|
Name |
Accession |
Description |
Interval |
E-value |
| UBAN |
cd09803 |
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ... |
269-355 |
5.13e-20 |
|
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: 83.94 E-value: 5.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 269 MQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVERKELLQEQLEQLQ 348
Cdd:cd09803 1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80
|
....*..
gi 564329414 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 |
2.69e-18 |
|
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: 79.64 E-value: 2.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 270 QLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVERKELLQEQLEQLQR 349
Cdd:pfam16516 15 EIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEYLQR 94
|
....*.
gi 564329414 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 |
7.19e-18 |
|
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: 77.52 E-value: 7.19e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564329414 62 EQGTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLE 128
Cdd:pfam11577 1 DEETLEQMKELLTENHQLKEAMKQSNQAMKERCEELSAWQEKQKEEREFLECRFREARELLRRLSLE 67
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
67-301 |
2.34e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 67 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQALEDLEHL 146
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 147 KKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQ---QHSVQVDQLRMQ 223
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLErleRLEEELEELEEA 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564329414 224 NQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQ 301
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA--LLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
|
| zf_C2H2_10 |
pfam18414 |
C2H2 type zinc-finger; This is a zinc finger domain C2H2 which can be found in optineurin ... |
404-429 |
2.68e-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: 2.68e-11
10 20
....*....|....*....|....*.
gi 564329414 404 PDFCCPKCQYQAPDMDTLQIHVMECI 429
Cdd:pfam18414 1 PKHCCPKCQEQLPDIDTLQIHVMDCI 26
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
105-332 |
9.86e-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: 63.92 E-value: 9.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 105 REEKEFLMCKFQEARKLVERLSLEKLDLRRQREQALEDLEHLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKE 184
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 185 RQTLEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIK 264
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEA----QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 265 SSKGM--QLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREK 332
Cdd:TIGR02168 839 RLEDLeeQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
77-301 |
2.40e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 77 QELRDAIRQsnqmlRERCEELLHFQVSQREEKEFLMcKFQEARKLVERLSLEKLDLRRQREQALEDLEHLKKCQQQMAED 156
Cdd:COG1196 216 RELKEELKE-----LEAELLLLKLRELEAELEELEA-ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 157 KASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRMQNQSVEAALRMERQ 236
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE----ELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564329414 237 AASEEKRKLAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQ 301
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALR-----AAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
135-336 |
3.38e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.32 E-value: 3.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 135 QREQALEDLEHLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHS 214
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 215 VQVDQLRMQnqsVEAALRMERQAASEEkrklaqlqaayhqLFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVAKQELIDK 294
Cdd:COG4942 101 AQKEELAEL---LRALYRLGRQPPLAL-------------LLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 564329414 295 LKEEAEQHKIVMETvpvLKAQADIYKADFQAERHAREKLVER 336
Cdd:COG4942 165 LRAELEAERAELEA---LLAELEEERAALEALKAERQKLLAR 203
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
131-336 |
1.22e-09 |
|
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: 59.78 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 131 DLRRQREQALEDLEHLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQ 210
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 211 QQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKgmQLEDLRQQLQQA----EEALV 286
Cdd:COG4942 104 EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA--ELAALRAELEAEraelEALLA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 564329414 287 AKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVER 336
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
67-303 |
1.85e-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: 60.07 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 67 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQRE---EKEFLMCKFQEARKLVERLSLEKLDLRRQREQA---- 139
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRleqQKQILRERLANLERQLEELEAQLEELESKLDELaeel 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 140 ------LEDLEhlkkcqqqmaEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVL-QQQ 212
Cdd:TIGR02168 340 aeleekLEELK----------EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLeARL 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 213 HSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQdydshiksskgmQLEDLRQQLQQAEEALVAKQELI 292
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQE------------ELERLEEALEELREELEEAEQAL 477
|
250
....*....|.
gi 564329414 293 DKLKEEAEQHK 303
Cdd:TIGR02168 478 DAAERELAQLQ 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
69-340 |
3.75e-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: 3.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 69 LQRCLEENQELRDAIRQsnqmLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQALEDLEHLKK 148
Cdd:TIGR02168 700 LAELRKELEELEEELEQ----LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 149 CQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVE 228
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 229 -AALRMERQAASEEK--RKLAQLQAAYHQLFQDYDSHIK------------SSKGMQLEDLRQQLQQAEEALVAKQE--- 290
Cdd:TIGR02168 856 sLAAEIEELEELIEEleSELEALLNERASLEEALALLRSeleelseelrelESKRSELRRELEELREKLAQLELRLEgle 935
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564329414 291 -LIDKLKEE-AEQHKIVMETVPVLKAQADIYKAdfQAERHAR--------------------EKLVERKELL 340
Cdd:TIGR02168 936 vRIDNLQERlSEEYSLTLEEAEALENKIEDDEE--EARRRLKrlenkikelgpvnlaaieeyEELKERYDFL 1005
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
116-290 |
4.88e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 4.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 116 QEARKLVERLSLEKLDLRRQREQALEDLEHLKKCQQQMAEDK---------ASVKAQVTSLL---GELQESQSRLEAATK 183
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvasaereiAELEAELERLDassDDLAALEEQLEELEA 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 184 ERQTLEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDShi 263
Cdd:COG4913 700 ELEELEEELDELKGEIGRLEKELEQAEE----ELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEE-- 773
|
170 180
....*....|....*....|....*..
