|
Name |
Accession |
Description |
Interval |
E-value |
| UBAN |
cd09803 |
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ... |
251-337 |
1.65e-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: 96.26 E-value: 1.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 251 MQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQ 330
Cdd:cd09803 1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80
|
....*..
gi 569009765 331 REFNKLK 337
Cdd:cd09803 81 RENQELK 87
|
|
| CC2-LZ |
pfam16516 |
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ... |
252-337 |
1.18e-21 |
|
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: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 252 QLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQR 331
Cdd:pfam16516 15 EIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEYLQR 94
|
....*.
gi 569009765 332 EFNKLK 337
Cdd:pfam16516 95 QNQQLK 100
|
|
| NEMO |
pfam11577 |
NF-kappa-B essential modulator NEMO; NEMO is a regulatory protein which is part of the IKK ... |
44-110 |
1.13e-15 |
|
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: 70.97 E-value: 1.13e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569009765 44 EQGTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLE 110
Cdd:pfam11577 1 DEETLEQMKELLTENHQLKEAMKQSNQAMKERCEELSAWQEKQKEEREFLECRFREARELLRRLSLE 67
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
87-338 |
7.56e-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: 70.47 E-value: 7.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 87 REEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKD 166
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 167 RQALEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIK 246
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEA----QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 247 SSKGM--QLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPV----LKAQADIYKADFQAERHAREKLVEKKE 320
Cdd:TIGR02168 839 RLEDLeeQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEalalLRSELEELSEELRELESKRSELRRELE 918
|
250
....*....|....*...
gi 569009765 321 YLQEQLEQLQREFNKLKV 338
Cdd:TIGR02168 919 ELREKLAQLELRLEGLEV 936
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
59-337 |
4.89e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 4.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 59 QELRDAIRQsnqmlRERCEELLHFQVSQREEKEFLMcKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKCQQQMAED 138
Cdd:COG1196 216 RELKEELKE-----LEAELLLLKLRELEAELEELEA-ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 139 KASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRMQNQSVEAALRMERQ 218
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE----ELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 219 AASEEKRKLAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETvpvLKAQA 298
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALR-----AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE---LEEEE 437
|
250 260 270
....*....|....*....|....*....|....*....
gi 569009765 299 DIYKADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLK 337
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
55-330 |
7.47e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 7.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 55 LEENQELRDAIRQSNQM--LRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKCQ 132
Cdd:COG1196 218 LKEELKELEAELLLLKLreLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 133 QQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAA 212
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 213 LR----------MERQAASEEKRKLAQLQAAYHQLFQDyDSHIKSSKGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAE 282
Cdd:COG1196 378 EEeleelaeellEALRAAAELAAQLEELEEAEEALLER-LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 569009765 283 QHKIVMETVPVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQ 330
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
116-332 |
8.31e-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: 66.33 E-value: 8.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 116 SQREQALKELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQH 195
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 196 SVQVDQLRMQnqsVEAALRMERQAA-----SEEKRKLAQLQAAYHQLFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVAK 270
Cdd:COG4942 100 EAQKEELAEL---LRALYRLGRQPPlalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569009765 271 QELIDKLKEEAEQHKIVMETVPVLKAQAdiyKADFQAERHAREKLVEKKEYLQEQLEQLQRE 332
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARL---EKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| zf_C2H2_10 |
pfam18414 |
C2H2 type zinc-finger; This is a zinc finger domain C2H2 which can be found in optineurin ... |
386-411 |
8.49e-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: 8.49e-12
10 20
....*....|....*....|....*.
gi 569009765 386 PDFCCPKCQYQAPDMDTLQIHVMECI 411
Cdd:pfam18414 1 PKHCCPKCQEQLPDIDTLQIHVMDCI 26
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
49-283 |
1.54e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 49 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQL 128
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 129 KKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQ---QHSVQVDQLRMQ 205
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLErleRLEEELEELEEA 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569009765 206 NQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQ 283
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA--LLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
117-375 |
7.23e-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: 61.23 E-value: 7.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 117 QREQALKELEQlkkCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQ--- 193
Cdd:TIGR02168 674 ERRREIEELEE---KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEEria 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 194 QHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQEL 273
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE-----ALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 274 IDKLKEEAEQHKIVMEtvpVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLKVGCHE--------SAR 345
Cdd:TIGR02168 826 LESLERRIAATERRLE---DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALlrseleelSEE 902
|
250 260 270
....*....|....*....|....*....|
gi 569009765 346 IEDMRKRHVETPQPPLLPAPAHHSFHLALS 375
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKLAQLELRLE 932
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
49-337 |
1.15e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 49 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFlmcKFQEarklverLSLEKLDLRSQREQALKELEQL 128
Cdd:TIGR02169 180 EEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREY---EGYE-------LLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 129 KKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATkdrqalEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLR-MQNQ 207
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG------EEEQLRVKEKIGELEAEIASLERSIAEKERELEdAEER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 208 SVEAALRMERQAASEE--KRKLAQLQAAYHQLFQDYDShikssKGMQLEDLRQQLQQAE-------EALVAKQELIDKLK 278
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEelEREIEEERKRRDKLTEEYAE-----LKEELEDLRAELEEVDkefaetrDELKDYREKLEKLK 398
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569009765 279 EEAEQHKIVMETVPVLKAQADIYKADFQAERHARE----KLVEKKEYLQEQLEQLQREFNKLK 337
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEakinELEEEKEDKALEIKKQEWKLEQLA 461
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
154-335 |
1.29e-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: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 154 QESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSV--QVDQLRMQNQSVEAA------LRMERQAASEEKR 225
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAlqRLAEYSWDEIDVASAereiaeLEAELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 226 KLAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADF 305
Cdd:COG4913 686 DLAALEEQLEELEAELEELEE-----ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALG 760
|
170 180 190
....*....|....*....|....*....|....*...
