|
Name |
Accession |
Description |
Interval |
E-value |
| UBAN |
cd09803 |
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ... |
263-349 |
3.27e-25 |
|
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) is a regulatory subunit of the kinase complex IKK, which is involved in the activation of NF-kappaB via phosporylation of inhibitory IkappaBs. This mechanism requires the binding of NEMO to ubiquinated substrates. Binding is achieved via the UBAN motif (ubiquitin binding in ABIN and NEMO), which is described in this model. This region of NEMO has also been named CoZi (for coiled-coil 2 and leucine zipper). ABINs (A20-binding inhibitors of NF-kappaB) are sensors for ubiquitin that are involved in regulation of apoptosis, ABIN-1 is presumed to inhibit signalling via the NF-kappaB route. The UBAN motif is also found in optineurin, the product of a gene associated with glaucoma, which has been characterized as a negative regulator of NF-kappaB as well.
Pssm-ID: 197361 [Multi-domain] Cd Length: 87 Bit Score: 98.19 E-value: 3.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 263 MQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQ 342
Cdd:cd09803 1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80
|
....*..
gi 238637312 343 REFNKLK 349
Cdd:cd09803 81 RENQELK 87
|
|
| CC2-LZ |
pfam16516 |
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ... |
264-349 |
2.60e-22 |
|
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a leucine-zipper domain associated with the CC2 coiled-coil region of NF-kappa-B essential modulator, NEMO. It plays a regulatory role, along with the very C-terminal zinc-finger; it contains a ubiquitin-binding domain (UBD) and represents one region that contributes to NEMO oligomerization. NEMO itself is an integral part of the IkappaB kinase complex and serves as a molecular switch via which the NF-kappaB signalling pathway is regulated.
Pssm-ID: 465155 [Multi-domain] Cd Length: 100 Bit Score: 90.81 E-value: 2.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 264 QLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQR 343
Cdd:pfam16516 15 EIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEYLQR 94
|
....*.
gi 238637312 344 EFNKLK 349
Cdd:pfam16516 95 QNQQLK 100
|
|
| NEMO |
pfam11577 |
NF-kappa-B essential modulator NEMO; NEMO is a regulatory protein which is part of the IKK ... |
56-122 |
4.60e-16 |
|
NF-kappa-B essential modulator NEMO; NEMO is a regulatory protein which is part of the IKK complex along with the catalytic IKKalpha and beta kinases. The IKK complex phosphorylates IkappaB targeting it for degradation which results in the release of NF-kappaB which initiates the inflammatory response, cell proliferation or cell differentiation. NEMO activates the IKK complex's activity by associating with the unphosphorylated IKK kinase C termini.The core domain of NEMO is a dimer which binds to two fragments of IKK.
Pssm-ID: 431942 [Multi-domain] Cd Length: 67 Bit Score: 72.13 E-value: 4.60e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 238637312 56 EQGTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLE 122
Cdd:pfam11577 1 DEETLEQMKELLTENHQLKEAMKQSNQAMKERCEELSAWQEKQKEEREFLECRFREARELLRRLSLE 67
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
99-350 |
3.10e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.01 E-value: 3.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 99 REEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKD 178
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 179 RQALEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIK 258
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEA----QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 259 SSKGM--QLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPV----LKAQADIYKADFQAERHAREKLVEKKE 332
Cdd:TIGR02168 839 RLEDLeeQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEalalLRSELEELSEELRELESKRSELRRELE 918
|
250
....*....|....*...
gi 238637312 333 YLQEQLEQLQREFNKLKV 350
Cdd:TIGR02168 919 ELREKLAQLELRLEGLEV 936
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
71-349 |
1.80e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 71 QELRDAIRQsnqmlRERCEELLHFQVSQREEKEFLMcKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKCQQQMAED 150
Cdd:COG1196 216 RELKEELKE-----LEAELLLLKLRELEAELEELEA-ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 151 KASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRMQNQSVEAALRMERQ 230
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE----ELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 231 AASEEKRKLAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETvpvLKAQA 310
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALR-----AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE---LEEEE 437
|
250 260 270
....*....|....*....|....*....|....*....
gi 238637312 311 DIYKADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLK 349
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
128-344 |
2.57e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 67.87 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 128 SQREQALKELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQH 207
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 208 SVQVDQLRMQnqsVEAALRMERQA------ASEEKRKLAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVA 281
Cdd:COG4942 100 EAQKEELAEL---LRALYRLGRQPplalllSPEDFLDAVRRLQYLKYLAPARREQAE-----ELRADLAELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 238637312 282 KQELIDKLKEEAEQHKIVMETVPVLKAQA-DIYKADFQAERHAREKLVEKKEYLQEQLEQLQRE 344
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLlARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
67-342 |
3.22e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 3.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 67 LEENQELRDAIRQSNQM--LRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKCQ 144
Cdd:COG1196 218 LKEELKELEAELLLLKLreLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 145 QQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAA 224
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 225 LR----------MERQAASEEKRKLAQLQAAYHQLFQDyDSHIKSSKGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAE 294
Cdd:COG1196 378 EEeleelaeellEALRAAAELAAQLEELEEAEEALLER-LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 238637312 295 QHKIVMETVPVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQ 342
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| zf_C2H2_10 |
pfam18414 |
C2H2 type zinc-finger; This is a zinc finger domain C2H2 which can be found in optineurin ... |
398-423 |
1.14e-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: 1.14e-11
10 20
....*....|....*....|....*.