gi 564329414 264 ksskgmQLEDLRQQLQQAEEALVAKQE 290
Cdd:COG4913 774 ------RIDALRARLNRAEEELERAMR 794
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
67-326 |
6.21e-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: 58.16 E-value: 6.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 67 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFlmcKFQEarklverLSLEKLDLRRQREQALEDLEHL 146
Cdd:TIGR02169 180 EEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREY---EGYE-------LLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 147 KKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATkerqtlEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLR-MQNQ 225
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG------EEEQLRVKEKIGELEAEIASLERSIAEKERELEdAEER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 226 SVEAALRMERQAASEE--KRKLAQLQAAYHQLFQDYDShikssKGMQLEDLRQQLQQAE-------EALVAKQELIDKLK 296
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEelEREIEEERKRRDKLTEEYAE-----LKEELEDLRAELEEVDkefaetrDELKDYREKLEKLK 398
|
250 260 270
....*....|....*....|....*....|
gi 564329414 297 EEAEQHKIVMETVPVLKAQADIYKADFQAE 326
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNAA 428
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
73-294 |
2.00e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.56 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 73 LEENQELR-DAIRQSNQMLRERCEELLHfQVSQREEKeflMCKFQEARKLV-----ERLSLEKL-DLRRQREQALEDLEH 145
Cdd:COG3206 162 LEQNLELRrEEARKALEFLEEQLPELRK-ELEEAEAA---LEEFRQKNGLVdlseeAKLLLQQLsELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 146 LKKCQQQMAEDKASVKAQVTSLLG--ELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQ 223
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILAS 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564329414 224 -------NQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDshIKSSKGMQLEDLRQQLQQAEEALVAKQELIDK 294
Cdd:COG3206 318 leaeleaLQAREASLQAQLAQLEARLAELPELEAELRRLEREVE--VARELYESLLQRLEEARLAEALTVGNVRVIDP 393
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
115-301 |
7.62e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 7.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 115 FQEARKLVE------RLSLEKLDLRRQREqALEDLEHLKKCQQQMAEDKASVKAQVTSLlgELQESQSRLEAATKERQTL 188
Cdd:COG4913 224 FEAADALVEhfddleRAHEALEDAREQIE-LLEPIRELAERYAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 189 EGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKG 268
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE 380
|
170 180 190
....*....|....*....|....*....|...
gi 564329414 269 mQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQ 301
Cdd:COG4913 381 -EFAALRAEAAALLEALEEELEALEEALAEAEA 412
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
67-300 |
9.77e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 9.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 67 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKL-------DLRRQREQA 139
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQilrerlaNLERQLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 140 LEDLEHLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQhsvqvdq 219
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ------- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 220 lrmqnqsvEAALRMERQAASEEKRklaqlqaayhqlfqdydshiksskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEA 299
Cdd:TIGR02168 395 --------IASLNNEIERLEARLE--------------------------RLEDRRERLQQEIEELLKKLEEAELKELQA 440
|
.
gi 564329414 300 E 300
Cdd:TIGR02168 441 E 441
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
66-324 |
1.42e-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: 53.92 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 66 PETLQRCLEENQELRDAIRQSNQMLRERC----EELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQale 141
Cdd:TIGR02169 261 SELEKRLEEIEQLLEELNKKIKDLGEEEQlrvkEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAE--- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 142 dLEHLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQ----------Q 211
Cdd:TIGR02169 338 -IEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKreldrlqeelQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 212 QHSVQVDQLRMQNQSVEAALRmERQAASEEKRklAQLQAAYHQLFQDYDSHIKSSKgmQLEDLRQQLQQAEEALVAKQEL 291
Cdd:TIGR02169 417 RLSEELADLNAAIAGIEAKIN-ELEEEKEDKA--LEIKKQEWKLEQLAADLSKYEQ--ELYDLKEEYDRVEKELSKLQRE 491
|
250 260 270
....*....|....*....|....*....|...
gi 564329414 292 IDKLKEEAeqhKIVMETVPVLKAQADIYKADFQ 324
Cdd:TIGR02169 492 LAEAEAQA---RASEERVRGGRAVEEVLKASIQ 521
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
132-301 |
4.86e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 132 LRRQREqaledLEHLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQ 211
Cdd:TIGR02168 673 LERRRE-----IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 212 ---QHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIK--SSKGMQLEDLRQQLQQAEEALV 286
Cdd:TIGR02168 748 riaQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREalDELRAELTLLNEEAANLRERLE 827
|
170
....*....|....*
gi 564329414 287 AKQELIDKLKEEAEQ 301
Cdd:TIGR02168 828 SLERRIAATERRLED 842
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
172-336 |
8.35e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 8.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 172 QESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSV--QVDQLRMQNQSVEAA------LRMERQAASEEKR 243
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAlqRLAEYSWDEIDVASAereiaeLEAELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 244 KLAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADF 323
Cdd:COG4913 686 DLAALEEQLEELEAELEELEE-----ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALG 760
|
170
....*....|....
gi 564329414 324 QA-ERHAREKLVER 336
Cdd:COG4913 761 DAvERELRENLEER 774
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
119-301 |
9.51e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 9.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 119 RKLVERLSLEKLDLRRQREQALEDLEHLKKCQQQMAEDKASVKAqvtslLGELQESQSRLEAATKERQTLEGRIRAVSEQ 198
Cdd:COG4913 210 DDFVREYMLEEPDTFEAADALVEHFDDLERAHEALEDAREQIEL-----LEPIRELAERYAAARERLAELEYLRAALRLW 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 199 VRQLesEREVLQQqhsvQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAyhqlfqdydshIKSSKGMQLEDLRQQL 278
Cdd:COG4913 285 FAQR--RLELLEA----ELEELRAELARLEAELERLEARLDALREELDELEAQ-----------IRGNGGDRLEQLEREI 347
|
170 180
....*....|....*....|...