gi 569009765 306 QAER--------HAREKLVEKKEYLQEQLEQLQREFNK 335
Cdd:COG4913 761 DAVErelrenleERIDALRARLNRAEEELERAMRAFNR 798
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
101-337 |
1.74e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 101 RKLVERLSLEKLDLRSQREQALKELEQLKKCQQQMAEDKASVKAqvtslLGELQESQSRLEAATKDRQALEGRIRAVSEQ 180
Cdd:COG4913 210 DDFVREYMLEEPDTFEAADALVEHFDDLERAHEALEDAREQIEL-----LEPIRELAERYAAARERLAELEYLRAALRLW 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 181 VRQLesEREVLQQqhsvQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAyhqlfqdydshIKSSKGMQLEDLRQQL 260
Cdd:COG4913 285 FAQR--RLELLEA----ELEELRAELARLEAELERLEARLDALREELDELEAQ-----------IRGNGGDRLEQLEREI 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 261 QQAEEALVAKQELIDKLKEEAEQ--------HKIVMETVPVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQRE 332
Cdd:COG4913 348 ERLERELEERERRRARLEALLAAlglplpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
....*
gi 569009765 333 FNKLK 337
Cdd:COG4913 428 IASLE 432
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
48-336 |
1.93e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 48 PETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQ 127
Cdd:TIGR02168 721 LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 128 LKkcqqqmaEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLrmqnq 207
Cdd:TIGR02168 801 LR-------EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI----- 868
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 208 sveAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIK--SSKGMQLEDLRQQLQQAEEALVAKQE----LIDKLKEE- 280
Cdd:TIGR02168 869 ---EELESELEALLNERASLEEALALLRSELEELSEELRelESKRSELRRELEELREKLAQLELRLEglevRIDNLQERl 945
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 569009765 281 AEQHKIVMETVPVLKaqadiykadfqaerharEKLVEKKEYLQEQLEQLQREFNKL 336
Cdd:TIGR02168 946 SEEYSLTLEEAEALE-----------------NKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
49-338 |
2.22e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 49 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALK----- 123
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERqleel 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 124 --ELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQhsvqvdq 201
Cdd:TIGR02168 322 eaQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ------- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 202 lrmqnqsvEAALRMERQAASEEKRklaqlqaayhqlfqdydshiksskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEA 281
Cdd:TIGR02168 395 --------IASLNNEIERLEARLE--------------------------RLEDRRERLQQEIEELLKKLEEAELKELQA 440
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 569009765 282 EQHKIVMETVPVLKAQADIYkadfQAERHAREKLVEKKEYLQEQLEQLQREFNKLKV 338
Cdd:TIGR02168 441 ELEELEEELEELQEELERLE----EALEELREELEEAEQALDAAERELAQLQARLDS 493
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
89-337 |
2.44e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 89 EKEFLMCKFQEARKLVERLSLEKLDLRSQREQALkelEQLKKCQQQMAEdkasVKAQVTSLLGELQESQSRLEAATKDRQ 168
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELT---AELQELEEKLEE----LRLEVSELEEEIEELQKELYALANEIS 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 169 ALEGRIRAVSEQVRQLESEREVLQQQH-----------------SVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQ 231
Cdd:TIGR02168 299 RLEQQKQILRERLANLERQLEELEAQLeeleskldelaeelaelEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 232 AAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAE--R 309
Cdd:TIGR02168 379 EQLETLRSKVAQLEL-----QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEelQ 453
|
250 260
....*....|....*....|....*...
gi 569009765 310 HAREKLVEKKEYLQEQLEQLQREFNKLK 337
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAE 481
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
70-352 |
4.94e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.46 E-value: 4.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 70 QMLRERCEEL---LHFQVSQREEKEFLM----CKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKCQQQMAEDKASV 142
Cdd:TIGR02169 677 QRLRERLEGLkreLSSLQSELRRIENRLdelsQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 143 KAQVTSLLGELQESQSRLEAATKDRQALEGRIRavSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASE 222
Cdd:TIGR02169 757 KSELKELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 223 EKRKLAQLQAAYHQlfqdydshiKSSKGMQLEDLRQQL----QQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQA 298
Cdd:TIGR02169 835 IQELQEQRIDLKEQ---------IKSIEKEIENLNGKKeeleEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI 905
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 569009765 299 DIYKADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLKVGCHESARIEDMRKR 352
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAE 959
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
55-276 |
6.52e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.64 E-value: 6.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 55 LEENQELR-DAIRQSNQMLRERCEELLHfQVSQREEKeflMCKFQEARKLV-----ERLSLEKL-DLRSQREQALKELEQ 127
Cdd:COG3206 162 LEQNLELRrEEARKALEFLEEQLPELRK-ELEEAEAA---LEEFRQKNGLVdlseeAKLLLQQLsELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 128 LKKCQQQMAEDKASVKAQVTSLLG--ELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQ 205
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILAS 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569009765 206 -------NQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDshIKSSKGMQLEDLRQQLQQAEEALVAKQELIDK 276
Cdd:COG3206 318 leaeleaLQAREASLQAQLAQLEARLAELPELEAELRRLEREVE--VARELYESLLQRLEEARLAEALTVGNVRVIDP 393
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
98-272 |
6.97e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 6.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 98 QEARKLVERLSLEKLDLRSQREQALKELEQLKKCQQQMAEDK---------ASVKAQVTSLL---GELQESQSRLEAATK 165
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvasaereiAELEAELERLDassDDLAALEEQLEELEA 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 166 DRQALEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDShi 245
Cdd:COG4913 700 ELEELEEELDELKGEIGRLEKELEQAEE----ELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEE-- 773
|
170 180
....*....|....*....|....*..
