|
Name |
Accession |
Description |
Interval |
E-value |
| UBAN |
cd09803 |
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ... |
269-355 |
2.05e-25 |
|
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) is a regulatory subunit of the kinase complex IKK, which is involved in the activation of NF-kappaB via phosporylation of inhibitory IkappaBs. This mechanism requires the binding of NEMO to ubiquinated substrates. Binding is achieved via the UBAN motif (ubiquitin binding in ABIN and NEMO), which is described in this model. This region of NEMO has also been named CoZi (for coiled-coil 2 and leucine zipper). ABINs (A20-binding inhibitors of NF-kappaB) are sensors for ubiquitin that are involved in regulation of apoptosis, ABIN-1 is presumed to inhibit signalling via the NF-kappaB route. The UBAN motif is also found in optineurin, the product of a gene associated with glaucoma, which has been characterized as a negative regulator of NF-kappaB as well.
Pssm-ID: 197361 [Multi-domain] Cd Length: 87 Bit Score: 98.96 E-value: 2.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 269 MQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQ 348
Cdd:cd09803 1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80
|
....*..
gi 209862941 349 REFNKLK 355
Cdd:cd09803 81 RENQELK 87
|
|
| CC2-LZ |
pfam16516 |
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ... |
270-355 |
1.82e-22 |
|
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a leucine-zipper domain associated with the CC2 coiled-coil region of NF-kappa-B essential modulator, NEMO. It plays a regulatory role, along with the very C-terminal zinc-finger; it contains a ubiquitin-binding domain (UBD) and represents one region that contributes to NEMO oligomerization. NEMO itself is an integral part of the IkappaB kinase complex and serves as a molecular switch via which the NF-kappaB signalling pathway is regulated.
Pssm-ID: 465155 [Multi-domain] Cd Length: 100 Bit Score: 91.20 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 270 QLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQR 349
Cdd:pfam16516 15 EIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEYLQR 94
|
....*.
gi 209862941 350 EFNKLK 355
Cdd:pfam16516 95 QNQQLK 100
|
|
| NEMO |
pfam11577 |
NF-kappa-B essential modulator NEMO; NEMO is a regulatory protein which is part of the IKK ... |
62-128 |
1.59e-16 |
|
NF-kappa-B essential modulator NEMO; NEMO is a regulatory protein which is part of the IKK complex along with the catalytic IKKalpha and beta kinases. The IKK complex phosphorylates IkappaB targeting it for degradation which results in the release of NF-kappaB which initiates the inflammatory response, cell proliferation or cell differentiation. NEMO activates the IKK complex's activity by associating with the unphosphorylated IKK kinase C termini.The core domain of NEMO is a dimer which binds to two fragments of IKK.
Pssm-ID: 431942 [Multi-domain] Cd Length: 67 Bit Score: 73.67 E-value: 1.59e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 209862941 62 EQGTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLE 128
Cdd:pfam11577 1 DEETLEQMKELLTENHQLKEAMKQSNQAMKERCEELSAWQEKQKEEREFLECRFREARELLRRLSLE 67
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
105-356 |
1.73e-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: 72.78 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 105 REEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKD 184
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 185 RQALEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIK 264
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEA----QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 265 SSKGM--QLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPV----LKAQADIYKADFQAERHAREKLVEKKE 338
Cdd:TIGR02168 839 RLEDLeeQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEalalLRSELEELSEELRELESKRSELRRELE 918
|
250
....*....|....*...
gi 209862941 339 YLQEQLEQLQREFNKLKV 356
Cdd:TIGR02168 919 ELREKLAQLELRLEGLEV 936
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
77-355 |
8.94e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 8.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 77 QELRDAIRQsnqmlRERCEELLHFQVSQREEKEFLMcKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKCQQQMAED 156
Cdd:COG1196 216 RELKEELKE-----LEAELLLLKLRELEAELEELEA-ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 157 KASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRMQNQSVEAALRMERQ 236
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE----ELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 237 AASEEKRKLAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETvpvLKAQA 316
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALR-----AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE---LEEEE 437
|
250 260 270
....*....|....*....|....*....|....*....
gi 209862941 317 DIYKADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLK 355
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
134-350 |
1.61e-12 |
|
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: 68.64 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 134 SQREQALKELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQH 213
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 214 SVQVDQLRMQnqsVEAALRMERQA------ASEEKRKLAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVA 287
Cdd:COG4942 100 EAQKEELAEL---LRALYRLGRQPplalllSPEDFLDAVRRLQYLKYLAPARREQAE-----ELRADLAELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 209862941 288 KQELIDKLKEEAEQHKIVMETVPVLKAQA-DIYKADFQAERHAREKLVEKKEYLQEQLEQLQRE 350
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLlARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
73-348 |
1.63e-12 |
|
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: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 73 LEENQELRDAIRQSNQM--LRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKCQ 150
Cdd:COG1196 218 LKEELKELEAELLLLKLreLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 151 QQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAA 230
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 231 LR----------MERQAASEEKRKLAQLQAAYHQLFQDyDSHIKSSKGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAE 300
Cdd:COG1196 378 EEeleelaeellEALRAAAELAAQLEELEEAEEALLER-LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 209862941 301 QHKIVMETVPVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQ 348
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| zf_C2H2_10 |
pfam18414 |
C2H2 type zinc-finger; This is a zinc finger domain C2H2 which can be found in optineurin ... |
404-429 |
2.00e-11 |
|
C2H2 type zinc-finger; This is a zinc finger domain C2H2 which can be found in optineurin (optic neuropathy inducing protein) and NF-kappa-B essential modulator (NEMO) furthermore, it can be found in kinase TBK1, a member of the IKK (inhibitor of nuclear factor kappa-B kinase) family. The C-terminal region, which carries the zinc finger domain, constitutes the regulatory domain of NEMO, as it receives the activation signal from upstream molecules, and subsequently transmits this activation to the kinases bound to the N-terminal domain. The isolated NEMO zinc finger is thought to be involved in protein-protein rather than protein-DNA interaction.
Pssm-ID: 436483 Cd Length: 26 Bit Score: 57.99 E-value: 2.00e-11
10 20
....*....|....*....|....*.
gi 209862941 404 PDFCCPKCQYQAPDMDTLQIHVMECI 429
Cdd:pfam18414 1 PKHCCPKCQEQLPDIDTLQIHVMDCI 26
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
67-301 |
4.32e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 4.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 67 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQL 146
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 147 KKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQ---QHSVQVDQLRMQ 223
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLErleRLEEELEELEEA 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 209862941 224 NQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQ 301
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA--LLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
69-354 |
6.37e-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: 64.69 E-value: 6.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 69 LQRCLEENQELRDAIRQsnqmLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKK 148
Cdd:TIGR02168 700 LAELRKELEELEEELEQ----LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 149 CQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVE 228
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 229 -AALRMERQAASEEK--RKLAQLQAAYHQLFQDYDSHIK------------SSKGMQLEDLRQQLQQAEEALVAKQE--- 290
Cdd:TIGR02168 856 sLAAEIEELEELIEEleSELEALLNERASLEEALALLRSeleelseelrelESKRSELRRELEELREKLAQLELRLEgle 935
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 291 -LIDKLKEE-AEQHKIVMETVPVLKAQADIYKAdfQAERHAR--------------------EKLVEKKEYLQEQLEQLQ 348
Cdd:TIGR02168 936 vRIDNLQERlSEEYSLTLEEAEALENKIEDDEE--EARRRLKrlenkikelgpvnlaaieeyEELKERYDFLTAQKEDLT 1013
|
....*.
