|
Name |
Accession |
Description |
Interval |
E-value |
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
48-282 |
9.78e-73 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organisation and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 425563 [Multi-domain] Cd Length: 235 Bit Score: 222.98 E-value: 9.78e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 48 KKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGM 127
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 128 KVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKSL 207
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 410060781 208 EAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISEELDHALNDMT 282
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
7-152 |
1.70e-25 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 98.15 E-value: 1.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 7 KMQMLKLDKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEgeva 86
Cdd:pfam12718 1 KMNSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNE---- 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 410060781 87 SLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAK 152
Cdd:pfam12718 77 NLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKEAK 142
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
21-275 |
4.23e-12 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 66.28 E-value: 4.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 21 RAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRIQLVEEELD 100
Cdd:COG1196 668 ELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 101 RAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTE 180
Cdd:COG1196 748 ELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 181 ERAELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSVAKLEKTIDDLEDEL 260
Cdd:COG1196 828 QEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEI 907
|
250
....*....|....*
gi 410060781 261 YAQKLKYKAISEELD 275
Cdd:COG1196 908 EKLRERLEELEAKLE 922
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
37-284 |
5.21e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.85 E-value: 5.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 37 KQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRIQLVEEELDRAQERLATALTKLEEA 116
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 117 EKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELSEGKCSELEEE 196
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 197 LKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISEELDH 276
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
|
....*...
gi 410060781 277 ALNDMTSI 284
Cdd:TIGR02168 927 LELRLEGL 934
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
4-284 |
4.05e-11 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 63.19 E-value: 4.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 4 IKKKMQMLKLDKENALDRAEQaESDKKAAEDrsKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEG 83
Cdd:COG1196 198 LEKQLEKLERQAEKAERYQEL-KAELRELEL--ALLLAKLKELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKS 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 84 EVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYE 163
Cdd:COG1196 275 ELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLA 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 164 EV-----------ARKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKL 232
Cdd:COG1196 355 ELeeakeeleeklSALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAEL 434
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 410060781 233 KEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISEELDHALNDMTSI 284
Cdd:COG1196 435 EELQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQRLEKELSSL 486
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
34-275 |
2.00e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.24 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 34 DRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRIQLVEEELDRAQERLATALTKL 113
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 114 EEAEKAADESErgmkvienrAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELSEGKCSEL 193
Cdd:TIGR02169 761 KELEARIEELE---------EDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 194 EEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISEE 273
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ 911
|
..
gi 410060781 274 LD 275
Cdd:TIGR02169 912 IE 913
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
44-284 |
1.29e-09 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 58.57 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 44 VALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADES 123
Cdd:COG1196 663 LAQKRELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 124 ERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNN 203
Cdd:COG1196 743 EEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQR 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 204 LKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISEELDHALNDMTS 283
Cdd:COG1196 823 RERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAE 902
|
.
gi 410060781 284 I 284
Cdd:COG1196 903 L 903
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
24-266 |
3.04e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 3.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 24 QAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRIQLVEEELDRAQ 103
Cdd:TIGR02168 208 QAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 104 ERLATALTKLEEaekaadesergmkvIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERA 183
Cdd:TIGR02168 288 KELYALANEISR--------------LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 184 ELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQ 263
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
...
gi 410060781 264 KLK 266
Cdd:TIGR02168 434 ELK 436
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
26-275 |
3.67e-09 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 57.42 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 26 ESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKI----ATDAEGEVASLNRRIQLVEEELDR 101
Cdd:COG1196 171 KERKEEAERKLERTEENLERLEDLLEELEKQLEKLERQAEKAERYQELKAELreleLALLLAKLKELRKELEELEEELSR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 102 AQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEE 181
Cdd:COG1196 251 LEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELKE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 182 RAELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEF----AERSVAKLEKTIDDLE 257
Cdd:COG1196 331 KIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAelaeIRNELEELKREIESLE 410
|
250
....*....|....*...
gi 410060781 258 DELYAQKLKYKAISEELD 275
Cdd:COG1196 411 ERLERLSERLEDLKEELK 428
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
18-259 |
6.83e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 6.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 18 ALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRIQLVEE 97
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 98 ELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLE 177
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 178 RTEER--------AELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSVAKL 249
Cdd:TIGR02168 940 NLQERlseeysltLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETL 1019
|
250
....*....|
gi 410060781 250 EKTIDDLEDE 259
Cdd:TIGR02168 1020 EEAIEEIDRE 1029
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
1-258 |
2.42e-08 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 54.72 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 1 MDAIKKKMQMLKLDKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATD 80
Cdd:COG1196 697 LRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAK 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 81 AEGEVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADR 160
Cdd:COG1196 777 LKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEK 856
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 161 KYEEVARKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAE 240
Cdd:COG1196 857 ELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERLEVELPELEEELE 936
|
250 260
....*....|....*....|....*..
