|
Name |
Accession |
Description |
Interval |
E-value |
| UBAN |
cd09803 |
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ... |
251-337 |
2.76e-19 |
|
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: 82.01 E-value: 2.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 251 MQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVERKELLQEQLEQLQ 330
Cdd:cd09803 1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80
|
....*..
gi 40018574 331 REFNKLK 337
Cdd:cd09803 81 RENQELK 87
|
|
| CC2-LZ |
pfam16516 |
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ... |
252-337 |
1.34e-17 |
|
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: 77.72 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 252 QLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVERKELLQEQLEQLQR 331
Cdd:pfam16516 15 EIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEYLQR 94
|
....*.
gi 40018574 332 EFNKLK 337
Cdd:pfam16516 95 QNQQLK 100
|
|
| NEMO |
pfam11577 |
NF-kappa-B essential modulator NEMO; NEMO is a regulatory protein which is part of the IKK ... |
44-110 |
7.19e-17 |
|
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: 74.44 E-value: 7.19e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40018574 44 EQGTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLE 110
Cdd:pfam11577 1 DEETLEQMKELLTENHQLKEAMKQSNQAMKERCEELSAWQEKQKEEREFLECRFREARELLRRLSLE 67
|
|
| zf_C2H2_10 |
pfam18414 |
C2H2 type zinc-finger; This is a zinc finger domain C2H2 which can be found in optineurin ... |
386-411 |
1.17e-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: 58.76 E-value: 1.17e-11
10 20
....*....|....*....|....*.
gi 40018574 386 PDFCCPKCQYQAPDMDTLQIHVMECI 411
Cdd:pfam18414 1 PKHCCPKCQEQLPDIDTLQIHVMDCI 26
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
49-283 |
9.04e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 9.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 49 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQALEDLEHL 128
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 129 KKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQ---QHSVQVDQLRMQ 205
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLErleRLEEELEELEEA 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 40018574 206 NQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQ 283
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA--LLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
87-314 |
3.62e-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: 62.00 E-value: 3.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 87 REEKEFLMCKFQEARKLVERLSLEKLDLRRQREQALEDLEHLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKE 166
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 167 RQTLEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIK 246
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEA----QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 247 SSKGM--QLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREK 314
Cdd:TIGR02168 839 RLEDLeeQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
59-283 |
1.15e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 59 QELRDAIRQsnqmlRERCEELLHFQVSQREEKEFLMcKFQEARKLVERLSLEKLDLRRQREQALEDLEHLKKCQQQMAED 138
Cdd:COG1196 216 RELKEELKE-----LEAELLLLKLRELEAELEELEA-ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 139 KASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRMQNQSVEAALRMERQ 218
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE----ELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40018574 219 AASEEKRKLAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQ 283
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALR-----AAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
117-318 |
1.70e-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: 59.01 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 117 QREQALEDLEHLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHS 196
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 197 VQVDQLRMQnqsVEAALRMERQAASEEkrklaqlqaayhqLFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVAKQELIDK 276
Cdd:COG4942 101 AQKEELAEL---LRALYRLGRQPPLAL-------------LLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 40018574 277 LKEEAEQHKIVMETvpvLKAQADIYKADFQAERHAREKLVER 318
Cdd:COG4942 165 LRAELEAERAELEA---LLAELEEERAALEALKAERQKLLAR 203
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
98-283 |
3.99e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 98 QEARKLVERLSLEKLDLRRQREQALEDLEHLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAV 177
Cdd:COG1196 207 RQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 178 SEQVRQLESEREVLQQQHSVQVDQLRmQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKgMQLEDLR 257
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRR-ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE-AELAEAE 364
|
170 180
....*....|....*....|....*.
gi 40018574 258 QQLQQAEEALVAKQELIDKLKEEAEQ 283
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLE 390
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
113-318 |
4.63e-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: 57.85 E-value: 4.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 113 DLRRQREQALEDLEHLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQ 192
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 193 QQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKgmQLEDLRQQLQQA----EEALV 268
Cdd:COG4942 104 EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA--ELAALRAELEAEraelEALLA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 40018574 269 AKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVER 318
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
49-285 |
1.06e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 49 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQRE---EKEFLMCKFQEARKLVERLSLEKLDLRRQREQA---- 121
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRleqQKQILRERLANLERQLEELEAQLEELESKLDELaeel 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 122 ------LEDLEhlkkcqqqmaEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVL-QQQ 194
Cdd:TIGR02168 340 aeleekLEELK----------EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLeARL 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 195 HSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQdydshiksskgmQLEDLRQQLQQAEEALVAKQELI 274
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQE------------ELERLEEALEELREELEEAEQAL 477
|
250
....*....|.
gi 40018574 275 DKLKEEAEQHK 285
Cdd:TIGR02168 478 DAAERELAQLQ 488
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
98-272 |
1.38e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 98 QEARKLVERLSLEKLDLRRQREQALEDLEHLKKCQQQMAEDK---------ASVKAQVTSLL---GELQESQSRLEAATK 165
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvasaereiAELEAELERLDassDDLAALEEQLEELEA 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 166 ERQTLEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDShi 245
Cdd:COG4913 700 ELEELEEELDELKGEIGRLEKELEQAEE----ELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEE-- 773
|
170 180
....*....|....*....|....*..
