:TIGR02168  747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190     86 ASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRkyeev 165
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE----- 901
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    166 arklviiesDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQ-AEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAER 244
Cdd:TIGR02168  902 ---------ELRELESKRSELRRELEELREKLAQLELRLEGLEVRiDNLQERLSEEYSLTLEEAEALENKIEDDEEEARR 972
                          250
                   ....*....|..
gi 78000190    245 SVTKLEKSIDDL 256
Cdd:TIGR02168  973 RLKRLENKIKEL 984
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1-276 2.06e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.06  E-value: 2.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190      1 MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATD 80
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190     81 AEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMeiqeiqlkeakhiaEDADR 160
Cdd:TIGR02168  321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL--------------ETLRS 386
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    161 KYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKslEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAE 240
Cdd:TIGR02168  387 KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQEELERLEEALE 464
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 78000190    241 FAERSVTKLEKSIDDLEEKVAHAKEENLSMHQMLDQ 276
Cdd:TIGR02168  465 ELREELEEAEQALDAAERELAQLQARLDSLERLQEN 500
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
23-262 2.72e-08

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 54.55  E-value: 2.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   23 EQAEADKKAAEDRSK--QLEDELVSLQKKLKGTEDELDKYS-----EALKDAQEKLELAEKKATDAEADVASLNRRIQLV 95
Cdd:PRK05771  40 LSNERLRKLRSLLTKlsEALDKLRSYLPKLNPLREEKKKVSvksleELIKDVEEELEKIEKEIKELEEEISELENEIKEL 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   96 EEELDRAQerlatALQKLEEAEKAADESERgMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVA---RKLVII 172
Cdd:PRK05771 120 EQEIERLE-----PWGNFDLDLSLLLGFKY-VSVFVGTVPEDKLEELKLESDVENVEYISTDKGYVYVVVVvlkELSDEV 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190  173 ESDLERAE-ERAELSEGKC-----AELEEELKTVTNNLKSLEAQAEKYSQkedKYEEEIKVLSDKL----KEAETRAEFA 242
Cdd:PRK05771 194 EEELKKLGfERLELEEEGTpseliREIKEELEEIEKERESLLEELKELAK---KYLEELLALYEYLeielERAEALSKFL 270
                        250       260       270
                 ....*....|....*....|....*....|...
gi 78000190  243 -------------ERSVTKLEKSIDDLEEKVAH 262
Cdd:PRK05771 271 ktdktfaiegwvpEDRVKKLKELIDKATGGSAY 303
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
20-246 6.65e-08

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 53.53  E-value: 6.65e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190     20 DRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQ------ 93
Cdd:TIGR02169  273 LLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEeerkrr 352
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190     94 -LVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVII 172
Cdd:TIGR02169  353 dKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78000190    173 ESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSV 246
Cdd:TIGR02169  433 EAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
66-266 4.27e-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: 4.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   66 DAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQERLAtALQKLEEaekaADESERGMKVIESRAQkdeekmeiqe 145
Cdd:COG4913  607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERRE-ALQRLAE----YSWDEIDVASAEREIA---------- 671
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190  146 iQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEi 225
Cdd:COG4913  672 -ELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA- 749
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 78000190  226 kvLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEE 266
Cdd:COG4913  750 --LLEERFAAALGDAVERELRENLEERIDALRARLNRAEEE 788
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
16-220 5.25e-07