gi 410060781 241 ---------FAERSVAKLEKTIDDLED 258
Cdd:COG1196 937 eeyedtletELEREIERLEEEIEALGP 963
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
43-258 |
3.08e-08 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 54.26 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 43 LVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRIQLVEEELDRAQERLATALTKLEEA------ 116
Cdd:COG4372 62 LFLLNRNLRSGVFQLDDIRPQLRALRTELGTAQGEKRAAETEREAARSELQKARQEREAVRQELAAARQNLAKAqqelar 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 117 --EKAADESERGMKVIENRAMKDEEKMELQEiQLKEAKHIAEEADRKYEEVARKLVIIEG---DLERTEERAELSEGKCS 191
Cdd:COG4372 142 ltKQAQDLQTRLKTLAEQRRQLEAQAQSLQA-SQKQLQASATQLKSQVLDLKLRSAQIEQeaqNLATRANAAQARTEELA 220
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 410060781 192 ELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSVAKLEKTIDDLED 258
Cdd:COG4372 221 RRAAAAQQTAQAIQQRDAQISQKAQQIAARAEQIRERERQLQRLETAQARLEQEVAQLEAYYQAYVR 287
|
|
| NtpI |
COG1269 |
Archaeal/vacuolar-type H+-ATPase subunit I/STV1 [Energy production and conversion]; |
55-278 |
3.92e-08 |
|
Archaeal/vacuolar-type H+-ATPase subunit I/STV1 [Energy production and conversion];
Pssm-ID: 224188 [Multi-domain] Cd Length: 660 Bit Score: 53.90 E-value: 3.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 55 DELDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRIQLVEEELdraqERLATALTKLEEAEKAADESERGMKVIENRA 134
Cdd:COG1269 50 KVAEVAQISLSSLLSEVLDYLRSVKGLEGRLFILPEEVEKLEAEL----KSLEEVIKPAEKFSSEVEELTRKLEERLSEL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 135 MKDEEKMELQEIQLKEAKHIAEEADRKYEevaRKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKSLEAQAEKY 214
Cdd:COG1269 126 DEELEDLEDLLEELEPLAYLDFDLSLLRG---LKFLLVRLGLVRREKLEALVGVIEDEVALYGENVEASVVIVVAHGAED 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 410060781 215 SQKEDKYEEEIKALTDKLKEAEtraEFAERSVAKLEKTIDDLEDELYAQKLKYKAISEELDHAL 278
Cdd:COG1269 203 LDKVSKILNELGFELYEVPEFD---GGPSELISELEEVIAEIQDELESLRSELEALAEKIAEEL 263
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
7-260 |
4.13e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 7 KMQMLKLDKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVA 86
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 87 SLNRRIQLVEEELdrAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVA 166
Cdd:TIGR02169 762 ELEARIEELEEDL--HKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQ 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 167 RKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSV 246
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRL 919
|
250
....*....|....
gi 410060781 247 AKLEKTIDDLEDEL 260
Cdd:TIGR02169 920 SELKAKLEALEEEL 933
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-277 |
4.87e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 4.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 1 MDAIKKKMQMLKLDKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATD 80
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 81 AEGEVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADR 160
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 161 KYEEVARKLVIIEGDLERTEERAELSEGKCSELeeELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAE 240
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478
|
250 260 270
....*....|....*....|....*....|....*..
gi 410060781 241 FAERSVAKLEKTIDDLEDELYAQKLKYKAISEELDHA 277
Cdd:TIGR02168 479 AAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQ 515
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2-275 |
7.79e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 7.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 2 DAIKKKMQMLKLDKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDA 81
Cdd:PRK02224 324 EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 82 EGEVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAadesergmkVIENRAMKDEEKMELQEIQLKEAKHI--AEEAD 159
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDELREREAELEATLRTARER---------VEEAEALLEAGKCPECGQPVEGSPHVetIEEDR 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 160 RKYEEVARKLVIIEGDLERTEERAELSEgKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRA 239
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEA 553
|
250 260 270
....*....|....*....|....*....|....*.
gi 410060781 240 EFAERSVAKLEKTIDDLEDELYAQKLKYKAISEELD 275
Cdd:PRK02224 554 EEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE 589
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
20-277 |
8.82e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 8.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 20 DRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLElaekiatDAEGEVASLNRRIQLVEEEL 99
Cdd:TIGR02169 660 RAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELS-------DASRKIGEIEKEIEQLEQEE 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 100 DRAQERLATALTKLEEAEKAADESERGMKviENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERT 179
Cdd:TIGR02169 733 EKLKERLEELEEDLSSLEQEIENVKSELK--ELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 180 EERAELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSVAKLEKTIDDLEDE 259
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE 890
|
250
....*....|....*...