gi 564329414 279 QQAEEALVAKQELIDKLKEEAEQ 301
Cdd:COG4913 348 ERLERELEERERRRARLEALLAA 370
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
107-355 |
1.39e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 107 EKEFLMCKFQEARKLVERLSLEKLDLRRQREQALEDLehlKKCQQQMAEdkasVKAQVTSLLGELQESQSRLEAATKERQ 186
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAEL---QELEEKLEE----LRLEVSELEEEIEELQKELYALANEIS 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 187 TLEGRIRAVSEQVRQLESEREVLQQQH-----------------SVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQ 249
Cdd:TIGR02168 299 RLEQQKQILRERLANLERQLEELEAQLeeleskldelaeelaelEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 250 AAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAE--R 327
Cdd:TIGR02168 379 EQLETLRSKVAQLEL-----QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEelQ 453
|
250 260
....*....|....*....|....*...
gi 564329414 328 HAREKLVERKELLQEQLEQLQREFNKLK 355
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAE 481
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
88-342 |
3.52e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.30 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 88 QMLRERCEEL---LHFQVSQREEKEFLM----CKFQEARKLVERLSLEKLDLRRQREQALEDLEHLKKCQQQMAEDKASV 160
Cdd:TIGR02169 677 QRLRERLEGLkreLSSLQSELRRIENRLdelsQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 161 KAQVTSLLGELQESQSRLEAATKERQTLEGRIRavSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASE 240
Cdd:TIGR02169 757 KSELKELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 241 EKRKLAQLQAAYHQlfqdydshiKSSKGMQLEDLRQQL----QQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQA 316
Cdd:TIGR02169 835 IQELQEQRIDLKEQ---------IKSIEKEIENLNGKKeeleEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI 905
|
250 260
....*....|....*....|....*.
gi 564329414 317 DIYKADFQAERHAREKLVERKELLQE 342
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKLEALEE 931
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
121-308 |
5.47e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 5.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 121 LVERLSLEKLDLRRQREQALE-DLEHLKKCQQQMAEdKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQV 199
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPElNLKELKELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 200 RQLESEREVLQQQHSV-----QVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGmQLEDL 274
Cdd:COG4717 126 QLLPLYQELEALEAELaelpeRLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE-ELEEL 204
|
170 180 190
....*....|....*....|....*....|....
gi 564329414 275 RQQLQQAEEALVAKQELIDKLKEEAEQHKIVMET 308
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
138-336 |
6.16e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 138 QALEDLEHLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESErevLQQQHSVQV 217
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE---IEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 218 DQLRMQNQSVEAALRMERQAASEEkrkLAQL--QAAYHQLFQDYDSHIKSskgmQLEDLRQQLQQAEEALVAKQELIDKL 295
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLLGSES---FSDFldRLSALSKIADADADLLE----ELKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 564329414 296 KEEAEQHKIVMETvpvLKAQADIYKADFQAERHAREKLVER 336
Cdd:COG3883 163 KAELEAAKAELEA---QQAEQEALLAQLSAEEAAAEAQLAE 200
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
67-250 |
7.68e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 7.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 67 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQALEDLEHL 146
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 147 KKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTL------------EGRIRAVSEQVRQLESEREVLQQQHS 214
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLqqeieellkkleEAELKELQAELEELEEELEELQEELE 457
|
170 180 190
....*....|....*....|....*....|....*.
gi 564329414 215 VQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQA 250
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
70-291 |
1.57e-05 |
|
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: 47.27 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 70 QRCLEENQELRDAIRQSNQMLRERCEELLhfQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQALEDLEHLKKC 149
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRAKLLMKRAAHVK--QQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 150 QQQMAEDKASVKAqVTSLLGELQESQSRLEAATKERQTLEGRIrAVSEQVRQLESEREVLQQQHSVQVDQLRMQNqsvEA 229
Cdd:TIGR00618 385 QQQKTTLTQKLQS-LCKELDILQREQATIDTRTSAFRDLQGQL-AHAKKQQELQQRYAELCAAAITCTAQCEKLE---KI 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564329414 230 ALRMERQAASEEKRKLAQLQAAyhqlfqdydsHIKSSKGMQLEDLRQQLQQAEEALVAKQEL 291
Cdd:TIGR00618 460 HLQESAQSLKEREQQLQTKEQI----------HLQETRKKAVVLARLLELQEEPCPLCGSCI 511
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
151-251 |
1.80e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 47.25 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 151 QQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQ--NQSVE 228
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKrkEITDQ 224
|
90 100
....*....|....*....|....*
gi 564329414 229 AALRMErqAASEEKRKL--AQLQAA 251
Cdd:PRK11448 225 AAKRLE--LSEEETRILidQQLRKA 247
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
69-318 |
4.17e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 69 LQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLrrqrEQALEDLEhlkk 148
Cdd:TIGR02169 714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKL----EEALNDLE---- 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 149 cqqqmAEDKASVKAQVTSLLGELQESQSRLEAATKErqtLEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRMQNQSVE 228
Cdd:TIGR02169 786 -----ARLSHSRIPEIQAELSKLEEEVSRIEARLRE---IEQKLNRLTLEKEYLEKEIQELQE----QRIDLKEQIKSIE 853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 229 AALRMERQAASEEKRKLAQLQAAYHQLfqdydshiksskGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMET 308
Cdd:TIGR02169 854 KEIENLNGKKEELEEELEELEAALRDL------------ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921
|
250
....*....|
gi 564329414 309 vpvLKAQADI 318
Cdd:TIGR02169 922 ---LKAKLEA 928
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
69-305 |
4.42e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 69 LQRCLEENQELRDAIRQsnqmLRERCEELlhfqvsqREEKEFLMCKFQEARKLVE--RLSLEKLD-----LRRQREQALE 141
Cdd:PRK02224 337 AQAHNEEAESLREDADD----LEERAEEL-------REEAAELESELEEAREAVEdrREEIEELEeeieeLRERFGDAPV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 142 DLEHLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKER---------QTLEG-----RIRAVSEQVRQLESERE 207
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLeagkcpecgQPVEGsphveTIEEDRERVEELEAELE 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 208 VLQQQHSVQVDQLRMQNQSVEAALRMERqaaSEEKRKLAQlqaayhQLFQDYDSHIKsSKGMQLEDLRQQLQQAEEALVA 287
Cdd:PRK02224 486 DLEEEVEEVEERLERAEDLVEAEDRIER---LEERREDLE------ELIAERRETIE-EKRERAEELRERAAELEAEAEE 555
|
250
....*....|....*...
