|
Name |
Accession |
Description |
Interval |
E-value |
| UBAN |
cd09803 |
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ... |
250-336 |
1.23e-24 |
|
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: 96.65 E-value: 1.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 250 MQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQ 329
Cdd:cd09803 1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80
|
....*..
gi 569009771 330 REFNKLK 336
Cdd:cd09803 81 RENQELK 87
|
|
| CC2-LZ |
pfam16516 |
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ... |
251-336 |
9.67e-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: 88.89 E-value: 9.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 251 QLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQR 330
Cdd:pfam16516 15 EIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEYLQR 94
|
....*.
gi 569009771 331 EFNKLK 336
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 |
9.81e-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: 71.36 E-value: 9.81e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569009771 44 EQGTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLE 110
Cdd:pfam11577 1 DEETLEQMKELLTENHQLKEAMKQSNQAMKERCEELSAWQEKQKEEREFLECRFREARELLRRLSLE 67
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
51-335 |
4.75e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.16 E-value: 4.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 51 LQRCLEENQELRDAIRQsnqmLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKK 130
Cdd:TIGR02168 700 LAELRKELEELEEELEQ----LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 131 CQQMAEDK-ASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVE 209
Cdd:TIGR02168 776 ELAEAEAEiEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 210 -AALRMERQAASEEK--RKLAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIV 286
Cdd:TIGR02168 856 sLAAEIEELEELIEEleSELEALLNERASLEEALALLRS-----ELEELSEELRELESKRSELRRELEELREKLAQLELR 930
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 569009771 287 METVPVLKAQ-----ADIYKADFQAERHAREKLVEKKEYLQEQLEQLQREFNKL 335
Cdd:TIGR02168 931 LEGLEVRIDNlqerlSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| zf_C2H2_10 |
pfam18414 |
C2H2 type zinc-finger; This is a zinc finger domain C2H2 which can be found in optineurin ... |
385-410 |
7.83e-12 |
|
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: 59.14 E-value: 7.83e-12
10 20
....*....|....*....|....*.
gi 569009771 385 PDFCCPKCQYQAPDMDTLQIHVMECI 410
Cdd:pfam18414 1 PKHCCPKCQEQLPDIDTLQIHVMDCI 26
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
49-284 |
1.16e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.54 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 49 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELE-- 126
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEel 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 127 --QLKKCQQMAEDKASVKAQVTSLLGELQESQ----SRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQ---HSVQ 197
Cdd:TIGR02168 322 eaQLEELESKLDELAEELAELEEKLEELKEELesleAELEELEAELEELESRLEELEEQLETLRSKVAQLELQiasLNNE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 198 VDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVAKQELIDKLK 277
Cdd:TIGR02168 402 IERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
....*..
gi 569009771 278 EEAEQHK 284
Cdd:TIGR02168 482 RELAQLQ 488
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
113-331 |
1.41e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.47 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 113 DLRSQREQALKELEQlkKCQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQ 192
Cdd:COG4942 20 DAAAEAEAELEQLQQ--EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 193 QHSVQVDQLRMQnqsVEAALRMERQA------ASEEKRKLAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEAL 266
Cdd:COG4942 98 ELEAQKEELAEL---LRALYRLGRQPplalllSPEDFLDAVRRLQYLKYLAPARREQAE-----ELRADLAELAALRAEL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569009771 267 VAKQELIDKLKEEAEQHKIVMETVPVLKAQA-DIYKADFQAERHAREKLVEKKEYLQEQLEQLQRE 331
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLlARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
117-374 |
2.16e-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: 62.77 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 117 QREQALKELEQlkKCQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQ---Q 193
Cdd:TIGR02168 674 ERRREIEELEE--KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEEriaQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 194 HSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQELI 273
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE-----ALDELRAELTLLNEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 274 DKLKEEAEQHKIVMEtvpVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLKVGCHE--------SARI 345
Cdd:TIGR02168 827 ESLERRIAATERRLE---DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALlrseleelSEEL 903
|
250 260
....*....|....*....|....*....
gi 569009771 346 EDMRKRHVETPQPPLLPAPAHHSFHLALS 374
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLE 932
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
110-331 |
1.25e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 110 EKLDLRSQREQALKELEQLKKCQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREV 189
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 190 LQQQHSVQVDQL-----RMQNQSVEAALRMERQAASEEKRKLAQLQAAyhqlfqdydshiksSKGMQLEDLRQQLQQAEE 264
Cdd:COG1196 300 LEQDIARLEERRreleeRLEELEEELAELEEELEELEEELEELEEELE--------------EAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569009771 265 ALVAKQELIDKLKEEAEQHKIVMETvpVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQRE 331
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLE--ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
153-334 |
1.27e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 153 QESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSV--QVDQLRMQNQSVEAA------LRMERQAASEEKR 224
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAlqRLAEYSWDEIDVASAereiaeLEAELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 225 KLAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADF 304
Cdd:COG4913 686 DLAALEEQLEELEAELEELEE-----ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALG 760
|
170 180 190
....*....|....*....|....*....|....*...