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: 50.99  E-value: 5.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    16 ENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTE------------DELDKYSEA----LKDAQEKLELAEKKAT 79
Cdd:NF012221 1558 QNALADKERAEADRQRLEQEKQQQLAAISGSQSQLESTDqnaletngqaqrDAILEESRAvtkeLTTLAQGLDALDSQAT 1637
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    80 DAEAdvASLNRRIQLVEEELDRAQERLATALQ----KLEEAEKAADESERGMK--VIESRA--QKDEEKMEIQEIQLKEA 151
Cdd:NF012221 1638 YAGE--SGDQWRNPFAGGLLDRVQEQLDDAKKisgkQLADAKQRHVDNQQKVKdaVAKSEAgvAQGEQNQANAEQDIDDA 1715
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 78000190   152 KhiaEDADRKYEEVARKlviiESDLERAEERAELSEGKcAELEEELKTVTNNLKSLEAQAEKYSQKEDK 220
Cdd:NF012221 1716 K---ADAEKRKDDALAK----QNEAQQAESDANAAAND-AQSRGEQDASAAENKANQAQADAKGAKQDE 1776
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
22-241 1.02e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 49.63  E-value: 1.02e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190  22 AEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEalkdaQEKLELAEKKATDAEADVASLNRRIQLVEEELDR 101
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQ-----KNGLVDLSEEAKLLLQQLSELESQLAEARAELAE 237
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190 102 AQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEI---------QLKEAKH-IAEDADRKYEEVARKLVI 171
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELsarytpnhpDVIALRAqIAALRAQLQQEAQRILAS 317
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190 172 IESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEeikvLSDKLKEAETRAEF 241
Cdd:COG3206 318 LEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES----LLQRLEEARLAEAL 383
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2-215 1.27e-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: 49.67  E-value: 1.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190      2 DAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDA 81
Cdd:TIGR02168  298 SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190     82 EADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESergmkviesRAQKDEEKMEIQEIQLKEAKHIAEDADRK 161
Cdd:TIGR02168  378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL---------QQEIEELLKKLEEAELKELQAELEELEEE 448
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 78000190    162 YEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYS 215
Cdd:TIGR02168  449 LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
20-276 1.84e-06