gi 209862941 349 REFNKL 354
Cdd:TIGR02168 1014 EAKETL 1019
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
135-393 |
1.65e-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: 63.15 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 135 QREQALKELEQlkkCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQ--- 211
Cdd:TIGR02168 674 ERRREIEELEE---KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEEria 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 212 QHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQEL 291
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE-----ALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 292 IDKLKEEAEQHKIVMEtvpVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLKVGCHE--------SAR 363
Cdd:TIGR02168 826 LESLERRIAATERRLE---DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALlrseleelSEE 902
|
250 260 270
....*....|....*....|....*....|
gi 209862941 364 IEDMRKRHVETPQPPLLPAPAHHSFHLALS 393
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKLAQLELRLE 932
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
67-355 |
1.91e-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: 60.08 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 67 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFlmcKFQEarklverLSLEKLDLRSQREQALKELEQL 146
Cdd:TIGR02169 180 EEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREY---EGYE-------LLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 147 KKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATkdrqalEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLR-MQNQ 225
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG------EEEQLRVKEKIGELEAEIASLERSIAEKERELEdAEER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 226 SVEAALRMERQAASEE--KRKLAQLQAAYHQLFQDYDShikssKGMQLEDLRQQLQQAE-------EALVAKQELIDKLK 296
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEelEREIEEERKRRDKLTEEYAE-----LKEELEDLRAELEEVDkefaetrDELKDYREKLEKLK 398
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 209862941 297 EEAEQHKIVMETVPVLKAQADIYKADFQAERHARE----KLVEKKEYLQEQLEQLQREFNKLK 355
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEakinELEEEKEDKALEIKKQEWKLEQLA 461
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
66-354 |
3.53e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 66 PETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQ 145
Cdd:TIGR02168 721 LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 146 LKkcqqqmaEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLrmqnq 225
Cdd:TIGR02168 801 LR-------EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI----- 868
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 226 sveAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIK--SSKGMQLEDLRQQLQQAEEALVAKQE----LIDKLKEE- 298
Cdd:TIGR02168 869 ---EELESELEALLNERASLEEALALLRSELEELSEELRelESKRSELRRELEELREKLAQLELRLEglevRIDNLQERl 945
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 209862941 299 AEQHKIVMETVPVLKaqadiykadfqaerharEKLVEKKEYLQEQLEQLQREFNKL 354
Cdd:TIGR02168 946 SEEYSLTLEEAEALE-----------------NKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
67-356 |
4.39e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 4.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 67 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALK----- 141
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERqleel 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 142 --ELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQhsvqvdq 219
Cdd:TIGR02168 322 eaQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ------- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 220 lrmqnqsvEAALRMERQAASEEKRklaqlqaayhqlfqdydshiksskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEA 299
Cdd:TIGR02168 395 --------IASLNNEIERLEARLE--------------------------RLEDRRERLQQEIEELLKKLEEAELKELQA 440
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 209862941 300 EQHKIVMETVPVLKAQADIYkadfQAERHAREKLVEKKEYLQEQLEQLQREFNKLKV 356
Cdd:TIGR02168 441 ELEELEEELEELQEELERLE----EALEELREELEEAEQALDAAERELAQLQARLDS 493
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
107-355 |
5.32e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 5.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 107 EKEFLMCKFQEARKLVERLSLEKLDLRSQREQALkelEQLKKCQQQMAEdkasVKAQVTSLLGELQESQSRLEAATKDRQ 186
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELT---AELQELEEKLEE----LRLEVSELEEEIEELQKELYALANEIS 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 187 ALEGRIRAVSEQVRQLESEREVLQQQH-----------------SVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQ 249
Cdd:TIGR02168 299 RLEQQKQILRERLANLERQLEELEAQLeeleskldelaeelaelEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 250 AAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAE--R 327
Cdd:TIGR02168 379 EQLETLRSKVAQLEL-----QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEelQ 453
|
250 260
....*....|....*....|....*...
gi 209862941 328 HAREKLVEKKEYLQEQLEQLQREFNKLK 355
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAE 481
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
172-353 |
5.56e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 5.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 172 QESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSV--QVDQLRMQNQSVEAA------LRMERQAASEEKR 243
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAlqRLAEYSWDEIDVASAereiaeLEAELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 244 KLAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADF 323
Cdd:COG4913 686 DLAALEEQLEELEAELEELEE-----ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALG 760
|
170 180 190
....*....|....*....|....*....|....*...
gi 209862941 324 QAER--------HAREKLVEKKEYLQEQLEQLQREFNK 353
Cdd:COG4913 761 DAVErelrenleERIDALRARLNRAEEELERAMRAFNR 798
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
119-355 |
6.45e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 6.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 119 RKLVERLSLEKLDLRSQREQALKELEQLKKCQQQMAEDKASVKAqvtslLGELQESQSRLEAATKDRQALEGRIRAVSEQ 198
Cdd:COG4913 210 DDFVREYMLEEPDTFEAADALVEHFDDLERAHEALEDAREQIEL-----LEPIRELAERYAAARERLAELEYLRAALRLW 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 199 VRQLesEREVLQQqhsvQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAyhqlfqdydshIKSSKGMQLEDLRQQL 278
Cdd:COG4913 285 FAQR--RLELLEA----ELEELRAELARLEAELERLEARLDALREELDELEAQ-----------IRGNGGDRLEQLEREI 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 279 QQAEEALVAKQELIDKLKEEAEQ--------HKIVMETVPVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQRE 350
Cdd:COG4913 348 ERLERELEERERRRARLEALLAAlglplpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
....*
gi 209862941 351 FNKLK 355
Cdd:COG4913 428 IASLE 432
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
88-370 |
1.00e-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: 57.77 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 88 QMLRERCEEL---LHFQVSQREEKEFLM----CKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKCQQQMAEDKASV 160
Cdd:TIGR02169 677 QRLRERLEGLkreLSSLQSELRRIENRLdelsQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 161 KAQVTSLLGELQESQSRLEAATKDRQALEGRIRavSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASE 240
Cdd:TIGR02169 757 KSELKELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 241 EKRKLAQLQAAYHQlfqdydshiKSSKGMQLEDLRQQL----QQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQA 316
Cdd:TIGR02169 835 IQELQEQRIDLKEQ---------IKSIEKEIENLNGKKeeleEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI 905
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 209862941 317 DIYKADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLKVGCHESARIEDMRKR 370
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAE 959
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
73-294 |
1.06e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.33 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 73 LEENQELR-DAIRQSNQMLRERCEELLHfQVSQREEKeflMCKFQEARKLV-----ERLSLEKL-DLRSQREQALKELEQ 145
Cdd:COG3206 162 LEQNLELRrEEARKALEFLEEQLPELRK-ELEEAEAA---LEEFRQKNGLVdlseeAKLLLQQLsELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 146 LKKCQQQMAEDKASVKAQVTSLLG--ELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQ 223
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILAS 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 209862941 224 -------NQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDshIKSSKGMQLEDLRQQLQQAEEALVAKQELIDK 294
Cdd:COG3206 318 leaeleaLQAREASLQAQLAQLEARLAELPELEAELRRLEREVE--VARELYESLLQRLEEARLAEALTVGNVRVIDP 393
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
132-350 |
1.37e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 132 LRSQREQALKELE------------------QLKKCQQQ--MAEDKASVKA-----QVTSLLGELQESQSRLEAATKDRQ 186
Cdd:COG1196 170 YKERKEEAERKLEateenlerledilgelerQLEPLERQaeKAERYRELKEelkelEAELLLLKLRELEAELEELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 187 ALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSV----------EAALRMERQAASEEKRKLAQLQAAYHQLF 256
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEyellaelarlEQDIARLEERRRELEERLEELEEELAELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 257 QDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQhkIVMETVPVLKAQADIYKADFQAERhAREKLVEK 336
Cdd:COG1196 330 EELEELEE-----ELEELEEELEEAEEELEEAEAELAEAEEALLE--AEAELAEAEEELEELAEELLEALR-AAAELAAQ 401
|
250
....*....|....