gi 569009771 305 QAER--------HAREKLVEKKEYLQEQLEQLQREFNK 334
Cdd:COG4913 761 DAVErelrenleERIDALRARLNRAEEELERAMRAFNR 798
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
49-336 |
2.06e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 49 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFlmcKFQEarklverLSLEKLDLRSQREQALKELEQL 128
Cdd:TIGR02169 180 EEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREY---EGYE-------LLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 129 KkcqqmaEDKASVKAQVTSLLGELQESQSRLEAATKDRQAL-EGRIRAVSEQVRQLESEREVLQQQHSVQVDQLR-MQNQ 206
Cdd:TIGR02169 250 E------EELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEdAEER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 207 SVEAALRMERQAASEE--KRKLAQLQAAYHQLFQDYDShikssKGMQLEDLRQQLQQAE-------EALVAKQELIDKLK 277
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEelEREIEEERKRRDKLTEEYAE-----LKEELEDLRAELEEVDkefaetrDELKDYREKLEKLK 398
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569009771 278 EEAEQHKIVMETVPVLKAQADIYKADFQAERHARE----KLVEKKEYLQEQLEQLQREFNKLK 336
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEakinELEEEKEDKALEIKKQEWKLEQLA 461
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
98-336 |
2.51e-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: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 98 QEARKLVERLSLEKLDLRSQREQALKELEQLKKCQQMAEDKASVKAQVTSLLGELQESQSRLEAatkDRQALEGRIRAVS 177
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE---RLEELEEELAELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 178 EQVRQLESEREVLQQqhsvQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQ 257
Cdd:COG1196 330 EELEELEEELEELEE----ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR-----AAAELAA 400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569009771 258 QLQQAEEALVAKQELIDKLKEEAEQHKIVMETvpvLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLK 336
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAE---LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
98-271 |
2.75e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 98 QEARKLVERLSLEKLDLRSQREQALKELEQLKKCQQMAEDK----------ASVKAQVTSLL---GELQESQSRLEAATK 164
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEidvasaereiAELEAELERLDassDDLAALEEQLEELEA 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 165 DRQALEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDShi 244
Cdd:COG4913 700 ELEELEEELDELKGEIGRLEKELEQAEE----ELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEE-- 773
|
170 180
....*....|....*....|....*..
gi 569009771 245 ksskgmQLEDLRQQLQQAEEALVAKQE 271
Cdd:COG4913 774 ------RIDALRARLNRAEEELERAMR 794
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
108-336 |
5.46e-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: 55.06 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 108 SLEKLDLRSQREQALKEL-EQLKKCQqmaedKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESE 186
Cdd:TIGR02168 201 QLKSLERQAEKAERYKELkAELRELE-----LALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 187 REVLQQQhsVQVDQLRMQNQSVEAAlRMERQAAsEEKRKLAQLQAAYHQLfQDYDSHIKSSKGMQLEDLRQQLQQAEEAL 266
Cdd:TIGR02168 276 VSELEEE--IEELQKELYALANEIS-RLEQQKQ-ILRERLANLERQLEEL-EAQLEELESKLDELAEELAELEEKLEELK 350
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 267 VAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLK 336
Cdd:TIGR02168 351 EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQ 420
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
114-331 |
7.14e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 7.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 114 LRSQREQALKELE------------------QLKKCQQMAED--------KASVKAQVTSLLGELQESQSRLEAATKDRQ 167
Cdd:COG1196 170 YKERKEEAERKLEateenlerledilgelerQLEPLERQAEKaeryrelkEELKELEAELLLLKLRELEAELEELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 168 ALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSV----------EAALRMERQAASEEKRKLAQLQAAYHQLF 237
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEyellaelarlEQDIARLEERRRELEERLEELEEELAELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 238 QDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQhkIVMETVPVLKAQADIYKADFQAERhAREKLVEK 317
Cdd:COG1196 330 EELEELEE-----ELEELEEELEEAEEELEEAEAELAEAEEALLE--AEAELAEAEEELEELAEELLEALR-AAAELAAQ 401
|
250
....*....|....