gi 40018574 246 ksskgmQLEDLRQQLQQAEEALVAKQE 272
Cdd:COG4913 774 ------RIDALRARLNRAEEELERAMR 794
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
51-322 |
2.64e-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: 56.22 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 51 LQRCLEENQELRDAIRQsnqmLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQALEDLEHLKK 130
Cdd:TIGR02168 700 LAELRKELEELEEELEQ----LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 131 CQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVE 210
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 211 -AALRMERQAASEEK--RKLAQLQAAYHQLFQDYDSHIK------------SSKGMQLEDLRQQLQQAEEALVAKQE--- 272
Cdd:TIGR02168 856 sLAAEIEELEELIEEleSELEALLNERASLEEALALLRSeleelseelrelESKRSELRRELEELREKLAQLELRLEgle 935
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40018574 273 -LIDKLKEE-AEQHKIVMETVPVLKAQADIYKAdfQAERHAR--------------------EKLVERKELL 322
Cdd:TIGR02168 936 vRIDNLQERlSEEYSLTLEEAEALENKIEDDEE--EARRRLKrlenkikelgpvnlaaieeyEELKERYDFL 1005
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
49-308 |
3.80e-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: 55.46 E-value: 3.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 49 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFlmcKFQEarklverLSLEKLDLRRQREQALEDLEHL 128
Cdd:TIGR02169 180 EEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREY---EGYE-------LLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 129 KKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATkerqtlEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLR-MQNQ 207
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG------EEEQLRVKEKIGELEAEIASLERSIAEKERELEdAEER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 208 SVEAALRMERQAASEE--KRKLAQLQAAYHQLFQDYDShikssKGMQLEDLRQQLQQAE-------EALVAKQELIDKLK 278
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEelEREIEEERKRRDKLTEEYAE-----LKEELEDLRAELEEVDkefaetrDELKDYREKLEKLK 398
|
250 260 270
....*....|....*....|....*....|
gi 40018574 279 EEAEQHKIVMETVPVLKAQADIYKADFQAE 308
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNAA 428
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
55-276 |
1.47e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.48 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 55 LEENQELR-DAIRQSNQMLRERCEELLHfQVSQREEKeflMCKFQEARKLV-----ERLSLEKL-DLRRQREQALEDLEH 127
Cdd:COG3206 162 LEQNLELRrEEARKALEFLEEQLPELRK-ELEEAEAA---LEEFRQKNGLVdlseeAKLLLQQLsELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 128 LKKCQQQMAEDKASVKAQVTSLLG--ELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQ 205
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILAS 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 40018574 206 -------NQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDshIKSSKGMQLEDLRQQLQQAEEALVAKQELIDK 276
Cdd:COG3206 318 leaeleaLQAREASLQAQLAQLEARLAELPELEAELRRLEREVE--VARELYESLLQRLEEARLAEALTVGNVRVIDP 393
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
97-283 |
1.85e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 97 FQEARKLVE------RLSLEKLDLRRQREqALEDLEHLKKCQQQMAEDKASVKAQVTSLlgELQESQSRLEAATKERQTL 170
Cdd:COG4913 224 FEAADALVEhfddleRAHEALEDAREQIE-LLEPIRELAERYAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 171 EGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKG 250
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE 380
|
170 180 190
....*....|....*....|....*....|...
gi 40018574 251 mQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQ 283
Cdd:COG4913 381 -EFAALRAEAAALLEALEEELEALEEALAEAEA 412
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
49-282 |
4.43e-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: 4.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 49 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKL-------DLRRQREQA 121
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQilrerlaNLERQLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 122 LEDLEHLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQhsvqvdq 201
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ------- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 202 lrmqnqsvEAALRMERQAASEEKRklaqlqaayhqlfqdydshiksskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEA 281
Cdd:TIGR02168 395 --------IASLNNEIERLEARLE--------------------------RLEDRRERLQQEIEELLKKLEEAELKELQA 440
|
.
gi 40018574 282 E 282
Cdd:TIGR02168 441 E 441
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
48-306 |
7.01e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 7.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 48 PETLQRCLEENQELRDAIRQSNQMLRERC----EELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQale 123
Cdd:TIGR02169 261 SELEKRLEEIEQLLEELNKKIKDLGEEEQlrvkEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAE--- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 124 dLEHLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQ----------Q 193
Cdd:TIGR02169 338 -IEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKreldrlqeelQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 194 QHSVQVDQLRMQNQSVEAALRmERQAASEEKRklAQLQAAYHQLFQDYDSHIKSSKgmQLEDLRQQLQQAEEALVAKQEL 273
Cdd:TIGR02169 417 RLSEELADLNAAIAGIEAKIN-ELEEEKEDKA--LEIKKQEWKLEQLAADLSKYEQ--ELYDLKEEYDRVEKELSKLQRE 491
|
250 260 270
....*....|....*....|....*....|...
gi 40018574 274 IDKLKEEAeqhKIVMETVPVLKAQADIYKADFQ 306
Cdd:TIGR02169 492 LAEAEAQA---RASEERVRGGRAVEEVLKASIQ 521
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
125-283 |
1.56e-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: 50.44 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 125 LEHLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQ---QHSVQVDQ 201
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEEriaQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 202 LRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIK--SSKGMQLEDLRQQLQQAEEALVAKQELIDKLKE 279
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREalDELRAELTLLNEEAANLRERLESLERRIAATER 838
|
....
