|
Name |
Accession |
Description |
Interval |
E-value |
| UBAN |
cd09803 |
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ... |
257-343 |
4.54e-25 |
|
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) is a regulatory subunit of the kinase complex IKK, which is involved in the activation of NF-kappaB via phosporylation of inhibitory IkappaBs. This mechanism requires the binding of NEMO to ubiquinated substrates. Binding is achieved via the UBAN motif (ubiquitin binding in ABIN and NEMO), which is described in this model. This region of NEMO has also been named CoZi (for coiled-coil 2 and leucine zipper). ABINs (A20-binding inhibitors of NF-kappaB) are sensors for ubiquitin that are involved in regulation of apoptosis, ABIN-1 is presumed to inhibit signalling via the NF-kappaB route. The UBAN motif is also found in optineurin, the product of a gene associated with glaucoma, which has been characterized as a negative regulator of NF-kappaB as well.
Pssm-ID: 197361 [Multi-domain] Cd Length: 87 Bit Score: 97.81 E-value: 4.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 257 MQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQ 336
Cdd:cd09803 1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80
|
....*..
gi 569009763 337 REFNKLK 343
Cdd:cd09803 81 RENQELK 87
|
|
| CC2-LZ |
pfam16516 |
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ... |
258-343 |
3.82e-22 |
|
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a leucine-zipper domain associated with the CC2 coiled-coil region of NF-kappa-B essential modulator, NEMO. It plays a regulatory role, along with the very C-terminal zinc-finger; it contains a ubiquitin-binding domain (UBD) and represents one region that contributes to NEMO oligomerization. NEMO itself is an integral part of the IkappaB kinase complex and serves as a molecular switch via which the NF-kappaB signalling pathway is regulated.
Pssm-ID: 465155 [Multi-domain] Cd Length: 100 Bit Score: 90.43 E-value: 3.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 258 QLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQR 337
Cdd:pfam16516 15 EIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEYLQR 94
|
....*.
gi 569009763 338 EFNKLK 343
Cdd:pfam16516 95 QNQQLK 100
|
|
| NEMO |
pfam11577 |
NF-kappa-B essential modulator NEMO; NEMO is a regulatory protein which is part of the IKK ... |
50-116 |
5.21e-16 |
|
NF-kappa-B essential modulator NEMO; NEMO is a regulatory protein which is part of the IKK complex along with the catalytic IKKalpha and beta kinases. The IKK complex phosphorylates IkappaB targeting it for degradation which results in the release of NF-kappaB which initiates the inflammatory response, cell proliferation or cell differentiation. NEMO activates the IKK complex's activity by associating with the unphosphorylated IKK kinase C termini.The core domain of NEMO is a dimer which binds to two fragments of IKK.
Pssm-ID: 431942 [Multi-domain] Cd Length: 67 Bit Score: 72.13 E-value: 5.21e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569009763 50 EQGTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLE 116
Cdd:pfam11577 1 DEETLEQMKELLTENHQLKEAMKQSNQAMKERCEELSAWQEKQKEEREFLECRFREARELLRRLSLE 67
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
93-344 |
3.77e-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: 71.63 E-value: 3.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 93 REEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKD 172
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 173 RQALEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIK 252
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEA----QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 253 SSKGM--QLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPV----LKAQADIYKADFQAERHAREKLVEKKE 326
Cdd:TIGR02168 839 RLEDLeeQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEalalLRSELEELSEELRELESKRSELRRELE 918
|
250
....*....|....*...
gi 569009763 327 YLQEQLEQLQREFNKLKV 344
Cdd:TIGR02168 919 ELREKLAQLELRLEGLEV 936
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
65-343 |
2.13e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 65 QELRDAIRQsnqmlRERCEELLHFQVSQREEKEFLMcKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKCQQQMAED 144
Cdd:COG1196 216 RELKEELKE-----LEAELLLLKLRELEAELEELEA-ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 145 KASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRMQNQSVEAALRMERQ 224
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE----ELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 225 AASEEKRKLAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETvpvLKAQA 304
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALR-----AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE---LEEEE 437
|
250 260 270
....*....|....*....|....*....|....*....