gi 209862941 337 KEYLQEQLEQLQRE 350
Cdd:COG1196 402 LEELEEAEEALLER 415
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
106-368 |
2.01e-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: 56.61 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 106 EEKEFLMCKFQEARKLVERLSL---EKLD----LRSQREQALKELEQLKKCQ-----------QQMAEDKASVKAQVTSL 167
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLiidEKRQqlerLRREREKAERYQALLKEKReyegyellkekEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 168 LGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVlqqqhsvqvdQLRMQNQSVEAALRMERQAASEEKRKLAQ 247
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL----------RVKEKIGELEAEIASLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 248 LQAAYHQLFQDYDShiksskgmqledLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETvpvLKAQADIYKADFQAER 327
Cdd:TIGR02169 320 AEERLAKLEAEIDK------------LLAEIEELEREIEEERKRRDKLTEEYAELKEELED---LRAELEEVDKEFAETR 384
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 209862941 328 HAREKLVEKKEYLQEQLEQLQREFNKLKVGCHE-SARIEDMR 368
Cdd:TIGR02169 385 DELKDYREKLEKLKREINELKRELDRLQEELQRlSEELADLN 426
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
116-290 |
2.95e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 116 QEARKLVERLSLEKLDLRSQREQALKELEQLKKCQQQMAEDK---------ASVKAQVTSLL---GELQESQSRLEAATK 183
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvasaereiAELEAELERLDassDDLAALEEQLEELEA 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 184 DRQALEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDShi 263
Cdd:COG4913 700 ELEELEEELDELKGEIGRLEKELEQAEE----ELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEE-- 773
|
170 180
....*....|....*....|....*..
gi 209862941 264 ksskgmQLEDLRQQLQQAEEALVAKQE 290
Cdd:COG4913 774 ------RIDALRARLNRAEEELERAMR 794
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
66-324 |
4.77e-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: 52.38 E-value: 4.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 66 PETLQRCLEENQELRDAIRQSNQMLRERC----EELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREqalk 141
Cdd:TIGR02169 261 SELEKRLEEIEQLLEELNKKIKDLGEEEQlrvkEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA---- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 142 ELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQ----------Q 211
Cdd:TIGR02169 337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKreldrlqeelQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 212 QHSVQVDQLRMQNQSVEAALRmERQAASEEKRklAQLQAAYHQLFQDYDSHIKSSKgmQLEDLRQQLQQAEEALVAKQEL 291
Cdd:TIGR02169 417 RLSEELADLNAAIAGIEAKIN-ELEEEKEDKA--LEIKKQEWKLEQLAADLSKYEQ--ELYDLKEEYDRVEKELSKLQRE 491
|
250 260 270
....*....|....*....|....*....|...
gi 209862941 292 IDKLKEEAeqhKIVMETVPVLKAQADIYKADFQ 324
Cdd:TIGR02169 492 LAEAEAQA---RASEERVRGGRAVEEVLKASIQ 521
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
138-350 |
2.66e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 138 QALKELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESErevLQQQHSVQV 217
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE---IEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 218 DQLRMQNQSVEAALRMERQAASEEkrkLAQL--QAAYHQLFQDYDSHIKSskgmQLEDLRQQLQQAEEALVAKQELIDKL 295
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLLGSES---FSDFldRLSALSKIADADADLLE----ELKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 209862941 296 KEEAEQHKIVMETvpvLKAQADIYKADFQAErhaREKLVEKKEYLQEQLEQLQRE 350
Cdd:COG3883 163 KAELEAAKAELEA---QQAEQEALLAQLSAE---EAAAEAQLAELEAELAAAEAA 211
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
67-373 |
4.42e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 4.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 67 ETLQRCLEENQELRDAirqsnqmlrERCEEllhfqVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQL 146
Cdd:PRK02224 436 RTARERVEEAEALLEA---------GKCPE-----CGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERA 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 147 KkcqqqmaedkasvkaqvtsllgELQESQSRLEAATKDRQALEGRIravSEQVRQLESEREVLQQQHSvQVDQLRMQNQS 226
Cdd:PRK02224 502 E----------------------DLVEAEDRIERLEERREDLEELI---AERRETIEEKRERAEELRE-RAAELEAEAEE 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 227 VEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDShiksskgmqLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVM 306
Cdd:PRK02224 556 KREAAAEAEEEAEEAREEVAELNSKLAELKERIES---------LERIRTLLAAIADAEDEIERLREKREALAELNDERR 626
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 209862941 307 ETVPVLKAQADIYKADFQAER--HAREKLVEKKEYLQ---EQLEQLQREFNKL--KVGCHESA--RIEDMRKRHVE 373
Cdd:PRK02224 627 ERLAEKRERKRELEAEFDEARieEAREDKERAEEYLEqveEKLDELREERDDLqaEIGAVENEleELEELRERREA 702
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
77-373 |
1.62e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 77 QELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVErlSLEKLDLRSQREQALKELEQLKKCQQQMAED 156
Cdd:PTZ00121 1428 EEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE--AKKKAEEAKKADEAKKKAEEAKKKADEAKKA 1505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 157 KASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQ 236
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEE 1585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 237 AASEEKRKLAQLQAAYH--------QLFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMET 308
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYEeekkmkaeEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 209862941 309 VPvLKAQADIYKAD----FQAERHAREKLVEKKEYLQEQLEQLQREFNKLKVGCHESARIEDMRKRHVE 373
Cdd:PTZ00121 1666 EA-KKAEEDKKKAEeakkAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAE 1733
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
69-371 |
1.65e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 69 LQRCLEENQELRDAIRQsnqmLRERCEELlhfqvsqREEKEFLMCKFQEARKLVE--RLSLEKLD-----LRSQREQALK 141
Cdd:PRK02224 337 AQAHNEEAESLREDADD----LEERAEEL-------REEAAELESELEEAREAVEdrREEIEELEeeieeLRERFGDAPV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 142 ELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDR---------QALEG-----RIRAVSEQVRQLESERE 207
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLeagkcpecgQPVEGsphveTIEEDRERVEELEAELE 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 208 VLQQQHSVQVDQLRMQNQSVEAALRMERqaaSEEKRKLAQlqaayhQLFQDYDSHIKsSKGMQLEDLRQQLQQAEEALVA 287
Cdd:PRK02224 486 DLEEEVEEVEERLERAEDLVEAEDRIER---LEERREDLE------ELIAERRETIE-EKRERAEELRERAAELEAEAEE 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 288 KQELIDKLKEEAEQHKIV-----------------METVPVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLqRE 350
Cdd:PRK02224 556 KREAAAEAEEEAEEAREEvaelnsklaelkeriesLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEK-RE 634
|
330 340
....*....|....*....|.