gi 569009765 246 ksskgmQLEDLRQQLQQAEEALVAKQE 272
Cdd:COG4913 774 ------RIDALRARLNRAEEELERAMR 794
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
114-332 |
9.49e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 9.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 114 LRSQREQALKELE------------------QLKKCQQQ--MAEDKASVKA-----QVTSLLGELQESQSRLEAATKDRQ 168
Cdd:COG1196 170 YKERKEEAERKLEateenlerledilgelerQLEPLERQaeKAERYRELKEelkelEAELLLLKLRELEAELEELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 169 ALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSV----------EAALRMERQAASEEKRKLAQLQAAYHQLF 238
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEyellaelarlEQDIARLEERRRELEERLEELEEELAELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 239 QDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQhkIVMETVPVLKAQADIYKADFQAERhAREKLVEK 318
Cdd:COG1196 330 EELEELEE-----ELEELEEELEEAEEELEEAEAELAEAEEALLE--AEAELAEAEEELEELAEELLEALR-AAAELAAQ 401
|
250
....*....|....
gi 569009765 319 KEYLQEQLEQLQRE 332
Cdd:COG1196 402 LEELEEAEEALLER 415
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
88-350 |
1.15e-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: 54.30 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 88 EEKEFLMCKFQEARKLVERLSL---EKLD----LRSQREQALKELEQLKKCQ-----------QQMAEDKASVKAQVTSL 149
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLiidEKRQqlerLRREREKAERYQALLKEKReyegyellkekEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 150 LGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVlqqqhsvqvdQLRMQNQSVEAALRMERQAASEEKRKLAQ 229
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL----------RVKEKIGELEAEIASLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 230 LQAAYHQLFQDYDShiksskgmqledLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETvpvLKAQADIYKADFQAER 309
Cdd:TIGR02169 320 AEERLAKLEAEIDK------------LLAEIEELEREIEEERKRRDKLTEEYAELKEELED---LRAELEEVDKEFAETR 384
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 569009765 310 HAREKLVEKKEYLQEQLEQLQREFNKLKVGCHE-SARIEDMR 350
Cdd:TIGR02169 385 DELKDYREKLEKLKREINELKRELDRLQEELQRlSEELADLN 426
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
48-306 |
2.26e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 48 PETLQRCLEENQELRDAIRQSNQMLRERC----EELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREqalk 123
Cdd:TIGR02169 261 SELEKRLEEIEQLLEELNKKIKDLGEEEQlrvkEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA---- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 124 ELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQ----------Q 193
Cdd:TIGR02169 337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKreldrlqeelQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 194 QHSVQVDQLRMQNQSVEAALRmERQAASEEKRklAQLQAAYHQLFQDYDSHIKSSKgmQLEDLRQQLQQAEEALVAKQEL 273
Cdd:TIGR02169 417 RLSEELADLNAAIAGIEAKIN-ELEEEKEDKA--LEIKKQEWKLEQLAADLSKYEQ--ELYDLKEEYDRVEKELSKLQRE 491
|
250 260 270
....*....|....*....|....*....|...
gi 569009765 274 IDKLKEEAeqhKIVMETVPVLKAQADIYKADFQ 306
Cdd:TIGR02169 492 LAEAEAQA---RASEERVRGGRAVEEVLKASIQ 521
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
120-332 |
1.67e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 120 QALKELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESErevLQQQHSVQV 199
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE---IEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 200 DQLRMQNQSVEAALRMERQAASEEKRKLAQlQAAYHQLFQDYDSHIKSskgmQLEDLRQQLQQAEEALVAKQELIDKLKE 279
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLLGSESFSDFLD-RLSALSKIADADADLLE----ELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 569009765 280 EAEQHKIVMETvpvLKAQADIYKADFQAErhaREKLVEKKEYLQEQLEQLQRE 332
Cdd:COG3883 165 ELEAAKAELEA---QQAEQEALLAQLSAE---EAAAEAQLAELEAELAAAEAA 211
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
49-355 |
1.85e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 49 ETLQRCLEENQELRDAirqsnqmlrERCEEllhfqVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQL 128
Cdd:PRK02224 436 RTARERVEEAEALLEA---------GKCPE-----CGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERA 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 129 KkcqqqmaedkasvkaqvtsllgELQESQSRLEAATKDRQALEGRIravSEQVRQLESEREVLQQQHSvQVDQLRMQNQS 208
Cdd:PRK02224 502 E----------------------DLVEAEDRIERLEERREDLEELI---AERRETIEEKRERAEELRE-RAAELEAEAEE 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 209 VEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDShiksskgmqLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVM 288
Cdd:PRK02224 556 KREAAAEAEEEAEEAREEVAELNSKLAELKERIES---------LERIRTLLAAIADAEDEIERLREKREALAELNDERR 626
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569009765 289 ETVPVLKAQADIYKADFQAER--HAREKLVEKKEYLQ---EQLEQLQREFNKL--KVGCHESA--RIEDMRKRHVE 355
Cdd:PRK02224 627 ERLAEKRERKRELEAEFDEARieEAREDKERAEEYLEqveEKLDELREERDDLqaEIGAVENEleELEELRERREA 702
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
133-233 |
2.20e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 46.87 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 133 QQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQ--NQSVE 210
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKrkEITDQ 224
|
90 100
....*....|....*....|....*
gi 569009765 211 AALRMErqAASEEKRKL--AQLQAA 233
Cdd:PRK11448 225 AAKRLE--LSEEETRILidQQLRKA 247
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
59-355 |
3.99e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 59 QELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVErlSLEKLDLRSQREQALKELEQLKKCQQQMAED 138
Cdd:PTZ00121 1428 EEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE--AKKKAEEAKKADEAKKKAEEAKKKADEAKKA 1505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 139 KASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQ 218
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEE 1585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 219 AASEEKRKLAQLQAAYH--------QLFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMET 290
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYEeekkmkaeEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569009765 291 VPvLKAQADIYKAD----FQAERHAREKLVEKKEYLQEQLEQLQREFNKLKVGCHESARIEDMRKRHVE 355
Cdd:PTZ00121 1666 EA-KKAEEDKKKAEeakkAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAE 1733
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
216-331 |
6.25e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 6.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 216 ERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMEtvpvlk 295
Cdd:PRK12704 48 KKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRN-ELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELE------ 120
|
90 100 110
....*....|....*....|....*....|....*.