gi 569009763 305 DIYKADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLK 343
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
61-336 |
3.43e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 3.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 61 LEENQELRDAIRQSNQM--LRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKCQ 138
Cdd:COG1196 218 LKEELKELEAELLLLKLreLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 139 QQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAA 218
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 219 LR----------MERQAASEEKRKLAQLQAAYHQLFQDyDSHIKSSKGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAE 288
Cdd:COG1196 378 EEeleelaeellEALRAAAELAAQLEELEEAEEALLER-LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 569009763 289 QHKIVMETVPVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQ 336
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
122-338 |
3.74e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 67.48 E-value: 3.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 122 SQREQALKELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQH 201
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 202 SVQVDQLRMQnqsVEAALRMERQA------ASEEKRKLAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVA 275
Cdd:COG4942 100 EAQKEELAEL---LRALYRLGRQPplalllSPEDFLDAVRRLQYLKYLAPARREQAE-----ELRADLAELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569009763 276 KQELIDKLKEEAEQHKIVMETVPVLKAQA-DIYKADFQAERHAREKLVEKKEYLQEQLEQLQRE 338
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLlARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| zf_C2H2_10 |
pfam18414 |
C2H2 type zinc-finger; This is a zinc finger domain C2H2 which can be found in optineurin ... |
392-417 |
1.02e-11 |
|
C2H2 type zinc-finger; This is a zinc finger domain C2H2 which can be found in optineurin (optic neuropathy inducing protein) and NF-kappa-B essential modulator (NEMO) furthermore, it can be found in kinase TBK1, a member of the IKK (inhibitor of nuclear factor kappa-B kinase) family. The C-terminal region, which carries the zinc finger domain, constitutes the regulatory domain of NEMO, as it receives the activation signal from upstream molecules, and subsequently transmits this activation to the kinases bound to the N-terminal domain. The isolated NEMO zinc finger is thought to be involved in protein-protein rather than protein-DNA interaction.
Pssm-ID: 436483 Cd Length: 26 Bit Score: 59.14 E-value: 1.02e-11
10 20
....*....|....*....|....*.
gi 569009763 392 PDFCCPKCQYQAPDMDTLQIHVMECI 417
Cdd:pfam18414 1 PKHCCPKCQEQLPDIDTLQIHVMDCI 26
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
55-289 |
7.81e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 7.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 55 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQL 134
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 135 KKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQ---QHSVQVDQLRMQ 211
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLErleRLEEELEELEEA 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569009763 212 NQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQ 289
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA--LLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
123-381 |
4.06e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 4.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 123 QREQALKELEQlkkCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQ--- 199
Cdd:TIGR02168 674 ERRREIEELEE---KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEEria 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 200 QHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQEL 279
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE-----ALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 280 IDKLKEEAEQHKIVMEtvpVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLKVGCHE--------SAR 351
Cdd:TIGR02168 826 LESLERRIAATERRLE---DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALlrseleelSEE 902
|
250 260 270
....*....|....*....|....*....|
gi 569009763 352 IEDMRKRHVETPQPPLLPAPAHHSFHLALS 381
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKLAQLELRLE 932
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
55-343 |
4.76e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.54 E-value: 4.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 55 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFlmcKFQEarklverLSLEKLDLRSQREQALKELEQL 134
Cdd:TIGR02169 180 EEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREY---EGYE-------LLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 135 KKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATkdrqalEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLR-MQNQ 213
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG------EEEQLRVKEKIGELEAEIASLERSIAEKERELEdAEER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 214 SVEAALRMERQAASEE--KRKLAQLQAAYHQLFQDYDShikssKGMQLEDLRQQLQQAE-------EALVAKQELIDKLK 284
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEelEREIEEERKRRDKLTEEYAE-----LKEELEDLRAELEEVDkefaetrDELKDYREKLEKLK 398
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569009763 285 EEAEQHKIVMETVPVLKAQADIYKADFQAERHARE----KLVEKKEYLQEQLEQLQREFNKLK 343
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEakinELEEEKEDKALEIKKQEWKLEQLA 461
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
160-341 |
7.33e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 7.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 160 QESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSV--QVDQLRMQNQSVEAA------LRMERQAASEEKR 231
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAlqRLAEYSWDEIDVASAereiaeLEAELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 232 KLAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADF 311
Cdd:COG4913 686 DLAALEEQLEELEAELEELEE-----ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALG 760
|
170 180 190
....*....|....*....|....*....|....*...