gi 569009771 318 KEYLQEQLEQLQRE 331
Cdd:COG1196 402 LEELEEAEEALLER 415
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
88-349 |
9.69e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 9.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 88 EEKEFLMCKFQEARKLVERLSL---EKLD----LRSQREQALK---------ELEQ---LKKCQQMAEDKASVKAQVTSL 148
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLiidEKRQqlerLRREREKAERyqallkekrEYEGyelLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 149 LGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVlqqqhsvqvdQLRMQNQSVEAALRMERQAASEEKRKLAQ 228
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL----------RVKEKIGELEAEIASLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 229 LQAAYHQLFQDYDShiksskgmqledLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETvpvLKAQADIYKADFQAER 308
Cdd:TIGR02169 320 AEERLAKLEAEIDK------------LLAEIEELEREIEEERKRRDKLTEEYAELKEELED---LRAELEEVDKEFAETR 384
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 569009771 309 HAREKLVEKKEYLQEQLEQLQREFNKLKVGCHE-SARIEDMR 349
Cdd:TIGR02169 385 DELKDYREKLEKLKREINELKRELDRLQEELQRlSEELADLN 426
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
55-281 |
3.43e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 55 LEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLkkcQQM 134
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL---EEE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 135 AEDKASVKAQVTSLLGELQESQSRLEAATKDRQAlegriRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVE-AALR 213
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEE-----ELEELAEELLEALRAAAELAAQLEELEEAEEALLERlERLE 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569009771 214 MERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAE 281
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
70-351 |
4.68e-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: 51.99 E-value: 4.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 70 QMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLK--------KCQQMAEDKASV 141
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKerleeleeDLSSLEQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 142 KAQVTSLLGELQESQSRLEAATKDRQALEGRIRavSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASE 221
Cdd:TIGR02169 757 KSELKELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 222 EKRKLAQLQAAYHQlfqdydshiKSSKGMQLEDLRQQL----QQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQA 297
Cdd:TIGR02169 835 IQELQEQRIDLKEQ---------IKSIEKEIENLNGKKeeleEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI 905
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 569009771 298 DIYKADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLKVGCHESARIEDMRKR 351
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAE 959
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
55-275 |
6.02e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 6.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 55 LEENQELR-DAIRQSNQMLRERCEELLHfQVSQREEKeflMCKFQEARKLV-----ERLSLEKL-DLRSQREQALKELEQ 127
Cdd:COG3206 162 LEQNLELRrEEARKALEFLEEQLPELRK-ELEEAEAA---LEEFRQKNGLVdlseeAKLLLQQLsELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 128 LKKCQQMAEDKASVKAQVTSLLGE---LQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQ 204
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQspvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILAS 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569009771 205 -------NQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDshIKSSKGMQLEDLRQQLQQAEEALVAKQELIDK 275
Cdd:COG3206 318 leaeleaLQAREASLQAQLAQLEARLAELPELEAELRRLEREVE--VARELYESLLQRLEEARLAEALTVGNVRVIDP 393
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
97-282 |
9.18e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 9.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 97 FQEARKLVERLSleklDLRSQREQALKELEQLKKCQQMAE-----DKASVKAQVTSLLGE---LQESQSRLEAATKDRQA 168
Cdd:COG4913 224 FEAADALVEHFD----DLERAHEALEDAREQIELLEPIRElaeryAAARERLAELEYLRAalrLWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 169 LEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSK 248
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASA 379
|
170 180 190
....*....|....*....|....*....|....
gi 569009771 249 GmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQ 282
Cdd:COG4913 380 E-EFAALRAEAAALLEALEEELEALEEALAEAEA 412
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
59-354 |
1.11e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 59 QELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVErlSLEKLDLRSQREQALKELEQLKKCQQMAEDK 138
Cdd:PTZ00121 1428 EEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE--AKKKAEEAKKADEAKKKAEEAKKKADEAKKA 1505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 139 ASVKAQVTSLL-GELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQ 217
Cdd:PTZ00121 1506 AEAKKKADEAKkAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEE 1585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 218 AASEEKRKLAQLQAAYH--------QLFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMET 289
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYEeekkmkaeEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569009771 290 VPvLKAQADIYKAD----FQAERHAREKLVEKKEYLQEQLEQLQREFNKLKVGCHESARIEDMRKRHVE 354
Cdd:PTZ00121 1666 EA-KKAEEDKKKAEeakkAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAE 1733
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
132-232 |
2.12e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 46.87 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 132 QQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQ--NQSVE 209
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKrkEITDQ 224
|
90 100
....*....|....*....|....*
gi 569009771 210 AALRMErqAASEEKRKL--AQLQAA 232
Cdd:PRK11448 225 AAKRLE--LSEEETRILidQQLRKA 247
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
215-330 |
6.23e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 215 ERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMEtvpvlk 294
Cdd:PRK12704 48 KKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRN-ELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELE------ 120
|
90 100 110
....*....|....*....|....*....|....*.
gi 569009771 295 aqadiykadfQAERHAREKLVEKKEYLQEQLEQLQR 330
Cdd:PRK12704 121 ----------QKQQELEKKEEELEELIEEQLQELER 146
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
49-344 |
1.86e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 49 ETLQRCLEENQELRDAIRQSNQMLRErceelLHFQVSQREEKeflmckFQEARKLVERLSLEKLDLRSQREQALKELEQL 128
Cdd:COG4913 664 ASAEREIAELEAELERLDASSDDLAA-----LEEQLEELEAE------LEELEEELDELKGEIGRLEKELEQAEEELDEL 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 129 KKCQQMAEDKASVkaQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHsVQVDQLRMQNQSV 208
Cdd:COG4913 733 QDRLEAAEDLARL--ELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAF-NREWPAETADLDA 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 209 EAAlrmerqAASEEKRKLAQLQA----AYHQLFQDYdshIKSSKGMQLEDLRQQLQQAEEALvakQELIDKLKEEAEQHK 284
Cdd:COG4913 810 DLE------SLPEYLALLDRLEEdglpEYEERFKEL---LNENSIEFVADLLSKLRRAIREI---KERIDPLNDSLKRIP 877
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569009771 285 ------IVMETVPVLKAQADIYKADFQAERHAREKLVEkkEYLQEQLEQLQREFNKLKVGCHESAR 344
Cdd:COG4913 878 fgpgryLRLEARPRPDPEVREFRQELRAVTSGASLFDE--ELSEARFAALKRLIERLRSEEEESDR 941
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
45-231 |
2.05e-04 |
|
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: 43.89 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 45 QGTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKE 124
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 125 LEQLKKCQQMAEdkasvkAQVTSLLGELQESQSRLEAAtkDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQ 204
Cdd:TIGR02168 395 IASLNNEIERLE------ARLERLEDRRERLQQEIEEL--LKKLEEAELKELQAELEELEEELEELQEELERLEEALEEL 466
|
170 180
....*....|....*....|....*..