gi 40018574 280 EAEQ 283
Cdd:TIGR02168 839 RLED 842
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
154-318 |
1.96e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 154 QESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSV--QVDQLRMQNQSVEAA------LRMERQAASEEKR 225
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAlqRLAEYSWDEIDVASAereiaeLEAELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 226 KLAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADF 305
Cdd:COG4913 686 DLAALEEQLEELEAELEELEE-----ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALG 760
|
170
....*....|....
gi 40018574 306 QA-ERHAREKLVER 318
Cdd:COG4913 761 DAvERELRENLEER 774
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
101-283 |
2.55e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 101 RKLVERLSLEKLDLRRQREQALEDLEHLKKCQQQMAEDKASVKAqvtslLGELQESQSRLEAATKERQTLEGRIRAVSEQ 180
Cdd:COG4913 210 DDFVREYMLEEPDTFEAADALVEHFDDLERAHEALEDAREQIEL-----LEPIRELAERYAAARERLAELEYLRAALRLW 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 181 VRQLesEREVLQQqhsvQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAyhqlfqdydshIKSSKGMQLEDLRQQL 260
Cdd:COG4913 285 FAQR--RLELLEA----ELEELRAELARLEAELERLEARLDALREELDELEAQ-----------IRGNGGDRLEQLEREI 347
|
170 180
....*....|....*....|...
gi 40018574 261 QQAEEALVAKQELIDKLKEEAEQ 283
Cdd:COG4913 348 ERLERELEERERRRARLEALLAA 370
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
89-337 |
6.19e-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: 6.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 89 EKEFLMCKFQEARKLVERLSLEKLDLRRQREQALEDLehlKKCQQQMAEdkasVKAQVTSLLGELQESQSRLEAATKERQ 168
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAEL---QELEEKLEE----LRLEVSELEEEIEELQKELYALANEIS 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 169 TLEGRIRAVSEQVRQLESEREVLQQQH-----------------SVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQ 231
Cdd:TIGR02168 299 RLEQQKQILRERLANLERQLEELEAQLeeleskldelaeelaelEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 232 AAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAE--R 309
Cdd:TIGR02168 379 EQLETLRSKVAQLEL-----QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEelQ 453
|
250 260
....*....|....*....|....*...
gi 40018574 310 HAREKLVERKELLQEQLEQLQREFNKLK 337
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAE 481
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
70-324 |
1.20e-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: 47.76 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 70 QMLRERCEEL---LHFQVSQREEKEFLM----CKFQEARKLVERLSLEKLDLRRQREQALEDLEHLKKCQQQMAEDKASV 142
Cdd:TIGR02169 677 QRLRERLEGLkreLSSLQSELRRIENRLdelsQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 143 KAQVTSLLGELQESQSRLEAATKERQTLEGRIRavSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASE 222
Cdd:TIGR02169 757 KSELKELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 223 EKRKLAQLQAAYHQlfqdydshiKSSKGMQLEDLRQQL----QQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQA 298
Cdd:TIGR02169 835 IQELQEQRIDLKEQ---------IKSIEKEIENLNGKKeeleEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI 905
|
250 260
....*....|....*....|....*.
gi 40018574 299 DIYKADFQAERHAREKLVERKELLQE 324
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKLEALEE 931
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
49-232 |
2.25e-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: 46.97 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 49 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQALEDLEHL 128
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 129 KKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTL------------EGRIRAVSEQVRQLESEREVLQQQHS 196
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLqqeieellkkleEAELKELQAELEELEEELEELQEELE 457
|
170 180 190
....*....|....*....|....*....|....*.
gi 40018574 197 VQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQA 232
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
133-233 |
2.34e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 46.87 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 133 QQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQ--NQSVE 210
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKrkEITDQ 224
|
90 100
....*....|....*....|....*
gi 40018574 211 AALRMErqAASEEKRKL--AQLQAA 233
Cdd:PRK11448 225 AAKRLE--LSEEETRILidQQLRKA 247
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
103-290 |
2.87e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 103 LVERLSLEKLDLRRQREQALE-DLEHLKKCQQQMAEdKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQV 181
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPElNLKELKELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 182 RQLESEREVLQQQHSV-----QVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGmQLEDL 256
Cdd:COG4717 126 QLLPLYQELEALEAELaelpeRLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE-ELEEL 204
|
170 180 190
....*....|....*....|....*....|....