gi 569009763 312 QAER--------HAREKLVEKKEYLQEQLEQLQREFNK 341
Cdd:COG4913 761 DAVErelrenleERIDALRARLNRAEEELERAMRAFNR 798
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
54-342 |
8.49e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 8.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 54 PETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQ 133
Cdd:TIGR02168 721 LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 134 LKkcqqqmaEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLrmqnq 213
Cdd:TIGR02168 801 LR-------EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI----- 868
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 214 sveAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIK--SSKGMQLEDLRQQLQQAEEALVAKQE----LIDKLKEE- 286
Cdd:TIGR02168 869 ---EELESELEALLNERASLEEALALLRSELEELSEELRelESKRSELRRELEELREKLAQLELRLEglevRIDNLQERl 945
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 569009763 287 AEQHKIVMETVPVLKaqadiykadfqaerharEKLVEKKEYLQEQLEQLQREFNKL 342
Cdd:TIGR02168 946 SEEYSLTLEEAEALE-----------------NKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
55-344 |
9.18e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 9.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 55 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALK----- 129
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERqleel 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 130 --ELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQhsvqvdq 207
Cdd:TIGR02168 322 eaQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ------- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 208 lrmqnqsvEAALRMERQAASEEKRklaqlqaayhqlfqdydshiksskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEA 287
Cdd:TIGR02168 395 --------IASLNNEIERLEARLE--------------------------RLEDRRERLQQEIEELLKKLEEAELKELQA 440
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 569009763 288 EQHKIVMETVPVLKAQADIYkadfQAERHAREKLVEKKEYLQEQLEQLQREFNKLKV 344
Cdd:TIGR02168 441 ELEELEEELEELQEELERLE----EALEELREELEEAEQALDAAERELAQLQARLDS 493
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
107-343 |
9.69e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 9.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 107 RKLVERLSLEKLDLRSQREQALKELEQLKKCQQQMAEDKASVKAqvtslLGELQESQSRLEAATKDRQALEGRIRAVSEQ 186
Cdd:COG4913 210 DDFVREYMLEEPDTFEAADALVEHFDDLERAHEALEDAREQIEL-----LEPIRELAERYAAARERLAELEYLRAALRLW 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 187 VRQLesEREVLQQqhsvQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAyhqlfqdydshIKSSKGMQLEDLRQQL 266
Cdd:COG4913 285 FAQR--RLELLEA----ELEELRAELARLEAELERLEARLDALREELDELEAQ-----------IRGNGGDRLEQLEREI 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 267 QQAEEALVAKQELIDKLKEEAEQ--------HKIVMETVPVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQRE 338
Cdd:COG4913 348 ERLERELEERERRRARLEALLAAlglplpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
....*
gi 569009763 339 FNKLK 343
Cdd:COG4913 428 IASLE 432
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
95-343 |
1.10e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 95 EKEFLMCKFQEARKLVERLSLEKLDLRSQREQALkelEQLKKCQQQMAEdkasVKAQVTSLLGELQESQSRLEAATKDRQ 174
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELT---AELQELEEKLEE----LRLEVSELEEEIEELQKELYALANEIS 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 175 ALEGRIRAVSEQVRQLESEREVLQQQH-----------------SVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQ 237
Cdd:TIGR02168 299 RLEQQKQILRERLANLERQLEELEAQLeeleskldelaeelaelEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 238 AAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAE--R 315
Cdd:TIGR02168 379 EQLETLRSKVAQLEL-----QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEelQ 453
|
250 260
....*....|....*....|....*...