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: 49.18  E-value: 1.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   20 DRAEQAEADKKAAEDRSkQLEDELVSLQKKLkgtedelDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEEL 99
Cdd:COG3096  320 ARESDLEQDYQAASDHL-NLVQTALRQQEKI-------ERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEV 391
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190  100 DRAQERLA-----------------TALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKH---IAEDAD 159
Cdd:COG3096  392 DSLKSQLAdyqqaldvqqtraiqyqQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQklsVADAAR 471
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190  160 RKYEEVARKLVIIESDLERAEE----RAELSEGKcaeleeELKTVTNNLKSLEAQ---AEKYSQKEDKYEEEIKVLSDKL 232
Cdd:COG3096  472 RQFEKAYELVCKIAGEVERSQAwqtaRELLRRYR------SQQALAQRLQQLRAQlaeLEQRLRQQQNAERLLEEFCQRI 545
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 78000190  233 KEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEENLSMHQMLDQ 276
Cdd:COG3096  546 GQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQ 589
PTZ00121 PTZ00121
MAEBL; Provisional
5-267 3.91e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 3.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190     5 KKKMQMLKLDKENALDRAEQ---AEADKKAAEDRSKQLEDELVSLQKKLKGTE----DELDKYSEALKDAQEKLELAEKK 77
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADElkkAAAAKKKADEAKKKAEEKKKADEAKKKAEEakkaDEAKKKAEEAKKAEEAKKKAEEA 1469
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    78 ATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIES-RAQKDEEKMEIQEIQLKEAKHIAE 156
Cdd:PTZ00121 1470 KKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAdEAKKAEEAKKADEAKKAEEKKKAD 1549
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   157 DADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAE 236
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
                         250       260       270
                  ....*....|....*....|....*....|.
gi 78000190   237 TRAEFAERSVTKLEKSIDDLEEkVAHAKEEN 267
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEE-LKKAEEEN 1659
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
24-240 4.00e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.52  E-value: 4.00e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190  24 QAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRA- 102
Cdd:COG3883  13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERa 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190 103 -----QERLATALQKLEEAEKAADESERgMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLE 177
Cdd:COG3883  93 ralyrSGGSVSYLDVLLGSESFSDFLDR-LSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 78000190 178 RAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAE 240
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
90-284 5.00e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 5.00e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190  90 RRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKL 169
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190 170 VIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKL 249
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
                       170       180       190
                ....*....|....*....|....*....|....*
gi 78000190 250 EKSIDDLEEKVAHAKEENLSMHQMLDQTLLELNNM 284
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
59-266 6.48e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 6.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190     59 KYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQE------------------RLATALQKLEEAEKAA 120
Cdd:TIGR02168  169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERykelkaelrelelallvlRLEELREELEELQEEL 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    121 DESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTV 200
Cdd:TIGR02168  249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 78000190    201 TNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEE 266
Cdd:TIGR02168  329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
52-266 1.27e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.57  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   52 GTEDELDKYSEALKDAQEklELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESErgmkviE 131
Cdd:PRK02224 177 GVERVLSDQRGSLDQLKA--QIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHE------E 248
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190  132 SRAQKDEEKMEIQEIQ----------------LKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEE 195
Cdd:PRK02224 249 RREELETLEAEIEDLRetiaeterereelaeeVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRD 328
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 78000190  196 ELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEE 266
Cdd:PRK02224 329 RLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRER 399
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2-179 1.55e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 1.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    2 DAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRS----------------KQLEDELVSLQKKLkgteDELDKYSEALK 65
Cdd:COG4913  613 AALEAELAELEEELAEAEERLEALEAELDALQERRealqrlaeyswdeidvASAEREIAELEAEL----ERLDASSDDLA 688
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   66 DAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERgmkviesraqKDEEKMEIQE 145
Cdd:COG4913  689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR----------ALLEERFAAA 758
                        170       180       190
                 ....*....|....*....|....*....|....
gi 78000190  146 IQLKEAKHIAEDADRKYEEVARKLVIIESDLERA 179
Cdd:COG4913  759 LGDAVERELRENLEERIDALRARLNRAEEELERA 792
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
15-229 3.04e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.01  E-value: 3.04e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190  15 KENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLK---------GTEDELDKYSEALKDAQEKLELAEKKATDAEADV 85
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEefrqknglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190  86 ASLNRRIQLVEEEL-----DRAQERLATALQKLE--EAEKAADESERGMKVIESRAQKDEEKMEIQEiqlkEAKHIAEDA 158
Cdd:COG3206 243 AALRAQLGSGPDALpellqSPVIQQLRAQLAELEaeLAELSARYTPNHPDVIALRAQIAALRAQLQQ----EAQRILASL 318
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78000190 159 DRKYEEVARKLVIIESDLERAEERAEL---SEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLS 229
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAElpeLEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVID 392
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
19-242 3.22e-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: 3.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   19 LDRAEQAEADKKAAEDRSKQLEDELVSLQKkLKGTEDELDKYSEALKD--AQEKLELAEKKATDAEADVASLNRRIQLVE 96
Cdd:COG4913  237 LERAHEALEDAREQIELLEPIRELAERYAA-ARERLAELEYLRAALRLwfAQRRLELLEAELEELRAELARLEAELERLE 315
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   97 EELDRAQERLATALQKLEEAE-KAADESERGMKVIESRAQKDEEKMEIQEIQLK----EAKHIAEDADRKYEEVARKLVI 171
Cdd:COG4913  316 ARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAalglPLPASAEEFAALRAEAAALLEA 395
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 78000190  172 IESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQkedKYEEEIKVLSDKLKEAETRAEFA 242
Cdd:COG4913  396 LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPA---RLLALRDALAEALGLDEAELPFV 463
PTZ00121 PTZ00121
MAEBL; Provisional
5-270 3.59e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 3.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190     5 KKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEAD 84
Cdd:PTZ00121 1342 KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAD 1421
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    85 VASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEE 164
Cdd:PTZ00121 1422 EAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADE 1501
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   165 VARKLVIIE--SDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVlsDKLKEAETRAEFA 242
Cdd:PTZ00121 1502 AKKAAEAKKkaDEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKA--EEAKKAEEDKNMA 1579
                         250       260
                  ....*....|....*....|....*...
gi 78000190   243 ERSVTKLEKSIDDLEEKVAHAKEENLSM 270
Cdd:PTZ00121 1580 LRKAEEAKKAEEARIEEVMKLYEEEKKM 1607
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
12-176 3.64e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 3.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   12 KLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEA---------------LKDAQEKLELAEK 76
Cdd:COG4913  280 ALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgnggdrleqlereIERLERELEERER 359
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   77 KATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEiQEIQLKEAKH--I 154
Cdd:COG4913  360 RRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE-AEIASLERRKsnI 438
                        170       180
                 ....*....|....*....|..
gi 78000190  155 AEDADRKYEEVARKLVIIESDL 176
Cdd:COG4913  439 PARLLALRDALAEALGLDEAEL 460
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
23-233 4.11e-05

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 45.04  E-value: 4.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    23 EQAEADKKAAE-DRSKQLEDELVSLQKKlKGTEDELDKYSEALKD---------AQEKLELAEKKATDAEADVASLNRRI 92
Cdd:PRK10929   33 EQAKAAKTPAQaEIVEALQSALNWLEER-KGSLERAKQYQQVIDNfpklsaelrQQLNNERDEPRSVPPNMSTDALEQEI 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    93 -----QLVEE------ELDRAQE---RLATALQKLEEAEKAADESERGMKVIESRAQKDEEkmeiqeiqlkeakhiAEDA 158
Cdd:PRK10929  112 lqvssQLLEKsrqaqqEQDRAREisdSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQ---------------AQLT 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   159 DRKYEEVARKLVIIESDL---------ERAEERAELSEGKCAELEEELKTVTNNLKSLEAQ-AEKYSQKEDKYEEEI--- 225
Cdd:PRK10929  177 ALQAESAALKALVDELELaqlsannrqELARLRSELAKKRSQQLDAYLQALRNQLNSQRQReAERALESTELLAEQSgdl 256