gi 40018574 257 RQQLQQAEEALVAKQELIDKLKEEAEQHKIVMET 290
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
120-318 |
3.45e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 120 QALEDLEHLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESErevLQQQHSVQV 199
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE---IEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 200 DQLRMQNQSVEAALRMERQAASEEkrkLAQL--QAAYHQLFQDYDSHIKSskgmQLEDLRQQLQQAEEALVAKQELIDKL 277
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLLGSES---FSDFldRLSALSKIADADADLLE----ELKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 40018574 278 KEEAEQHKIVMETvpvLKAQADIYKADFQAERHAREKLVER 318
Cdd:COG3883 163 KAELEAAKAELEA---QQAEQEALLAQLSAEEAAAEAQLAE 200
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
52-273 |
8.07e-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: 44.96 E-value: 8.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 52 QRCLEENQELRDAIRQSNQMLRERCEELLhfQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQALEDLEHLKKC 131
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRAKLLMKRAAHVK--QQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 132 QQQMAEDKASVKAqVTSLLGELQESQSRLEAATKERQTLEGRIrAVSEQVRQLESEREVLQQQHSVQVDQLRMQNqsvEA 211
Cdd:TIGR00618 385 QQQKTTLTQKLQS-LCKELDILQREQATIDTRTSAFRDLQGQL-AHAKKQQELQQRYAELCAAAITCTAQCEKLE---KI 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40018574 212 ALRMERQAASEEKRKLAQLQAAyhqlfqdydsHIKSSKGMQLEDLRQQLQQAEEALVAKQEL 273
Cdd:TIGR00618 460 HLQESAQSLKEREQQLQTKEQI----------HLQETRKKAVVLARLLELQEEPCPLCGSCI 511
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
49-203 |
1.71e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 49 ETLQRCLEENQELRDAIRQSNQMLRERCEELL--HFQVSQREEkeflmckfQEARKLVERLSLEKLDLRRQREQALEDLE 126
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEaqIRGNGGDRL--------EQLEREIERLERELEERERRRARLEALLA 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 127 HLKkcqQQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSV---QVDQLR 203
Cdd:COG4913 370 ALG---LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNipaRLLALR 446
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
51-282 |
1.76e-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: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 51 LQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLrrqrEQALEDLEhlkk 130
Cdd:TIGR02169 714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKL----EEALNDLE---- 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 131 cqqqmAEDKASVKAQVTSLLGELQESQSRLEAATKErqtLEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVE 210
Cdd:TIGR02169 786 -----ARLSHSRIPEIQAELSKLEEEVSRIEARLRE---IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE 857
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40018574 211 AALRMERQAASEEKRK---LAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAE 282
Cdd:TIGR02169 858 NLNGKKEELEEELEELeaaLRDLESRLGDLKKERDELEA-----QLRELERKIEELEAQIEKKRKRLSELKAKLE 927
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
51-287 |
1.86e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 51 LQRCLEENQELRDAIRQsnqmLRERCEELlhfqvsqREEKEFLMCKFQEARKLVE--RLSLEKLD-----LRRQREQALE 123
Cdd:PRK02224 337 AQAHNEEAESLREDADD----LEERAEEL-------REEAAELESELEEAREAVEdrREEIEELEeeieeLRERFGDAPV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 124 DLEHLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKER---------QTLEG-----RIRAVSEQVRQLESERE 189
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLeagkcpecgQPVEGsphveTIEEDRERVEELEAELE 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 190 VLQQQHSVQVDQLRMQNQSVEAALRMERqaaSEEKRKLAQlqaayhQLFQDYDSHIKsSKGMQLEDLRQQLQQAEEALVA 269
Cdd:PRK02224 486 DLEEEVEEVEERLERAEDLVEAEDRIER---LEERREDLE------ELIAERRETIE-EKRERAEELRERAAELEAEAEE 555
|
250
....*....|....*...
gi 40018574 270 KQELIDKLKEEAEQHKIV 287
Cdd:PRK02224 556 KREAAAEAEEEAEEAREE 573
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
120-289 |
2.11e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.14 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 120 QALEDLEHLKKCQQQMAEDKASVKAQV---TSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHS 196
Cdd:PRK11637 41 HASDNRDQLKSIQQDIAAKEKSVRQQQqqrASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 197 VQVDQLRMQnqsVEAALRMERQAA------SEEKRKLAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAK 270
Cdd:PRK11637 121 AQERLLAAQ---LDAAFRQGEHTGlqlilsGEESQRGERILAYFGYLNQARQETIA-----ELKQTREELAAQKAELEEK 192
|
170
....*....|....*....
gi 40018574 271 QELIDKLKEEAEQHKIVME 289
Cdd:PRK11637 193 QSQQKTLLYEQQAQQQKLE 211
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
49-228 |
2.67e-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: 42.83 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 49 ETLQRCLEENQELRDAIRQSNQMLRERCEELL--HFQVSQREEKEFLMcKFQEARKLVERLSLEKlDLRRQREQALEDLE 126
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQKEELAELLraLYRLGRQPPLALLL-SPEDFLDAVRRLQYLK-YLAPARREQAEELR 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 127 HLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQT----LEGRIRAVSEQVRQLESEREVLQQQHSvqvdql 202
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKllarLEKELAELAAELAELQQEAEELEALIA------ 230
|
170 180
....*....|....*....|....*.