gi 564329414 288 KQELIDKLKEEAEQHKIV 305
Cdd:PRK02224 556 KREAAAEAEEEAEEAREE 573
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
67-221 |
7.18e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 7.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 67 ETLQRCLEENQELRDAIRQSNQMLRERCEELL--HFQVSQREEkeflmckfQEARKLVERLSLEKLDLRRQREQALEDLE 144
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEaqIRGNGGDRL--------EQLEREIERLERELEERERRRARLEALLA 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 145 HLKkcqQQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSV---QVDQLR 221
Cdd:COG4913 370 ALG---LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNipaRLLALR 446
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
63-303 |
7.30e-05 |
|
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: 45.34 E-value: 7.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 63 QGTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEF--LMCKFQEARKLVERLSL--EKLDLRRQREQ 138
Cdd:TIGR00618 215 DTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLkqLRARIEELRAQEAVLEEtqERINRARKAAP 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 139 ALEDLEHLKKCQQQMAEDKASVKAQVTSLLGELQESQSRL--EAATKERQTLEGRIRAVSEQVRQLESE----REVLQQQ 212
Cdd:TIGR00618 295 LAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVkqQSSIEEQRRLLQTLHSQEIHIRDAHEVatsiREISCQQ 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 213 HSVQvDQLRMQNQSVEAALRMERQAAS--EEKRKLAQLQAAYHQLFQDYDSHIKSSKGMQLEDLR----------QQLQQ 280
Cdd:TIGR00618 375 HTLT-QHIHTLQQQKTTLTQKLQSLCKelDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRyaelcaaaitCTAQC 453
|
250 260
....*....|....*....|...
gi 564329414 281 AEEALVAKQELIDKLKEEAEQHK 303
Cdd:TIGR00618 454 EKLEKIHLQESAQSLKEREQQLQ 476
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
67-246 |
7.35e-05 |
|
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: 44.75 E-value: 7.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 67 ETLQRCLEENQELRDAIRQSNQMLRERCEELL--HFQVSQREEKEFLMcKFQEARKLVERLSLEKlDLRRQREQALEDLE 144
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQKEELAELLraLYRLGRQPPLALLL-SPEDFLDAVRRLQYLK-YLAPARREQAEELR 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 145 HLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQT----LEGRIRAVSEQVRQLESEREVLQQQHSvqvdql 220
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKllarLEKELAELAAELAELQQEAEELEALIA------ 230
|
170 180
....*....|....*....|....*.
gi 564329414 221 RMQNQSVEAALRMERQAASEEKRKLA 246
Cdd:COG4942 231 RLEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
138-307 |
1.08e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.30 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 138 QALEDLEHLKKCQQQMAEDKASVKAQV---TSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHS 214
Cdd:PRK11637 41 HASDNRDQLKSIQQDIAAKEKSVRQQQqqrASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 215 VQVDQLRMQnqsVEAALRMERQAA------SEEKRKLAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAK 288
Cdd:PRK11637 121 AQERLLAAQ---LDAAFRQGEHTGlqlilsGEESQRGERILAYFGYLNQARQETIA-----ELKQTREELAAQKAELEEK 192
|
170
....*....|....*....
gi 564329414 289 QELIDKLKEEAEQHKIVME 307
Cdd:PRK11637 193 QSQQKTLLYEQQAQQQKLE 211
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
59-321 |
1.22e-04 |
|
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: 44.18 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 59 LPSEQGTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEflmckfQEARKLVERLSLEKldLRRQREQ 138
Cdd:COG5185 245 LEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTK------EKIAEYTKSIDIKK--ATESLEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 139 ALEDLEHLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEG--RIRAVSEQVR----QLESEREVLQQQ 212
Cdd:COG5185 317 QLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGevELSKSSEELDsfkdTIESTKESLDEI 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 213 HSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKS-SKGMQLEDLRQQLQQAEEALVAKQEL 291
Cdd:COG5185 397 PQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISElNKVMREADEESQSRLEEAYDEINRSV 476
|
250 260 270
....*....|....*....|....*....|
gi 564329414 292 IDKLKEEAEQHKIVMETVPVLKAQADIYKA 321
Cdd:COG5185 477 RSKKEDLNEELTQIESRVSTLKATLEKLRA 506
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
98-336 |
1.22e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 98 LHFQVSQREEKEfLMCKFQEARKLVERLSLEKLDLRRQREQALEDLEHLkkcqQQMAEDKASVKAQVTSLLGELQESQSR 177
Cdd:PRK02224 192 LKAQIEEKEEKD-LHERLNGLESELAELDEEIERYEEQREQARETRDEA----DEVLEEHEERREELETLEAEIEDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 178 LEAATKERQTLEGRIRAVSEQVRQLESEREVL----------QQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQ 247
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERLEELEEERDDLlaeaglddadAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAES 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 248 LQAAYHQLFQDYDshiksSKGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAER 327
Cdd:PRK02224 347 LREDADDLEERAE-----ELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREER 421
|
250
....*....|
gi 564329414 328 -HAREKLVER 336
Cdd:PRK02224 422 dELREREAEL 431