gi 569009771 205 NQSVEAALRMERQAASEEKRKLAQLQA 231
Cdd:TIGR02168 467 REELEEAEQALDAAERELAQLQARLDS 493
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
165-336 |
2.84e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 165 DRQALEGRIRAVSEQVRQLES----------EREVLQQ---------------------QHSVQVDQLRMQNQSVEAALR 213
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERahealedareQIELLEPirelaeryaaarerlaeleylRAALRLWFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 214 MERQAASEEKRKLAQLQAAYHQLFQDYDSH---IKSSKGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQ-------- 282
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELeaqIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAlglplpas 378
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 569009771 283 HKIVMETVPVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLK 336
Cdd:COG4913 379 AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
85-336 |
3.97e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 85 SQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLK-KCQQMAEDKASVKAQVTSLLGELQESQSRLEAAT 163
Cdd:TIGR04523 194 NKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQqEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQ 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 164 KDRQALEGRIRAVSEQVRQLESEREVLQQQHSV-----------------------------QVDQLRMQNQSVEAALRM 214
Cdd:TIGR04523 274 KELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwnkelkselknqekkleeiqnqisqnnkIISQLNEQISQLKKELTN 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 215 ERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGM--QLEDLRQQLQQAEEALVAKQELIDKLKEEAE----QHKIVME 288
Cdd:TIGR04523 354 SESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLesQINDLESKIQNQEKLNQQKDEQIKKLQQEKEllekEIERLKE 433
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 569009771 289 TVPVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLK 336
Cdd:TIGR04523 434 TIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK 481
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
137-335 |
4.76e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.37 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 137 DKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLES------EREVLQQQHSV--QVDQLRMQNQSV 208
Cdd:COG0497 152 GLEELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAaalqpgEEEELEEERRRlsNAEKLREALQEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 209 EAALRMERQAAseekrkLAQLQAAYHQL--FQDYDSHIKSSKGM------QLEDLRQQLQQA-------EEALVAKQELI 273
Cdd:COG0497 232 LEALSGGEGGA------LDLLGQALRALerLAEYDPSLAELAERlesaliELEEAASELRRYldslefdPERLEEVEERL 305
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569009771 274 DKLKEEAEQHKIVMETVPVLKAQAdiykadfQAERHAREKLVEKKEYLQEQLEQLQREFNKL 335
Cdd:COG0497 306 ALLRRLARKYGVTVEELLAYAEEL-------RAELAELENSDERLEELEAELAEAEAELLEA 360
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
51-352 |
4.83e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 51 LQRCLEENQELRDAIRQsnqmLRERCEELlhfqvsqREEKEFLMCKFQEARKLVE--RLSLEKLD--LRSQREQ------ 120
Cdd:PRK02224 337 AQAHNEEAESLREDADD----LEERAEEL-------REEAAELESELEEAREAVEdrREEIEELEeeIEELRERfgdapv 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 121 ALKELEQLKkcQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDR---------QALEG-----RIRAVSEQVRQLESE 186
Cdd:PRK02224 406 DLGNAEDFL--EELREERDELREREAELEATLRTARERVEEAEALLeagkcpecgQPVEGsphveTIEEDRERVEELEAE 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 187 REVLQQQHSVQVDQLRMQNQSVEAALRMERqaaSEEKRKLAQlqaayhQLFQDYDSHIKsSKGMQLEDLRQQLQQAEEAL 266
Cdd:PRK02224 484 LEDLEEEVEEVEERLERAEDLVEAEDRIER---LEERREDLE------ELIAERRETIE-EKRERAEELRERAAELEAEA 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 267 VAKQELIDKLKEEAEQHKIV-----------------METVPVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLq 329
Cdd:PRK02224 554 EEKREAAAEAEEEAEEAREEvaelnsklaelkeriesLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEK- 632
|
330 340
....*....|....*....|...
gi 569009771 330 REFNKLKVGCHESARIEDMRKRH 352
Cdd:PRK02224 633 RERKRELEAEFDEARIEEAREDK 655
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
59-355 |
4.92e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 59 QELRDAIRQSNQMLRE-RCEEllhfqVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKCQQmAED 137
Cdd:PRK02224 436 RTARERVEEAEALLEAgKCPE-----CGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVE-AED 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 138 KASVKAQVTSLLGEL----------------------QESQSRLEAATKDRQALEGRIRAVSEQVRQLESER----EVLQ 191
Cdd:PRK02224 510 RIERLEERREDLEELiaerretieekreraeelreraAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLaelkERIE 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 192 QQHSVQVDQLRMQNQSVEAALRMERQAA-----SEEKRKLAQLQAAYHQLFQDYDshiksskGMQLEDLRQQLQQAEEAL 266
Cdd:PRK02224 590 SLERIRTLLAAIADAEDEIERLREKREAlaelnDERRERLAEKRERKRELEAEFD-------EARIEEAREDKERAEEYL 662
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 267 vakQELIDKLKEEAEQHKIVMETVPVLKAQADIYKaDFQAERHAREKLVEKKEYLQEQLEQLQREFNKLKVgchesarie 346
Cdd:PRK02224 663 ---EQVEEKLDELREERDDLQAEIGAVENELEELE-ELRERREALENRVEALEALYDEAEELESMYGDLRA--------- 729
|
....*....