gi 569009763 316 HAREKLVEKKEYLQEQLEQLQREFNKLK 343
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAE 481
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
76-358 |
2.37e-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: 56.23 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 76 QMLRERCEEL---LHFQVSQREEKEFLM----CKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKCQQQMAEDKASV 148
Cdd:TIGR02169 677 QRLRERLEGLkreLSSLQSELRRIENRLdelsQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 149 KAQVTSLLGELQESQSRLEAATKDRQALEGRIRavSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASE 228
Cdd:TIGR02169 757 KSELKELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 229 EKRKLAQLQAAYHQlfqdydshiKSSKGMQLEDLRQQL----QQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQA 304
Cdd:TIGR02169 835 IQELQEQRIDLKEQ---------IKSIEKEIENLNGKKeeleEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI 905
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 569009763 305 DIYKADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLKVGCHESARIEDMRKR 358
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAE 959
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
61-282 |
2.87e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.79 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 61 LEENQELR-DAIRQSNQMLRERCEELLHfQVSQREEKeflMCKFQEARKLV-----ERLSLEKL-DLRSQREQALKELEQ 133
Cdd:COG3206 162 LEQNLELRrEEARKALEFLEEQLPELRK-ELEEAEAA---LEEFRQKNGLVdlseeAKLLLQQLsELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 134 LKKCQQQMAEDKASVKAQVTSLLG--ELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQ 211
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILAS 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569009763 212 -------NQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDshIKSSKGMQLEDLRQQLQQAEEALVAKQELIDK 282
Cdd:COG3206 318 leaeleaLQAREASLQAQLAQLEARLAELPELEAELRRLEREVE--VARELYESLLQRLEEARLAEALTVGNVRVIDP 393
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
120-338 |
3.56e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 120 LRSQREQALKELE------------------QLKKCQQQ--MAEDKASVKA-----QVTSLLGELQESQSRLEAATKDRQ 174
Cdd:COG1196 170 YKERKEEAERKLEateenlerledilgelerQLEPLERQaeKAERYRELKEelkelEAELLLLKLRELEAELEELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 175 ALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSV----------EAALRMERQAASEEKRKLAQLQAAYHQLF 244
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEyellaelarlEQDIARLEERRRELEERLEELEEELAELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 245 QDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQhkIVMETVPVLKAQADIYKADFQAERhAREKLVEK 324
Cdd:COG1196 330 EELEELEE-----ELEELEEELEEAEEELEEAEAELAEAEEALLE--AEAELAEAEEELEELAEELLEALR-AAAELAAQ 401
|
250
....*....|....
gi 569009763 325 KEYLQEQLEQLQRE 338
Cdd:COG1196 402 LEELEEAEEALLER 415
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
104-278 |
3.91e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 3.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 104 QEARKLVERLSLEKLDLRSQREQALKELEQLKKCQQQMAEDK---------ASVKAQVTSLL---GELQESQSRLEAATK 171
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvasaereiAELEAELERLDassDDLAALEEQLEELEA 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 172 DRQALEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDShi 251
Cdd:COG4913 700 ELEELEEELDELKGEIGRLEKELEQAEE----ELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEE-- 773
|
170 180
....*....|....*....|....*..