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
101-355 |
2.06e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 101 QVSQREEKEFLMCKfqEARKLVERLSLEKLDLRRQRE-----QALEDLEHLKKcQQQMAEDKASVKAQVTSLLGELQESQ 175
Cdd:TIGR02169 181 EVEENIERLDLIID--EKRQQLERLRREREKAERYQAllkekREYEGYELLKE-KEALERQKEAIERQLASLEEELEKLT 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 176 SRLEAATKERQTLEGRIRAVSEQVRQLESEREVlqqqhsvqvdQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQL 255
Cdd:TIGR02169 258 EEISELEKRLEEIEQLLEELNKKIKDLGEEEQL----------RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 256 FQDYDShiksskgmqledLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETvpvLKAQADIYKADFQAERHAREKLVE 335
Cdd:TIGR02169 328 EAEIDK------------LLAEIEELEREIEEERKRRDKLTEEYAELKEELED---LRAELEEVDKEFAETRDELKDYRE 392
|
250 260
....*....|....*....|
gi 564329414 336 RKEllqeqleQLQREFNKLK 355
Cdd:TIGR02169 393 KLE-------KLKREINELK 405
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
157-304 |
2.89e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.65 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 157 KASVKAQVTSLLGELQESQSrLEAATKerQTLEGRIRAVSEQVRQLESEREVLQQQH---SVQVDQLRMQNQSVEAALRM 233
Cdd:PRK09039 51 KDSALDRLNSQIAELADLLS-LERQGN--QDLQDSVANLRASLSAAEAERSRLQALLaelAGAGAAAEGRAGELAQELDS 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564329414 234 ERQAASEEKRKLAQLQAayhqlfqdydshiksskgmQLEDLRQQLQQAEEALVAKQElidklKEEAEQHKI 304
Cdd:PRK09039 128 EKQVSARALAQVELLNQ-------------------QIAALRRQLAALEAALDASEK-----RDRESQAKI 174
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
64-301 |
2.98e-04 |
|
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: 43.02 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 64 GTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFlmcKFQEARKLVERLSLEkldlrrqREQALEDL 143
Cdd:COG5185 272 ENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQL---AAAEAEQELEESKRE-------TETGIQNL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 144 EH-LKKCQQQMAEDKASVKAQVTSLLGELQESQSRlEAATKERQTLEGRIRAVSEQVR-QLESEREVLQ----------Q 211
Cdd:COG5185 342 TAeIEQGQESLTENLEAIKEEIENIVGEVELSKSS-EELDSFKDTIESTKESLDEIPQnQRGYAQEILAtledtlkaadR 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 212 QHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVAKQEL 291
Cdd:COG5185 421 QIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKAT 500
|
250
....*....|
gi 564329414 292 IDKLKEEAEQ 301
Cdd:COG5185 501 LEKLRAKLER 510
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
67-283 |
4.21e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 67 ETLQRCLEENQELRDAIRQSNQMLRErceelLHFQVSQREEKeflmckFQEARKLVERLSLEKLDLRRQREQALEDLEHL 146
Cdd:COG4913 664 ASAEREIAELEAELERLDASSDDLAA-----LEEQLEELEAE------LEELEEELDELKGEIGRLEKELEQAEEELDEL 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 147 KKCQQQMAEDkasVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHsVQVDQLRMQNQS 226
Cdd:COG4913 733 QDRLEAAEDL---ARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAF-NREWPAETADLD 808
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564329414 227 VEAAlrmerqAASEEKRKLAQLQA----AYHQLFQDYdshIKSSKGMQLEDLRQQLQQAEE 283
Cdd:COG4913 809 ADLE------SLPEYLALLDRLEEdglpEYEERFKEL---LNENSIEFVADLLSKLRRAIR 860
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
161-313 |
4.87e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 161 KAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRMQNQSVEAALRMERQAASE 240
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEA----ELEEKDERIERLERELSEARSEERR 459
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564329414 241 EKRKlaqlqaayhqlfqdyDSHIKSSKGMqLEDLRQQLQQAEEALvakQELIDKLKEEAEQHKIVM--ETVPVLK 313
Cdd:COG2433 460 EIRK---------------DREISRLDRE-IERLERELEEERERI---EELKRKLERLKELWKLEHsgELVPVKV 515
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
131-300 |
6.20e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 131 DLRRQREQALEDLEHLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQ 210
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 211 QQHSV---QVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVA 287
Cdd:COG4372 122 KERQDleqQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEE 201
|
170
....*....|...
gi 564329414 288 KQELIDKLKEEAE 300
Cdd:COG4372 202 LAEAEKLIESLPR 214
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
77-303 |
6.58e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.25 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 77 QELRDAIRQSNQMLRERcEELLHFQVSQREEKEFLMCKFQEARKLVERLSL-------EKLD-LRRQREQALEDLEHLKK 148
Cdd:COG3096 836 AELAALRQRRSELEREL-AQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLladetlaDRLEeLREELDAAQEAQAFIQQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 149 CQQQMA--EDKASVKAQVTSLLGELQEsqsRLEAATKERQTLEGRIRAVSEQVRQLE----SEREVLQQQHSVQVDQLRM 222
Cdd:COG3096 915 HGKALAqlEPLVAVLQSDPEQFEQLQA---DYLQAKEQQRRLKQQIFALSEVVQRRPhfsyEDAVGLLGENSDLNEKLRA 991
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 223 QNQSVEAALRMERQAASEEKRKLAQlqaaYHQLFQDYDSHiKSSKGMQLEDLRQQLQQ-----AEEALVAKQELIDKLKE 297
Cdd:COG3096 992 RLEQAEEARREAREQLRQAQAQYSQ----YNQVLASLKSS-RDAKQQTLQELEQELEElgvqaDAEAEERARIRRDELHE 1066
|
....*.