gi 40018574 203 RMQNQSVEAALRMERQAASEEKRKLA 228
Cdd:COG4942 231 RLEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
80-318 |
3.26e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 80 LHFQVSQREEKEfLMCKFQEARKLVERLSLEKLDLRRQREQALEDLEHLkkcqQQMAEDKASVKAQVTSLLGELQESQSR 159
Cdd:PRK02224 192 LKAQIEEKEEKD-LHERLNGLESELAELDEEIERYEEQREQARETRDEA----DEVLEEHEERREELETLEAEIEDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 160 LEAATKERQTLEGRIRAVSEQVRQLESEREVL----------QQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQ 229
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERLEELEEERDDLlaeaglddadAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAES 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 230 LQAAYHQLFQDYDshiksSKGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAER 309
Cdd:PRK02224 347 LREDADDLEERAE-----ELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREER 421
|
250
....*....|
gi 40018574 310 -HAREKLVER 318
Cdd:PRK02224 422 dELREREAEL 431
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
45-285 |
4.79e-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: 42.65 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 45 QGTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEF--LMCKFQEARKLVERLSL--EKLDLRRQREQ 120
Cdd:TIGR00618 215 DTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLkqLRARIEELRAQEAVLEEtqERINRARKAAP 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 121 ALEDLEHLKKCQQQMAEDKASVKAQVTSLLGELQESQSRL--EAATKERQTLEGRIRAVSEQVRQLESE----REVLQQQ 194
Cdd:TIGR00618 295 LAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVkqQSSIEEQRRLLQTLHSQEIHIRDAHEVatsiREISCQQ 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 195 HSVQvDQLRMQNQSVEAALRMERQAAS--EEKRKLAQLQAAYHQLFQDYDSHIKSSKGMQLEDLR----------QQLQQ 262
Cdd:TIGR00618 375 HTLT-QHIHTLQQQKTTLTQKLQSLCKelDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRyaelcaaaitCTAQC 453
|
250 260
....*....|....*....|...
gi 40018574 263 AEEALVAKQELIDKLKEEAEQHK 285
Cdd:TIGR00618 454 EKLEKIHLQESAQSLKEREQQLQ 476
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
41-303 |
6.13e-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: 41.87 E-value: 6.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 41 LPSEQGTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEflmckfQEARKLVERLSLEKldLRRQREQ 120
Cdd:COG5185 245 LEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTK------EKIAEYTKSIDIKK--ATESLEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 121 ALEDLEHLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEG--RIRAVSEQVR----QLESEREVLQQQ 194
Cdd:COG5185 317 QLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGevELSKSSEELDsfkdTIESTKESLDEI 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 195 HSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKS-SKGMQLEDLRQQLQQAEEALVAKQEL 273
Cdd:COG5185 397 PQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISElNKVMREADEESQSRLEEAYDEINRSV 476
|
250 260 270
....*....|....*....|....*....|
gi 40018574 274 IDKLKEEAEQHKIVMETVPVLKAQADIYKA 303
Cdd:COG5185 477 RSKKEDLNEELTQIESRVSTLKATLEKLRA 506
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
139-286 |
6.49e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.49 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 139 KASVKAQVTSLLGELQESQSrLEAATKerQTLEGRIRAVSEQVRQLESEREVLQQQH---SVQVDQLRMQNQSVEAALRM 215
Cdd:PRK09039 51 KDSALDRLNSQIAELADLLS-LERQGN--QDLQDSVANLRASLSAAEAERSRLQALLaelAGAGAAAEGRAGELAQELDS 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40018574 216 ERQAASEEKRKLAQLQAayhqlfqdydshiksskgmQLEDLRQQLQQAEEALVAKQElidklKEEAEQHKI 286
Cdd:PRK09039 128 EKQVSARALAQVELLNQ-------------------QIAALRRQLAALEAALDASEK-----RDRESQAKI 174
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
83-337 |
9.47e-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: 41.59 E-value: 9.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 83 QVSQREEKEFLMCKfqEARKLVERLSLEKLDLRRQRE-----QALEDLEHLKKcQQQMAEDKASVKAQVTSLLGELQESQ 157
Cdd:TIGR02169 181 EVEENIERLDLIID--EKRQQLERLRREREKAERYQAllkekREYEGYELLKE-KEALERQKEAIERQLASLEEELEKLT 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 158 SRLEAATKERQTLEGRIRAVSEQVRQLESEREVlqqqhsvqvdQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQL 237
Cdd:TIGR02169 258 EEISELEKRLEEIEQLLEELNKKIKDLGEEEQL----------RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 238 FQDYDShiksskgmqledLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETvpvLKAQADIYKADFQAERHAREKLVE 317
Cdd:TIGR02169 328 EAEIDK------------LLAEIEELEREIEEERKRRDKLTEEYAELKEELED---LRAELEEVDKEFAETRDELKDYRE 392