gi 569009763 252 ksskgmQLEDLRQQLQQAEEALVAKQE 278
Cdd:COG4913 774 ------RIDALRARLNRAEEELERAMR 794
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
94-356 |
4.96e-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: 4.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 94 EEKEFLMCKFQEARKLVERLSL---EKLD----LRSQREQALKELEQLKKCQ-----------QQMAEDKASVKAQVTSL 155
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLiidEKRQqlerLRREREKAERYQALLKEKReyegyellkekEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 156 LGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVlqqqhsvqvdQLRMQNQSVEAALRMERQAASEEKRKLAQ 235
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL----------RVKEKIGELEAEIASLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 236 LQAAYHQLFQDYDShiksskgmqledLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETvpvLKAQADIYKADFQAER 315
Cdd:TIGR02169 320 AEERLAKLEAEIDK------------LLAEIEELEREIEEERKRRDKLTEEYAELKEELED---LRAELEEVDKEFAETR 384
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 569009763 316 HAREKLVEKKEYLQEQLEQLQREFNKLKVGCHE-SARIEDMR 356
Cdd:TIGR02169 385 DELKDYREKLEKLKREINELKRELDRLQEELQRlSEELADLN 426
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
54-312 |
1.01e-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: 51.22 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 54 PETLQRCLEENQELRDAIRQSNQMLRERC----EELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREqalk 129
Cdd:TIGR02169 261 SELEKRLEEIEQLLEELNKKIKDLGEEEQlrvkEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA---- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 130 ELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVD--- 206
Cdd:TIGR02169 337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEelq 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 207 QLRMQNQSVEAALR--MERQAASEEKRKLAQ--LQAAYHQLFQDYDSHIKSSKgmQLEDLRQQLQQAEEALVAKQELIDK 282
Cdd:TIGR02169 417 RLSEELADLNAAIAgiEAKINELEEEKEDKAleIKKQEWKLEQLAADLSKYEQ--ELYDLKEEYDRVEKELSKLQRELAE 494
|
250 260 270
....*....|....*....|....*....|
gi 569009763 283 LKEEAeqhKIVMETVPVLKAQADIYKADFQ 312
Cdd:TIGR02169 495 AEAQA---RASEERVRGGRAVEEVLKASIQ 521
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
126-338 |
5.88e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 126 QALKELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESErevLQQQHSVQV 205
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE---IEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 206 DQLRMQNQSVEAALRMERQAASEEKRKLAQlQAAYHQLFQDYDSHIKSskgmQLEDLRQQLQQAEEALVAKQELIDKLKE 285
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLLGSESFSDFLD-RLSALSKIADADADLLE----ELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 569009763 286 EAEQHKIVMETvpvLKAQADIYKADFQAErhaREKLVEKKEYLQEQLEQLQRE 338
Cdd:COG3883 165 ELEAAKAELEA---QQAEQEALLAQLSAE---EAAAEAQLAELEAELAAAEAA 211
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
55-361 |
7.64e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 7.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 55 ETLQRCLEENQELRDAirqsnqmlrERCEEllhfqVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQL 134
Cdd:PRK02224 436 RTARERVEEAEALLEA---------GKCPE-----CGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERA 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 135 KkcqqqmaedkasvkaqvtsllgELQESQSRLEAATKDRQALEGRIravSEQVRQLESEREVLQQQHSvQVDQLRMQNQS 214
Cdd:PRK02224 502 E----------------------DLVEAEDRIERLEERREDLEELI---AERRETIEEKRERAEELRE-RAAELEAEAEE 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 215 VEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDShiksskgmqLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVM 294
Cdd:PRK02224 556 KREAAAEAEEEAEEAREEVAELNSKLAELKERIES---------LERIRTLLAAIADAEDEIERLREKREALAELNDERR 626