gi 569009765 296 aqadiykadfQAERHAREKLVEKKEYLQEQLEQLQR 331
Cdd:PRK12704 121 ----------QKQQELEKKEEELEELIEEQLQELER 146
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
51-353 |
6.51e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 6.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 51 LQRCLEENQELRDAIRQsnqmLRERCEELlhfqvsqREEKEFLMCKFQEARKLVE--RLSLEKLD-----LRSQREQALK 123
Cdd:PRK02224 337 AQAHNEEAESLREDADD----LEERAEEL-------REEAAELESELEEAREAVEdrREEIEELEeeieeLRERFGDAPV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 124 ELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDR---------QALEG-----RIRAVSEQVRQLESERE 189
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLeagkcpecgQPVEGsphveTIEEDRERVEELEAELE 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 190 VLQQQHSVQVDQLRMQNQSVEAALRMERqaaSEEKRKLAQlqaayhQLFQDYDSHIKsSKGMQLEDLRQQLQQAEEALVA 269
Cdd:PRK02224 486 DLEEEVEEVEERLERAEDLVEAEDRIER---LEERREDLE------ELIAERRETIE-EKRERAEELRERAAELEAEAEE 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 270 KQELIDKLKEEAEQHKIV-----------------METVPVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLqRE 332
Cdd:PRK02224 556 KREAAAEAEEEAEEAREEvaelnsklaelkeriesLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEK-RE 634
|
330 340
....*....|....*....|.
gi 569009765 333 FNKLKVGCHESARIEDMRKRH 353
Cdd:PRK02224 635 RKRELEAEFDEARIEEAREDK 655
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
45-222 |
7.29e-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: 45.05 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 45 QGTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKE 124
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 125 LEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAAtkDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRM 204
Cdd:TIGR02168 395 IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
170
....*....|....*...
gi 569009765 205 QNQSVEAALRMERQAASE 222
Cdd:TIGR02168 473 AEQALDAAERELAQLQAR 490
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
101-350 |
1.09e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 101 RKLVERLslekLDLR--SQREQALKEL-----EQLKKCQQQMAEDKASVKAQvtsllgelQESQSRLEAATKDRQAlegR 173
Cdd:PHA02562 153 RKLVEDL----LDISvlSEMDKLNKDKirelnQQIQTLDMKIDHIQQQIKTY--------NKNIEEQRKKNGENIA---R 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 174 IRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAyHQLFQDYD------SHIKS 247
Cdd:PHA02562 218 KQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKV-IKMYEKGGvcptctQQISE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 248 SKGMqLEDLRQQLQQAEEALVAKQELIDKLKEEAeqHKIVMETVPVLKAQADIYKADFQAERHAREKLVEKKEYLQ---- 323
Cdd:PHA02562 297 GPDR-ITKIKDKLKELQHSLEKLDTAIDELEEIM--DEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEElqae 373
|
250 260 270
....*....|....*....|....*....|..
gi 569009765 324 -----EQLEQLQREFNKLKVGCHESARIEDMR 350
Cdd:PHA02562 374 fvdnaEELAKLQDELDKIVKTKSELVKEKYHR 405
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
21-283 |
1.26e-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: 44.28 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 21 AEDQDMLGEESSLGKPAMLHLPSEQGTPETLQRCLEEN----QELRDAIRQSN---QMLRERCEELLHFQVSQREEKEFL 93
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALrealDELRAELTLLNeeaANLRERLESLERRIAATERRLEDL 843
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 94 MCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGR 173
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 174 IRAVSEQVRQLESEREVLQQQHSVQVdQLRMQNQSVEAALRMERQAASEekRKLAQLQAAYHQL----------FQDYDS 243
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQERLSEEY-SLTLEEAEALENKIEDDEEEAR--RRLKRLENKIKELgpvnlaaieeYEELKE 1000
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 569009765 244 hiksskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQ 283
Cdd:TIGR02168 1001 --------RYDFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
103-290 |
1.90e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 103 LVERLSLEKLDL-RSQREQALKELEQLKKCQQQMAEdKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQV 181
Cdd:COG4717 47 LLERLEKEADELfKPQGRKPELNLKELKELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 182 RQLESEREVLQQQHSV-----QVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGmQLEDL 256
Cdd:COG4717 126 QLLPLYQELEALEAELaelpeRLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE-ELEEL 204
|
170 180 190
....*....|....*....|....*....|....