gi 238637312 398 PDFCCPKCQYQAPDMDTLQIHVMECI 423
Cdd:pfam18414 1 PKHCCPKCQEQLPDIDTLQIHVMDCI 26
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
61-295 |
7.10e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 7.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 61 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQL 140
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 141 KKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQ---QHSVQVDQLRMQ 217
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLErleRLEEELEELEEA 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 238637312 218 NQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQ 295
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA--LLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
129-387 |
3.21e-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: 62.38 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 129 QREQALKELEQlkkCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQ--- 205
Cdd:TIGR02168 674 ERRREIEELEE---KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEEria 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 206 QHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQEL 285
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE-----ALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 286 IDKLKEEAEQHKIVMEtvpVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLKVGCHE--------SAR 357
Cdd:TIGR02168 826 LESLERRIAATERRLE---DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALlrseleelSEE 902
|
250 260 270
....*....|....*....|....*....|
gi 238637312 358 IEDMRKRHVETPQPPLLPAPAHHSFHLALS 387
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKLAQLELRLE 932
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
61-349 |
3.18e-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: 59.31 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 61 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFlmcKFQEarklverLSLEKLDLRSQREQALKELEQL 140
Cdd:TIGR02169 180 EEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREY---EGYE-------LLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 141 KKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATkdrqalEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLR-MQNQ 219
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG------EEEQLRVKEKIGELEAEIASLERSIAEKERELEdAEER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 220 SVEAALRMERQAASEE--KRKLAQLQAAYHQLFQDYDShikssKGMQLEDLRQQLQQAE-------EALVAKQELIDKLK 290
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEelEREIEEERKRRDKLTEEYAE-----LKEELEDLRAELEEVDkefaetrDELKDYREKLEKLK 398
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 238637312 291 EEAEQHKIVMETVPVLKAQADIYKADFQAERHARE----KLVEKKEYLQEQLEQLQREFNKLK 349
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEakinELEEEKEDKALEIKKQEWKLEQLA 461
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
166-347 |
6.47e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 6.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 166 QESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSV--QVDQLRMQNQSVEAA------LRMERQAASEEKR 237
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAlqRLAEYSWDEIDVASAereiaeLEAELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 238 KLAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADF 317
Cdd:COG4913 686 DLAALEEQLEELEAELEELEE-----ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALG 760
|
170 180 190
....*....|....*....|....*....|....*...
gi 238637312 318 QAER--------HAREKLVEKKEYLQEQLEQLQREFNK 347
Cdd:COG4913 761 DAVErelrenleERIDALRARLNRAEEELERAMRAFNR 798
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
60-348 |
6.69e-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: 58.14 E-value: 6.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 60 PETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQ 139
Cdd:TIGR02168 721 LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 140 LKkcqqqmaEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLrmqnq 219
Cdd:TIGR02168 801 LR-------EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI----- 868
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 220 sveAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIK--SSKGMQLEDLRQQLQQAEEALVAKQE----LIDKLKEE- 292
Cdd:TIGR02168 869 ---EELESELEALLNERASLEEALALLRSELEELSEELRelESKRSELRRELEELREKLAQLELRLEglevRIDNLQERl 945
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 238637312 293 AEQHKIVMETVPVLKaqadiykadfqaerharEKLVEKKEYLQEQLEQLQREFNKL 348
Cdd:TIGR02168 946 SEEYSLTLEEAEALE-----------------NKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
61-350 |
8.03e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 8.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 61 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALK----- 135
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERqleel 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 136 --ELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQhsvqvdq 213
Cdd:TIGR02168 322 eaQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ------- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 214 lrmqnqsvEAALRMERQAASEEKRklaqlqaayhqlfqdydshiksskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEA 293
Cdd:TIGR02168 395 --------IASLNNEIERLEARLE--------------------------RLEDRRERLQQEIEELLKKLEEAELKELQA 440
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 238637312 294 EQHKIVMETVPVLKAQADIYkadfQAERHAREKLVEKKEYLQEQLEQLQREFNKLKV 350
Cdd:TIGR02168 441 ELEELEEELEELQEELERLE----EALEELREELEEAEQALDAAERELAQLQARLDS 493
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
113-349 |
8.18e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 8.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 113 RKLVERLSLEKLDLRSQREQALKELEQLKKCQQQMAEDKASVKAqvtslLGELQESQSRLEAATKDRQALEGRIRAVSEQ 192
Cdd:COG4913 210 DDFVREYMLEEPDTFEAADALVEHFDDLERAHEALEDAREQIEL-----LEPIRELAERYAAARERLAELEYLRAALRLW 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 193 VRQLesEREVLQQqhsvQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAyhqlfqdydshIKSSKGMQLEDLRQQL 272
Cdd:COG4913 285 FAQR--RLELLEA----ELEELRAELARLEAELERLEARLDALREELDELEAQ-----------IRGNGGDRLEQLEREI 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 273 QQAEEALVAKQELIDKLKEEAEQ--------HKIVMETVPVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQRE 344
Cdd:COG4913 348 ERLERELEERERRRARLEALLAAlglplpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
....*
gi 238637312 345 FNKLK 349
Cdd:COG4913 428 IASLE 432
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-349 |
9.40e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 9.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 101 EKEFLMCKFQEARKLVERLSLEKLDLRSQREQALkelEQLKKCQQQMAEdkasVKAQVTSLLGELQESQSRLEAATKDRQ 180
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELT---AELQELEEKLEE----LRLEVSELEEEIEELQKELYALANEIS 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 181 ALEGRIRAVSEQVRQLESEREVLQQQH-----------------SVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQ 243
Cdd:TIGR02168 299 RLEQQKQILRERLANLERQLEELEAQLeeleskldelaeelaelEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 244 AAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAE--R 321
Cdd:TIGR02168 379 EQLETLRSKVAQLEL-----QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEelQ 453
|
250 260
....*....|....*....|....*...
gi 238637312 322 HAREKLVEKKEYLQEQLEQLQREFNKLK 349
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAE 481
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
82-364 |
1.77e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 82 QMLRERCEEL---LHFQVSQREEKEFLM----CKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKCQQQMAEDKASV 154
Cdd:TIGR02169 677 QRLRERLEGLkreLSSLQSELRRIENRLdelsQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 155 KAQVTSLLGELQESQSRLEAATKDRQALEGRIRavSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASE 234
Cdd:TIGR02169 757 KSELKELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 235 EKRKLAQLQAAYHQlfqdydshiKSSKGMQLEDLRQQL----QQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQA 310
Cdd:TIGR02169 835 IQELQEQRIDLKEQ---------IKSIEKEIENLNGKKeeleEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI 905
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 238637312 311 DIYKADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLKVGCHESARIEDMRKR 364
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAE 959
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
67-288 |
1.80e-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: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 67 LEENQELR-DAIRQSNQMLRERCEELLHfQVSQREEKeflMCKFQEARKLV-----ERLSLEKL-DLRSQREQALKELEQ 139
Cdd:COG3206 162 LEQNLELRrEEARKALEFLEEQLPELRK-ELEEAEAA---LEEFRQKNGLVdlseeAKLLLQQLsELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 140 LKKCQQQMAEDKASVKAQVTSLLG--ELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQ 217
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILAS 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 238637312 218 -------NQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDshIKSSKGMQLEDLRQQLQQAEEALVAKQELIDK 288
Cdd:COG3206 318 leaeleaLQAREASLQAQLAQLEARLAELPELEAELRRLEREVE--VARELYESLLQRLEEARLAEALTVGNVRVIDP 393
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
126-344 |
2.98e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 126 LRSQREQALKELE------------------QLKKCQQQ--MAEDKASVKA-----QVTSLLGELQESQSRLEAATKDRQ 180
Cdd:COG1196 170 YKERKEEAERKLEateenlerledilgelerQLEPLERQaeKAERYRELKEelkelEAELLLLKLRELEAELEELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 181 ALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSV----------EAALRMERQAASEEKRKLAQLQAAYHQLF 250
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEyellaelarlEQDIARLEERRRELEERLEELEEELAELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 251 QDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQhkIVMETVPVLKAQADIYKADFQAERhAREKLVEK 330
Cdd:COG1196 330 EELEELEE-----ELEELEEELEEAEEELEEAEAELAEAEEALLE--AEAELAEAEEELEELAEELLEALR-AAAELAAQ 401
|
250
....*....|....