gi 569009771 347 DMRKRHVET 355
Cdd:PRK02224 730 ELRQRNVET 738
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
119-270 |
6.44e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.21 E-value: 6.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 119 EQALKELEQLKKCQQMAEDkasVKAQVTSLLGELQESQSRLEAATKDRQAlEGRIRAVSEQVRQLESE-REVLQQQHSVQ 197
Cdd:PRK11281 66 EQTLALLDKIDRQKEETEQ---LKQQLAQAPAKLRQAQAELEALKDDNDE-ETRETLSTLSLRQLESRlAQTLDQLQNAQ 141
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569009771 198 VDQLRMQNQSVEAALRMERqAASEEKRKLAQLQAAYHQLFQDYDShiksskGMQLEDLRQQLQQAEEALVAKQ 270
Cdd:PRK11281 142 NDLAEYNSQLVSLQTQPER-AQAALYANSQRLQQIRNLLKGGKVG------GKALRPSQRVLLQAEQALLNAQ 207
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
21-282 |
6.57e-04 |
|
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: 41.97 E-value: 6.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 21 AEDQDMLGEESSLGKPAMLHLPSEQGTPETLQRCLEEN----QELRDAIRQSN---QMLRERCEELLHFQVSQREEKEFL 93
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALrealDELRAELTLLNeeaANLRERLESLERRIAATERRLEDL 843
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 94 MCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKcqqmaeDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRI 173
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEELEELIEELESELEALLN------ERASLEEALALLRSELEELSEELRELESKRSELRREL 917
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 174 RAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQ-SVEAALRMERQAASEE---KRKLAQLQAAYHQL----------FQD 239
Cdd:TIGR02168 918 EELREKLAQLELRLEGLEVRIDNLQERLSEEYSlTLEEAEALENKIEDDEeeaRRRLKRLENKIKELgpvnlaaieeYEE 997
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 569009771 240 YDShiksskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQ 282
Cdd:TIGR02168 998 LKE--------RYDFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
101-349 |
7.08e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 7.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 101 RKLVERLslekLDLR--SQREQALK----ELEQLKKCQQMAEDkaSVKAQVTSLlgelQESQSRLEAATKDRQAlegRIR 174
Cdd:PHA02562 153 RKLVEDL----LDISvlSEMDKLNKdkirELNQQIQTLDMKID--HIQQQIKTY----NKNIEEQRKKNGENIA---RKQ 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 175 AVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAyHQLFQDYD------SHIKSSK 248
Cdd:PHA02562 220 NKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKV-IKMYEKGGvcptctQQISEGP 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 249 GMqLEDLRQQLQQAEEALVAKQELIDKLKEEAeqHKIVMETVPVLKAQADIYKADFQAERHAREKLVEKKEYLQ------ 322
Cdd:PHA02562 299 DR-ITKIKDKLKELQHSLEKLDTAIDELEEIM--DEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEElqaefv 375
|
250 260 270
....*....|....*....|....*....|
gi 569009771 323 ---EQLEQLQREFNKLKVGCHESARIEDMR 349
Cdd:PHA02562 376 dnaEELAKLQDELDKIVKTKSELVKEKYHR 405
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
41-336 |
7.21e-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: 7.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 41 LPSEQGTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLveRLSLEKLDLRSQREQ 120
Cdd:COG5185 245 LEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDI--KKATESLEEQLAAAE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 121 ALKELEQLKKCQQMAEDKAsvKAQVTSLLGELQESQSRLEAAtKDRQALEGRIRAVSEQVR----QLESEREVLQQQHSV 196
Cdd:COG5185 323 AEQELEESKRETETGIQNL--TAEIEQGQESLTENLEAIKEE-IENIVGEVELSKSSEELDsfkdTIESTKESLDEIPQN 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 197 QVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKS-SKGMQLEDLRQQLQQAEEALVAKQELIDK 275
Cdd:COG5185 400 QRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISElNKVMREADEESQSRLEEAYDEINRSVRSK 479
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569009771 276 LKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLK 336
Cdd:COG5185 480 KEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILA 540
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
80-323 |
7.78e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 7.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 80 LHFQVSQREEKEfLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLkkcQQMAEDKASVKAQVTSLLGELQESQSRL 159
Cdd:PRK02224 192 LKAQIEEKEEKD-LHERLNGLESELAELDEEIERYEEQREQARETRDEA---DEVLEEHEERREELETLEAEIEDLRETI 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 160 EAATKDRQALEGRIRAVSEQVRQLESEREVL----------QQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQL 229
Cdd:PRK02224 268 AETEREREELAEEVRDLRERLEELEEERDDLlaeaglddadAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 230 QAAYHQLFQDYDshiksSKGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAER- 308
Cdd:PRK02224 348 REDADDLEERAE-----ELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERd 422
|
250
....*....|....*
gi 569009771 309 HAREKLVEKKEYLQE 323
Cdd:PRK02224 423 ELREREAELEATLRT 437
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
49-227 |
8.49e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 8.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 49 ETLQRCLEENQELRDAIRQSNQMLRERCEELL--HFQVSQREEKEFLMcKFQEARKLVERLSLEKLDLRSQREQALKELE 126
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQKEELAELLraLYRLGRQPPLALLL-SPEDFLDAVRRLQYLKYLAPARREQAEELRA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 127 QLKKCQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQA----LEGRIRAVSEQVRQLESEREVLQQQHSvqvdqlR 202
Cdd:COG4942 158 DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKllarLEKELAELAAELAELQQEAEELEALIA------R 231
|
170 180
....*....|....*....|....*
gi 569009771 203 MQNQSVEAALRMERQAASEEKRKLA 227
Cdd:COG4942 232 LEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
49-195 |
8.89e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 8.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 49 ETLQRCLEENQELRDAIRQSNQMLRERCEELL--HFQVSQREEkeflmckfQEARKLVERLSLEKLDLRSQREQALKELE 126
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEaqIRGNGGDRL--------EQLEREIERLERELEERERRRARLEALLA 369