gi 209862941 351 FNKLKVGCHESARIEDMRKRH 371
Cdd:PRK02224 635 RKRELEAEFDEARIEEAREDK 655
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
151-251 |
1.69e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 47.25 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 151 QQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQ--NQSVE 228
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKrkEITDQ 224
|
90 100
....*....|....*....|....*
gi 209862941 229 AALRMErqAASEEKRKL--AQLQAA 251
Cdd:PRK11448 225 AAKRLE--LSEEETRILidQQLRKA 247
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
39-301 |
3.01e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 39 AEDQDMLGEESSLGKPAMLHLPSEQGTPETLQRCLEEN----QELRDAIRQSN---QMLRERCEELLHFQVSQREEKEFL 111
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALrealDELRAELTLLNeeaANLRERLESLERRIAATERRLEDL 843
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 112 MCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGR 191
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 192 IRAVSEQVRQLESEREVLQQQHSVQVdQLRMQNQSVEAALRMERQAASEekRKLAQLQAAYHQL----------FQDYDS 261
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQERLSEEY-SLTLEEAEALENKIEDDEEEAR--RRLKRLENKIKELgpvnlaaieeYEELKE 1000
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 209862941 262 hiksskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQ 301
Cdd:TIGR02168 1001 --------RYDFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
63-240 |
3.03e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 63 QGTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKE 142
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 143 LEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAAtkDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRM 222
Cdd:TIGR02168 395 IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
170
....*....|....*...
gi 209862941 223 QNQSVEAALRMERQAASE 240
Cdd:TIGR02168 473 AEQALDAAERELAQLQAR 490
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
234-349 |
3.43e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 234 ERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMEtvpvlk 313
Cdd:PRK12704 48 KKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRN-ELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELE------ 120
|
90 100 110
....*....|....*....|....*....|....*.
gi 209862941 314 aqadiykadfQAERHAREKLVEKKEYLQEQLEQLQR 349
Cdd:PRK12704 121 ----------QKQQELEKKEEELEELIEEQLQELER 146
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
121-308 |
5.53e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 121 LVERLSLEKLDL-RSQREQALKELEQLKKCQQQMAEdKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQV 199
Cdd:COG4717 47 LLERLEKEADELfKPQGRKPELNLKELKELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 200 RQLESEREVLQQQHSV-----QVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGmQLEDL 274
Cdd:COG4717 126 QLLPLYQELEALEAELaelpeRLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE-ELEEL 204
|
170 180 190
....*....|....*....|....*....|....
gi 209862941 275 RQQLQQAEEALVAKQELIDKLKEEAEQHKIVMET 308
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
119-368 |
6.00e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.39 E-value: 6.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 119 RKLVERLslekLDLR--SQREQALKEL-----EQLKKCQQQMAEDKASVKAQvtsllgelQESQSRLEAATKDRQAlegR 191
Cdd:PHA02562 153 RKLVEDL----LDISvlSEMDKLNKDKirelnQQIQTLDMKIDHIQQQIKTY--------NKNIEEQRKKNGENIA---R 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 192 IRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAyHQLFQDYD------SHIKS 265
Cdd:PHA02562 218 KQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKV-IKMYEKGGvcptctQQISE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 266 SKGMqLEDLRQQLQQAEEALVAKQELIDKLKEEAeqHKIVMETVPVLKAQADIYKADFQAERHAREKLVEKKEYLQ---- 341
Cdd:PHA02562 297 GPDR-ITKIKDKLKELQHSLEKLDTAIDELEEIM--DEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEElqae 373
|
250 260 270
....*....|....*....|....*....|..
gi 209862941 342 -----EQLEQLQREFNKLKVGCHESARIEDMR 368
Cdd:PHA02562 374 fvdnaEELAKLQDELDKIVKTKSELVKEKYHR 405
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
59-355 |
8.01e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.95 E-value: 8.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 59 LPSEQGTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEflmckfQEARKLVERLSLEKldLRSQREQ 138
Cdd:COG5185 245 LEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTK------EKIAEYTKSIDIKK--ATESLEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 139 ALKELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEG--RIRAVSEQVR----QLESEREVLQQQ 212
Cdd:COG5185 317 QLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGevELSKSSEELDsfkdTIESTKESLDEI 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 213 HSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKS-SKGMQLEDLRQQLQQAEEALVAKQEL 291
Cdd:COG5185 397 PQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISElNKVMREADEESQSRLEEAYDEINRSV 476
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 209862941 292 IDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLK 355
Cdd:COG5185 477 RSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILA 540
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
77-374 |
1.01e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 77 QELRDAIRQSNQMLRE-RCEEllhfqVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKK------- 148
Cdd:PRK02224 436 RTARERVEEAEALLEAgKCPE-----CGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDlveaedr 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 149 ----------CQQQMAEDKASVKA---QVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESER----EVLQQ 211
Cdd:PRK02224 511 ierleerredLEELIAERRETIEEkreRAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLaelkERIES 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 212 QHSVQVDQLRMQNQSVEAALRMERQAA-----SEEKRKLAQLQAAYHQLFQDYDshiksskGMQLEDLRQQLQQAEEALv 286
Cdd:PRK02224 591 LERIRTLLAAIADAEDEIERLREKREAlaelnDERRERLAEKRERKRELEAEFD-------EARIEEAREDKERAEEYL- 662
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 287 akQELIDKLKEEAEQHKIVMETVPVLKAQADIYKaDFQAERHAREKLVEKKEYLQEQLEQLQREFNKLKVgchesarieD 366
Cdd:PRK02224 663 --EQVEEKLDELREERDDLQAEIGAVENELEELE-ELRERREALENRVEALEALYDEAEELESMYGDLRA---------E 730
|
....*...