gi 410060781 260 LYAQKLKYKAISEELDHA 277
Cdd:TIGR02169 891 RDELEAQLRELERKIEEL 908
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
68-280 |
9.75e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 9.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 68 QEKLELAEKIAtDAEGEVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQ 147
Cdd:TIGR02168 677 REIEELEEKIE-ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 148 LKEAKHIAEEADRKYE-------EVARKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDK 220
Cdd:TIGR02168 756 LTELEAEIEELEERLEeaeeelaEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 221 YEEEIKALTDKLKEAETRAEFAERSVAKLEKTIDDLEDELyAQKLKYKAISEELDHALND 280
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL-EALLNERASLEEALALLRS 894
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-256 |
1.63e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 2 DAIKKKMQMLKLDKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDA 81
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 82 EGEVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRK 161
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA 888
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 162 YEEVARKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKSLEAQ-AEKYSQKEDKYEEEIKALTDKLKEAETRAE 240
Cdd:TIGR02168 889 LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRiDNLQERLSEEYSLTLEEAEALENKIEDDEE 968
|
250
....*....|....*.
gi 410060781 241 FAERSVAKLEKTIDDL 256
Cdd:TIGR02168 969 EARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
11-260 |
2.44e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 11 LKLDKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKL-ELAEKIAT---------- 79
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELyALANEISRleqqkqilre 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 80 ---DAEGEVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADEsergmkvIENRAMKDEEKMELQEIQLKEAKHIAE 156
Cdd:TIGR02168 310 rlaNLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELES-------LEAELEELEAELEELESRLEELEEQLE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 157 EADRKYEEVARKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKslEAQAEKYSQKEDKYEEEIKALTDKLKEAE 236
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQEELERLE 460
|
250 260
....*....|....*....|....
gi 410060781 237 TRAEFAERSVAKLEKTIDDLEDEL 260
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAEREL 484
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-259 |
2.74e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 2 DAIKKKMQMLKLDKENALDRAEQAESDKKAAEDRSKQL-EDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATD 80
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 81 AEGEVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADR 160
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 161 KYEEVARKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAE 240
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELS 486
|
250
....*....|....*....
gi 410060781 241 FAERSVAKLEKTIDDLEDE 259
Cdd:TIGR02169 487 KLQRELAEAEAQARASEER 505
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
89-275 |
2.06e-06 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 48.94 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 89 NRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARK 168
Cdd:COG1196 659 KRSSLAQKRELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSR 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 169 LVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSVAK 248
Cdd:COG1196 739 LEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELES 818
|
170 180
....*....|....*....|....*..
gi 410060781 249 LEKTIDDLEDELYAQKLKYKAISEELD 275
Cdd:COG1196 819 LEQRRERLEQEIEELEEEIEELEEKLD 845
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
47-284 |
7.11e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 7.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 47 QKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEgevASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERG 126
Cdd:TIGR02168 178 ERKLERTRENLDRLEDILNELERQLKSLERQAEKAE---RYKELKAELRELELALLVLRLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 127 MKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKS 206
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE 334
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 410060781 207 LEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISEELDHALNDMTSI 284
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
|
|
| NtpI |
COG1269 |
Archaeal/vacuolar-type H+-ATPase subunit I/STV1 [Energy production and conversion]; |
13-284 |
8.18e-06 |
|
Archaeal/vacuolar-type H+-ATPase subunit I/STV1 [Energy production and conversion];
Pssm-ID: 224188 [Multi-domain] Cd Length: 660 Bit Score: 46.97 E-value: 8.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 13 LDKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRI 92
Cdd:COG1269 43 LKELEKLKVAEVAQISLSSLLSEVLDYLRSVKGLEGRLFILPEEVEKLEAELKSLEEVIKPAEKFSSEVEELTRKLEERL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 93 QLVEEELDRAQERLaTALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQeiqlkeAKHIAEEADRKYEEVARKLVII 172
Cdd:COG1269 123 SELDEELEDLEDLL-EELEPLAYLDFDLSLLRGLKFLLVRLGLVRREKLEAL------VGVIEDEVALYGENVEASVVIV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 173 ----EGDL--------ERTEERAELSEGK------CSELEEELKTVTNNLKSLEAQAEKYSqkeDKYEEEIKALTDKLKE 234
Cdd:COG1269 196 vahgAEDLdkvskilnELGFELYEVPEFDggpselISELEEVIAEIQDELESLRSELEALA---EKIAEELLAVREILEI 272
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 410060781 235 AETRAEFAErsvaKLEKTIDDLEDELYAQKLKYKAISEELDHALNDMTSI 284
Cdd:COG1269 273 EKALGDVLS----KLARTEYTLAIEGWVPADEVEKLKKIINRATGGAAYF 318
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
28-248 |
1.44e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 45.87 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 28 DKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRIQLVEEELDRAQERLA 107
Cdd:COG4942 32 SAAADDKQLKQIQKEIAALEKKIREQQDQRAKLEKQLKSLETEIASLEAQLIETADDLKKLRKQIADLNARLNALEVQER 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 108 TALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELSE 187
Cdd:COG4942 112 EQRRRLAEQLAALQRSGRNPPPALLVSPEDAQRSVRLAIYYGALNPARAERIDALKATLKQLAAVRAEIAAEQAELTTLL 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 410060781 188 GKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSVAK 248
Cdd:COG4942 192 SEQRAQQAKLAQLLEERKKTLAQLNSELSADQKKLEELRANESRLKNEIASAEAAAAKARE 252
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
23-261 |
1.52e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.07 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 23 EQAESDKKAAEDRSK--QLEDDLVALQKKLKGTEDELDKYS-----EALKDAQEKLELAEKIATDAEGEVASLNRRIQLV 95
Cdd:PRK05771 40 LSNERLRKLRSLLTKlsEALDKLRSYLPKLNPLREEKKKVSvksleELIKDVEEELEKIEKEIKELEEEISELENEIKEL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 96 EEELDRAQerlatALTKLEEAEKAADESERgMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKY----------EEV 165
Cdd:PRK05771 120 EQEIERLE-----PWGNFDLDLSLLLGFKY-VSVFVGTVPEDKLEELKLESDVENVEYISTDKGYVYvvvvvlkelsDEV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 166 ARKLVIIEGDLERTEERAELSEgKCSELEEELKTVTNNLKSLEAQAEKYSQkedKYEEEIKALTDKL----KEAETRAEF 241
Cdd:PRK05771 194 EEELKKLGFERLELEEEGTPSE-LIREIKEELEEIEKERESLLEELKELAK---KYLEELLALYEYLeielERAEALSKF 269
|
250 260 270
....*....|....*....|....*....|...