gi 238637312 331 KEYLQEQLEQLQRE 344
Cdd:COG1196 402 LEELEEAEEALLER 415
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
110-284 |
3.27e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 110 QEARKLVERLSLEKLDLRSQREQALKELEQLKKCQQQMAEDK---------ASVKAQVTSLL---GELQESQSRLEAATK 177
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvasaereiAELEAELERLDassDDLAALEEQLEELEA 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 178 DRQALEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDShi 257
Cdd:COG4913 700 ELEELEEELDELKGEIGRLEKELEQAEE----ELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEE-- 773
|
170 180
....*....|....*....|....*..
gi 238637312 258 ksskgmQLEDLRQQLQQAEEALVAKQE 284
Cdd:COG4913 774 ------RIDALRARLNRAEEELERAMR 794
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
100-362 |
3.52e-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: 55.84 E-value: 3.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 100 EEKEFLMCKFQEARKLVERLSL---EKLD----LRSQREQALKELEQLKKCQ-----------QQMAEDKASVKAQVTSL 161
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLiidEKRQqlerLRREREKAERYQALLKEKReyegyellkekEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 162 LGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVlqqqhsvqvdQLRMQNQSVEAALRMERQAASEEKRKLAQ 241
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL----------RVKEKIGELEAEIASLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 242 LQAAYHQLFQDYDShiksskgmqledLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETvpvLKAQADIYKADFQAER 321
Cdd:TIGR02169 320 AEERLAKLEAEIDK------------LLAEIEELEREIEEERKRRDKLTEEYAELKEELED---LRAELEEVDKEFAETR 384
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 238637312 322 HAREKLVEKKEYLQEQLEQLQREFNKLKVGCHE-SARIEDMR 362
Cdd:TIGR02169 385 DELKDYREKLEKLKREINELKRELDRLQEELQRlSEELADLN 426
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
60-318 |
8.15e-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: 8.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 60 PETLQRCLEENQELRDAIRQSNQMLRERC----EELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREqalk 135
Cdd:TIGR02169 261 SELEKRLEEIEQLLEELNKKIKDLGEEEQlrvkEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA---- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 136 ELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQ----------Q 205
Cdd:TIGR02169 337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKreldrlqeelQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 206 QHSVQVDQLRMQNQSVEAALRmERQAASEEKRklAQLQAAYHQLFQDYDSHIKSSKgmQLEDLRQQLQQAEEALVAKQEL 285
Cdd:TIGR02169 417 RLSEELADLNAAIAGIEAKIN-ELEEEKEDKA--LEIKKQEWKLEQLAADLSKYEQ--ELYDLKEEYDRVEKELSKLQRE 491
|
250 260 270
....*....|....*....|....*....|...
gi 238637312 286 IDKLKEEAeqhKIVMETVPVLKAQADIYKADFQ 318
Cdd:TIGR02169 492 LAEAEAQA---RASEERVRGGRAVEEVLKASIQ 521
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
132-344 |
3.54e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 132 QALKELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESErevLQQQHSVQV 211
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE---IEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 212 DQLRMQNQSVEAALRMERQAASEEKRKLAQlQAAYHQLFQDYDSHIKSskgmQLEDLRQQLQQAEEALVAKQELIDKLKE 291
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLLGSESFSDFLD-RLSALSKIADADADLLE----ELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 238637312 292 EAEQHKIVMETvpvLKAQADIYKADFQAErhaREKLVEKKEYLQEQLEQLQRE 344
Cdd:COG3883 165 ELEAAKAELEA---QQAEQEALLAQLSAE---EAAAEAQLAELEAELAAAEAA 211
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
61-367 |
7.13e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 7.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 61 ETLQRCLEENQELRDAirqsnqmlrERCEEllhfqVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQL 140
Cdd:PRK02224 436 RTARERVEEAEALLEA---------GKCPE-----CGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERA 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 141 KkcqqqmaedkasvkaqvtsllgELQESQSRLEAATKDRQALEGRIravSEQVRQLESEREVLQQQHSvQVDQLRMQNQS 220
Cdd:PRK02224 502 E----------------------DLVEAEDRIERLEERREDLEELI---AERRETIEEKRERAEELRE-RAAELEAEAEE 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 221 VEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDShiksskgmqLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVM 300
Cdd:PRK02224 556 KREAAAEAEEEAEEAREEVAELNSKLAELKERIES---------LERIRTLLAAIADAEDEIERLREKREALAELNDERR 626
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 238637312 301 ETVPVLKAQADIYKADFQAER--HAREKLVEKKEYLQ---EQLEQLQREFNKL--KVGCHESA--RIEDMRKRHVE 367
Cdd:PRK02224 627 ERLAEKRERKRELEAEFDEARieEAREDKERAEEYLEqveEKLDELREERDDLqaEIGAVENEleELEELRERREA 702
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
145-245 |
1.61e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 47.25 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 145 QQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQ--NQSVE 222
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKrkEITDQ 224
|
90 100
....*....|....*....|....*
gi 238637312 223 AALRMErqAASEEKRKL--AQLQAA 245
Cdd:PRK11448 225 AAKRLE--LSEEETRILidQQLRKA 247
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
71-367 |
2.52e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 71 QELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVErlSLEKLDLRSQREQALKELEQLKKCQQQMAED 150
Cdd:PTZ00121 1428 EEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE--AKKKAEEAKKADEAKKKAEEAKKKADEAKKA 1505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 151 KASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQ 230
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEE 1585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 231 AASEEKRKLAQLQAAYH--------QLFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMET 302
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYEeekkmkaeEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 238637312 303 VPvLKAQADIYKAD----FQAERHAREKLVEKKEYLQEQLEQLQREFNKLKVGCHESARIEDMRKRHVE 367
Cdd:PTZ00121 1666 EA-KKAEEDKKKAEeakkAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAE 1733
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
63-365 |
2.55e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 63 LQRCLEENQELRDAIRQsnqmLRERCEELlhfqvsqREEKEFLMCKFQEARKLVE--RLSLEKLD-----LRSQREQALK 135
Cdd:PRK02224 337 AQAHNEEAESLREDADD----LEERAEEL-------REEAAELESELEEAREAVEdrREEIEELEeeieeLRERFGDAPV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 136 ELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDR---------QALEG-----RIRAVSEQVRQLESERE 201
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLeagkcpecgQPVEGsphveTIEEDRERVEELEAELE 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 202 VLQQQHSVQVDQLRMQNQSVEAALRMERqaaSEEKRKLAQlqaayhQLFQDYDSHIKsSKGMQLEDLRQQLQQAEEALVA 281
Cdd:PRK02224 486 DLEEEVEEVEERLERAEDLVEAEDRIER---LEERREDLE------ELIAERRETIE-EKRERAEELRERAAELEAEAEE 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 282 KQELIDKLKEEAEQHKIV-----------------METVPVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLqRE 344
Cdd:PRK02224 556 KREAAAEAEEEAEEAREEvaelnsklaelkeriesLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEK-RE 634
|
330 340
....*....|....*....|.