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569009771 127 QLKkcQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHS 195
Cdd:COG4913 370 ALG--LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
51-281 |
9.85e-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: 9.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 51 LQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREqALKELEQLKK 130
Cdd:TIGR02169 714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALN-DLEARLSHSR 792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 131 CQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRMQNQSVEA 210
Cdd:TIGR02169 793 IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK----EIENLNGKKEELEE 868
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569009771 211 ALRmerqaasEEKRKLAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAE 281
Cdd:TIGR02169 869 ELE-------ELEAALRDLESRLGDLKKERDELEA-----QLRELERKIEELEAQIEKKRKRLSELKAKLE 927
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
138-285 |
1.06e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 138 KASVKAQVTSLLGELQESQSrLEAATKdrQALEGRIRAVSEQVRQLESEREVLQQQH---SVQVDQLRMQNQSVEAALRM 214
Cdd:PRK09039 51 KDSALDRLNSQIAELADLLS-LERQGN--QDLQDSVANLRASLSAAEAERSRLQALLaelAGAGAAAEGRAGELAQELDS 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569009771 215 ERQAASEEKRKLAQLQAayhqlfqdydshiksskgmQLEDLRQQLQQAEEALVAKQElidklKEEAEQHKI 285
Cdd:PRK09039 128 EKQVSARALAQVELLNQ-------------------QIAALRRQLAALEAALDASEK-----RDRESQAKI 174
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
48-282 |
1.53e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.82 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 48 PETLQRCLEENQELRDAIRQSNQMLRERC----EELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREqalk 123
Cdd:TIGR02169 261 SELEKRLEEIEQLLEELNKKIKDLGEEEQlrvkEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA---- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 124 ELEQLKK-CQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQhsvqVDQLR 202
Cdd:TIGR02169 337 EIEELEReIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRE----LDRLQ 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 203 MQNQSVEAALRMERQAASEEKRKLAQLQAAyhqlfqdydshiKSSKGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQ 282
Cdd:TIGR02169 413 EELQRLSEELADLNAAIAGIEAKINELEEE------------KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR 480
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
104-335 |
1.91e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 104 VERLSLEKLDLRSQREQALKELEQLKKCQQMAEDKASVKAQVTSLLGELQESQS---RLEAATKDRQALEGRIRAVSEQV 180
Cdd:COG1196 574 ATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLvaaRLEAALRRAVTLAGRLREVTLEG 653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 181 RQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDyDSHIKSSKGMQLEDLRQQLQ 260
Cdd:COG1196 654 EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEA-EEERLEEELEEEALEEQLEA 732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 261 QAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQA---------ERHAREKlvEKKEYLQEQLEQLQRE 331
Cdd:COG1196 733 EREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvnllaiEEYEELE--ERYDFLSEQREDLEEA 810
|
....
gi 569009771 332 FNKL 335
Cdd:COG1196 811 RETL 814
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
49-337 |
2.13e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.45 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 49 ETLQRCLEENQELRDAIRQSNQMlreRCEELLHFQVSQREEKEFLMckfqEARKLVERLSlekldlRSqrEQALKELEQL 128
Cdd:COG5022 800 QPLLSLLGSRKEYRSYLACIIKL---QKTIKREKKLRETEEVEFSL----KAEVLIQKFG------RS--LKAKKRFSLL 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 129 KKCQQMAEDKASVKAQVTSLLgELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSV 208
Cdd:COG5022 865 KKETIYLQSAQRVELAERQLQ-ELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLE 943
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 209 EAALRMERQaaSEEKRKLAQLQAAYHQLFQDYDSHIKSSKGM--QLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIV 286
Cdd:COG5022 944 EGPSIEYVK--LPELNKLHEVESKLKETSEEYEDLLKKSTILvrEGNKANSELKNFKKELAELSKQYGALQESTKQLKEL 1021
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 569009771 287 METVPVLKAQADIYKADfQAERHAREKLVEKKEYLQEQLEQLQREFNKLKV 337
Cdd:COG5022 1022 PVEVAELQSASKIISSE-STELSILKPLQKLKGLLLLENNQLQARYKALKL 1071
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
52-348 |
2.28e-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: 40.34 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 52 QRCLEENQELRDAIRQSNQMLRERCEELLhfQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKC 131
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRAKLLMKRAAHVK--QQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 132 QQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIrAVSEQVRQLESEREVLQQQHSVQVDQLRMQNqsvEAA 211
Cdd:TIGR00618 385 QQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQL-AHAKKQQELQQRYAELCAAAITCTAQCEKLE---KIH 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 212 LRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGMQLED--LRQQLQQAEEALV------AKQELIDKLKEEAEQH 283
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPcpLCGSCIHPNPARQdidnpgPLTRRMQRGEQTYAQL 540
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569009771 284 KIVMETV----PVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLKVGCHESARIEDM 348
Cdd:TIGR00618 541 ETSEEDVyhqlTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDM 609
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
85-268 |
2.69e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 85 SQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQA---LKELEQLKKCQQMAEDKASVKAQVTSLLGELQESQSRLEA 161
Cdd:COG4717 78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEELreeLEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 162 ATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLfqdyd 241
Cdd:COG4717 158 LRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL----- 232
|
170 180
....*....|....*....|....*..