gi 410060781 242 A-------------ERSVAKLEKTIDDLEDELY 261
Cdd:PRK05771 270 LktdktfaiegwvpEDRVKKLKELIDKATGGSA 302
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-269 |
1.63e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 2 DAIKKKMQMLKLDKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQE--KLELAEKIAT 79
Cdd:PTZ00121 1119 EAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEvrKAEELRKAED 1198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 80 DAEGEVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEAd 159
Cdd:PTZ00121 1199 ARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA- 1277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 160 RKYEEVARKLVIIEGD-LERTEERAELSEG--------KCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTD 230
Cdd:PTZ00121 1278 RKADELKKAEEKKKADeAKKAEEKKKADEAkkkaeeakKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD 1357
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 410060781 231 KLKEAETRAEFAERSVAKLEKTIDDL----EDELYAQKLKYKA 269
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKKKEEAKKKADAAkkkaEEKKKADEAKKKA 1400
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
52-260 |
2.26e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 52 GTEDELDKYSEALKDAQEKLELAE-----KIATDAEGEVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERG 126
Cdd:PRK02224 177 GVERVLSDQRGSLDQLKAQIEEKEekdlhERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 127 MKVIENRAMK---DEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNN 203
Cdd:PRK02224 257 EAEIEDLRETiaeTEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVA 336
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 410060781 204 LKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSVAKLEKTIDDLEDEL 260
Cdd:PRK02224 337 AQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
4-218 |
4.47e-05 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 44.71 E-value: 4.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 4 IKKKMQMLKLDKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEG 83
Cdd:COG1196 293 LKEEIEELEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 84 EVASlnrRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYE 163
Cdd:COG1196 373 ELEE---LFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELE 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 410060781 164 EVARKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKE 218
Cdd:COG1196 450 ELEEQLEELRDRLKELERELAELQEELQRLEKELSSLEARLDRLEAEQRASQGVR 504
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
14-258 |
6.35e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 6.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 14 DKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRIQ 93
Cdd:PRK02224 273 EREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDAD 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 94 LVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIE 173
Cdd:PRK02224 353 DLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 174 GDLERTEERAE-----LSEGKCSELEEELK--TVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEfAERSV 246
Cdd:PRK02224 433 ATLRTARERVEeaealLEAGKCPECGQPVEgsPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVE-AEDRI 511
|
250
....*....|..
gi 410060781 247 AKLEKTIDDLED 258
Cdd:PRK02224 512 ERLEERREDLEE 523
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
5-269 |
8.35e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 8.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 5 KKKMQMLKLDKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKlkgtEDELDKYSEALKDAQEKLELAEKIATDAEGE 84
Cdd:PTZ00121 1342 KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK----AEEKKKADEAKKKAEEDKKKADELKKAAAAK 1417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 85 VASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGmkviENRAMKDEEKMELQEIQLK--------EAKHIAE 156
Cdd:PTZ00121 1418 KKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKA----EEAKKKAEEAKKADEAKKKaeeakkadEAKKKAE 1493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 157 EADRKYEEVARKlviiegdLERTEERAELSEGKCSELEEELKTVTNNLKSLEAQA--EKYSQKEDKYEEEIKALTDKLKE 234
Cdd:PTZ00121 1494 EAKKKADEAKKA-------AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKaeEKKKADELKKAEELKKAEEKKKA 1566
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 410060781 235 AETRAEFAERSVA--------KLEKTIDDLEDELYAQKLKYKA 269
Cdd:PTZ00121 1567 EEAKKAEEDKNMAlrkaeeakKAEEARIEEVMKLYEEEKKMKA 1609
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
6-269 |
9.04e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 9.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 6 KKMQMLKLDKENA--LDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKySEALKDAQEKLELAEKIATDAEG 83
Cdd:PTZ00121 1230 KKAEEAKKDAEEAkkAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK-AEEKKKADEAKKAEEKKKADEAK 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 84 EVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYE 163
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE 1388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 164 EVARKlviiegdlERTEERAELSEGKCSELE--EELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEF 241
Cdd:PTZ00121 1389 EKKKA--------DEAKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAE 1460
|
250 260 270
....*....|....*....|....*....|..