gi 569009765 257 RQQLQQAEEALVAKQELIDKLKEEAEQHKIVMET 290
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
41-337 |
3.45e-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: 42.64 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 41 LPSEQGTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEflmckfQEARKLVERLSLEKldLRSQREQ 120
Cdd:COG5185 245 LEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTK------EKIAEYTKSIDIKK--ATESLEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 121 ALKELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEG--RIRAVSEQVR----QLESEREVLQQQ 194
Cdd:COG5185 317 QLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGevELSKSSEELDsfkdTIESTKESLDEI 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 195 HSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKS-SKGMQLEDLRQQLQQAEEALVAKQEL 273
Cdd:COG5185 397 PQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISElNKVMREADEESQSRLEEAYDEINRSV 476
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569009765 274 IDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLK 337
Cdd:COG5185 477 RSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILA 540
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
59-356 |
3.71e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 59 QELRDAIRQSNQMLRE-RCEEllhfqVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKK------- 130
Cdd:PRK02224 436 RTARERVEEAEALLEAgKCPE-----CGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDlveaedr 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 131 ----------CQQQMAEDKASVKA---QVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESER----EVLQQ 193
Cdd:PRK02224 511 ierleerredLEELIAERRETIEEkreRAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLaelkERIES 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 194 QHSVQVDQLRMQNQSVEAALRMERQAA-----SEEKRKLAQLQAAYHQLFQDYDshiksskGMQLEDLRQQLQQAEEALv 268
Cdd:PRK02224 591 LERIRTLLAAIADAEDEIERLREKREAlaelnDERRERLAEKRERKRELEAEFD-------EARIEEAREDKERAEEYL- 662
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 269 akQELIDKLKEEAEQHKIVMETVPVLKAQADIYKaDFQAERHAREKLVEKKEYLQEQLEQLQREFNKLKVgchesarieD 348
Cdd:PRK02224 663 --EQVEEKLDELREERDDLQAEIGAVENELEELE-ELRERREALENRVEALEALYDEAEELESMYGDLRA---------E 730
|
....*...
gi 569009765 349 MRKRHVET 356
Cdd:PRK02224 731 LRQRNVET 738
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
49-345 |
4.03e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 49 ETLQRCLEENQELRDAIRQSNQMLRErceelLHFQVSQREEkeflmcKFQEARKLVERLSLEKLDLRSQREQALKELEQL 128
Cdd:COG4913 664 ASAEREIAELEAELERLDASSDDLAA-----LEEQLEELEA------ELEELEEELDELKGEIGRLEKELEQAEEELDEL 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 129 KKCQQQMAEDkasVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHsVQVDQLRMQNQS 208
Cdd:COG4913 733 QDRLEAAEDL---ARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAF-NREWPAETADLD 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 209 VEAAlrmerqAASEEKRKLAQLQA----AYHQLFQDYdshIKSSKGMQLEDLRQQLQQAEEALvakQELIDKLKEEAEQH 284
Cdd:COG4913 809 ADLE------SLPEYLALLDRLEEdglpEYEERFKEL---LNENSIEFVADLLSKLRRAIREI---KERIDPLNDSLKRI 876
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569009765 285 K------IVMETVPVLKAQADIYKADFQAERHAREKLVEkkEYLQEQLEQLQREFNKLKVGCHESAR 345
Cdd:COG4913 877 PfgpgryLRLEARPRPDPEVREFRQELRAVTSGASLFDE--ELSEARFAALKRLIERLRSEEEESDR 941
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
138-336 |
4.94e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.37 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 138 DKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLES------EREVLQQQHSV--QVDQLRMQNQSV 209
Cdd:COG0497 152 GLEELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAaalqpgEEEELEEERRRlsNAEKLREALQEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 210 EAALRMERQAAseekrkLAQLQAAYHQL--FQDYDSHIKSSKGM------QLEDLRQQLQQA-------EEALVAKQELI 274
Cdd:COG0497 232 LEALSGGEGGA------LDLLGQALRALerLAEYDPSLAELAERlesaliELEEAASELRRYldslefdPERLEEVEERL 305
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569009765 275 DKLKEEAEQHKIVMETVPVLKAQAdiykadfQAERHAREKLVEKKEYLQEQLEQLQREFNKL 336
Cdd:COG0497 306 ALLRRLARKYGVTVEELLAYAEEL-------RAELAELENSDERLEELEAELAEAEAELLEA 360
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
120-289 |
5.30e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.99 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 120 QALKELEQLKKCQQQMAEDKASVKAQV---TSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHS 196
Cdd:PRK11637 41 HASDNRDQLKSIQQDIAAKEKSVRQQQqqrASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 197 VQVDQLRMQnqsVEAALRMERQAA------SEEKRKLAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAK 270
Cdd:PRK11637 121 AQERLLAAQ---LDAAFRQGEHTGlqlilsGEESQRGERILAYFGYLNQARQETIA-----ELKQTREELAAQKAELEEK 192
|
170
....*....|....*....
gi 569009765 271 QELIDKLKEEAEQHKIVME 289
Cdd:PRK11637 193 QSQQKTLLYEQQAQQQKLE 211
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
55-196 |
1.06e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 55 LEENQELRDAIR-----QSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLD--------LRSQREQA 121
Cdd:COG4913 271 LAELEYLRAALRlwfaqRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdrleqLEREIERL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 122 LKELEQLKKCQQQMAE-----------DKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREV 190
Cdd:COG4913 351 ERELEERERRRARLEAllaalglplpaSAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
....*.