gi 209862941 367 MRKRHVET 374
Cdd:PRK02224 731 LRQRNVET 738
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
67-363 |
1.29e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 67 ETLQRCLEENQELRDAIRQSNQMLRErceelLHFQVSQREEkeflmcKFQEARKLVERLSLEKLDLRSQREQALKELEQL 146
Cdd:COG4913 664 ASAEREIAELEAELERLDASSDDLAA-----LEEQLEELEA------ELEELEEELDELKGEIGRLEKELEQAEEELDEL 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 147 KKCQQQMAEDkasVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHsVQVDQLRMQNQS 226
Cdd:COG4913 733 QDRLEAAEDL---ARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAF-NREWPAETADLD 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 227 VEAAlrmerqAASEEKRKLAQLQA----AYHQLFQDYdshIKSSKGMQLEDLRQQLQQAEEALvakQELIDKLKEEAEQH 302
Cdd:COG4913 809 ADLE------SLPEYLALLDRLEEdglpEYEERFKEL---LNENSIEFVADLLSKLRRAIREI---KERIDPLNDSLKRI 876
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 209862941 303 K------IVMETVPVLKAQADIYKADFQAERHAREKLVEkkEYLQEQLEQLQREFNKLKVGCHESAR 363
Cdd:COG4913 877 PfgpgryLRLEARPRPDPEVREFRQELRAVTSGASLFDE--ELSEARFAALKRLIERLRSEEEESDR 941
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
70-367 |
2.11e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.80 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 70 QRCLEENQELRDAIRQSNQMLRERCEELLhfQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKC 149
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRAKLLMKRAAHVK--QQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 150 QQQMAEDKASVKAqVTSLLGELQESQSRLEAATKDRQALEGRIrAVSEQVRQLESEREVLQQQHSVQVDQLRMQNqsvEA 229
Cdd:TIGR00618 385 QQQKTTLTQKLQS-LCKELDILQREQATIDTRTSAFRDLQGQL-AHAKKQQELQQRYAELCAAAITCTAQCEKLE---KI 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 230 ALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGMQLED--LRQQLQQAEEALV------AKQELIDKLKEEAEQ 301
Cdd:TIGR00618 460 HLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPcpLCGSCIHPNPARQdidnpgPLTRRMQRGEQTYAQ 539
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 302 HKIVMETV----PVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLKVGCHESARIEDM 367
Cdd:TIGR00618 540 LETSEEDVyhqlTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDM 609
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
156-354 |
2.40e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.14 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 156 DKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLES------EREVLQQQHSV--QVDQLRMQNQSV 227
Cdd:COG0497 152 GLEELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAaalqpgEEEELEEERRRlsNAEKLREALQEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 228 EAALRMERQAAseekrkLAQLQAAYHQL--FQDYDSHIKSSKGM------QLEDLRQQLQQA-------EEALVAKQELI 292
Cdd:COG0497 232 LEALSGGEGGA------LDLLGQALRALerLAEYDPSLAELAERlesaliELEEAASELRRYldslefdPERLEEVEERL 305
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 209862941 293 DKLKEEAEQHKIVMETVPVLKAQAdiykadfQAERHAREKLVEKKEYLQEQLEQLQREFNKL 354
Cdd:COG0497 306 ALLRRLARKYGVTVEELLAYAEEL-------RAELAELENSDERLEELEAELAEAEAELLEA 360
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
138-307 |
2.76e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.14 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 138 QALKELEQLKKCQQQMAEDKASVKAQV---TSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHS 214
Cdd:PRK11637 41 HASDNRDQLKSIQQDIAAKEKSVRQQQqqrASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 215 VQVDQLRMQnqsVEAALRMERQAA------SEEKRKLAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAK 288
Cdd:PRK11637 121 AQERLLAAQ---LDAAFRQGEHTGlqlilsGEESQRGERILAYFGYLNQARQETIA-----ELKQTREELAAQKAELEEK 192
|
170
....*....|....*....
gi 209862941 289 QELIDKLKEEAEQHKIVME 307
Cdd:PRK11637 193 QSQQKTLLYEQQAQQQKLE 211
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
69-355 |
4.83e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 69 LQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKldlrSQREQALKELEqlkk 148
Cdd:TIGR02169 714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL----HKLEEALNDLE---- 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 149 cqqqmAEDKASVKAQVTSLLGELQESQSRLEAATkdrQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVE 228
Cdd:TIGR02169 786 -----ARLSHSRIPEIQAELSKLEEEVSRIEARL---REIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 229 AALRMERQAASEEKRK---LAQLQAAYHQLFQDYDSHIKSSKGMQ---------LEDLRQQLQQAEEALVAKQELIDKLK 296
Cdd:TIGR02169 858 NLNGKKEELEEELEELeaaLRDLESRLGDLKKERDELEAQLRELErkieeleaqIEKKRKRLSELKAKLEALEEELSEIE 937
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 209862941 297 EEAEQHKIVMETVPVL--------KAQADIYK---------ADFQAERHAREKLVEKKEYLQEQLEQLQR---EFNKLK 355
Cdd:TIGR02169 938 DPKGEDEEIPEEELSLedvqaelqRVEEEIRAlepvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILErieEYEKKK 1016
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
73-221 |
4.83e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 73 LEENQELRDAIR-----QSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLD--------LRSQREQA 139
Cdd:COG4913 271 LAELEYLRAALRlwfaqRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdrleqLEREIERL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 140 LKELEQLKKCQQQMAE-----------DKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREV 208
Cdd:COG4913 351 ERELEERERRRARLEAllaalglplpaSAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
170
....*....|....*.
gi 209862941 209 LQQQHSV---QVDQLR 221
Cdd:COG4913 431 LERRKSNipaRLLALR 446
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
157-304 |
5.91e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.88 E-value: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 157 KASVKAQVTSLLGELQESQSrLEAATKdrQALEGRIRAVSEQVRQLESEREVLQQQH---SVQVDQLRMQNQSVEAALRM 233
Cdd:PRK09039 51 KDSALDRLNSQIAELADLLS-LERQGN--QDLQDSVANLRASLSAAEAERSRLQALLaelAGAGAAAEGRAGELAQELDS 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 209862941 234 ERQAASEEKRKLAQLQAayhqlfqdydshiksskgmQLEDLRQQLQQAEEALVAKQElidklKEEAEQHKI 304
Cdd:PRK09039 128 EKQVSARALAQVELLNQ-------------------QIAALRRQLAALEAALDASEK-----RDRESQAKI 174
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
62-373 |
6.96e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 6.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 62 EQGTPETLQRCLEENQELRDAIRQSNQMlRERCEELLHFQVSQREEKEflMCKFQEARKLVErlsLEKLDLRSQREQALK 141
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKKADEAKKKAEEA-KKKADEAKKAAEAKKKADE--AKKAEEAKKADE---AKKAEEAKKADEAKK 1541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 142 ELEQLKKCQQQMAED--KASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVS---EQVRQLESEREVLQQQHSVQ 216
Cdd:PTZ00121 1542 AEEKKKADELKKAEElkKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMklyEEEKKMKAEEAKKAEEAKIK 1621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 217 VDQLRmQNQSVEAALRMERQAASEEKRKLAQLQAAyhqlfQDYDSHIKSSKGMQLEDLRQQLQQAEEALVAKQELIDKLK 296
Cdd:PTZ00121 1622 AEELK-KAEEEKKKVEQLKKKEAEEKKKAEELKKA-----EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALK 1695
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 209862941 297 EEAEQHKIVMETvpvlkaqadiyKADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLKVGCHEsARIEDMRKRHVE 373
Cdd:PTZ00121 1696 KEAEEAKKAEEL-----------KKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE-AKKDEEEKKKIA 1760
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
67-246 |
7.56e-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: 41.67 E-value: 7.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 67 ETLQRCLEENQELRDAIRQSNQMLRERCEELL--HFQVSQREEKEFLMcKFQEARKLVERLSLEKLDLRSQREQAlKELE 144
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQKEELAELLraLYRLGRQPPLALLL-SPEDFLDAVRRLQYLKYLAPARREQA-EELR 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 145 QLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQA----LEGRIRAVSEQVRQLESEREVLQQQHSvqvdql 220
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKllarLEKELAELAAELAELQQEAEELEALIA------ 230
|
170 180
....*....|....*....|....*.