                  ....*....
gi 78000190   226 -KVLSDKLK 233
Cdd:PRK10929  257 pKSIVAQFK 265
PTZ00121 PTZ00121
MAEBL; Provisional
20-271 4.44e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 4.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    20 DRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEEL 99
Cdd:PTZ00121 1513 DEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEA 1592
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   100 DRAQERLATALQKLEEAEKAADESERGMKVIESRaQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERA 179
Cdd:PTZ00121 1593 RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK-KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE 1671
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   180 EERAELSEGKCAEleEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEK 259
Cdd:PTZ00121 1672 EDKKKAEEAKKAE--EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA 1749
                         250
                  ....*....|..
gi 78000190   260 VAHAKEENLSMH 271
Cdd:PTZ00121 1750 KKDEEEKKKIAH 1761
PTZ00121 PTZ00121
MAEBL; Provisional
6-265 5.25e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 5.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190     6 KKMQMLKLDKENA--LDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKySEALKDAQEKLELAEKKATDAEA 83
Cdd:PTZ00121 1230 KKAEEAKKDAEEAkkAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK-AEEKKKADEAKKAEEKKKADEAK 1308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    84 DVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYE 163
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE 1388
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   164 EVARKlviiesdlERAEERAELSEGKCAELE--EELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEF 241
Cdd:PTZ00121 1389 EKKKA--------DEAKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAE 1460
                         250       260
                  ....*....|....*....|....
gi 78000190   242 AERSVTKLEKSIDDLEEKVAHAKE 265
Cdd:PTZ00121 1461 EAKKKAEEAKKADEAKKKAEEAKK 1484
mukB PRK04863
chromosome partition protein MukB;
15-276 8.19e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 44.18  E-value: 8.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    15 KENALDRAEQA-EADKKAAEDRsKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEAdvaslnrRIQ 93
Cdd:PRK04863  315 ELAELNEAESDlEQDYQAASDH-LNLVQTALRQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEA-------RAE 386
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    94 LVEEELDRAQERLA-----------------TALQKLEEAEK---AADESERGMKVIESRAQKDEEKMEIQEIQLKEAKH 153
Cdd:PRK04863  387 AAEEEVDELKSQLAdyqqaldvqqtraiqyqQAVQALERAKQlcgLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLS 466
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   154 IAEDADRKYEEVARKLVIIESDLERAEERAELSEgKCAELEEElKTVTNNLKSLEAQ---AEKYSQKEDKYEEEIKVLSD 230
Cdd:PRK04863  467 VAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARE-LLRRLREQ-RHLAEQLQQLRMRlseLEQRLRQQQRAERLLAEFCK 544
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 78000190   231 KLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEENLSMHQMLDQ 276
Cdd:PRK04863  545 RLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQ 590
PTZ00121 PTZ00121
MAEBL; Provisional
14-226 8.55e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 8.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    14 DKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQ 93
Cdd:PTZ00121 1575 DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK 1654
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    94 LVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIE 173
Cdd:PTZ00121 1655 AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE 1734
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 78000190   174 SDLERAEERAELSEGKCAElEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIK 226
Cdd:PTZ00121 1735 AKKEAEEDKKKAEEAKKDE-EEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELD 1786
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
47-240 9.95e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 9.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   47 QKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQerLATALQKLEEAEKAADESERG 126
Cdd:COG4913  609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAS--AEREIAELEAELERLDASSDD 686
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190  127 MKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGkcAELEEELKTvtnnlks 206
Cdd:COG4913  687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR--ALLEERFAA------- 757
                        170       180       190
                 ....*....|....*....|....*....|....
gi 78000190  207 lEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAE 240
Cdd:COG4913  758 -ALGDAVERELRENLEERIDALRARLNRAEEELE 790
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
15-265 1.22e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.49  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   15 KENALDRAEQAEADKKAAEDRSKQLED---ELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDA-------EAD 84
Cdd:PRK02224 229 REQARETRDEADEVLEEHEERREELETleaEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLlaeagldDAD 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   85 VASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDA------ 158
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRreeiee 388
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190  159 -DRKYEEVARKLVIIESDLERAEERAELSE-------GKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSD 230
Cdd:PRK02224 389 lEEEIEELRERFGDAPVDLGNAEDFLEELReerdelrEREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVE 468
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 78000190  231 KLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKE 265
Cdd:PRK02224 469 TIEEDRERVEELEAELEDLEEEVEEVEERLERAED 503
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
52-235 1.36e-04