gi 569009771 242 shiksSKGMQLEDLRQQLQQAEEALVA 268
Cdd:COG4717 233 -----ENELEAAALEERLKEARLLLLI 254
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
142-294 |
3.14e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.84 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 142 KAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRMQNQSVEAALRMERQAASE 221
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEA----ELEEKDERIERLERELSEARSEERR 459
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569009771 222 EKRKlaqlqaayhqlfqdyDSHIKSSKGMqLEDLRQQLQQAEEALvakQELIDKLKEEAEQHKIVM--ETVPVLK 294
Cdd:COG2433 460 EIRK---------------DREISRLDRE-IERLERELEEERERI---EELKRKLERLKELWKLEHsgELVPVKV 515
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
113-331 |
3.88e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.04 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 113 DLRSQREQALKELEQLKKCQQMAEdkaSVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVrqleSEREVLQQ 192
Cdd:COG3883 24 ELSELQAELEAAQAELDALQAELE---ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL----GERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 193 QHSVQVDQLRM--QNQSVEAALrmERQAAseekrkLAQLQAAYHQLFQdydshiksskgmQLEDLRQQLQQAEEALVAKQ 270
Cdd:COG3883 97 RSGGSVSYLDVllGSESFSDFL--DRLSA------LSKIADADADLLE------------ELKADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569009771 271 ELIDKLKEEAEQHKIVMETvpvLKAQADIYKADFQAErhaREKLVEKKEYLQEQLEQLQRE 331
Cdd:COG3883 157 AELEALKAELEAAKAELEA---QQAEQEALLAQLSAE---EAAAEAQLAELEAELAAAEAA 211
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
153-336 |
4.58e-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: 39.27 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 153 QESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQ-----------QHSVQVDQLRMQNQSVEAALRMERQAASE 221
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERykelkaelrelELALLVLRLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 222 EKRKLAQLQAAYHQLfqdydshikSSKGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKivmETVPVLKAQADIYK 301
Cdd:TIGR02168 255 LEELTAELQELEEKL---------EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR---ERLANLERQLEELE 322
|
170 180 190
....*....|....*....|....*....|....*
gi 569009771 302 ADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLK 336
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
49-329 |
4.59e-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: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 49 ETLQRCLEENQELRDAIRQSNQMLRERCEellhfQVSQREEKeflmckFQEARKLVERL---------SLEKLDLRS-QR 118
Cdd:COG3096 347 EKIERYQEDLEELTERLEEQEEVVEEAAE-----QLAEAEAR------LEAAEEEVDSLksqladyqqALDVQQTRAiQY 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 119 EQALKELEQLKKCQQMAEdkasvkAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQ------- 191
Cdd:COG3096 416 QQAVQALEKARALCGLPD------LTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCkiageve 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 192 --QQHSVQVDQLRMQNQSVEAALRME--RQAASEEKRKLAQLQAAyHQLFQDYDSHIKS--SKGMQLEDLRQQL------ 259
Cdd:COG3096 490 rsQAWQTARELLRRYRSQQALAQRLQqlRAQLAELEQRLRQQQNA-ERLLEEFCQRIGQqlDAAEELEELLAELeaqlee 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 260 --QQAEEALVAKQELIDKLKEEAEQHKIVMETVPV-LKAQADIYK---------ADFQA-----------ERHA---REK 313
Cdd:COG3096 569 leEQAAEAVEQRSELRQQLEQLRARIKELAARAPAwLAAQDALERlreqsgealADSQEvtaamqqllerEREAtveRDE 648
|
330
....*....|....*.