gi 209862941 221 RMQNQSVEAALRMERQAASEEKRKLA 246
Cdd:COG4942 231 RLEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
103-287 |
8.80e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 8.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 103 SQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKkcQQQMAEDKASVKAQVTSLLGELQESQSRLEAAT 182
Cdd:COG4717 78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE--KLLQLLPLYQELEALEAELAELPERLEELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 183 KDRQALEGRIRAVSEQVRQLESEREVLQQQHSV----QVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLfqd 258
Cdd:COG4717 156 EELRELEEELEELEAELAELQEELEELLEQLSLateeELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL--- 232
|
170 180
....*....|....*....|....*....
gi 209862941 259 ydshiksSKGMQLEDLRQQLQQAEEALVA 287
Cdd:COG4717 233 -------ENELEAAALEERLKEARLLLLI 254
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
43-348 |
9.05e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.75 E-value: 9.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 43 DMLGEESSLGKPAMLHLPSEQGTPETLQRCLEENQELRDAIRQS-NQMLRERCEELLHFQVSQREEKEFLMCKFQEARKL 121
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAElNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 122 VERLSLEKLDLRSQR-EQALKELEQLKKCQQQMAEDKASVKAQVTSLlGELQESQSRLEAATKDRQAL------EGRIRA 194
Cdd:pfam12128 324 LEALEDQHGAFLDADiETAAADQEQLPSWQSELENLEERLKALTGKH-QDVTAKYNRRRSKIKEQNNRdiagikDKLAKI 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 195 VSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAyhqlfqdydshiksskgmqlEDL 274
Cdd:pfam12128 403 REARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATAT--------------------PEL 462
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 209862941 275 RQQLQQaeealvaKQELIDKLKEEAEQhkivmETVPVLKAQADIYKADFQAERhAREKLVEKKEYLQEQLEQLQ 348
Cdd:pfam12128 463 LLQLEN-------FDERIERAREEQEA-----ANAEVERLQSELRQARKRRDQ-ASEALRQASRRLEERQSALD 523
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
135-372 |
1.17e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.26 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 135 QREQALKELEQLKKCQQQMAEdkaSVKAQVTSLLGELqESQSRLEAATKDRQALEGRIRAVSEQVRQLESERE-----VL 209
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQE---RLRQEKEEKAREV-ERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERErelerIR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 210 QQQHSVQVDQLRMQNQSVEAA-------LRMERQAASEEKRKlaQLQAAYHQLFQDYDSHIKSSKGM-QLEDLRQQLQQA 281
Cdd:pfam17380 355 QEERKRELERIRQEEIAMEISrmrelerLQMERQQKNERVRQ--ELEAARKVKILEEERQRKIQQQKvEMEQIRAEQEEA 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 282 EEALVAKQElidklKEEAEQHKIVMETVPVLKAQADIYKADfQAERHAREKLVEKKEYLQEQLEQLQREFNKLKVGCHES 361
Cdd:pfam17380 433 RQREVRRLE-----EERAREMERVRLEEQERQQQVERLRQQ-EEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQ 506
|
250
....*....|.
gi 209862941 362 ARIEDMRKRHV 372
Cdd:pfam17380 507 AMIEEERKRKL 517
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
61-302 |
1.26e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.11 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 61 SEQGTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVE-RLSLEKLDLRSQREQA 139
Cdd:TIGR00618 567 EIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDvRLHLQQCSQELALKLT 646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 140 LKELEQLKKCQQQMAEDKASVKAQ----VTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSV 215
Cdd:TIGR00618 647 ALHALQLTLTQERVREHALSIRVLpkelLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENA 726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 216 QVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSskGMQLEDLRQQLQQAEEALVAKQELIDKL 295
Cdd:TIGR00618 727 SSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQT--GAELSHLAAEIQFFNRLREEDTHLLKTL 804
|
....*..
gi 209862941 296 KEEAEQH 302
Cdd:TIGR00618 805 EAEIGQE 811
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
124-370 |
1.46e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 124 RLSLEKLDLRSQREQALKELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRL---EAATKDRQALEGRIRAVSEQVR 200
Cdd:PRK04863 283 VHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLnlvQTALRQQEKIERYQADLEELEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 201 QLESEREVLQQQHSVQ-------------VDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAyHQLFQDYDSHIKSSK 267
Cdd:PRK04863 363 RLEEQNEVVEEADEQQeenearaeaaeeeVDELKSQLADYQQALDVQQTRAIQYQQAVQALERA-KQLCGLPDLTADNAE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 268 GMqLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVpvLKAQADIYKADfqAERHAREKL--VEKKEYLQEQLE 345
Cdd:PRK04863 442 DW-LEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLV--RKIAGEVSRSE--AWDVARELLrrLREQRHLAEQLQ 516
|
250 260
....*....|....*....|....*
gi 209862941 346 QLQREFNKLKVGCHESARIEDMRKR 370
Cdd:PRK04863 517 QLRMRLSELEQRLRQQQRAERLLAE 541
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
161-313 |
1.53e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 161 KAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRMQNQSVEAALRMERQAASE 240
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEA----ELEEKDERIERLERELSEARSEERR 459
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 209862941 241 EKRKlaqlqaayhqlfqdyDSHIKSSKGMqLEDLRQQLQQAEEALvakQELIDKLKEEAEQHKIVM--ETVPVLK 313
Cdd:COG2433 460 EIRK---------------DREISRLDRE-IERLERELEEERERI---EELKRKLERLKELWKLEHsgELVPVKV 515
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
67-356 |
1.65e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.83 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 67 ETLQRCLEENQELRDAIRQSNQMlreRCEELLHFQVSQREEKEF------LMCKFQEARKLVERLSLEKLDlrSQREQAL 140
Cdd:COG5022 800 QPLLSLLGSRKEYRSYLACIIKL---QKTIKREKKLRETEEVEFslkaevLIQKFGRSLKAKKRFSLLKKE--TIYLQSA 874
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 141 KELEQLKKCQQQMAEDKASVKaqvtsllgELQESQSRLEAatkdrQALEgriraVSEQVRQLESEREVLQQQHSVQVDQL 220
Cdd:COG5022 875 QRVELAERQLQELKIDVKSIS--------SLKLVNLELES-----EIIE-----LKKSLSSDLIENLEFKTELIARLKKL 936
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 221 RMQNQSVEAALRMERQaaSEEKRKLAQLQAAYHQLFQDYDSHIKSSKGM--QLEDLRQQLQQAEEALVAKQELIDKLKEE 298
Cdd:COG5022 937 LNNIDLEEGPSIEYVK--LPELNKLHEVESKLKETSEEYEDLLKKSTILvrEGNKANSELKNFKKELAELSKQYGALQES 1014
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 209862941 299 AEQHKIVMETVPVLKAQADIYKADfQAERHAREKLVEKKEYLQEQLEQLQREFNKLKV 356
Cdd:COG5022 1015 TKQLKELPVEVAELQSASKIISSE-STELSILKPLQKLKGLLLLENNQLQARYKALKL 1071
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
172-355 |
1.69e-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: 40.81 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 172 QESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQ-----------QHSVQVDQLRMQNQSVEAALRMERQAASE 240
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERykelkaelrelELALLVLRLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 241 EKRKLAQLQAAYHQLfqdydshikSSKGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKivmETVPVLKAQADIYK 320
Cdd:TIGR02168 255 LEELTAELQELEEKL---------EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR---ERLANLERQLEELE 322
|
170 180 190
....*....|....*....|....*....|....*