gi 238637312 345 FNKLKVGCHESARIEDMRKRH 365
Cdd:PRK02224 635 RKRELEAEFDEARIEEAREDK 655
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
57-234 |
4.18e-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: 45.82 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 57 QGTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKE 136
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 137 LEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAAtkDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRM 216
Cdd:TIGR02168 395 IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
170
....*....|....*...
gi 238637312 217 QNQSVEAALRMERQAASE 234
Cdd:TIGR02168 473 AEQALDAAERELAQLQAR 490
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
228-343 |
4.24e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 228 ERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMEtvpvlk 307
Cdd:PRK12704 48 KKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRN-ELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELE------ 120
|
90 100 110
....*....|....*....|....*....|....*.
gi 238637312 308 aqadiykadfQAERHAREKLVEKKEYLQEQLEQLQR 343
Cdd:PRK12704 121 ----------QKQQELEKKEEELEELIEEQLQELER 146
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
33-295 |
5.42e-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: 45.82 E-value: 5.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 33 AEDQDMLGEESSLGKPAMLHLPSEQGTPETLQRCLEEN----QELRDAIRQSN---QMLRERCEELLHFQVSQREEKEFL 105
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALrealDELRAELTLLNeeaANLRERLESLERRIAATERRLEDL 843
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 106 MCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGR 185
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 186 IRAVSEQVRQLESEREVLQQQHSVQVdQLRMQNQSVEAALRMERQAASEekRKLAQLQAAYHQL----------FQDYDS 255
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQERLSEEY-SLTLEEAEALENKIEDDEEEAR--RRLKRLENKIKELgpvnlaaieeYEELKE 1000
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 238637312 256 hiksskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQ 295
Cdd:TIGR02168 1001 --------RYDFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
113-362 |
5.71e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.39 E-value: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 113 RKLVERLslekLDLR--SQREQALKEL-----EQLKKCQQQMAEDKASVKAQvtsllgelQESQSRLEAATKDRQAlegR 185
Cdd:PHA02562 153 RKLVEDL----LDISvlSEMDKLNKDKirelnQQIQTLDMKIDHIQQQIKTY--------NKNIEEQRKKNGENIA---R 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 186 IRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAyHQLFQDYD------SHIKS 259
Cdd:PHA02562 218 KQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKV-IKMYEKGGvcptctQQISE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 260 SKGMqLEDLRQQLQQAEEALVAKQELIDKLKEEAeqHKIVMETVPVLKAQADIYKADFQAERHAREKLVEKKEYLQ---- 335
Cdd:PHA02562 297 GPDR-ITKIKDKLKELQHSLEKLDTAIDELEEIM--DEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEElqae 373
|
250 260 270
....*....|....*....|....*....|..
gi 238637312 336 -----EQLEQLQREFNKLKVGCHESARIEDMR 362
Cdd:PHA02562 374 fvdnaEELAKLQDELDKIVKTKSELVKEKYHR 405
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
115-302 |
7.78e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 7.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 115 LVERLSLEKLDL-RSQREQALKELEQLKKCQQQMAEdKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQV 193
Cdd:COG4717 47 LLERLEKEADELfKPQGRKPELNLKELKELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 194 RQLESEREVLQQQHSV-----QVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGmQLEDL 268
Cdd:COG4717 126 QLLPLYQELEALEAELaelpeRLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE-ELEEL 204
|
170 180 190
....*....|....*....|....*....|....
gi 238637312 269 RQQLQQAEEALVAKQELIDKLKEEAEQHKIVMET 302
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
53-349 |
1.08e-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: 44.56 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 53 LPSEQGTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEflmckfQEARKLVERLSLEKldLRSQREQ 132
Cdd:COG5185 245 LEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTK------EKIAEYTKSIDIKK--ATESLEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 133 ALKELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEG--RIRAVSEQVR----QLESEREVLQQQ 206
Cdd:COG5185 317 QLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGevELSKSSEELDsfkdTIESTKESLDEI 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 207 HSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKS-SKGMQLEDLRQQLQQAEEALVAKQEL 285
Cdd:COG5185 397 PQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISElNKVMREADEESQSRLEEAYDEINRSV 476
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 238637312 286 IDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLK 349
Cdd:COG5185 477 RSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILA 540
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
61-357 |
1.55e-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: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 61 ETLQRCLEENQELRDAIRQSNQMLRErceelLHFQVSQREEkeflmcKFQEARKLVERLSLEKLDLRSQREQALKELEQL 140
Cdd:COG4913 664 ASAEREIAELEAELERLDASSDDLAA-----LEEQLEELEA------ELEELEEELDELKGEIGRLEKELEQAEEELDEL 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 141 KKCQQQMAEDkasVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHsVQVDQLRMQNQS 220
Cdd:COG4913 733 QDRLEAAEDL---ARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAF-NREWPAETADLD 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 221 VEAAlrmerqAASEEKRKLAQLQA----AYHQLFQDYdshIKSSKGMQLEDLRQQLQQAEEALvakQELIDKLKEEAEQH 296
Cdd:COG4913 809 ADLE------SLPEYLALLDRLEEdglpEYEERFKEL---LNENSIEFVADLLSKLRRAIREI---KERIDPLNDSLKRI 876
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 238637312 297 K------IVMETVPVLKAQADIYKADFQAERHAREKLVEkkEYLQEQLEQLQREFNKLKVGCHESAR 357
Cdd:COG4913 877 PfgpgryLRLEARPRPDPEVREFRQELRAVTSGASLFDE--ELSEARFAALKRLIERLRSEEEESDR 941
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
71-368 |
1.73e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 71 QELRDAIRQSNQMLRE-RCEEllhfqVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKK------- 142
Cdd:PRK02224 436 RTARERVEEAEALLEAgKCPE-----CGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDlveaedr 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 143 ----------CQQQMAEDKASVKA---QVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESER----EVLQQ 205
Cdd:PRK02224 511 ierleerredLEELIAERRETIEEkreRAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLaelkERIES 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 206 QHSVQVDQLRMQNQSVEAALRMERQAA-----SEEKRKLAQLQAAYHQLFQDYDshiksskGMQLEDLRQQLQQAEEALv 280
Cdd:PRK02224 591 LERIRTLLAAIADAEDEIERLREKREAlaelnDERRERLAEKRERKRELEAEFD-------EARIEEAREDKERAEEYL- 662
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 281 akQELIDKLKEEAEQHKIVMETVPVLKAQADIYKaDFQAERHAREKLVEKKEYLQEQLEQLQREFNKLKVgchesarieD 360
Cdd:PRK02224 663 --EQVEEKLDELREERDDLQAEIGAVENELEELE-ELRERREALENRVEALEALYDEAEELESMYGDLRA---------E 730
|
....*...