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 43.14  E-value: 1.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190  52 GTEDELDKYSEALKDAQEklelAEKKATDAEADVASLNRRIQLVE---EELDRA------QERLATALQKLEEAEK---- 118
Cdd:COG0497 152 GLEELLEEYREAYRAWRA----LKKELEELRADEAERARELDLLRfqlEELEAAalqpgeEEELEEERRRLSNAEKlrea 227
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190 119 ------AADESERG--------MKVIESRAQKDEEKMEIQEiQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEER-- 182
Cdd:COG0497 228 lqealeALSGGEGGaldllgqaLRALERLAEYDPSLAELAE-RLESALIELEEAASELRRYLDSLEFDPERLEEVEERla 306
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 78000190 183 -------------AELSEgKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEA 235
Cdd:COG0497 307 llrrlarkygvtvEELLA-YAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKKA 371
PTZ00121 PTZ00121
MAEBL; Provisional
1-252 2.02e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 2.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190     1 MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKL--KGTEDELDKYSEalkDAQEKLELAEKKA 78
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAeeAKKADEAKKKAE---EAKKKADAAKKKA 1338
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    79 TDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE----SERGMKVIESRAQKDEEKMEIQEIQLK-EAKH 153
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAakkkAEEKKKADEAKKKAEEDKKKADELKKAaAAKK 1418
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   154 IAEDADRKYEEVARKlviiESDLERAEERAELSEGKcAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLK 233
Cdd:PTZ00121 1419 KADEAKKKAEEKKKA----DEAKKKAEEAKKADEAK-KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE 1493
                         250
                  ....*....|....*....
gi 78000190   234 EAETRAEFAERSVTKLEKS 252
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKA 1512
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
40-265 2.06e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.51  E-value: 2.06e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190  40 EDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKA 119
Cdd:COG3883  15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190 120 ADESERGMKVIEsraqkdeekmeiqeiQLKEAKHIAEDADRkyeeVARKLVIIESD---LERAEERAELSEGKCAELEEE 196
Cdd:COG3883  95 LYRSGGSVSYLD---------------VLLGSESFSDFLDR----LSALSKIADADadlLEELKADKAELEAKKAELEAK 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 78000190 197 LKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKE 265
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
12-129 2.73e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 42.15  E-value: 2.73e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190  12 KLDKENALDRAEQAEADKKAA--EDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKatdaEADVASLN 89
Cdd:COG2433 396 EAEREKEHEERELTEEEEEIRrlEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRK----DREISRLD 471
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 78000190  90 RRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKV 129
Cdd:COG2433 472 REIERLERELEEERERIEELKRKLERLKELWKLEHSGELV 511
PTZ00121 PTZ00121
MAEBL; Provisional
15-273 4.16e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 4.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    15 KENALDRAEQAEADKKAAEDRSKqleDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRiql 94
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEEAKKA---DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK--- 1523
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    95 vEEELDRAQE-RLATALQKLEEAEKAAD--ESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVI 171
Cdd:PTZ00121 1524 -ADEAKKAEEaKKADEAKKAEEKKKADElkKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYE 1602
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   172 IESDLERAEERAELSEGKCAE---LEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTK 248
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAEelkKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682
                         250       260
                  ....*....|....*....|....*
gi 78000190   249 LEKSIDDLEEKVAHAKEENLSMHQM 273
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEAKKAEEL 1707
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
47-284 4.87e-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: 41.58  E-value: 4.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190     47 QKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEAdvaSLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERG 126
Cdd:TIGR02168  178 ERKLERTRENLDRLEDILNELERQLKSLERQAEKAER---YKELKAELRELELALLVLRLEELREELEELQEELKEAEEE 254
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    127 MKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTvtnnlks 206
Cdd:TIGR02168  255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE------- 327
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 78000190    207 LEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEENLSMHQMLDQTLLELNNM 284
Cdd:TIGR02168  328 LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
14-266 5.10e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 5.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   14 DKENALDRAEQAEADKKAAEDRSKQLEDELVSLqkklkgtEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQ 93
Cdd:PRK02224 294 ERDDLLAEAGLDDADAEAVEARREELEDRDEEL-------RDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAA 366
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   94 LVEEELDRAQERLATALQKLEEAEKAADESergmkviesraqkdEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIE 173
Cdd:PRK02224 367 ELESELEEAREAVEDRREEIEELEEEIEEL--------------RERFGDAPVDLGNAEDFLEELREERDELREREAELE 432
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190  174 SDLERAEERAE-----LSEGKCAELEEELK--TVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEfAERSV 246
Cdd:PRK02224 433 ATLRTARERVEeaealLEAGKCPECGQPVEgsPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVE-AEDRI 511
                        250       260
                 ....*....|....*....|
gi 78000190  247 TKLEKSIDDLEEKVAHAKEE 266
Cdd:PRK02224 512 ERLEERREDLEELIAERRET 531
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
3-270 8.19e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 8.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   3 AIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAE 82
Cdd:COG4372  28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190  83 ADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKY 162
Cdd:COG4372 108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDE 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190 163 EEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFA 242
Cdd:COG4372 188 LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
                       250       260
                ....*....|....*....|....*...
gi 78000190 243 ERSVTKLEKSIDDLEEKVAHAKEENLSM 270
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALEL 295
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
74-276 8.23e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.52  E-value: 8.23e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190  74 AEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKh 153
Cdd:COG4942  18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR- 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190 154 iaEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLK 233
Cdd:COG4942  97 --AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 78000190 234 EAETRAEFAERSVTKLEKSIDDLEEKVAHAKEENLSMHQMLDQ 276
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
2-186 8.40e-04