gi 410060781 242 AERSVAKLEKTIDDL----EDELYAQKLKYKA 269
Cdd:PTZ00121 1461 EAKKKAEEAKKADEAkkkaEEAKKADEAKKKA 1492
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
14-238 |
1.02e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 14 DKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRIQ 93
Cdd:PTZ00121 1575 DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK 1654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 94 LVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIE 173
Cdd:PTZ00121 1655 AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE 1734
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 410060781 174 GDLERTEERAELSEGKCSElEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETR 238
Cdd:PTZ00121 1735 AKKEAEEDKKKAEEAKKDE-EEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
57-260 |
1.13e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 57 LDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIEN---- 132
Cdd:PRK04863 350 IERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERakql 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 133 -----------RAMKDEEKMELQEI--QLKEAKH---IAEEADRKYEEVARKLVIIEGDLERtEERAELSEGKCSELEEE 196
Cdd:PRK04863 430 cglpdltadnaEDWLEEFQAKEQEAteELLSLEQklsVAQAAHSQFEQAYQLVRKIAGEVSR-SEAWDVARELLRRLREQ 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 410060781 197 lKTVTNNLKSLEAQ---AEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSVAKLEKTIDDLEDEL 260
Cdd:PRK04863 509 -RHLAEQLQQLRMRlseLEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESV 574
|
|
| GumC |
COG3206 |
Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane ... |
18-243 |
1.43e-04 |
|
Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225747 [Multi-domain] Cd Length: 458 Bit Score: 42.82 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 18 ALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYsealkDAQEKLELAEKIATDAEGEVASLNRRIQLVEE 97
Cdd:COG3206 179 QAYLADQLEAQLEAFRRASDSLDERLEELRARLQEAEAQVEDF-----RAQHGLTDAARGQLLSEQQLSALNTQLQSARA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 98 ELDRAQERLATALTKLEEAEKAADESErgmkVIENRAMkdeEKMELQEIQLKeakhiAEEADRKYEEVARKLVIIEGDLE 177
Cdd:COG3206 254 RLAQAEARLASLLQLLPLGREAAALRE----VLESPTI---QDLRQQYAQVR-----QQIADLSTELGAKHPQLVALEAQ 321
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 410060781 178 RTEERAELSEgkcsELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTD---KLKEAETRAEFAE 243
Cdd:COG3206 322 LAELRQQIAA----ELRQILASLPNELALLEQQEAALEKELAQLKGRLSKLPKlqvQLRELEREAEAAR 386
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
4-284 |
1.79e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 42.83 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 4 IKKKMQMLKLDKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKG----TEDELDKYSEALKDAQEKLELAEKIAT 79
Cdd:COG0419 166 LEKYEKLSELLKEVIKEAKAKIEELEGQLSELLEDIEDLLEALEEELKElkklEEIQEEQEEEELEQEIEALEERLAELE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 80 DAEGEVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEAD 159
Cdd:COG0419 246 EEKERLEELKARLLEIESLELEALKIREEELRELERLLEELEEKIERLEELEREIEELEEELEGLRALLEELEELLEKLK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 160 RKYEEVARKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRA 239
Cdd:COG0419 326 SLEERLEKLEEKLEKLESELEELAEEKNELAKLLEERLKELEERLEELEKELEKALERLKQLEEAIQELKEELAELSAAL 405
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 410060781 240 EFAERSVAKLEKTIDDLEDELYAQKLKYKAISEELDHALNDMTSI 284
Cdd:COG0419 406 EEIQEELEELEKELEELERELEELEEEIKKLEEQINQLESKELMI 450
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
85-264 |
1.88e-04 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 42.78 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 85 VASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKeakhiaeeadRKYEE 164
Cdd:COG1196 167 VSKYKERKEEAERKLERTEENLERLEDLLEELEKQLEKLERQAEKAERYQELKAELRELELALLL----------AKLKE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 165 VARKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAER 244
Cdd:COG1196 237 LRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELEN 316
|
170 180
....*....|....*....|
gi 410060781 245 SVAKLEKTIDDLEDELYAQK 264
Cdd:COG1196 317 ELEELEERLEELKEKIEALK 336
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
23-233 |
2.50e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 42.35 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 23 EQAESDKKAAE-DRSKQLEDDLVALQKKlKGTEDELDKYSEALKD--------AQEKLELAEKIATDAEG-EVASLNRRI 92
Cdd:PRK10929 33 EQAKAAKTPAQaEIVEALQSALNWLEER-KGSLERAKQYQQVIDNfpklsaelRQQLNNERDEPRSVPPNmSTDALEQEI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 93 -----QLVEE------ELDRAQErLATALTKL----EEAEKAADESERGMKVIENRAMKDEEkmelqeiqlkeakhiAEE 157