gi 209862941 321 ADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLK 355
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
132-356 |
1.82e-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: 40.71 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 132 LRSQREQALKELEQLKKCQQQMAEDKASVKAQVtSLLGELQESQSRLEAATkdrqaLEGRIRAVSEQVRQLESEREVLQQ 211
Cdd:COG3096 841 LRQRRSELERELAQHRAQEQQLRQQLDQLKEQL-QLLNKLLPQANLLADET-----LADRLEELREELDAAQEAQAFIQQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 212 QHSV------QVDQLRMQNQSVEaALRMERQAASEEKRKLAQLQAAYHQLFQDYdSHIKSSKGMQL--------EDLRQQ 277
Cdd:COG3096 915 HGKAlaqlepLVAVLQSDPEQFE-QLQADYLQAKEQQRRLKQQIFALSEVVQRR-PHFSYEDAVGLlgensdlnEKLRAR 992
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 209862941 278 LQQAEEALvakqeliDKLKEEAEQHkivmetvpvlKAQADIYKADFQAERHAREKlvekkeyLQEQLEQLQREFNKLKV 356
Cdd:COG3096 993 LEQAEEAR-------REAREQLRQA----------QAQYSQYNQVLASLKSSRDA-------KQQTLQELEQELEELGV 1047
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
114-355 |
2.05e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 114 KFQEARKLVERLSLEKLDLRSQREQALKELEQLKKcqqqMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIR 193
Cdd:PRK03918 201 ELEEVLREINEISSELPELREELEKLEKEVKELEE----LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 194 AVSEQVRQLESEREVLQQQhsvqvdqlrmqnqsveAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKsskgmQLED 273
Cdd:PRK03918 277 ELEEKVKELKELKEKAEEY----------------IKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-----ELEE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 274 LRQQLQQAEEALVAKQELIDKLKEEAEQHkivmETVPVLKAQADIYKADFQAErhAREKLVEKKEYLQEQLEQLQREFNK 353
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLEELEERHELY----EEAKAKKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIEEEISK 409
|
..
gi 209862941 354 LK 355
Cdd:PRK03918 410 IT 411
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
124-354 |
2.45e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 124 RLSLEKLDLRSQREQALKELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLE 203
Cdd:COG1196 592 LARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 204 SEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQlfqdydshiksskgmQLEDLRQQLQQAEE 283
Cdd:COG1196 672 AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELE---------------EEALEEQLEAEREE 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 284 ALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQA---------ERHAREKlvEKKEYLQEQLEQLQREFNKL 354
Cdd:COG1196 737 LLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvnllaiEEYEELE--ERYDFLSEQREDLEEARETL 814
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
130-289 |
2.66e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.28 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 130 LDLRSQREQALKELEQLKKcqqqmaedkasvkaQVTSLLGELQESQSRLEAATKDRQAlEGRIRAVSEQVRQLESE-REV 208
Cdd:PRK11281 69 LALLDKIDRQKEETEQLKQ--------------QLAQAPAKLRQAQAELEALKDDNDE-ETRETLSTLSLRQLESRlAQT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 209 LQQQHSVQVDQLRMQNQSVEAALRMERqAASEEKRKLAQLQAAYHQLFQDYDShiksskGMQLEDLRQQLQQAEEALVAK 288
Cdd:PRK11281 134 LDQLQNAQNDLAEYNSQLVSLQTQPER-AQAALYANSQRLQQIRNLLKGGKVG------GKALRPSQRVLLQAEQALLNA 206
|
.
gi 209862941 289 Q 289
Cdd:PRK11281 207 Q 207
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
141-251 |
3.13e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.56 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 141 KELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQV-----------RQLESER--- 206
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGaaaegragelaQELDSEKqvs 132
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 209862941 207 -------EVLQQqhsvQVDQLRMQNQSVEAALRmerqaASEEKRKLAQLQAA 251
Cdd:PRK09039 133 aralaqvELLNQ----QIAALRRQLAALEAALD-----ASEKRDRESQAKIA 175
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
92-342 |
3.24e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 92 ERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKCQQQMAEDKASVKAQVTSLLGEL 171
Cdd:PRK02224 223 ERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 172 QESQSRLEAATKDRQALEGRIravsEQVRQLESEREVLQQQHSVQVDQLRmqnqsvEAALRMERQAasEEKRKLAqlqaa 251
Cdd:PRK02224 303 GLDDADAEAVEARREELEDRD----EELRDRLEECRVAAQAHNEEAESLR------EDADDLEERA--EELREEA----- 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 252 yhqlfqdydshiksskgmqlEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAER-HAR 330
Cdd:PRK02224 366 --------------------AELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERdELR 425
|
250
....*....|..
gi 209862941 331 EKLVEKKEYLQE 342
Cdd:PRK02224 426 EREAELEATLRT 437
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
105-370 |
3.55e-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: 39.94 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 105 REEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKkcqQQMAEDKASVKAQVT------SLLGELQESQSRL 178
Cdd:COG3096 353 QEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLK---SQLADYQQALDVQQTraiqyqQAVQALEKARALC 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 179 EAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRM----ERQAASEEKRKLAQlQAAYHQ 254
Cdd:COG3096 430 GLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIagevERSQAWQTARELLR-RYRSQQ 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 255 LFQDYDSHIKsskgMQLEDLRQQLQQAEEAlvakQELIDKLKEEAEQHKIVMETVPVLKAQADIykadfqaerhAREKLV 334
Cdd:COG3096 509 ALAQRLQQLR----AQLAELEQRLRQQQNA----ERLLEEFCQRIGQQLDAAEELEELLAELEA----------QLEELE 570
|
250 260 270
....*....|....*....|....*....|....*.
gi 209862941 335 EKKEYLQEQLEQLQREFNKLKvgchesARIEDMRKR 370
Cdd:COG3096 571 EQAAEAVEQRSELRQQLEQLR------ARIKELAAR 600
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
67-354 |
4.20e-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: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 67 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQRE-----EKEFLMCKFQEARKLVERLSLEKLDLRSQREQALK 141
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEalndlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ 819
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 142 ELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLR 221
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 222 MQNQSVEaalrmERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKG---------MQLEDLRQQLQQAEEALVAKQELI 292
Cdd:TIGR02169 900 ELERKIE-----ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGedeeipeeeLSLEDVQAELQRVEEEIRALEPVN 974
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 209862941 293 DKLKEEAEqhkIVMETVPVLKAQadiyKADFQAERHAREKLVE-----KKEYLQEQLEQLQREFNKL 354
Cdd:TIGR02169 975 MLAIQEYE---EVLKRLDELKEK----RAKLEEERKAILERIEeyekkKREVFMEAFEAINENFNEI 1034
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
131-300 |
4.28e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.12 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 131 DLRSQREQALKELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQ 210
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 211 QQHSV---QVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVA 287
Cdd:COG4372 122 KERQDleqQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEE 201
|
170
....*....|...