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569009763 295 ETVPVLKAQADIYKADFQAER--HAREKLVEKKEYLQ---EQLEQLQREFNKL--KVGCHESA--RIEDMRKRHVE 361
Cdd:PRK02224 627 ERLAEKRERKRELEAEFDEARieEAREDKERAEEYLEqveEKLDELREERDDLqaEIGAVENEleELEELRERREA 702
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
139-239 |
1.73e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 47.25 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 139 QQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQ--NQSVE 216
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKrkEITDQ 224
|
90 100
....*....|....*....|....*
gi 569009763 217 AALRMErqAASEEKRKL--AQLQAA 239
Cdd:PRK11448 225 AAKRLE--LSEEETRILidQQLRKA 247
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
65-361 |
2.42e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 65 QELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVErlSLEKLDLRSQREQALKELEQLKKCQQQMAED 144
Cdd:PTZ00121 1428 EEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE--AKKKAEEAKKADEAKKKAEEAKKKADEAKKA 1505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 145 KASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQ 224
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEE 1585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 225 AASEEKRKLAQLQAAYH--------QLFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMET 296
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYEeekkmkaeEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569009763 297 VPvLKAQADIYKAD----FQAERHAREKLVEKKEYLQEQLEQLQREFNKLKVGCHESARIEDMRKRHVE 361
Cdd:PTZ00121 1666 EA-KKAEEDKKKAEeakkAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAE 1733
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
57-359 |
2.71e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 57 LQRCLEENQELRDAIRQsnqmLRERCEELlhfqvsqREEKEFLMCKFQEARKLVE--RLSLEKLD-----LRSQREQALK 129
Cdd:PRK02224 337 AQAHNEEAESLREDADD----LEERAEEL-------REEAAELESELEEAREAVEdrREEIEELEeeieeLRERFGDAPV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 130 ELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDR---------QALEG-----RIRAVSEQVRQLESERE 195
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLeagkcpecgQPVEGsphveTIEEDRERVEELEAELE 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 196 VLQQQHSVQVDQLRMQNQSVEAALRMERqaaSEEKRKLAQlqaayhQLFQDYDSHIKsSKGMQLEDLRQQLQQAEEALVA 275
Cdd:PRK02224 486 DLEEEVEEVEERLERAEDLVEAEDRIER---LEERREDLE------ELIAERRETIE-EKRERAEELRERAAELEAEAEE 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 276 KQELIDKLKEEAEQHKIV-----------------METVPVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLqRE 338
Cdd:PRK02224 556 KREAAAEAEEEAEEAREEvaelnsklaelkeriesLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEK-RE 634
|
330 340
....*....|....*....|.
gi 569009763 339 FNKLKVGCHESARIEDMRKRH 359
Cdd:PRK02224 635 RKRELEAEFDEARIEEAREDK 655
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
222-337 |
4.33e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 222 ERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMEtvpvlk 301
Cdd:PRK12704 48 KKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRN-ELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELE------ 120
|
90 100 110
....*....|....*....|....*....|....*.
gi 569009763 302 aqadiykadfQAERHAREKLVEKKEYLQEQLEQLQR 337
Cdd:PRK12704 121 ----------QKQQELEKKEEELEELIEEQLQELER 146
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
51-228 |
4.53e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.82 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 51 QGTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKE 130
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 131 LEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAAtkDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRM 210
Cdd:TIGR02168 395 IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
170
....*....|....*...