gi 564329414 298 EAEQHK 303
Cdd:COG3096 1067 ELSQNR 1072
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
43-302 |
1.00e-03 |
|
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: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 43 DMLGEESSLGKPAMLHLPSEQGTPETLQRCLEENQELRDAIRQS-NQMLRERCEELLHFQVSQREEKEFLMCKFQEARKL 121
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAElNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 122 VERLSLEKLDLRRQR-EQALEDLEHLKKCQQQMAEDKASVKAQVTSLlGELQESQSRLEAATKERQTL------EGRIRA 194
Cdd:pfam12128 324 LEALEDQHGAFLDADiETAAADQEQLPSWQSELENLEERLKALTGKH-QDVTAKYNRRRSKIKEQNNRdiagikDKLAKI 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 195 VSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQdydshiKSSKGMQLEDL 274
Cdd:pfam12128 403 REARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQ------LENFDERIERA 476
|
250 260 270
....*....|....*....|....*....|.
gi 564329414 275 RQQLQQA---EEALVAKQELIDKLKEEAEQH 302
Cdd:pfam12128 477 REEQEAAnaeVERLQSELRQARKRRDQASEA 507
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
234-303 |
1.17e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 1.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 234 ERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHK 303
Cdd:PRK12704 48 KKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRN-ELQKLEKRLLQKEENLDRKLELLEKREEELEKKE 116
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
171-306 |
1.31e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 171 LQESQSRLEAATKERqtlegrIRAVSEQVRQL--ESEREVLQQQHSVQVDQLRMQNQsvEAALRMERQAASEEKRKLAQL 248
Cdd:PRK12704 44 LEEAKKEAEAIKKEA------LLEAKEEIHKLrnEFEKELRERRNELQKLEKRLLQK--EENLDRKLELLEKREEELEKK 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564329414 249 QAAYHQLFQDYDSHIKSSKGMQLEdLRQQLQQ-----AEEAlvaKQELIDKLKEEAEQHKIVM 306
Cdd:PRK12704 116 EKELEQKQQELEKKEEELEELIEE-QLQELERisgltAEEA---KEILLEKVEEEARHEAAVL 174
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
67-301 |
1.48e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 67 ETLQRCLEENQELRDAirqsnqmlrERCEEllhfqVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQALEDLEHL 146
Cdd:PRK02224 436 RTARERVEEAEALLEA---------GKCPE-----CGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERA 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 147 KkcqqqmaedkasvkaqvtsllgELQESQSRLEAATKERQTLEGRIravSEQVRQLESEREVLQQQHSvQVDQLRMQNQS 226
Cdd:PRK02224 502 E----------------------DLVEAEDRIERLEERREDLEELI---AERRETIEEKRERAEELRE-RAAELEAEAEE 555
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564329414 227 VEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDShiksskgmqLEDLRQQLQQAEEALVAKQELIDKLKEEAEQ 301
Cdd:PRK02224 556 KREAAAEAEEEAEEAREEVAELNSKLAELKERIES---------LERIRTLLAAIADAEDEIERLREKREALAEL 621
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
147-304 |
1.53e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 147 KKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQhsvqvdqlrmQNQS 226
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEE----------AEKE 574
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564329414 227 VEAALRMERQAASEEKRKLAQLQAAYHqlfqdydSHIKSSkgmQLEDLRQQLQQAEEALVAKqelidKLKEEAEQHKI 304
Cdd:PRK00409 575 AQQAIKEAKKEADEIIKELRQLQKGGY-------ASVKAH---ELIEARKRLNKANEKKEKK-----KKKQKEKQEEL 637
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
83-287 |
1.95e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 83 IRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQaledLEHLKKCQQQMAEdkasvKA 162
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK----LEKLLQLLPLYQE-----LE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 163 QVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSV----QVDQLRMQNQSVEAALRMERQAA 238
Cdd:COG4717 136 ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLateeELQDLAEELEELQQRLAELEEEL 215
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 564329414 239 SEEKRKLAQLQAAYHQLfqdydshiksSKGMQLEDLRQQLQQAEEALVA 287
Cdd:COG4717 216 EEAQEELEELEEELEQL----------ENELEAAALEERLKEARLLLLI 254
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
67-302 |
2.05e-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: 40.72 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 67 ETLQRCLEENQELRDAIrQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQALED--LE 144
Cdd:TIGR00618 584 EDIPNLQNITVRLQDLT-EKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQErvRE 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 145 HLKKCQQQMAEDKASVKAqvtsllgELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQN 224
Cdd:TIGR00618 663 HALSIRVLPKELLASRQL-------ALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLA 735
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564329414 225 QSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSskGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQH 302
Cdd:TIGR00618 736 AREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQT--GAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQE 811
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
77-298 |
2.12e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 77 QELRDAIRQSNQMLRE-RCEEllhfqVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQR---EQALEDLEHLKKC--- 149
Cdd:PRK02224 436 RTARERVEEAEALLEAgKCPE-----CGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVeevEERLERAEDLVEAedr 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 150 -----------QQQMAEDKASVKA---QVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESER----EVLQQ 211
Cdd:PRK02224 511 ierleerredlEELIAERRETIEEkreRAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLaelkERIES 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 212 QHSVQVDQLRMQNQSVEAALRMERQAA-----SEEKRKLAQLQAAYHQLFQDYDshiksskGMQLEDLRQQLQQAEEALV 286
Cdd:PRK02224 591 LERIRTLLAAIADAEDEIERLREKREAlaelnDERRERLAEKRERKRELEAEFD-------EARIEEAREDKERAEEYLE 663
|
250
....*....|..
gi 564329414 287 AKQELIDKLKEE 298
Cdd:PRK02224 664 QVEEKLDELREE 675
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
173-298 |
2.16e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 39.74 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 173 ESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAY 252
Cdd:pfam09787 44 ALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEEL 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 253 HQLFQD-------YDSHIKSsKGMQLEDLRQQL--------QQAE---------EALVAKQELIDKLKEE 298
Cdd:pfam09787 124 RYLEEElrrskatLQSRIKD-REAEIEKLRNQLtsksqsssSQSElenrlhqltETLIQKQTMLEALSTE 192
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
175-354 |
2.41e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 175 QSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSV-----QVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQ 249
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLvdlseEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 250 AayhQLFQDYDSHIKSSKGMQLEDLRQQLQQAEealvakQELIDKLKEEAEQHKIVMEtvpvLKAQADIYKADFQAE--- 326
Cdd:COG3206 247 A---QLGSGPDALPELLQSPVIQQLRAQLAELE------AELAELSARYTPNHPDVIA----LRAQIAALRAQLQQEaqr 313
|
170 180 190
....*....|....*....|....*....|...