gi 238637312 361 MRKRHVET 368
Cdd:PRK02224 731 LRQRNVET 738
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
64-361 |
3.26e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.03 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 64 QRCLEENQELRDAIRQSNQMLRERCEELLhfQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKC 143
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRAKLLMKRAAHVK--QQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 144 QQQMAEDKASVKAqVTSLLGELQESQSRLEAATKDRQALEGRIrAVSEQVRQLESEREVLQQQHSVQVDQLRMQNqsvEA 223
Cdd:TIGR00618 385 QQQKTTLTQKLQS-LCKELDILQREQATIDTRTSAFRDLQGQL-AHAKKQQELQQRYAELCAAAITCTAQCEKLE---KI 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 224 ALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGMQLED--LRQQLQQAEEALV------AKQELIDKLKEEAEQ 295
Cdd:TIGR00618 460 HLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPcpLCGSCIHPNPARQdidnpgPLTRRMQRGEQTYAQ 539
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 296 HKIVMETV----PVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLKVGCHESARIEDM 361
Cdd:TIGR00618 540 LETSEEDVyhqlTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDM 609
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
150-348 |
3.29e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.75 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 150 DKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLES------EREVLQQQHSV--QVDQLRMQNQSV 221
Cdd:COG0497 152 GLEELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAaalqpgEEEELEEERRRlsNAEKLREALQEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 222 EAALRMERQAAseekrkLAQLQAAYHQL--FQDYDSHIKSSKGM------QLEDLRQQLQQA-------EEALVAKQELI 286
Cdd:COG0497 232 LEALSGGEGGA------LDLLGQALRALerLAEYDPSLAELAERlesaliELEEAASELRRYldslefdPERLEEVEERL 305
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 238637312 287 DKLKEEAEQHKIVMETVPVLKAQAdiykadfQAERHAREKLVEKKEYLQEQLEQLQREFNKL 348
Cdd:COG0497 306 ALLRRLARKYGVTVEELLAYAEEL-------RAELAELENSDERLEELEAELAEAEAELLEA 360
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
132-301 |
3.52e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.76 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 132 QALKELEQLKKCQQQMAEDKASVKAQV---TSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHS 208
Cdd:PRK11637 41 HASDNRDQLKSIQQDIAAKEKSVRQQQqqrASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 209 VQVDQLRMQnqsVEAALRMERQAA------SEEKRKLAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAK 282
Cdd:PRK11637 121 AQERLLAAQ---LDAAFRQGEHTGlqlilsGEESQRGERILAYFGYLNQARQETIA-----ELKQTREELAAQKAELEEK 192
|
170
....*....|....*....
gi 238637312 283 QELIDKLKEEAEQHKIVME 301
Cdd:PRK11637 193 QSQQKTLLYEQQAQQQKLE 211
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
67-215 |
6.18e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 6.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 67 LEENQELRDAIR-----QSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLD--------LRSQREQA 133
Cdd:COG4913 271 LAELEYLRAALRlwfaqRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdrleqLEREIERL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 134 LKELEQLKKCQQQMAE-----------DKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREV 202
Cdd:COG4913 351 ERELEERERRRARLEAllaalglplpaSAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
170
....*....|....*.
gi 238637312 203 LQQQHSV---QVDQLR 215
Cdd:COG4913 431 LERRKSNipaRLLALR 446
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
63-349 |
7.92e-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: 41.98 E-value: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 63 LQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKldlrSQREQALKELEqlkk 142
Cdd:TIGR02169 714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL----HKLEEALNDLE---- 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 143 cqqqmAEDKASVKAQVTSLLGELQESQSRLEAATkdrQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVE 222
Cdd:TIGR02169 786 -----ARLSHSRIPEIQAELSKLEEEVSRIEARL---REIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 223 AALRMERQAASEEKRK---LAQLQAAYHQLFQDYDSHIKSSKGMQ---------LEDLRQQLQQAEEALVAKQELIDKLK 290
Cdd:TIGR02169 858 NLNGKKEELEEELEELeaaLRDLESRLGDLKKERDELEAQLRELErkieeleaqIEKKRKRLSELKAKLEALEEELSEIE 937
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 238637312 291 EEAEQHKIVMETVPVL--------KAQADIYK---------ADFQAERHAREKLVEKKEYLQEQLEQLQR---EFNKLK 349
Cdd:TIGR02169 938 DPKGEDEEIPEEELSLedvqaelqRVEEEIRAlepvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILErieEYEKKK 1016
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
151-298 |
7.95e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.49 E-value: 7.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 151 KASVKAQVTSLLGELQESQSrLEAATKdrQALEGRIRAVSEQVRQLESEREVLQQQH---SVQVDQLRMQNQSVEAALRM 227
Cdd:PRK09039 51 KDSALDRLNSQIAELADLLS-LERQGN--QDLQDSVANLRASLSAAEAERSRLQALLaelAGAGAAAEGRAGELAQELDS 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 238637312 228 ERQAASEEKRKLAQLQAayhqlfqdydshiksskgmQLEDLRQQLQQAEEALVAKQElidklKEEAEQHKI 298
Cdd:PRK09039 128 EKQVSARALAQVELLNQ-------------------QIAALRRQLAALEAALDASEK-----RDRESQAKI 174
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
61-240 |
1.04e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 61 ETLQRCLEENQELRDAIRQSNQMLRERCEELL--HFQVSQREEKEFLMcKFQEARKLVERLSLEKlDLRSQREQALKELE 138
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQKEELAELLraLYRLGRQPPLALLL-SPEDFLDAVRRLQYLK-YLAPARREQAEELR 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 139 QLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQA----LEGRIRAVSEQVRQLESEREVLQQQHSvqvdql 214
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKllarLEKELAELAAELAELQQEAEELEALIA------ 230
|
170 180
....*....|....*....|....*.