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 40.10  E-value: 8.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190     2 DAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDE---LVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKA 78
Cdd:pfam00529  40 DRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAEldrLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQL 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    79 TDAEADvasLNRRIQLVEEELdRAQERLATALQKLEEAEKAADESergmkvIESRAQKDEEKMEIQEIQLKEAKHIAEDA 158
Cdd:pfam00529 120 AQAQID---LARRRVLAPIGG-ISRESLVTAGALVAQAQANLLAT------VAQLDQIYVQITQSAAENQAEVRSELSGA 189
                         170       180
                  ....*....|....*....|....*...
gi 78000190   159 DRKYEEVARKLVIIESDLERAEERAELS 186
Cdd:pfam00529 190 QLQIAEAEAELKLAKLDLERTEIRAPVD 217
PTZ00121 PTZ00121
MAEBL; Provisional
4-265 1.34e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190     4 IKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKlkgteDELDKYSEALKDAqEKLELAEKKATDAEA 83
Cdd:PTZ00121 1187 VRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKA-----EEAKKDAEEAKKA-EEERNNEEIRKFEEA 1260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    84 DVASLNRRIQLVEEEldraQERLATALQKLEEAEKA--ADESERGMKVIESRaQKDEEKMEIQEIQLK--EAKHIAEDAD 159
Cdd:PTZ00121 1261 RMAHFARRQAAIKAE----EARKADELKKAEEKKKAdeAKKAEEKKKADEAK-KKAEEAKKADEAKKKaeEAKKKADAAK 1335
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   160 RKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKED--KYEEEIKVLSDKLKEAET 237
Cdd:PTZ00121 1336 KKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEakKKAEEDKKKADELKKAAA 1415
                         250       260       270
                  ....*....|....*....|....*....|
gi 78000190   238 RAEFAERSVTKLE--KSIDDLEEKVAHAKE 265
Cdd:PTZ00121 1416 AKKKADEAKKKAEekKKADEAKKKAEEAKK 1445
PTZ00121 PTZ00121
MAEBL; Provisional
2-240 1.72e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190     2 DAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDA 81
Cdd:PTZ00121 1543 EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    82 EAdvaslNRRIQLVEEELDRAQERLATALQKLEEAEKAadESERGMKVIESRAQKDEEKMEIQEI-QLKEAKHIAEDADR 160
Cdd:PTZ00121 1623 EE-----LKKAEEEKKKVEQLKKKEAEEKKKAEELKKA--EEENKIKAAEEAKKAEEDKKKAEEAkKAEEDEKKAAEALK 1695
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   161 KYEEVARKLVIIESDLERAEERAElsegKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAE 240
Cdd:PTZ00121 1696 KEAEEAKKAEELKKKEAEEKKKAE----ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAE 1771
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
83-283 1.88e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 1.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190  83 ADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKA----ADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDA 158
Cdd:COG1196 165 AGISKYKERKEEAERKLEATEENLERLEDILGELERQleplERQAEKAERYRELKEELKELEAELLLLKLRELEAELEEL 244
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190 159 DRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETR 238
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 78000190 239 AEFAERSVTKLEKSIDDLEEKVAHAKEENLSMHQMLDQTLLELNN 283
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2-217 1.98e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.67  E-value: 1.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190      2 DAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDA 81
Cdd:TIGR02169  815 REIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL 894
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190     82 EADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKviesraqkdeekmeiQEIQLKEAKHIAEDADRK 161
Cdd:TIGR02169  895 EAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKG---------------EDEEIPEEELSLEDVQAE 959
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 78000190    162 YEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQK 217
Cdd:TIGR02169  960 LQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
PRK09039 PRK09039
peptidoglycan -binding protein;
46-199 2.79e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 38.79  E-value: 2.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   46 LQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESEr 125
Cdd:PRK09039  44 LSREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELA- 122
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78000190  126 gmkviesrAQKDEEKMEIQeiqlkEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKT 199
Cdd:PRK09039 123 --------QELDSEKQVSA-----RALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNV 183
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
2-100 3.82e-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: 3.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190     2 DAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSE-ALKDAQEKLELAEKKATD 80
Cdd:TIGR04320 257 AALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTAQnNLATAQAALANAEARLAK 336
                          90       100
                  ....*....|....*....|
gi 78000190    81 AEADVASLNRRIQLVEEELD 100
Cdd:TIGR04320 337 AKEALANLNADLAKKQAALD 356
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1-184 4.05e-03