gi 569009765 191 LQQQHS 196
Cdd:COG4913 431 LERRKS 436
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
139-286 |
1.18e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 139 KASVKAQVTSLLGELQESQSrLEAATKdrQALEGRIRAVSEQVRQLESEREVLQQQH---SVQVDQLRMQNQSVEAALRM 215
Cdd:PRK09039 51 KDSALDRLNSQIAELADLLS-LERQGN--QDLQDSVANLRASLSAAEAERSRLQALLaelAGAGAAAEGRAGELAQELDS 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569009765 216 ERQAASEEKRKLAQLQAayhqlfqdydshiksskgmQLEDLRQQLQQAEEALVAKQElidklKEEAEQHKI 286
Cdd:PRK09039 128 EKQVSARALAQVELLNQ-------------------QIAALRRQLAALEAALDASEK-----RDRESQAKI 174
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
52-349 |
1.23e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.11 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 52 QRCLEENQELRDAIRQSNQMLRERCEELLhfQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKC 131
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRAKLLMKRAAHVK--QQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 132 QQQMAEDKASVKAqVTSLLGELQESQSRLEAATKDRQALEGRIrAVSEQVRQLESEREVLQQQHSVQVDQLRMQNqsvEA 211
Cdd:TIGR00618 385 QQQKTTLTQKLQS-LCKELDILQREQATIDTRTSAFRDLQGQL-AHAKKQQELQQRYAELCAAAITCTAQCEKLE---KI 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 212 ALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGMQLED--LRQQLQQAEEALV------AKQELIDKLKEEAEQ 283
Cdd:TIGR00618 460 HLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPcpLCGSCIHPNPARQdidnpgPLTRRMQRGEQTYAQ 539
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 284 HKIVMETV----PVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLKVGCHESARIEDM 349
Cdd:TIGR00618 540 LETSEEDVyhqlTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDM 609
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
51-282 |
2.45e-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: 40.44 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 51 LQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKldlrSQREQALKELEqlkk 130
Cdd:TIGR02169 714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL----HKLEEALNDLE---- 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 131 cqqqmAEDKASVKAQVTSLLGELQESQSRLEAATkdrQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVE 210
Cdd:TIGR02169 786 -----ARLSHSRIPEIQAELSKLEEEVSRIEARL---REIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE 857
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569009765 211 AALRMERQAASEEKRK---LAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAE 282
Cdd:TIGR02169 858 NLNGKKEELEEELEELeaaLRDLESRLGDLKKERDELEA-----QLRELERKIEELEAQIEKKRKRLSELKAKLE 927
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
49-228 |
2.49e-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: 39.75 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 49 ETLQRCLEENQELRDAIRQSNQMLRERCEELL--HFQVSQREEKEFLMcKFQEARKLVERLSLEKLDLRSQREQAlKELE 126
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQKEELAELLraLYRLGRQPPLALLL-SPEDFLDAVRRLQYLKYLAPARREQA-EELR 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 127 QLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQA----LEGRIRAVSEQVRQLESEREVLQQQHSvqvdql 202
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKllarLEKELAELAAELAELQQEAEELEALIA------ 230
|
170 180
....*....|....*....|....*.
gi 569009765 203 RMQNQSVEAALRMERQAASEEKRKLA 228
Cdd:COG4942 231 RLEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
49-338 |
2.72e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.06 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 49 ETLQRCLEENQELRDAIRQSNQMlreRCEELLHFQVSQREEKEF------LMCKFQEARKLVERLSLEKLDlrSQREQAL 122
Cdd:COG5022 800 QPLLSLLGSRKEYRSYLACIIKL---QKTIKREKKLRETEEVEFslkaevLIQKFGRSLKAKKRFSLLKKE--TIYLQSA 874
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 123 KELEQLKKCQQQMAEDKASVKaqvtsllgELQESQSRLEAatkdrQALEgriraVSEQVRQLESEREVLQQQHSVQVDQL 202
Cdd:COG5022 875 QRVELAERQLQELKIDVKSIS--------SLKLVNLELES-----EIIE-----LKKSLSSDLIENLEFKTELIARLKKL 936
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 203 RMQNQSVEAALRMERQaaSEEKRKLAQLQAAYHQLFQDYDSHIKSSKGM--QLEDLRQQLQQAEEALVAKQELIDKLKEE 280
Cdd:COG5022 937 LNNIDLEEGPSIEYVK--LPELNKLHEVESKLKETSEEYEDLLKKSTILvrEGNKANSELKNFKKELAELSKQYGALQES 1014
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 569009765 281 AEQHKIVMETVPVLKAQADIYKADfQAERHAREKLVEKKEYLQEQLEQLQREFNKLKV 338
Cdd:COG5022 1015 TKQLKELPVEVAELQSASKIISSE-STELSILKPLQKLKGLLLLENNQLQARYKALKL 1071
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
25-330 |
2.88e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.21 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 25 DMLGEESSLGKPAMLHLPSEQGTPETLQRCLEENQELRDAIRQS-NQMLRERCEELLHFQVSQREEKEFLMCKFQEARKL 103
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAElNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 104 VERLSLEKLDLRSQR-EQALKELEQLKKCQQQMAEDKASVKAQVTSLlGELQESQSRLEAATKDRQAL------EGRIRA 176
Cdd:pfam12128 324 LEALEDQHGAFLDADiETAAADQEQLPSWQSELENLEERLKALTGKH-QDVTAKYNRRRSKIKEQNNRdiagikDKLAKI 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 177 VSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAyhqlfqdydshiksskgmqlEDL 256
Cdd:pfam12128 403 REARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATAT--------------------PEL 462
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569009765 257 RQQLQQaeealvaKQELIDKLKEEAEQhkivmETVPVLKAQADIYKADFQAERhAREKLVEKKEYLQEQLEQLQ 330
Cdd:pfam12128 463 LLQLEN-------FDERIERAREEQEA-----ANAEVERLQSELRQARKRRDQ-ASEALRQASRRLEERQSALD 523
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
85-269 |
2.90e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 85 SQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKCQQ--QMAEDKASVKAQVTSLLGELQESQSRLEA 162
Cdd:COG4717 78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEERLEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 163 ATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLfqdyd 242
Cdd:COG4717 158 LRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL----- 232
|
170 180
....*....|....*....|....*..