gi 238637312 215 RMQNQSVEAALRMERQAASEEKRKLA 240
Cdd:COG4942 231 RLEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
37-342 |
1.18e-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: 41.36 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 37 DMLGEESSLGKPAMLHLPSEQGTPETLQRCLEENQELRDAIRQS-NQMLRERCEELLHFQVSQREEKEFLMCKFQEARKL 115
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAElNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 116 VERLSLEKLDLRSQR-EQALKELEQLKKCQQQMAEDKASVKAQVTSLlGELQESQSRLEAATKDRQAL------EGRIRA 188
Cdd:pfam12128 324 LEALEDQHGAFLDADiETAAADQEQLPSWQSELENLEERLKALTGKH-QDVTAKYNRRRSKIKEQNNRdiagikDKLAKI 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 189 VSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAyhqlfqdydshiksskgmqlEDL 268
Cdd:pfam12128 403 REARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATAT--------------------PEL 462
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 238637312 269 RQQLQQaeealvaKQELIDKLKEEAEQhkivmETVPVLKAQADIYKADFQAERhAREKLVEKKEYLQEQLEQLQ 342
Cdd:pfam12128 463 LLQLEN-------FDERIERAREEQEA-----ANAEVERLQSELRQARKRRDQ-ASEALRQASRRLEERQSALD 523
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
97-281 |
1.32e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 97 SQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKkcQQQMAEDKASVKAQVTSLLGELQESQSRLEAAT 176
Cdd:COG4717 78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE--KLLQLLPLYQELEALEAELAELPERLEELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 177 KDRQALEGRIRAVSEQVRQLESEREVLQQQHSV----QVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLfqd 252
Cdd:COG4717 156 EELRELEEELEELEAELAELQEELEELLEQLSLateeELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL--- 232
|
170 180
....*....|....*....|....*....
gi 238637312 253 ydshiksSKGMQLEDLRQQLQQAEEALVA 281
Cdd:COG4717 233 -------ENELEAAALEERLKEARLLLLI 254
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
118-364 |
1.63e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 118 RLSLEKLDLRSQREQALKELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRL---EAATKDRQALEGRIRAVSEQVR 194
Cdd:PRK04863 283 VHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLnlvQTALRQQEKIERYQADLEELEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 195 QLESEREVLQQQHSVQ-------------VDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAyHQLFQDYDSHIKSSK 261
Cdd:PRK04863 363 RLEEQNEVVEEADEQQeenearaeaaeeeVDELKSQLADYQQALDVQQTRAIQYQQAVQALERA-KQLCGLPDLTADNAE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 262 GMqLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVpvLKAQADIYKADfqAERHAREKL--VEKKEYLQEQLE 339
Cdd:PRK04863 442 DW-LEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLV--RKIAGEVSRSE--AWDVARELLrrLREQRHLAEQLQ 516
|
250 260
....*....|....*....|....*
gi 238637312 340 QLQREFNKLKVGCHESARIEDMRKR 364
Cdd:PRK04863 517 QLRMRLSELEQRLRQQQRAERLLAE 541
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
61-350 |
1.71e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.83 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 61 ETLQRCLEENQELRDAIRQSNQMlreRCEELLHFQVSQREEKEF------LMCKFQEARKLVERLSLEKLDlrSQREQAL 134
Cdd:COG5022 800 QPLLSLLGSRKEYRSYLACIIKL---QKTIKREKKLRETEEVEFslkaevLIQKFGRSLKAKKRFSLLKKE--TIYLQSA 874
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 135 KELEQLKKCQQQMAEDKASVKaqvtsllgELQESQSRLEAatkdrQALEgriraVSEQVRQLESEREVLQQQHSVQVDQL 214
Cdd:COG5022 875 QRVELAERQLQELKIDVKSIS--------SLKLVNLELES-----EIIE-----LKKSLSSDLIENLEFKTELIARLKKL 936
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 215 RMQNQSVEAALRMERQaaSEEKRKLAQLQAAYHQLFQDYDSHIKSSKGM--QLEDLRQQLQQAEEALVAKQELIDKLKEE 292
Cdd:COG5022 937 LNNIDLEEGPSIEYVK--LPELNKLHEVESKLKETSEEYEDLLKKSTILvrEGNKANSELKNFKKELAELSKQYGALQES 1014
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 238637312 293 AEQHKIVMETVPVLKAQADIYKADfQAERHAREKLVEKKEYLQEQLEQLQREFNKLKV 350
Cdd:COG5022 1015 TKQLKELPVEVAELQSASKIISSE-STELSILKPLQKLKGLLLLENNQLQARYKALKL 1071
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
155-307 |
1.83e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.61 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 155 KAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRMQNQSVEAALRMERQAASE 234
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEA----ELEEKDERIERLERELSEARSEERR 459
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 238637312 235 EKRKlaqlqaayhqlfqdyDSHIKSSKGMqLEDLRQQLQQAEEALvakQELIDKLKEEAEQHKIVM--ETVPVLK 307
Cdd:COG2433 460 EIRK---------------DREISRLDRE-IERLERELEEERERI---EELKRKLERLKELWKLEHsgELVPVKV 515
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
55-296 |
1.94e-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: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 55 SEQGTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVE-RLSLEKLDLRSQREQA 133
Cdd:TIGR00618 567 EIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDvRLHLQQCSQELALKLT 646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 134 LKELEQLKKCQQQMAEDKASVKAQ----VTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSV 209
Cdd:TIGR00618 647 ALHALQLTLTQERVREHALSIRVLpkelLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENA 726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 210 QVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSskGMQLEDLRQQLQQAEEALVAKQELIDKL 289
Cdd:TIGR00618 727 SSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQT--GAELSHLAAEIQFFNRLREEDTHLLKTL 804
|
....*..