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: 38.50  E-value: 4.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190      1 MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATD 80
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190     81 AEADVASLNRRIQLVEEELDRAQERLATALQKL-EEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDAD 159
Cdd:TIGR02168  913 LRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAI 992
                          170       180
                   ....*....|....*....|....*...
gi 78000190    160 RKYEEVARKLVIIES---DLERAEERAE 184
Cdd:TIGR02168  993 EEYEELKERYDFLTAqkeDLTEAKETLE 1020
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
14-121 4.41e-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: 4.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    14 DKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEK-LELAEKKATDAEADVASLnrri 92
Cdd:TIGR04320 255 SLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQaLQTAQNNLATAQAALANA---- 330
                          90       100
                  ....*....|....*....|....*....
gi 78000190    93 qlvEEELDRAQERLATALQKLEEAEKAAD 121
Cdd:TIGR04320 331 ---EARLAKAKEALANLNADLAKKQAALD 356
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
107-268 4.55e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 37.96  E-value: 4.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190 107 ATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELS 186
Cdd:COG4372  27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190 187 EGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEE 266
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALD 186

                ..
gi 78000190 267 NL 268
Cdd:COG4372 187 EL 188
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
144-239 4.69e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 38.39  E-value: 4.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   144 QEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEE 223
Cdd:PRK11448  140 PENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRK 219
                          90
                  ....*....|....*....
gi 78000190   224 EIKVLSDK---LKEAETRA 239
Cdd:PRK11448  220 EITDQAAKrleLSEEETRI 238
outer_NodT TIGR01845
efflux transporter, outer membrane factor (OMF) lipoprotein, NodT family; Members of this ...
16-112 4.86e-03

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: 38.16  E-value: 4.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    16 ENALDRAEQAEADKKAAEdrsKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKK----------ATDAEADV 85
Cdd:TIGR01845 147 ESALAQLEAAEADSQAAR---LTLSASIANAYVQLAALRAQLDVYHAALASRRKTLELTQKRyaagvaaasdVRQAEAAV 223
                          90       100
                  ....*....|....*....|....*..
gi 78000190    86 ASLNRRIQLVEEELDRAQERLATALQK 112
Cdd:TIGR01845 224 ASAEAELPSLDVQIAQARNALAALLGK 250
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
16-231 5.26e-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: 5.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   16 ENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLkgteDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLV 95
Cdd:COG3096  371 EEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQAL----DVQQTRAIQYQQAVQALEKARALCGLPDLTPENAEDYLAAF 446
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   96 EEELDRAQERLATALQKLEEAEKAADESERGMKVIE------SRAQKDEEKMEIQEiQLKEAKHIAEDAdrkyEEVARKL 169
Cdd:COG3096  447 RAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCkiagevERSQAWQTARELLR-RYRSQQALAQRL----QQLRAQL 521
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 78000190  170 VIIESDLERAEERAELSEGKC-----------------AELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDK 231
Cdd:COG3096  522 AELEQRLRQQQNAERLLEEFCqrigqqldaaeeleellAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAAR 600
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
7-234 6.20e-03