gi 569009765 243 shiksSKGMQLEDLRQQLQQAEEALVA 269
Cdd:COG4717 233 -----ENELEAAALEERLKEARLLLLI 254
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
106-352 |
3.02e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 106 RLSLEKLDLRSQREQALKELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRL---EAATKDRQALEGRIRAVSEQVR 182
Cdd:PRK04863 283 VHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLnlvQTALRQQEKIERYQADLEELEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 183 QLESEREVLQQQHSVQ-------------VDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAyHQLFQDYDSHIKSSK 249
Cdd:PRK04863 363 RLEEQNEVVEEADEQQeenearaeaaeeeVDELKSQLADYQQALDVQQTRAIQYQQAVQALERA-KQLCGLPDLTADNAE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 250 GMqLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVpvLKAQADIYKADfqAERHAREKL--VEKKEYLQEQLE 327
Cdd:PRK04863 442 DW-LEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLV--RKIAGEVSRSE--AWDVARELLrrLREQRHLAEQLQ 516
|
250 260
....*....|....*....|....*
gi 569009765 328 QLQREFNKLKVGCHESARIEDMRKR 352
Cdd:PRK04863 517 QLRMRLSELEQRLRQQQRAERLLAE 541
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
143-295 |
3.10e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.84 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 143 KAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRMQNQSVEAALRMERQAASE 222
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEA----ELEEKDERIERLERELSEARSEERR 459
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569009765 223 EKRKlaqlqaayhqlfqdyDSHIKSSKGMqLEDLRQQLQQAEEALvakQELIDKLKEEAEQHKIVM--ETVPVLK 295
Cdd:COG2433 460 EIRK---------------DREISRLDRE-IERLERELEEERERI---EELKRKLERLKELWKLEHsgELVPVKV 515
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
112-271 |
3.30e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.89 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 112 LDLRSQREQALKELEQLKKcqqqmaedkasvkaQVTSLLGELQESQSRLEAATKDRQAlEGRIRAVSEQVRQLESE-REV 190
Cdd:PRK11281 69 LALLDKIDRQKEETEQLKQ--------------QLAQAPAKLRQAQAELEALKDDNDE-ETRETLSTLSLRQLESRlAQT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 191 LQQQHSVQVDQLRMQNQSVEAALRMERqAASEEKRKLAQLQAAYHQLFQDYDShiksskGMQLEDLRQQLQQAEEALVAK 270
Cdd:PRK11281 134 LDQLQNAQNDLAEYNSQLVSLQTQPER-AQAALYANSQRLQQIRNLLKGGKVG------GKALRPSQRVLLQAEQALLNA 206
|
.
gi 569009765 271 Q 271
Cdd:PRK11281 207 Q 207
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
113-282 |
4.02e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.12 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 113 DLRSQREQALKELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQ 192
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 193 QQHSV---QVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVA 269
Cdd:COG4372 122 KERQDleqQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEE 201
|
170
....*....|...
gi 569009765 270 KQELIDKLKEEAE 282
Cdd:COG4372 202 LAEAEKLIESLPR 214
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
43-284 |
4.07e-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: 39.57 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 43 SEQGTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVE-RLSLEKLDLRSQREQA 121
Cdd:TIGR00618 567 EIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDvRLHLQQCSQELALKLT 646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 122 LKELEQLKKCQQQMAEDKASVKAQ----VTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSV 197
Cdd:TIGR00618 647 ALHALQLTLTQERVREHALSIRVLpkelLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENA 726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 198 QVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSskGMQLEDLRQQLQQAEEALVAKQELIDKL 277
Cdd:TIGR00618 727 SSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQT--GAELSHLAAEIQFFNRLREEDTHLLKTL 804
|
....*..
gi 569009765 278 KEEAEQH 284
Cdd:TIGR00618 805 EAEIGQE 811
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
114-338 |
4.81e-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: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 114 LRSQREQALKELEQLKKCQQQMAEDKASVKAQVtSLLGELQESQSRLEAATkdrqaLEGRIRAVSEQVRQLESEREVLQQ 193
Cdd:COG3096 841 LRQRRSELERELAQHRAQEQQLRQQLDQLKEQL-QLLNKLLPQANLLADET-----LADRLEELREELDAAQEAQAFIQQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 194 QHSV------QVDQLRMQNQSVEaALRMERQAASEEKRKLAQLQAAYHQLFQDYdSHIKSSKGMQL--------EDLRQQ 259
Cdd:COG3096 915 HGKAlaqlepLVAVLQSDPEQFE-QLQADYLQAKEQQRRLKQQIFALSEVVQRR-PHFSYEDAVGLlgensdlnEKLRAR 992
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569009765 260 LQQAEEALvakqeliDKLKEEAEQHkivmetvpvlKAQADIYKADFQAERHAREKlvekkeyLQEQLEQLQREFNKLKV 338
Cdd:COG3096 993 LEQAEEAR-------REAREQLRQA----------QAQYSQYNQVLASLKSSRDA-------KQQTLQELEQELEELGV 1047
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
154-337 |
4.84e-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: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 154 QESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQ-----------QHSVQVDQLRMQNQSVEAALRMERQAASE 222
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERykelkaelrelELALLVLRLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 223 EKRKLAQLQAAYHQLfqdydshikSSKGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKivmETVPVLKAQADIYK 302
Cdd:TIGR02168 255 LEELTAELQELEEKL---------EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR---ERLANLERQLEELE 322
|
170 180 190
....*....|....*....|....*....|....*
gi 569009765 303 ADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLK 337
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
117-354 |
4.87e-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: 39.34 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 117 QREQALKELEQLKKCQQQMAEdkaSVKAQVTSLLGELqESQSRLEAATKDRQALEGRIRAVSEQVRQLESERE-----VL 191
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQE---RLRQEKEEKAREV-ERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERErelerIR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 192 QQQHSVQVDQLRMQNQSVEAA-------LRMERQAASEEKRKlaQLQAAYHQLFQDYDSHIKSSKGM-QLEDLRQQLQQA 263
Cdd:pfam17380 355 QEERKRELERIRQEEIAMEISrmrelerLQMERQQKNERVRQ--ELEAARKVKILEEERQRKIQQQKvEMEQIRAEQEEA 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 264 EEALVAKQElidklKEEAEQHKIVMETVPVLKAQADIYKADfQAERHAREKLVEKKEYLQEQLEQLQREFNKLKVGCHES 343
Cdd:pfam17380 433 RQREVRRLE-----EERAREMERVRLEEQERQQQVERLRQQ-EEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQ 506
|
250
....*....|.