|
250 260
....*....|....*....|
gi 40018574 318 RKEllqeqleQLQREFNKLK 337
Cdd:TIGR02169 393 KLE-------KLKREINELK 405
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
143-295 |
1.10e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 143 KAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRMQNQSVEAALRMERQAASE 222
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEA----ELEEKDERIERLERELSEARSEERR 459
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40018574 223 EKRKlaqlqaayhqlfqdyDSHIKSSKGMqLEDLRQQLQQAEEALvakQELIDKLKEEAEQHKIVM--ETVPVLK 295
Cdd:COG2433 460 EIRK---------------DREISRLDRE-IERLERELEEERERI---EELKRKLERLKELWKLEHsgELVPVKV 515
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
49-265 |
1.16e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 49 ETLQRCLEENQELRDAIRQSNQMLRErceelLHFQVSQREEKeflmckFQEARKLVERLSLEKLDLRRQREQALEDLEHL 128
Cdd:COG4913 664 ASAEREIAELEAELERLDASSDDLAA-----LEEQLEELEAE------LEELEEELDELKGEIGRLEKELEQAEEELDEL 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 129 KKCQQQMAEDkasVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHsVQVDQLRMQNQS 208
Cdd:COG4913 733 QDRLEAAEDL---ARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAF-NREWPAETADLD 808
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40018574 209 VEAAlrmerqAASEEKRKLAQLQA----AYHQLFQDYdshIKSSKGMQLEDLRQQLQQAEE 265
Cdd:COG4913 809 ADLE------SLPEYLALLDRLEEdglpEYEERFKEL---LNENSIEFVADLLSKLRRAIR 860
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
46-283 |
1.65e-03 |
|
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: 40.71 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 46 GTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFlmcKFQEARKLVERLSLEkldlrrqREQALEDL 125
Cdd:COG5185 272 ENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQL---AAAEAEQELEESKRE-------TETGIQNL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 126 EH-LKKCQQQMAEDKASVKAQVTSLLGELQESQSRlEAATKERQTLEGRIRAVSEQVR-QLESEREVLQ----------Q 193
Cdd:COG5185 342 TAeIEQGQESLTENLEAIKEEIENIVGEVELSKSS-EELDSFKDTIESTKESLDEIPQnQRGYAQEILAtledtlkaadR 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 194 QHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVAKQEL 273
Cdd:COG5185 421 QIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKAT 500
|
250
....*....|
gi 40018574 274 IDKLKEEAEQ 283
Cdd:COG5185 501 LEKLRAKLER 510
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
216-285 |
1.86e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 1.86e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 216 ERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHK 285
Cdd:PRK12704 48 KKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRN-ELQKLEKRLLQKEENLDRKLELLEKREEELEKKE 116
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
59-285 |
2.05e-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: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 59 QELRDAIRQSNQMLRERcEELLHFQVSQREEKEFLMCKFQEARKLVERLSL-------EKLD-LRRQREQALEDLEHLKK 130
Cdd:COG3096 836 AELAALRQRRSELEREL-AQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLladetlaDRLEeLREELDAAQEAQAFIQQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 131 CQQQMA--EDKASVKAQVTSLLGELQEsqsRLEAATKERQTLEGRIRAVSEQVRQLE----SEREVLQQQHSVQVDQLRM 204
Cdd:COG3096 915 HGKALAqlEPLVAVLQSDPEQFEQLQA---DYLQAKEQQRRLKQQIFALSEVVQRRPhfsyEDAVGLLGENSDLNEKLRA 991
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 205 QNQSVEAALRMERQAASEEKRKLAQlqaaYHQLFQDYDSHiKSSKGMQLEDLRQQLQQ-----AEEALVAKQELIDKLKE 279
Cdd:COG3096 992 RLEQAEEARREAREQLRQAQAQYSQ----YNQVLASLKSS-RDAKQQTLQELEQELEElgvqaDAEAEERARIRRDELHE 1066
|
....*.
gi 40018574 280 EAEQHK 285
Cdd:COG3096 1067 ELSQNR 1072
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
25-284 |
2.66e-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: 40.21 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 25 DMLGEESSLGKPAMLHLPSEQGTPETLQRCLEENQELRDAIRQS-NQMLRERCEELLHFQVSQREEKEFLMCKFQEARKL 103
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAElNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 104 VERLSLEKLDLRRQR-EQALEDLEHLKKCQQQMAEDKASVKAQVTSLlGELQESQSRLEAATKERQTL------EGRIRA 176
Cdd:pfam12128 324 LEALEDQHGAFLDADiETAAADQEQLPSWQSELENLEERLKALTGKH-QDVTAKYNRRRSKIKEQNNRdiagikDKLAKI 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 177 VSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQdydshiKSSKGMQLEDL 256
Cdd:pfam12128 403 REARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQ------LENFDERIERA 476
|
250 260 270
....*....|....*....|....*....|.