Cdd:PRK10929 112 lqvssQLLEKsrqaqqEQDRARE-ISDSLSQLpqqqTEARRQLNEIERRLQTLGTPNTPLAQ---------------AQL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 158 ADRKYEEVARKLVIIEGDLE------RTE---ERAELSEGKCSELEEELKTVTNNLKSLEAQ-AEKYSQKEDKYEEEI-- 225
Cdd:PRK10929 176 TALQAESAALKALVDELELAqlsannRQElarLRSELAKKRSQQLDAYLQALRNQLNSQRQReAERALESTELLAEQSgd 255
|
250
....*....|
gi 410060781 226 --KALTDKLK 233
Cdd:PRK10929 256 lpKSIVAQFK 265
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
13-278 |
2.59e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 13 LDKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRI 92
Cdd:PRK02224 307 ADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 93 QLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVII 172
Cdd:PRK02224 387 EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPH 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 173 EGDLERTEERAELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKyEEEIKALTDKLKEAETRAEFAERSVAKLEKT 252
Cdd:PRK02224 467 VETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERL-EERREDLEELIAERRETIEEKRERAEELRER 545
|
250 260
....*....|....*....|....*.
gi 410060781 253 IDDLEDELYAQKLKYKAISEELDHAL 278
Cdd:PRK02224 546 AAELEAEAEEKREAAAEAEEEAEEAR 571
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
16-220 |
2.85e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 380155 [Multi-domain] Cd Length: 1848 Bit Score: 42.13 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 16 ENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTE------------DELDKYSEA----LKDAQEKLELAEKIAT 79
Cdd:NF012221 1558 QNALADKERAEADRQRLEQEKQQQLAAISGSQSQLESTDqnaletngqaqrDAILEESRAvtkeLTTLAQGLDALDSQAT 1637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 80 DAE--GEvaslNRRIQLVEEELDRAQERL-ATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAK---- 152
Cdd:NF012221 1638 YAGesGD----QWRNPFAGGLLDRVQEQLdDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGVAQGEQNQANAEqdid 1713
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 410060781 153 HIAEEADRKYEEVARKlviiEGDLERTEERAELSEGKC-SELEEELKTVTNnlKSLEAQAEKYSQKEDK 220
Cdd:NF012221 1714 DAKADAEKRKDDALAK----QNEAQQAESDANAAANDAqSRGEQDASAAEN--KANQAQADAKGAKQDE 1776
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-259 |
3.15e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 2 DAIKKKMQMLKLDKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDA 81
Cdd:PTZ00121 1543 EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 82 EGEvaslnRRIQLVEEELDRAQERLATALTKLEEAEKAadESERGMKVIENRAMKDEEKMELQEI-QLKEAKHIAEEADR 160
Cdd:PTZ00121 1623 EEL-----KKAEEEKKKVEQLKKKEAEEKKKAEELKKA--EEENKIKAAEEAKKAEEDKKKAEEAkKAEEDEKKAAEALK 1695
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 161 KYEEVARKLVIIEGDLERTEERAElsegKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAE 240
Cdd:PTZ00121 1696 KEAEEAKKAEELKKKEAEEKKKAE----ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
250
....*....|....*....
gi 410060781 241 FAERSVAKLEKTIDDLEDE 259
Cdd:PTZ00121 1772 EIRKEKEAVIEEELDEEDE 1790
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
16-260 |
7.83e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 7.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 16 ENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAE--KIATDAEGE-----VASL 88
Cdd:PRK02224 394 EELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpECGQPVEGSphvetIEED 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 89 NRRIQLVEEELDRAQERLATALTKLEEAEKAAdESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARK 168
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAE 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 169 LVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDkYEEEIKALTDKLKEAETRAEFAERSVAK 248
Cdd:PRK02224 553 AEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIAD-AEDEIERLREKREALAELNDERRERLAE 631
|
250
....*....|..
gi 410060781 249 LEKTIDDLEDEL 260
Cdd:PRK02224 632 KRERKRELEAEF 643
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
20-258 |
7.87e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 7.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 20 DRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTE---DELDKYSEALKDAQEK-----LELAEKIATDAEGEVASLNRR 91
Cdd:PTZ00121 1480 EEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEakkAEEAKKADEAKKAEEAkkadeAKKAEEKKKADELKKAEELKK 1559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 92 IQLVE--EELDRAQERLATALTKLEEAEKAadesERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKL 169
Cdd:PTZ00121 1560 AEEKKkaEEAKKAEEDKNMALRKAEEAKKA----EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV 1635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 170 VIIEGDLERTEERAElsegKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSVAKL 249
Cdd:PTZ00121 1636 EQLKKKEAEEKKKAE----ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711
|
....*....