gi 569009765 344 ARIEDMRKRHV 354
Cdd:pfam17380 507 AMIEEERKRKL 517
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
123-233 |
5.74e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 38.41 E-value: 5.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 123 KELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQV-----------RQLESER--- 188
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGaaaegragelaQELDSEKqvs 132
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 569009765 189 -------EVLQQqhsvQVDQLRMQNQSVEAALRmerqaASEEKRKLAQLQAA 233
Cdd:PRK09039 133 aralaqvELLNQ----QIAALRRQLAALEAALD-----ASEKRDRESQAKIA 175
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
106-336 |
6.81e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 38.76 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 106 RLSLEKLDLRSQREQALKELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLE 185
Cdd:COG1196 592 LARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 186 SEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQlfqdydshiksskgmQLEDLRQQLQQAEE 265
Cdd:COG1196 672 AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELE---------------EEALEEQLEAEREE 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 266 ALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQA---------ERHAREKlvEKKEYLQEQLEQLQREFNKL 336
Cdd:COG1196 737 LLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvnllaiEEYEELE--ERYDFLSEQREDLEEARETL 814
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
74-324 |
7.39e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.48 E-value: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 74 ERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKCQQQMAEDKASVKAQVTSLLGEL 153
Cdd:PRK02224 223 ERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 154 QESQSRLEAATKDRQALEGRIravsEQVRQLESEREVLQQQHSVQVDQLRmqnqsvEAALRMERQAasEEKRKLAqlqaa 233
Cdd:PRK02224 303 GLDDADAEAVEARREELEDRD----EELRDRLEECRVAAQAHNEEAESLR------EDADDLEERA--EELREEA----- 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 234 yhqlfqdydshiksskgmqlEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAER-HAR 312
Cdd:PRK02224 366 --------------------AELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERdELR 425
|
250
....*....|..
gi 569009765 313 EKLVEKKEYLQE 324
Cdd:PRK02224 426 EREAELEATLRT 437
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
87-352 |
7.99e-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: 38.78 E-value: 7.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 87 REEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKkcqQQMAEDKASVKAQVT------SLLGELQESQSRL 160
Cdd:COG3096 353 QEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLK---SQLADYQQALDVQQTraiqyqQAVQALEKARALC 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 161 EAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRM----ERQAASEEKRKLAQlQAAYHQ 236
Cdd:COG3096 430 GLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIagevERSQAWQTARELLR-RYRSQQ 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 237 LFQDYDSHIKsskgMQLEDLRQQLQQAEEAlvakQELIDKLKEEAEQHKIVMETVPVLKAQADIykadfqaerhAREKLV 316
Cdd:COG3096 509 ALAQRLQQLR----AQLAELEQRLRQQQNA----ERLLEEFCQRIGQQLDAAEELEELLAELEA----------QLEELE 570
|
250 260 270
....*....|....*....|....*....|....*.
gi 569009765 317 EKKEYLQEQLEQLQREFNKLKvgchesARIEDMRKR 352
Cdd:COG3096 571 EQAAEAVEQRSELRQQLEQLR------ARIKELAAR 600
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
113-338 |
8.69e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 38.40 E-value: 8.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 113 DLRSQREQALKELEQLKKCQQQMAEDKASVKAQVtSLLGELQES---------QSRLEAATKDRQALEGRIRAVSEQ--- 180
Cdd:PRK04863 841 QLNRRRVELERALADHESQEQQQRSQLEQAKEGL-SALNRLLPRlnlladetlADRVEEIREQLDEAEEAKRFVQQHgna 919
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 181 VRQLESEREVLQQQHSvQVDQLRMQNQSVEAALRMERQAAseekRKLAQL-QAAYHQLFQDYDSHIKSSKGMQlEDLRQQ 259
Cdd:PRK04863 920 LAQLEPIVSVLQSDPE-QFEQLKQDYQQAQQTQRDAKQQA----FALTEVvQRRAHFSYEDAAEMLAKNSDLN-EKLRQR 993
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569009765 260 LQQAEEALvakqeliDKLKEEAEQHkivmetvpvlKAQADIYKADFQAERHAREKlvekkeyLQEQLEQLQREFNKLKV 338
Cdd:PRK04863 994 LEQAEQER-------TRAREQLRQA----------QAQLAQYNQVLASLKSSYDA-------KRQMLQELKQELQDLGV 1048
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
247-354 |
8.74e-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: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 247 SSKGMQLEDLRQQLQQAE---EALVAKQ-----ELIDKLKEEAEQhkivmetvpvLKAQADIYKADFQAERHAREKLVEK 318
Cdd:COG0542 407 DSKPEELDELERRLEQLEiekEALKKEQdeasfERLAELRDELAE----------LEEELEALKARWEAEKELIEEIQEL 476
|
90 100 110
....*....|....*....|....*....|....*.
gi 569009765 319 KEYLQEQLEQLQREFNKLKVGCHESARIEDMRKRHV 354
Cdd:COG0542 477 KEELEQRYGKIPELEKELAELEEELAELAPLLREEV 512
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
96-337 |
9.50e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.12 E-value: 9.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 96 KFQEARKLVERLSLEKLDLRSQREQALKELEQLKKcqqqMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIR 175
Cdd:PRK03918 201 ELEEVLREINEISSELPELREELEKLEKEVKELEE----LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 176 AVSEQVRQLESEREVLQQQhsvqvdqlrmqnqsveAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKsskgmQLED 255
Cdd:PRK03918 277 ELEEKVKELKELKEKAEEY----------------IKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-----ELEE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009765 256 LRQQLQQAEEALVAKQELIDKLKEEAEQHkivmETVPVLKAQADIYKADFQAErhAREKLVEKKEYLQEQLEQLQREFNK 335
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLEELEERHELY----EEAKAKKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIEEEISK 409
|
..
gi 569009765 336 LK 337
Cdd:PRK03918 410 IT 411
|
|
| |