gi 238637312 290 KEEAEQH 296
Cdd:TIGR00618 805 EAEIGQE 811
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
129-366 |
2.00e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.49 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 129 QREQALKELEQLKKCQQQMAEdkaSVKAQVTSLLGELqESQSRLEAATKDRQALEGRIRAVSEQVRQLESERE-----VL 203
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQE---RLRQEKEEKAREV-ERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERErelerIR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 204 QQQHSVQVDQLRMQNQSVEAA-------LRMERQAASEEKRKlaQLQAAYHQLFQDYDSHIKSSKGM-QLEDLRQQLQQA 275
Cdd:pfam17380 355 QEERKRELERIRQEEIAMEISrmrelerLQMERQQKNERVRQ--ELEAARKVKILEEERQRKIQQQKvEMEQIRAEQEEA 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 276 EEALVAKQElidklKEEAEQHKIVMETVPVLKAQADIYKADfQAERHAREKLVEKKEYLQEQLEQLQREFNKLKVGCHES 355
Cdd:pfam17380 433 RQREVRRLE-----EERAREMERVRLEEQERQQQVERLRQQ-EEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQ 506
|
250
....*....|.
gi 238637312 356 ARIEDMRKRHV 366
Cdd:pfam17380 507 AMIEEERKRKL 517
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
166-368 |
2.52e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.43 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 166 QESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQ-----------QHSVQVDQLRMQNQSVEAALRMERQAASE 234
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERykelkaelrelELALLVLRLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 235 EKRKLAQLQAAYHQLfqdydshikSSKGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKivmETVPVLKAQADIYK 314
Cdd:TIGR02168 255 LEELTAELQELEEKL---------EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR---ERLANLERQLEELE 322
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 238637312 315 ADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLKVGCHESARIEDMRKRHVET 368
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
126-350 |
2.57e-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: 40.32 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 126 LRSQREQALKELEQLKKCQQQMAEDKASVKAQVtSLLGELQESQSRLEAATkdrqaLEGRIRAVSEQVRQLESEREVLQQ 205
Cdd:COG3096 841 LRQRRSELERELAQHRAQEQQLRQQLDQLKEQL-QLLNKLLPQANLLADET-----LADRLEELREELDAAQEAQAFIQQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 206 QHSV------QVDQLRMQNQSVEaALRMERQAASEEKRKLAQLQAAYHQLFQDYdSHIKSSKGMQL--------EDLRQQ 271
Cdd:COG3096 915 HGKAlaqlepLVAVLQSDPEQFE-QLQADYLQAKEQQRRLKQQIFALSEVVQRR-PHFSYEDAVGLlgensdlnEKLRAR 992
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 238637312 272 LQQAEEALvakqeliDKLKEEAEQHkivmetvpvlKAQADIYKADFQAERHAREKlvekkeyLQEQLEQLQREFNKLKV 350
Cdd:COG3096 993 LEQAEEAR-------REAREQLRQA----------QAQYSQYNQVLASLKSSRDA-------KQQTLQELEQELEELGV 1047
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
124-283 |
2.88e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.89 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 124 LDLRSQREQALKELEQLKKcqqqmaedkasvkaQVTSLLGELQESQSRLEAATKDRQAlEGRIRAVSEQVRQLESE-REV 202
Cdd:PRK11281 69 LALLDKIDRQKEETEQLKQ--------------QLAQAPAKLRQAQAELEALKDDNDE-ETRETLSTLSLRQLESRlAQT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 203 LQQQHSVQVDQLRMQNQSVEAALRMERqAASEEKRKLAQLQAAYHQLFQDYDShiksskGMQLEDLRQQLQQAEEALVAK 282
Cdd:PRK11281 134 LDQLQNAQNDLAEYNSQLVSLQTQPER-AQAALYANSQRLQQIRNLLKGGKVG------GKALRPSQRVLLQAEQALLNA 206
|
.
gi 238637312 283 Q 283
Cdd:PRK11281 207 Q 207
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
135-245 |
3.96e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.18 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 135 KELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQV-----------RQLESER--- 200
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGaaaegragelaQELDSEKqvs 132
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 238637312 201 -------EVLQQqhsvQVDQLRMQNQSVEAALRmerqaASEEKRKLAQLQAA 245
Cdd:PRK09039 133 aralaqvELLNQ----QIAALRRQLAALEAALD-----ASEKRDRESQAKIA 175
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
86-336 |
4.00e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 86 ERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKCQQQMAEDKASVKAQVTSLLGEL 165
Cdd:PRK02224 223 ERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 166 QESQSRLEAATKDRQALEGRIravsEQVRQLESEREVLQQQHSVQVDQLRmqnqsvEAALRMERQAasEEKRKLAqlqaa 245
Cdd:PRK02224 303 GLDDADAEAVEARREELEDRD----EELRDRLEECRVAAQAHNEEAESLR------EDADDLEERA--EELREEA----- 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 246 yhqlfqdydshiksskgmqlEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAER-HAR 324
Cdd:PRK02224 366 --------------------AELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERdELR 425
|
250
....*....|..
gi 238637312 325 EKLVEKKEYLQE 336
Cdd:PRK02224 426 EREAELEATLRT 437
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
125-350 |
4.01e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.56 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 125 DLRSQREQALKELEQLKKCQQQMAEDKASVKAQVtSLLGELQES---------QSRLEAATKDRQALEGRIRAVSEQ--- 192
Cdd:PRK04863 841 QLNRRRVELERALADHESQEQQQRSQLEQAKEGL-SALNRLLPRlnlladetlADRVEEIREQLDEAEEAKRFVQQHgna 919
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 193 VRQLESEREVLQQQHSvQVDQLRMQNQSVEAALRMERQAAseekRKLAQL-QAAYHQLFQDYDSHIKSSKGMQlEDLRQQ 271
Cdd:PRK04863 920 LAQLEPIVSVLQSDPE-QFEQLKQDYQQAQQTQRDAKQQA----FALTEVvQRRAHFSYEDAAEMLAKNSDLN-EKLRQR 993
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 238637312 272 LQQAEEALvakqeliDKLKEEAEQHkivmetvpvlKAQADIYKADFQAERHAREKlvekkeyLQEQLEQLQREFNKLKV 350
Cdd:PRK04863 994 LEQAEQER-------TRAREQLRQA----------QAQLAQYNQVLASLKSSYDA-------KRQMLQELKQELQDLGV 1048
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
99-364 |
4.06e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 39.55 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 99 REEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKkcqQQMAEDKASVKAQVT------SLLGELQESQSRL 172
Cdd:COG3096 353 QEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLK---SQLADYQQALDVQQTraiqyqQAVQALEKARALC 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 173 EAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRM----ERQAASEEKRKLAQlQAAYHQ 248
Cdd:COG3096 430 GLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIagevERSQAWQTARELLR-RYRSQQ 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 249 LFQDYDSHIKsskgMQLEDLRQQLQQAEEAlvakQELIDKLKEEAEQHKIVMETVPVLKAQADIykadfqaerhAREKLV 328
Cdd:COG3096 509 ALAQRLQQLR----AQLAELEQRLRQQQNA----ERLLEEFCQRIGQQLDAAEELEELLAELEA----------QLEELE 570
|
250 260 270
....*....|....*....|....*....|....*.