gi 569009763 211 QNQSVEAALRMERQAASE 228
Cdd:TIGR02168 473 AEQALDAAERELAQLQAR 490
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
27-289 |
6.29e-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: 45.43 E-value: 6.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 27 AEDQDMLGEESSLGKPAMLHLPSEQGTPETLQRCLEEN----QELRDAIRQSN---QMLRERCEELLHFQVSQREEKEFL 99
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALrealDELRAELTLLNeeaANLRERLESLERRIAATERRLEDL 843
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 100 MCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGR 179
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 180 IRAVSEQVRQLESEREVLQQQHSVQVdQLRMQNQSVEAALRMERQAASEekRKLAQLQAAYHQL----------FQDYDS 249
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQERLSEEY-SLTLEEAEALENKIEDDEEEAR--RRLKRLENKIKELgpvnlaaieeYEELKE 1000
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 569009763 250 hiksskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQ 289
Cdd:TIGR02168 1001 --------RYDFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
107-356 |
7.63e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 7.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 107 RKLVERLslekLDLR--SQREQALKEL-----EQLKKCQQQMAEDKASVKAQvtsllgelQESQSRLEAATKDRQAlegR 179
Cdd:PHA02562 153 RKLVEDL----LDISvlSEMDKLNKDKirelnQQIQTLDMKIDHIQQQIKTY--------NKNIEEQRKKNGENIA---R 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 180 IRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAyHQLFQDYD------SHIKS 253
Cdd:PHA02562 218 KQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKV-IKMYEKGGvcptctQQISE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 254 SKGMqLEDLRQQLQQAEEALVAKQELIDKLKEEAeqHKIVMETVPVLKAQADIYKADFQAERHAREKLVEKKEYLQ---- 329
Cdd:PHA02562 297 GPDR-ITKIKDKLKELQHSLEKLDTAIDELEEIM--DEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEElqae 373
|
250 260 270
....*....|....*....|....*....|..
gi 569009763 330 -----EQLEQLQREFNKLKVGCHESARIEDMR 356
Cdd:PHA02562 374 fvdnaEELAKLQDELDKIVKTKSELVKEKYHR 405
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
109-296 |
1.10e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 109 LVERLSLEKLDL-RSQREQALKELEQLKKCQQQMAEdKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQV 187
Cdd:COG4717 47 LLERLEKEADELfKPQGRKPELNLKELKELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 188 RQLESEREVLQQQHSV-----QVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGmQLEDL 262
Cdd:COG4717 126 QLLPLYQELEALEAELaelpeRLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE-ELEEL 204
|
170 180 190
....*....|....*....|....*....|....
gi 569009763 263 RQQLQQAEEALVAKQELIDKLKEEAEQHKIVMET 296
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
47-343 |
1.63e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.79 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 47 LPSEQGTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEflmckfQEARKLVERLSLEKldLRSQREQ 126
Cdd:COG5185 245 LEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTK------EKIAEYTKSIDIKK--ATESLEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 127 ALKELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEG--RIRAVSEQVR----QLESEREVLQQQ 200
Cdd:COG5185 317 QLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGevELSKSSEELDsfkdTIESTKESLDEI 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 201 HSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKS-SKGMQLEDLRQQLQQAEEALVAKQEL 279
Cdd:COG5185 397 PQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISElNKVMREADEESQSRLEEAYDEINRSV 476
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569009763 280 IDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLK 343
Cdd:COG5185 477 RSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILA 540
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
65-362 |
1.73e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 65 QELRDAIRQSNQMLRE-RCEEllhfqVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKK------- 136
Cdd:PRK02224 436 RTARERVEEAEALLEAgKCPE-----CGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDlveaedr 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 137 ----------CQQQMAEDKASVKA---QVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESER----EVLQQ 199
Cdd:PRK02224 511 ierleerredLEELIAERRETIEEkreRAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLaelkERIES 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 200 QHSVQVDQLRMQNQSVEAALRMERQAA-----SEEKRKLAQLQAAYHQLFQDYDshiksskGMQLEDLRQQLQQAEEALv 274
Cdd:PRK02224 591 LERIRTLLAAIADAEDEIERLREKREAlaelnDERRERLAEKRERKRELEAEFD-------EARIEEAREDKERAEEYL- 662
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 275 akQELIDKLKEEAEQHKIVMETVPVLKAQADIYKaDFQAERHAREKLVEKKEYLQEQLEQLQREFNKLKVgchesarieD 354
Cdd:PRK02224 663 --EQVEEKLDELREERDDLQAEIGAVENELEELE-ELRERREALENRVEALEALYDEAEELESMYGDLRA---------E 730
|
....*...