gi 410060781 250 EKTIDDLED 258
Cdd:PTZ00121 1712 AEEKKKAEE 1720
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
2-201 |
1.23e-03 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 40.08 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 2 DAIKKKMQMLKLDKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDA----QEKLELAEKI 77
Cdd:COG1196 312 EELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELfealREELAELEAE 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 78 ATDAEGEVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEE 157
Cdd:COG1196 392 LAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAE 471
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 410060781 158 ADRKYEEVARKLVIIEGDLERTEERAELSEGKCSELEEELKTVT 201
Cdd:COG1196 472 LQEELQRLEKELSSLEARLDRLEAEQRASQGVRAVLEALESGLP 515
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1-211 |
1.41e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.05 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 1 MDAIKKKMQMLKLDKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATD 80
Cdd:TIGR02169 289 QLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELED 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 81 AEGEVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADR 160
Cdd:TIGR02169 369 LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 410060781 161 KYEEVARKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKSLEAQA 211
Cdd:TIGR02169 449 EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQA 499
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
15-260 |
1.96e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 15 KENALDRAEQAESDKKAAEDRSKQLED---DLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVA----- 86
Cdd:PRK02224 229 REQARETRDEADEVLEEHEERREELETleaEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlddad 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 87 --SLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEE 164
Cdd:PRK02224 309 aeAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 165 VARKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKA--------------LTD 230
Cdd:PRK02224 389 LEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegspHVE 468
|
250 260 270
....*....|....*....|....*....|
gi 410060781 231 KLKEAETRAEFAERSVAKLEKTIDDLEDEL 260
Cdd:PRK02224 469 TIEEDRERVEELEAELEDLEEEVEEVEERL 498
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
20-261 |
2.09e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 20 DRAEQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRIQLVEEEL 99
Cdd:PRK02224 509 DRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERI 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 100 DRAqERLATALTKLEEAEKAADE------------SERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVAR 167
Cdd:PRK02224 589 ESL-ERIRTLLAAIADAEDEIERlrekrealaelnDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEE 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 168 KLVIIEGDLERTEERAELSEGKCSELE---EELKTVTNNLKSLEAQAEKYSQKEDKYeeeikaltdklkeAETRAEFAER 244
Cdd:PRK02224 668 KLDELREERDDLQAEIGAVENELEELEelrERREALENRVEALEALYDEAEELESMY-------------GDLRAELRQR 734
|
250
....*....|....*..
gi 410060781 245 SVAKLEKTIDDLEDELY 261
Cdd:PRK02224 735 NVETLERMLNETFDLVY 751
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
11-278 |
2.89e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.12 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 11 LKLDKENALDRAEQAESDKKAAEDRSKQLEDdlvaLQKKLKGTEDELDKYSEALKDAQ----EKLELAEkiatdAEGEVA 86
Cdd:PRK11281 61 VQQDLEQTLALLDKIDRQKEETEQLKQQLAQ----APAKLRQAQAELEALKDDNDEETretlSTLSLRQ-----LESRLA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 87 SLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENR---------AMKDEEKMELQ-EIQLKEAKHiae 156
Cdd:PRK11281 132 QTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLlkggkvggkALRPSQRVLLQaEQALLNAQN--- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 157 EADRKYEEVARKLViiegDLErTEERAELSEgKCSELEEELKTVTN--NLKSLEaQAEKYSQKEDKYEEEIKALTDKL-- 232
Cdd:PRK11281 209 DLQRKSLEGNTQLQ----DLL-QKQRDYLTA-RIQRLEHQLQLLQEaiNSKRLT-LSEKTVQEAQSQDEAARIQANPLva 281
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 410060781 233 KEAETRAEFAERSVAKLEKTiddleDELYAQKLKYKAIseeLDHAL 278
Cdd:PRK11281 282 QELEINLQLSQRLLKATEKL-----NTLTQQNLRVKNW---LDRLT 319
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
58-235 |
3.36e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 38.45 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 58 DKYSEALKDAQEK-LELAEKIATDAEGEVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMK 136
Cdd:pfam05262 180 KKVVEALREDNEKgVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKN 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 137 DEEKMELQEIqlKEAKHIAEEADRKYEEVARKLViiegdlERTEERAELSEGKCSELEEElktvtnnLKSLEAQAEKYSQ 216
Cdd:pfam05262 260 LPKPADTSSP--KEDKQVAENQKREIEKAQIEIK------KNDEEALKAKDHKAFDLKQE-------SKASEKEAEDKEL 324
|
170
....*....|....*....