gi 40018574 257 RQQLQQA---EEALVAKQELIDKLKEEAEQH 284
Cdd:pfam12128 477 REEQEAAnaeVERLQSELRQARKRRDQASEA 507
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
153-288 |
2.68e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 153 LQESQSRLEAATKERqtlegrIRAVSEQVRQL--ESEREVLQQQHSVQVDQLRMQNQsvEAALRMERQAASEEKRKLAQL 230
Cdd:PRK12704 44 LEEAKKEAEAIKKEA------LLEAKEEIHKLrnEFEKELRERRNELQKLEKRLLQK--EENLDRKLELLEKREEELEKK 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40018574 231 QAAYHQLFQDYDSHIKSSKGMQLEdLRQQLQQ-----AEEAlvaKQELIDKLKEEAEQHKIVM 288
Cdd:PRK12704 116 EKELEQKQQELEKKEEELEELIEE-QLQELERisgltAEEA---KEILLEKVEEEARHEAAVL 174
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
129-286 |
2.72e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.20 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 129 KKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQhsvqvdqlrmQNQS 208
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEE----------AEKE 574
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 40018574 209 VEAALRMERQAASEEKRKLAQLQAAYHqlfqdydSHIKSSkgmQLEDLRQQLQQAEEALVAKqelidKLKEEAEQHKI 286
Cdd:PRK00409 575 AQQAIKEAKKEADEIIKELRQLQKGGY-------ASVKAH---ELIEARKRLNKANEKKEKK-----KKKQKEKQEEL 637
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
49-302 |
3.65e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 39.68 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 49 ETLQRCLEENQELRDAIRQSNQMlreRCEELLHFQVSQREEKEFLMckfqEARKLVERLSLEKLDLRRQREqaLEDLEHL 128
Cdd:COG5022 800 QPLLSLLGSRKEYRSYLACIIKL---QKTIKREKKLRETEEVEFSL----KAEVLIQKFGRSLKAKKRFSL--LKKETIY 870
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 129 KKCQQQMAEDKASVKaqvtsllgELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQS 208
Cdd:COG5022 871 LQSAQRVELAERQLQ--------ELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDL 942
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 209 VEAALRMERQaaSEEKRKLAQLQAAYHQLFQDYDSHIKSSKGM--QLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKI 286
Cdd:COG5022 943 EEGPSIEYVK--LPELNKLHEVESKLKETSEEYEDLLKKSTILvrEGNKANSELKNFKKELAELSKQYGALQESTKQLKE 1020
|
250
....*....|....*.
gi 40018574 287 VMETVPVLKAQADIYK 302
Cdd:COG5022 1021 LPVEVAELQSASKIIS 1036
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
49-283 |
5.23e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.25 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 49 ETLQRCLEENQELRDAirqsnqmlrERCEEllhfqVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQALEDLEHL 128
Cdd:PRK02224 436 RTARERVEEAEALLEA---------GKCPE-----CGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERA 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 129 KkcqqqmaedkasvkaqvtsllgELQESQSRLEAATKERQTLEGRIravSEQVRQLESEREVLQQQHSvQVDQLRMQNQS 208
Cdd:PRK02224 502 E----------------------DLVEAEDRIERLEERREDLEELI---AERRETIEEKRERAEELRE-RAAELEAEAEE 555
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40018574 209 VEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDShiksskgmqLEDLRQQLQQAEEALVAKQELIDKLKEEAEQ 283
Cdd:PRK02224 556 KREAAAEAEEEAEEAREEVAELNSKLAELKERIES---------LERIRTLLAAIADAEDEIERLREKREALAEL 621
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
155-280 |
5.24e-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: 38.59 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 155 ESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAY 234
Cdd:pfam09787 44 ALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEEL 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 40018574 235 HQLFQDYDSHIKSSKG------MQLEDLRQQL--------QQAE---------EALVAKQELIDKLKEE 280
Cdd:pfam09787 124 RYLEEELRRSKATLQSrikdreAEIEKLRNQLtsksqsssSQSElenrlhqltETLIQKQTMLEALSTE 192
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
83-271 |
6.55e-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: 38.95 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 83 QVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQALEDLE-----------HLKKCQQQMAEDKASVKAQVTSLLG 151
Cdd:pfam15921 305 QEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEkqlvlanseltEARTERDQFSQESGNLDDQLQKLLA 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 152 ELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESErevlqqqhsvqVDQLRMQNQSVEAALR-MERQAASEEKRKLAQL 230
Cdd:pfam15921 385 DLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRE-----------LDDRNMEVQRLEALLKaMKSECQGQMERQMAAI 453
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 40018574 231 QAAYHQLFQdydshiKSSKGMQLEDLRQQLQQAEEALVAKQ 271
Cdd:pfam15921 454 QGKNESLEK------VSSLTAQLESTKEMLRKVVEELTAKK 488
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
49-284 |
6.83e-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: 38.80 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 49 ETLQRCLEENQELRDAIrQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQALED--LE 126
Cdd:TIGR00618 584 EDIPNLQNITVRLQDLT-EKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQErvRE 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 127 HLKKCQQQMAEDKASVKAqvtsllgELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQN 206
Cdd:TIGR00618 663 HALSIRVLPKELLASRQL-------ALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLA 735
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 40018574 207 QSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSskGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQH 284
Cdd:TIGR00618 736 AREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQT--GAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQE 811
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
59-355 |
7.16e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.97 E-value: 7.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 59 QELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVErlSLEKLDLRRQREQALEDLEHLKKCQQQMAED 138
Cdd:PTZ00121 1428 EEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE--AKKKAEEAKKADEAKKKAEEAKKKADEAKKA 1505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 139 KASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQ 218
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEE 1585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 219 AASEEKRKLAQLQAAYH--------QLFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMET 290
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYEeekkmkaeEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 40018574 291 VPvLKAQADIYKAD----FQAERHAREKLVERKELLQEQLEQLQREFNKLKVGCHESARIEDMRKRHVE 355
Cdd:PTZ00121 1666 EA-KKAEEDKKKAEeakkAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAE 1733
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
59-280 |
7.45e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.48 E-value: 7.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 59 QELRDAIRQSNQMLRE-RCEEllhfqVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQR---EQALEDLEHLKKC--- 131
Cdd:PRK02224 436 RTARERVEEAEALLEAgKCPE-----CGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVeevEERLERAEDLVEAedr 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 132 -----------QQQMAEDKASVKA---QVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESER----EVLQQ 193
Cdd:PRK02224 511 ierleerredlEELIAERRETIEEkreRAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLaelkERIES 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 194 QHSVQVDQLRMQNQSVEAALRMERQAA-----SEEKRKLAQLQAAYHQLFQDYDshiksskGMQLEDLRQQLQQAEEALV 268
Cdd:PRK02224 591 LERIRTLLAAIADAEDEIERLREKREAlaelnDERRERLAEKRERKRELEAEFD-------EARIEEAREDKERAEEYLE 663
|
250
....*....|..