gi 569009771 314 LVEKKEYLQEQLEQLQ 329
Cdd:COG3096 649 LAARKQALESQIERLS 664
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
87-351 |
5.84e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 39.17 E-value: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 87 REEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKkcQQMAEDKASVKAQVT------SLLGELQESQSRLE 160
Cdd:COG3096 353 QEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLK--SQLADYQQALDVQQTraiqyqQAVQALEKARALCG 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 161 AATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRM----ERQAASEEKRKLAQlQAAYHQL 236
Cdd:COG3096 431 LPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIagevERSQAWQTARELLR-RYRSQQA 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 237 FQDYDSHIKsskgMQLEDLRQQLQQAEEAlvakQELIDKLKEEAEQHKIVMETVPVLKAQADIykadfqaerhAREKLVE 316
Cdd:COG3096 510 LAQRLQQLR----AQLAELEQRLRQQQNA----ERLLEEFCQRIGQQLDAAEELEELLAELEA----------QLEELEE 571
|
250 260 270
....*....|....*....|....*....|....*
gi 569009771 317 KKEYLQEQLEQLQREFNKLKvgchesARIEDMRKR 351
Cdd:COG3096 572 QAAEAVEQRSELRQQLEQLR------ARIKELAAR 600
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
114-329 |
5.98e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.17 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 114 LRSQREQALKELEQLKKCQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEG--RIRAVSEQVRQLESEREVLQ 191
Cdd:PRK04863 447 FQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRlrEQRHLAEQLQQLRMRLSELE 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 192 QQHSVQVDQLRMQNqsvEAALRMERQAASEEKrkLAQLQAAYHQLFQDYDSHiKSSKGMQLEDLRQQLQQAeealvakQE 271
Cdd:PRK04863 527 QRLRQQQRAERLLA---EFCKRLGKNLDDEDE--LEQLQEELEARLESLSES-VSEARERRMALRQQLEQL-------QA 593
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569009771 272 LIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQA-----------ERHA---REKLVEKKEYLQEQLEQLQ 329
Cdd:PRK04863 594 RIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDvteymqqllerERELtveRDELAARKQALDEEIERLS 665
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
52-350 |
6.51e-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: 38.95 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 52 QRCLEENQELRDAIRQSNQMLRERCEELLHfQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKC 131
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEKEEKAR-EVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERK 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 132 QQMAEDKASVKAQVTSLLGELQESQsrleaatKDRQALEGRIRAVSEQVRQ---LESEREVLQQQHSVQVDQLRMQNQSV 208
Cdd:pfam17380 360 RELERIRQEEIAMEISRMRELERLQ-------MERQQKNERVRQELEAARKvkiLEEERQRKIQQQKVEMEQIRAEQEEA 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 209 --EAALRMERQAASEEKRKLAQLQAAYHQ---LFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVAKQELID---KLKEEA 280
Cdd:pfam17380 433 rqREVRRLEEERAREMERVRLEEQERQQQverLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEErkqAMIEEE 512
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 281 EQHKIVMetvpvlKAQADIYKADFQAErhaREKLVEKKEYLQEQLEQLQREFNKLKVGCHESARIEDMRK 350
Cdd:pfam17380 513 RKRKLLE------KEMEERQKAIYEEE---RRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMER 573
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
110-351 |
7.35e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 38.78 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 110 EKLDLRSQREQALK-ELEQLKKCQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEre 188
Cdd:PRK04863 314 RELAELNEAESDLEqDYQAASDHLNLVQTALRQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEE-- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 189 vlqqqhsvqVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAyHQLFQDYDSHIKSSKGMqLEDLRQQLQQAEEALVA 268
Cdd:PRK04863 392 ---------VDELKSQLADYQQALDVQQTRAIQYQQAVQALERA-KQLCGLPDLTADNAEDW-LEEFQAKEQEATEELLS 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 269 KQELIDKLKEEAEQHKIVMETVpvLKAQADIYKADfqAERHAREKL--VEKKEYLQEQLEQLQREFNKLKVGCHESARIE 346
Cdd:PRK04863 461 LEQKLSVAQAAHSQFEQAYQLV--RKIAGEVSRSE--AWDVARELLrrLREQRHLAEQLQQLRMRLSELEQRLRQQQRAE 536
|
....*
gi 569009771 347 DMRKR 351
Cdd:PRK04863 537 RLLAE 541
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
96-336 |
7.76e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.51 E-value: 7.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 96 KFQEARKLVERLSLEKLDLRSQREQALKELEQLKKcqqMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRA 175
Cdd:PRK03918 201 ELEEVLREINEISSELPELREELEKLEKEVKELEE---LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 176 VSEQVRQLESEREVLQQQhsvqvdqlrmqnqsveAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKsskgmQLEDL 255
Cdd:PRK03918 278 LEEKVKELKELKEKAEEY----------------IKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-----ELEEK 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 256 RQQLQQAEEALVAKQELIDKLKEEAEQHkivmETVPVLKAQADIYKADFQAErhAREKLVEKKEYLQEQLEQLQREFNKL 335
Cdd:PRK03918 337 EERLEELKKKLKELEKRLEELEERHELY----EEAKAKKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIEEEISKI 410
|
.
gi 569009771 336 K 336
Cdd:PRK03918 411 T 411
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
246-353 |
8.71e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 38.52 E-value: 8.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009771 246 SSKGMQLEDLRQQLQQAE---EALVAKQ-----ELIDKLKEEAEQhkivmetvpvLKAQADIYKADFQAERHAREKLVEK 317
Cdd:COG0542 407 DSKPEELDELERRLEQLEiekEALKKEQdeasfERLAELRDELAE----------LEEELEALKARWEAEKELIEEIQEL 476
|
90 100 110
....*....|....*....|....*....|....*.
gi 569009771 318 KEYLQEQLEQLQREFNKLKVGCHESARIEDMRKRHV 353
Cdd:COG0542 477 KEELEQRYGKIPELEKELAELEEELAELAPLLREEV 512
|
|
| |