gi 410060781 217 KEDKYEEEIKALTDKLKEA 235
Cdd:pfam05262 325 EAQKKREPVAEDLQKTKPQ 343
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2-275 |
3.95e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.51 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 2 DAIKKKMQMLKLDKENALDRAEQAESDKKAAEDRSKQLEDDLVALQKK---LKGTEDELDKYSEALKDAQEKLELAEKIA 78
Cdd:PRK03918 366 EAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARigeLKKEIKELKKAIEELKKAKGKCPVCGREL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 79 TDAEGE--VASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAkhiaE 156
Cdd:PRK03918 446 TEEHRKelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEEL----E 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 157 EADRKYEEVARKLVIIEGDLERTE---ERAELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQK-EDKYEEEIKALTD-- 230
Cdd:PRK03918 522 KKAEEYEKLKEKLIKLKGEIKSLKkelEKLEELKKKLAELEKKLDELEEELAELLKELEELGFEsVEELEERLKELEPfy 601
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 410060781 231 ----KLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISEELD 275
Cdd:PRK03918 602 neylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE 650
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
23-240 |
4.41e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 38.44 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 23 EQAESDKKAAEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAqEKLELAEKIATDAEGEVASLNRRIQL-VEEELDR 101
Cdd:TIGR00927 679 NESEGEIPAERKGEQEGEGEIEAKEADHKGETEAEEVEHEGETEA-EGTEDEGEIETGEEGEEVEDEGEGEAeGKHEVET 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 102 AQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEkmelQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEE 181
Cdd:TIGR00927 758 EGDRKETEHEGETEAEGKEDEDEGEIQAGEDGEMKGDE----GAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETG 833
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 410060781 182 RAELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAE 240
Cdd:TIGR00927 834 EQELNAENQGEAKQDEKGVDGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEE 892
|
|
| PLN03223 |
PLN03223 |
Polycystin cation channel protein; Provisional |
3-152 |
4.81e-03 |
|
Polycystin cation channel protein; Provisional
Pssm-ID: 215637 [Multi-domain] Cd Length: 1634 Bit Score: 38.39 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 3 AIKKKMQMLKLDKENALDRAEQAESDKkAAEDRSKQLEDDLVALQKKLKGTEDE-LDKYSEALKDAQEKLELAEKIATDA 81
Cdd:PLN03223 796 SLDTQIETLKTQQDRANQEAEAHHADN-SLETLINAGFTDIKAGQAALEAKLDEiLGKQQQALAAAQESLAIQQRTNGLA 874
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 410060781 82 EGEVAslnrriqlveeeldrAQERLATALTKLEEAEKAADESERGMKV-----IENRAMKDeekmelQEIQLKEAK 152
Cdd:PLN03223 875 ERQAA---------------AIEKLAKAVEKQLSSIKSAYTYGAFISLtqylaIQERARRT------RELTAKANF 929
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
85-275 |
7.51e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 37.74 E-value: 7.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 85 VASLNRRIQLVEEELDRAQERLATALTKLEEAEkaaDESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEE 164
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKR---QQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 165 VARKLVIIEGDLERTEERAELSEGKCSELEEELKTVTNNLKSL-EAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAE 243
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190
....*....|....*....|....*....|....*....
gi 410060781 244 RSVAKLE-------KTIDDLEDELYAQKLKYKAISEELD 275
Cdd:TIGR02169 322 ERLAKLEaeidkllAEIEELEREIEEERKRRDKLTEEYA 360
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump [Defense mechanisms]; |
38-183 |
8.28e-03 |
|
Multidrug resistance efflux pump [Defense mechanisms];
Pssm-ID: 224482 [Multi-domain] Cd Length: 352 Bit Score: 37.31 E-value: 8.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 38 QLEDDLVALQKKLKGTEDELDKYSEALkdAQEKLELAEKIATDAEgEVASLNRRIQLVEEELDRAQerlaTALTKLEEAE 117
Cdd:COG1566 95 QAEAALAAAEAQLRNLRAQLASAQALI--AQAEAQDLDQAQNELE-RRAELAQRGVVSREELDRAR----AALQAAEAAL 167
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 410060781 118 KAADESERgmkviENRAMKDEEKMELQEiQLKEAKHIAEEAdrkyeevarklviiEGDLERTEERA 183
Cdd:COG1566 168 AAAQAAQK-----QNLALLESEVSGAQA-QVASAEAALDQA--------------KLDLERTVIRA 213
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
33-284 |
8.70e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 37.72 E-value: 8.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 33 EDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKIATDAEGEVASLNRRIQLVEEELDRAQERLATALTK 112
Cdd:TIGR00606 701 QSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPE 780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 113 LEEAEKAADE----SERGMKVIENRAMKDEEKMELQEIQL----KEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAE 184
Cdd:TIGR00606 781 EESAKVCLTDvtimERFQMELKDVERKIAQQAAKLQGSDLdrtvQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQ 860
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410060781 185 LSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKALTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQK 264
Cdd:TIGR00606 861 HLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQ 940
|
250 260
....*....|....*....|
gi 410060781 265 LKYKAISEELDHALNDMTSI 284
Cdd:TIGR00606 941 DKVNDIKEKVKNIHGYMKDI 960
|
|
|