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 38.07  E-value: 6.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    7 KMQMLKLDKENALDRAEQAEADKKAA----EDRS-------KQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAE 75
Cdd:NF033838 131 KKDTLEPGKKVAEATKKVEEAEKKAKdqkeEDRRnyptntyKTLELEIAESDVEVKKAELELVKEEAKEPRDEEKIKQAK 210
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   76 KKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESER------------------------------ 125
Cdd:NF033838 211 AKVESKKAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKpkrrakrgvlgepatpdkkendakssdssv 290
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190  126 GMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDAD----RKYEEVARK---LVIIESDLERAEERAEL--SEGKCAELEEE 196
Cdd:NF033838 291 GEETLPSPSLKPEKKVAEAEKKVEEAKKKAKDQKeedrRNYPTNTYKtleLEIAESDVKVKEAELELvkEEAKEPRNEEK 370
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 78000190  197 LKTVTNNLKSLEAQA---EKYSQKEDKYEEEIK---VLSDKLKE 234
Cdd:NF033838 371 IKQAKAKVESKKAEAtrlEKIKTDRKKAEEEAKrkaAEEDKVKE 414
mukB PRK04863
chromosome partition protein MukB;
27-152 7.53e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 38.01  E-value: 7.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    27 ADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELdRAQERL 106
Cdd:PRK04863  272 ADYMRHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTAL-RQQEKI 350
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 78000190   107 ATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAK 152
Cdd:PRK04863  351 ERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELK 396
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
74-266 7.69e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 37.50  E-value: 7.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190  74 AEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEakh 153
Cdd:COG3883  14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE--- 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190 154 IAEDADRKYEEVARKLVIIES-DLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKL 232
Cdd:COG3883  91 RARALYRSGGSVSYLDVLLGSeSFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
                       170       180       190
                ....*....|....*....|....*....|....
gi 78000190 233 KEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEE 266
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAE 204
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
128-268 7.91e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 37.59  E-value: 7.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190  128 KVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELsegkcAELEEELKTVTNN---L 204
Cdd:COG4913  613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREI-----AELEAELERLDASsddL 687
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78000190  205 KSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEENL 268
Cdd:COG4913  688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL 751
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
23-281 8.86e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 37.74  E-value: 8.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190     23 EQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKyseALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRA 102
Cdd:TIGR02169  173 EKALEELEEVEENIERLDLIIDEKRQQLERLRREREK---AERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASL 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    103 QERLAtalQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEakhiaedadrKYEEVARKLVIIESDLERAEER 182
Cdd:TIGR02169  250 EEELE---KLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKE----------KIGELEAEIASLERSIAEKERE 316
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    183 AELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAH 262
Cdd:TIGR02169  317 LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK 396
                          250
                   ....*....|....*....
gi 78000190    263 AKEENLSMHQMLDQTLLEL 281
Cdd:TIGR02169  397 LKREINELKRELDRLQEEL 415
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
58-237 9.14e-03

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


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 37.29  E-value: 9.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    58 DKYSEALKDAQEK-LELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQK 136
Cdd:pfam05262 180 KKVVEALREDNEKgVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKN 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   137 DE---------EKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLER-AEERAELSEGKCAELEEELKTVTNNLKS 206
Cdd:pfam05262 260 LPkpadtsspkEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQeSKASEKEAEDKELEAQKKREPVAEDLQK 339
                         170       180       190
                  ....*....|....*....|....*....|...
gi 78000190   207 L--EAQAEKYSQKEDKYEEEIKVLSDKLKEAET 237
Cdd:pfam05262 340 TkpQVEAQPTSLNEDAIDSSNPVYGLKVVDPIT 372
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
3-265 9.94e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 37.35  E-value: 9.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190    3 AIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKatdaE 82
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEEL----E 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190   83 ADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEiQLKEAKHIAEDADRKY 162
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLD-ELREIEKRLSRLEEEI 323
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78000190  163 EEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFA 242
Cdd:PRK03918 324 NGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEI 403
                        250       260
                 ....*....|....*....|...
gi 78000190  243 ERSVTKLEKSIDDLEEKVAHAKE 265
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKK 426
 
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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