gi 564329414 327 -----RHAREKLVERKELLQEQLEQLQREFNKL 354
Cdd:COG3206 314 ilaslEAELEALQAREASLQAQLAQLEARLAEL 346
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
65-246 |
2.51e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.14 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 65 TPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVsqreekeflmcKFQEARKLVERLSLEKLDLRRQREQALEDLE 144
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELED-----------ELAALEARLEAAKTELEDLEKEIKRLELEIE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 145 HLkkcQQQMAEDKASVKAQVTSllGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHS---VQVDQLR 221
Cdd:COG1579 70 EV---EARIKKYEEQLGNVRNN--KEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAeleAELEEKK 144
|
170 180
....*....|....*....|....*
gi 564329414 222 MQNQSVEAALRMERQAASEEKRKLA 246
Cdd:COG1579 145 AELDEELAELEAELEELEAEREELA 169
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
67-320 |
2.56e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.45 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 67 ETLQRCLEENQELRDAIRQSNQMlreRCEELLHFQVSQREEKEFLMckfqEARKLVERLSLEKLDLRRQREqaLEDLEHL 146
Cdd:COG5022 800 QPLLSLLGSRKEYRSYLACIIKL---QKTIKREKKLRETEEVEFSL----KAEVLIQKFGRSLKAKKRFSL--LKKETIY 870
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 147 KKCQQQMAEDKASVKaqvtsllgELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQS 226
Cdd:COG5022 871 LQSAQRVELAERQLQ--------ELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDL 942
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 227 VEAALRMERQaaSEEKRKLAQLQAAYHQLFQDYDSHIKSSKGM--QLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKI 304
Cdd:COG5022 943 EEGPSIEYVK--LPELNKLHEVESKLKETSEEYEDLLKKSTILvrEGNKANSELKNFKKELAELSKQYGALQESTKQLKE 1020
|
250
....*....|....*.
gi 564329414 305 VMETVPVLKAQADIYK 320
Cdd:COG5022 1021 LPVEVAELQSASKIIS 1036
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
101-289 |
2.80e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.10 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 101 QVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQALEDLE-----------HLKKCQQQMAEDKASVKAQVTSLLG 169
Cdd:pfam15921 305 QEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEkqlvlanseltEARTERDQFSQESGNLDDQLQKLLA 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 170 ELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESErevlqqqhsvqVDQLRMQNQSVEAALR-MERQAASEEKRKLAQL 248
Cdd:pfam15921 385 DLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRE-----------LDDRNMEVQRLEALLKaMKSECQGQMERQMAAI 453
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 564329414 249 QAAYHQLFQdydshiKSSKGMQLEDLRQQLQQAEEALVAKQ 289
Cdd:pfam15921 454 QGKNESLEK------VSSLTAQLESTKEMLRKVVEELTAKK 488
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
103-315 |
3.28e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.00 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 103 SQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQALEDLEHLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAAT 182
Cdd:TIGR04523 194 NKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQ 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 183 KERQTLEGRIRAVSEQVRQLESEREVLQQQHSV---------------QVDQLRMQ-NQSVEAALRMERQAA-------- 238
Cdd:TIGR04523 274 KELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwnkelkselknqekKLEEIQNQiSQNNKIISQLNEQISqlkkeltn 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 239 -----SEEKRKLAQLQAAYHQLFQDYDSHIKSSKGM--QLEDLRQQLQQAEEALVAKQELIDKLKEEAE----QHKIVME 307
Cdd:TIGR04523 354 sesenSEKQRELEEKQNEIEKLKKENQSYKQEIKNLesQINDLESKIQNQEKLNQQKDEQIKKLQQEKEllekEIERLKE 433
|
....*...
gi 564329414 308 TVPVLKAQ 315
Cdd:TIGR04523 434 TIIKNNSE 441
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
115-312 |
3.52e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 39.45 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 115 FQEARKLVERLSlekldlRRQREQALEDLE--------HLKKCQQQMAE--DKASV---KAQVTSLLGELQESQSRLEAA 181
Cdd:COG3524 160 LAESEELVNQLS------ERAREDAVRFAEeeveraeeRLRDAREALLAfrNRNGIldpEATAEALLQLIATLEGQLAEL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 182 TKERQTLEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRmqnqsveaalrmERQAASEEKRKLAQLQAAYhqlfqdyds 261
Cdd:COG3524 234 EAELAALRSYLSPNSPQVRQLRRRIAALEK----QIAAER------------ARLTGASGGDSLASLLAEY--------- 288
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564329414 262 hiksskgmqlEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETV--PVL 312
Cdd:COG3524 289 ----------ERLELEREFAEKAYTSALAALEQARIEAARQQRYLAVIvqPTL 331
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
77-373 |
3.59e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 77 QELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVErlSLEKLDLRRQREQALEDLEHLKKCQQQMAED 156
Cdd:PTZ00121 1428 EEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE--AKKKAEEAKKADEAKKKAEEAKKKADEAKKA 1505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 157 KASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQ 236
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEE 1585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 237 AASEEKRKLAQLQAAYH--------QLFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMET 308
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYEeekkmkaeEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564329414 309 VPvLKAQADIYKAD----FQAERHAREKLVERKELLQEQLEQLQREFNKLKVGCHESARIEDMRKRHVE 373
Cdd:PTZ00121 1666 EA-KKAEEDKKKAEeakkAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAE 1733
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
184-303 |
3.63e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 184 ERQTLEGRIRAVSEQVRQLES-EREVLQQQHsvQVDQLRmqnQSVEAALRmeRQAASEEKRKLAQLQAAYHQLFqdyDSH 262
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERaHEALEDARE--QIELLE---PIRELAER--YAAARERLAELEYLRAALRLWF---AQR 288
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 564329414 263 IKSSKGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHK 303
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELE 329
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
143-251 |
4.04e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.18 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 143 LEHLKKcqQQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLE--SER-----EVLQQQhsv 215
Cdd:PRK09039 71 LERQGN--QDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKqvSARalaqvELLNQQ--- 145
|
90 100 110
....*....|....*....|....*....|....*.