gi 238637312 329 EKKEYLQEQLEQLQREFNKLKvgchesARIEDMRKR 364
Cdd:COG3096 571 EQAAEAVEQRSELRQQLEQLR------ARIKELAAR 600
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
118-348 |
4.13e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.53 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 118 RLSLEKLDLRSQREQALKELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLE 197
Cdd:COG1196 592 LARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 198 SEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQlfqdydshiksskgmQLEDLRQQLQQAEE 277
Cdd:COG1196 672 AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELE---------------EEALEEQLEAEREE 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 278 ALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQA---------ERHAREKlvEKKEYLQEQLEQLQREFNKL 348
Cdd:COG1196 737 LLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvnllaiEEYEELE--ERYDFLSEQREDLEEARETL 814
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
125-294 |
4.19e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.12 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 125 DLRSQREQALKELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQ 204
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 205 QQHSV---QVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVA 281
Cdd:COG4372 122 KERQDleqQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEE 201
|
170
....*....|...
gi 238637312 282 KQELIDKLKEEAE 294
Cdd:COG4372 202 LAEAEKLIESLPR 214
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
108-349 |
4.72e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 108 KFQEARKLVERLSLEKLDLRSQREQALKELEQLKKcqqqMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIR 187
Cdd:PRK03918 201 ELEEVLREINEISSELPELREELEKLEKEVKELEE----LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 188 AVSEQVRQLESEREVLQQQhsvqvdqlrmqnqsveAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKsskgmQLED 267
Cdd:PRK03918 277 ELEEKVKELKELKEKAEEY----------------IKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-----ELEE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 268 LRQQLQQAEEALVAKQELIDKLKEEAEQHkivmETVPVLKAQADIYKADFQAErhAREKLVEKKEYLQEQLEQLQREFNK 347
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLEELEERHELY----EEAKAKKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIEEEISK 409
|
..
gi 238637312 348 LK 349
Cdd:PRK03918 410 IT 411
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
61-348 |
6.54e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 38.90 E-value: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 61 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQRE-----EKEFLMCKFQEARKLVERLSLEKLDLRSQREQALK 135
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEalndlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ 819
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 136 ELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLR 215
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 216 MQNQSVEaalrmERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKG---------MQLEDLRQQLQQAEEALVAKQELI 286
Cdd:TIGR02169 900 ELERKIE-----ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGedeeipeeeLSLEDVQAELQRVEEEIRALEPVN 974
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 238637312 287 DKLKEEAEqhkIVMETVPVLKAQadiyKADFQAERHAREKLVE-----KKEYLQEQLEQLQREFNKL 348
Cdd:TIGR02169 975 MLAIQEYE---EVLKRLDELKEK----RAKLEEERKAILERIEeyekkKREVFMEAFEAINENFNEI 1034
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
259-366 |
6.93e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 38.91 E-value: 6.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 259 SSKGMQLEDLRQQLQQAE---EALVAKQ-----ELIDKLKEEAEQhkivmetvpvLKAQADIYKADFQAERHAREKLVEK 330
Cdd:COG0542 407 DSKPEELDELERRLEQLEiekEALKKEQdeasfERLAELRDELAE----------LEEELEALKARWEAEKELIEEIQEL 476
|
90 100 110
....*....|....*....|....*....|....*.
gi 238637312 331 KEYLQEQLEQLQREFNKLKVGCHESARIEDMRKRHV 366
Cdd:COG0542 477 KEELEQRYGKIPELEKELAELEEELAELAPLLREEV 512
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
165-300 |
8.61e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.22 E-value: 8.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 165 LQESQSRLEAATKDRqalegrIRAVSEQVRQL--ESEREVLQQQHSVQVDQLRMQNQsvEAALRMERQAASEEKRKLAQL 242
Cdd:PRK12704 44 LEEAKKEAEAIKKEA------LLEAKEEIHKLrnEFEKELRERRNELQKLEKRLLQK--EENLDRKLELLEKREEELEKK 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 238637312 243 QAAYHQLFQDYDSHIKSSKGMQLEdLRQQLQQ-----AEEAlvaKQELIDKLKEEAEQHKIVM 300
Cdd:PRK12704 116 EKELEQKQQELEKKEEELEELIEE-QLQELERisgltAEEA---KEILLEKVEEEARHEAAVL 174
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
61-342 |
9.42e-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: 9.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 61 ETLQRCLEENQELRDAIRQSNQMLRERCEellhfQVSQREEKeflmckFQEARKLVERL---------SLEKLDLRS-QR 130
Cdd:COG3096 347 EKIERYQEDLEELTERLEEQEEVVEEAAE-----QLAEAEAR------LEAAEEEVDSLksqladyqqALDVQQTRAiQY 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 131 EQALKELEQLKKCQQQMAEDKASVKaqvtsllGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQ------ 204
Cdd:COG3096 416 QQAVQALEKARALCGLPDLTPENAE-------DYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCkiagev 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 205 ---QQHSVQVDQLRMQNQSVEAALRME--RQAASEEKRKLAQLQAAyHQLFQDYDSHIKS--SKGMQLEDLRQQL----- 272
Cdd:COG3096 489 ersQAWQTARELLRRYRSQQALAQRLQqlRAQLAELEQRLRQQQNA-ERLLEEFCQRIGQqlDAAEELEELLAELeaqle 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238637312 273 ---QQAEEALVAKQELIDKLKEEAEQHKIVMETVPV-LKAQADIYK---------ADFQA-----------ERHA---RE 325
Cdd:COG3096 568 eleEQAAEAVEQRSELRQQLEQLRARIKELAARAPAwLAAQDALERlreqsgealADSQEvtaamqqllerEREAtveRD 647
|
330
....*....|....*..
gi 238637312 326 KLVEKKEYLQEQLEQLQ 342
Cdd:COG3096 648 ELAARKQALESQIERLS 664
|
|
| |