gi 40018574 269 AKQELIDKLKEE 280
Cdd:PRK02224 664 QVEEKLDELREE 675
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
157-336 |
7.59e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 38.46 E-value: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 157 QSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSV-----QVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQ 231
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLvdlseEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 232 AayhQLFQDYDSHIKSSKGMQLEDLRQQLQQAEealvakQELIDKLKEEAEQHKIVMEtvpvLKAQADIYKADFQAE--- 308
Cdd:COG3206 247 A---QLGSGPDALPELLQSPVIQQLRAQLAELE------AELAELSARYTPNHPDVIA----LRAQIAALRAQLQQEaqr 313
|
170 180 190
....*....|....*....|....*....|...
gi 40018574 309 -----RHAREKLVERKELLQEQLEQLQREFNKL 336
Cdd:COG3206 314 ilaslEAELEALQAREASLQAQLAQLEARLAEL 346
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
110-233 |
7.61e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 38.02 E-value: 7.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 110 EKLDLRRQREQALED-LEHLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLegriRAVSEQVRqleSER 188
Cdd:PRK09039 67 DLLSLERQGNQDLQDsVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSE----KQVSARAL---AQV 139
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 40018574 189 EVLQQQhsvqVDQLRMQNQSVEAALRmerqaASEEKRKLAQLQAA 233
Cdd:PRK09039 140 ELLNQQ----IAALRRQLAALEAALD-----ASEKRDRESQAKIA 175
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
166-285 |
8.33e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 38.36 E-value: 8.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 166 ERQTLEGRIRAVSEQVRQLES-EREVLQQQHsvQVDQLRmqnQSVEAALRmeRQAASEEKRKLAQLQAAYHQLFqdyDSH 244
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERaHEALEDARE--QIELLE---PIRELAER--YAAARERLAELEYLRAALRLWF---AQR 288
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 40018574 245 IKSSKGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHK 285
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELE 329
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
65-269 |
8.41e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.21 E-value: 8.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 65 IRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQaledLEHLKKCQQQMAEdkasvKA 144
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK----LEKLLQLLPLYQE-----LE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 145 QVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSV----QVDQLRMQNQSVEAALRMERQAA 220
Cdd:COG4717 136 ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLateeELQDLAEELEELQQRLAELEEEL 215
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 40018574 221 SEEKRKLAQLQAAYHQLfqdydshiksSKGMQLEDLRQQLQQAEEALVA 269
Cdd:COG4717 216 EEAQEELEELEEELEQL----------ENELEAAALEERLKEARLLLLI 254
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
97-294 |
8.55e-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: 8.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 97 FQEARKLVERLSlekldlRRQREQALEDLE--------HLKKCQQQMAE--DKASV---KAQVTSLLGELQESQSRLEAA 163
Cdd:COG3524 160 LAESEELVNQLS------ERAREDAVRFAEeeveraeeRLRDAREALLAfrNRNGIldpEATAEALLQLIATLEGQLAEL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 164 TKERQTLEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRmqnqsveaalrmERQAASEEKRKLAQLQAAYhqlfqdyds 243
Cdd:COG3524 234 EAELAALRSYLSPNSPQVRQLRRRIAALEK----QIAAER------------ARLTGASGGDSLASLLAEY--------- 288
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 40018574 244 hiksskgmqlEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETV--PVL 294
Cdd:COG3524 289 ----------ERLELEREFAEKAYTSALAALEQARIEAARQQRYLAVIvqPTL 331
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
47-228 |
9.18e-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: 37.60 E-value: 9.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 47 TPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVsqreekeflmcKFQEARKLVERLSLEKLDLRRQREQALEDLE 126
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELED-----------ELAALEARLEAAKTELEDLEKEIKRLELEIE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 127 HLkkcQQQMAEDKASVKAQVTSllGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHS---VQVDQLR 203
Cdd:COG1579 70 EV---EARIKKYEEQLGNVRNN--KEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAeleAELEEKK 144
|
170 180
....*....|....*....|....*
gi 40018574 204 MQNQSVEAALRMERQAASEEKRKLA 228
Cdd:COG1579 145 AELDEELAELEAELEELEAEREELA 169
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
113-282 |
9.34e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 37.96 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 113 DLRRQREQALEDLEHLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQ 192
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018574 193 QQHSV---QVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVA 269
Cdd:COG4372 122 KERQDleqQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEE 201
|
170
....*....|...
gi 40018574 270 KQELIDKLKEEAE 282
Cdd:COG4372 202 LAEAEKLIESLPR 214
|
|
| |