gi 564329414 216 qVDQLRMQNQSVEAALRmerqaASEEKRKLAQLQAA 251
Cdd:PRK09039 146 -IAALRRQLAALEAALD-----ASEKRDRESQAKIA 175
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
101-303 |
8.53e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.58 E-value: 8.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 101 QVSQREEKEflmcKFQEARKLVERLSLEKL-----------DLRRQREQALEDLEHLKKCQQQMAEDKASVKAQVTSLLG 169
Cdd:PTZ00121 1282 ELKKAEEKK----KADEAKKAEEKKKADEAkkkaeeakkadEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD 1357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 170 ELQESQSRLEAATKERQTLEGRIRAV---SEQVRQLESEREVLQQQHSvQVDQLRMQNQSVEAALRMERQAasEEKRKLA 246
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKKKEEAKKKADAAkkkAEEKKKADEAKKKAEEDKK-KADELKKAAAAKKKADEAKKKA--EEKKKAD 1434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564329414 247 QLQAAYHQLFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVAKQEL-----IDKLKEEAEQHK 303
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAeeakkADEAKKKAEEAK 1496
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
67-331 |
9.54e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 38.39 E-value: 9.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 67 ETLQRCLEENQELRDAIRQSNQMLRERCEellhfQVSQREEkeflmcKFQEARKLVERLSLEKLDLRR----------QR 136
Cdd:COG3096 347 EKIERYQEDLEELTERLEEQEEVVEEAAE-----QLAEAEA------RLEAAEEEVDSLKSQLADYQQaldvqqtraiQY 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 137 EQALEDLEhlkKCQQQMAEDKASVKaqvtSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQ------ 210
Cdd:COG3096 416 QQAVQALE---KARALCGLPDLTPE----NAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCkiagev 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 211 ---QQHSVQVDQLRMQNQSVEAALRME--RQAASEEKRKLAQLQAAyHQLFQDYDSHIKS--SKGMQLEDLRQQLQQAEE 283
Cdd:COG3096 489 ersQAWQTARELLRRYRSQQALAQRLQqlRAQLAELEQRLRQQQNA-ERLLEEFCQRIGQqlDAAEELEELLAELEAQLE 567
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 564329414 284 ALVAKQ-ELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHARE 331
Cdd:COG3096 568 ELEEQAaEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLRE 616
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
69-294 |
9.85e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 38.40 E-value: 9.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 69 LQRCLEENQELRDAIRQSNQMLR--ERCEELLHFQvsqreEKEFLMCKFQEARKLVERLSLEKLDLRRQrEQALEDLEHL 146
Cdd:PRK04863 853 LADHESQEQQQRSQLEQAKEGLSalNRLLPRLNLL-----ADETLADRVEEIREQLDEAEEAKRFVQQH-GNALAQLEPI 926
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 147 KKCQQQMAEDKASVKAQVtsllgelqesqsrlEAATKERQTLEGRIRAVSEQVRQLE----SEREVLQQQHSVQVDQLRM 222
Cdd:PRK04863 927 VSVLQSDPEQFEQLKQDY--------------QQAQQTQRDAKQQAFALTEVVQRRAhfsyEDAAEMLAKNSDLNEKLRQ 992
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 223 QNQSVEAALRMERQAASEEKRKLAQlqaaYHQLFQDYDSHIkSSKGMQLEDLRQQLQQ--------AEEALVAKQELIDK 294
Cdd:PRK04863 993 RLEQAEQERTRAREQLRQAQAQLAQ----YNQVLASLKSSY-DAKRQMLQELKQELQDlgvpadsgAEERARARRDELHA 1067
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
67-299 |
9.85e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 38.56 E-value: 9.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 67 ETLQRCLEE-NQELRDAIRQSNQM--LRERCEELLHFQVSQREEKEFLMCKFQEARKLVERL-SLEKLDLRRQREQALED 142
Cdd:pfam15921 74 EHIERVLEEySHQVKDLQRRLNESneLHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRReSQSQEDLRNQLQNTVHE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 143 LEHLKKCQQQMAEDKASVKAQVTSLL----GELQESQSRL----EAATK-----------------------------ER 185
Cdd:pfam15921 154 LEAAKCLKEDMLEDSNTQIEQLRKMMlsheGVLQEIRSILvdfeEASGKkiyehdsmstmhfrslgsaiskilreldtEI 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329414 186 QTLEGRIRAVSEQVRQLESER----EVLQQQHSVQVDQL------------------RMQNQSVEAALRMERQAASEEK- 242
Cdd:pfam15921 234 SYLKGRIFPVEDQLEALKSESqnkiELLLQQHQDRIEQLiseheveitgltekassaRSQANSIQSQLEIIQEQARNQNs 313
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564329414 243 ---RKLAQLQAAYHQLfqdyDSHIKSSKGM---QLEDLRQQLQQAEEALVAKQELIDKLKEEA 299
Cdd:pfam15921 314 mymRQLSDLESTVSQL----RSELREAKRMyedKIEELEKQLVLANSELTEARTERDQFSQES 372
|
|
| |