gi 209862941 288 KQELIDKLKEEAE 300
Cdd:COG4372 202 LAEAEKLIESLPR 214
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
265-372 |
5.90e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 38.91 E-value: 5.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 265 SSKGMQLEDLRQQLQQAE---EALVAKQ-----ELIDKLKEEAEQhkivmetvpvLKAQADIYKADFQAERHAREKLVEK 336
Cdd:COG0542 407 DSKPEELDELERRLEQLEiekEALKKEQdeasfERLAELRDELAE----------LEEELEALKARWEAEKELIEEIQEL 476
|
90 100 110
....*....|....*....|....*....|....*.
gi 209862941 337 KEYLQEQLEQLQREFNKLKVGCHESARIEDMRKRHV 372
Cdd:COG0542 477 KEELEQRYGKIPELEKELAELEEELAELAPLLREEV 512
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
67-348 |
6.48e-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: 39.17 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 67 ETLQRCLEENQELRDAIRQSNQMLRERCEellhfQVSQREEKeflmckFQEARKLVERL---------SLEKLDLRS-QR 136
Cdd:COG3096 347 EKIERYQEDLEELTERLEEQEEVVEEAAE-----QLAEAEAR------LEAAEEEVDSLksqladyqqALDVQQTRAiQY 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 137 EQALKELEQLKKCQQQMAEDKASVKaqvtsllGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQ------ 210
Cdd:COG3096 416 QQAVQALEKARALCGLPDLTPENAE-------DYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCkiagev 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 211 ---QQHSVQVDQLRMQNQSVEAALRME--RQAASEEKRKLAQLQAAyHQLFQDYDSHIKS--SKGMQLEDLRQQL----- 278
Cdd:COG3096 489 ersQAWQTARELLRRYRSQQALAQRLQqlRAQLAELEQRLRQQQNA-ERLLEEFCQRIGQqlDAAEELEELLAELeaqle 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 279 ---QQAEEALVAKQELIDKLKEEAEQHKIVMETVPV-LKAQADIYK---------ADFQA-----------ERHA---RE 331
Cdd:COG3096 568 eleEQAAEAVEQRSELRQQLEQLRARIKELAARAPAwLAAQDALERlreqsgealADSQEvtaamqqllerEREAtveRD 647
|
330
....*....|....*..
gi 209862941 332 KLVEKKEYLQEQLEQLQ 348
Cdd:COG3096 648 ELAARKQALESQIERLS 664
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
171-306 |
6.83e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.61 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 171 LQESQSRLEAATKDRqalegrIRAVSEQVRQL--ESEREVLQQQHSVQVDQLRMQNQsvEAALRMERQAASEEKRKLAQL 248
Cdd:PRK12704 44 LEEAKKEAEAIKKEA------LLEAKEEIHKLrnEFEKELRERRNELQKLEKRLLQK--EENLDRKLELLEKREEELEKK 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 209862941 249 QAAYHQLFQDYDSHIKSSKGMQLEdLRQQLQQ-----AEEAlvaKQELIDKLKEEAEQHKIVM 306
Cdd:PRK12704 116 EKELEQKQQELEKKEEELEELIEE-QLQELERisgltAEEA---KEILLEKVEEEARHEAAVL 174
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
101-369 |
7.76e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.97 E-value: 7.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 101 QVSQREEKEflmcKFQEARKLVERLSLEKL-----------DLRSQREQALKELEQLKKCQQQMAEDKASVKAQVTSLLG 169
Cdd:PTZ00121 1282 ELKKAEEKK----KADEAKKAEEKKKADEAkkkaeeakkadEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD 1357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 170 ELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQ 249
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAK 1437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 250 AAYHQLFQDYDSHIKSSKGMQLEDLRQQLQQAEEAlvakqeliDKLKEEAEQHKIVMETVPvlKAQADIYKADfqaerHA 329
Cdd:PTZ00121 1438 KKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA--------DEAKKKAEEAKKADEAKK--KAEEAKKKAD-----EA 1502
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 209862941 330 REKLVEKKEYLQEQLEQLQREFNKLKvGCHESARIEDMRK 369
Cdd:PTZ00121 1503 KKAAEAKKKADEAKKAEEAKKADEAK-KAEEAKKADEAKK 1541
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
147-304 |
8.55e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 38.65 E-value: 8.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 147 KKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQhsvqvdqlrmQNQS 226
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEE----------AEKE 574
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 209862941 227 VEAALRMERQAASEEKRKLAQLQAAYHqlfqdydSHIKSSkgmQLEDLRQQLQQAEEALVAKqelidKLKEEAEQHKI 304
Cdd:PRK00409 575 AQQAIKEAKKEADEIIKELRQLQKGGY-------ASVKAH---ELIEARKRLNKANEKKEKK-----KKKQKEKQEEL 637
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
143-281 |
9.16e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 38.02 E-value: 9.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 143 LEQLKKcqQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQvrqLESEREVLQQQHSvQVDQLrm 222
Cdd:PRK09039 71 LERQGN--QDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQE---LDSEKQVSARALA-QVELL-- 142
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 209862941 223 qNQSVeAALRmerqaaseekRKLAQLQAAyhqlFQDYDSHIKSSKGmQLEDLRQQLQQA 281
Cdd:PRK09039 143 -NQQI-AALR----------RQLAALEAA----LDASEKRDRESQA-KIADLGRRLNVA 184
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
74-370 |
9.72e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 38.41 E-value: 9.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 74 EENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKCQQqm 153
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQ-- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 154 aEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRM 233
Cdd:pfam02463 251 -EEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 234 ERQAASEEKRKLAQLQAAYHQlFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLK 313
Cdd:pfam02463 330 LKKEKEEIEELEKELKELEIK-REAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQ 408
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 209862941 314 AQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLKVGCHESARIEDMRKR 370
Cdd:pfam02463 409 LLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDEL 465
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
115-312 |
9.93e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 37.91 E-value: 9.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 115 FQEARKLVERLSLekldlRSQREQ---ALKELEQ----LKKCQQQMAE--DKASV---KAQVTSLLGELQESQSRLEAAT 182
Cdd:COG3524 160 LAESEELVNQLSE-----RAREDAvrfAEEEVERaeerLRDAREALLAfrNRNGIldpEATAEALLQLIATLEGQLAELE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862941 183 KDRQALEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRmqnqsveaalrmERQAASEEKRKLAQLQAAYhqlfqdydsh 262
Cdd:COG3524 235 AELAALRSYLSPNSPQVRQLRRRIAALEK----QIAAER------------ARLTGASGGDSLASLLAEY---------- 288
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 209862941 263 iksskgmqlEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETV--PVL 312
Cdd:COG3524 289 ---------ERLELEREFAEKAYTSALAALEQARIEAARQQRYLAVIvqPTL 331
|
|
| |