gi 569009763 355 MRKRHVET 362
Cdd:PRK02224 731 LRQRNVET 738
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
55-351 |
1.95e-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: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 55 ETLQRCLEENQELRDAIRQSNQMLRErceelLHFQVSQREEkeflmcKFQEARKLVERLSLEKLDLRSQREQALKELEQL 134
Cdd:COG4913 664 ASAEREIAELEAELERLDASSDDLAA-----LEEQLEELEA------ELEELEEELDELKGEIGRLEKELEQAEEELDEL 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 135 KKCQQQMAEDkasVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHsVQVDQLRMQNQS 214
Cdd:COG4913 733 QDRLEAAEDL---ARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAF-NREWPAETADLD 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 215 VEAAlrmerqAASEEKRKLAQLQA----AYHQLFQDYdshIKSSKGMQLEDLRQQLQQAEEALvakQELIDKLKEEAEQH 290
Cdd:COG4913 809 ADLE------SLPEYLALLDRLEEdglpEYEERFKEL---LNENSIEFVADLLSKLRRAIREI---KERIDPLNDSLKRI 876
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569009763 291 K------IVMETVPVLKAQADIYKADFQAERHAREKLVEkkEYLQEQLEQLQREFNKLKVGCHESAR 351
Cdd:COG4913 877 PfgpgryLRLEARPRPDPEVREFRQELRAVTSGASLFDE--ELSEARFAALKRLIERLRSEEEESDR 941
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
144-342 |
3.54e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.75 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 144 DKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLES------EREVLQQQHSV--QVDQLRMQNQSV 215
Cdd:COG0497 152 GLEELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAaalqpgEEEELEEERRRlsNAEKLREALQEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 216 EAALRMERQAAseekrkLAQLQAAYHQL--FQDYDSHIKSSKGM------QLEDLRQQLQQA-------EEALVAKQELI 280
Cdd:COG0497 232 LEALSGGEGGA------LDLLGQALRALerLAEYDPSLAELAERlesaliELEEAASELRRYldslefdPERLEEVEERL 305
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569009763 281 DKLKEEAEQHKIVMETVPVLKAQAdiykadfQAERHAREKLVEKKEYLQEQLEQLQREFNKL 342
Cdd:COG0497 306 ALLRRLARKYGVTVEELLAYAEEL-------RAELAELENSDERLEELEAELAEAEAELLEA 360
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
126-295 |
4.02e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.37 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 126 QALKELEQLKKCQQQMAEDKASVKAQV---TSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHS 202
Cdd:PRK11637 41 HASDNRDQLKSIQQDIAAKEKSVRQQQqqrASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 203 VQVDQLRMQnqsVEAALRMERQAA------SEEKRKLAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAK 276
Cdd:PRK11637 121 AQERLLAAQ---LDAAFRQGEHTGlqlilsGEESQRGERILAYFGYLNQARQETIA-----ELKQTREELAAQKAELEEK 192
|
170
....*....|....*....
gi 569009763 277 QELIDKLKEEAEQHKIVME 295
Cdd:PRK11637 193 QSQQKTLLYEQQAQQQKLE 211
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
58-355 |
4.99e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.65 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 58 QRCLEENQELRDAIRQSNQMLRERCEELLhfQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKC 137
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRAKLLMKRAAHVK--QQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 138 QQQMAEDKASVKAqVTSLLGELQESQSRLEAATKDRQALEGRIrAVSEQVRQLESEREVLQQQHSVQVDQLRMQNqsvEA 217
Cdd:TIGR00618 385 QQQKTTLTQKLQS-LCKELDILQREQATIDTRTSAFRDLQGQL-AHAKKQQELQQRYAELCAAAITCTAQCEKLE---KI 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 218 ALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGMQLED--LRQQLQQAEEALV------AKQELIDKLKEEAEQ 289
Cdd:TIGR00618 460 HLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPcpLCGSCIHPNPARQdidnpgPLTRRMQRGEQTYAQ 539
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 290 HKIVMETV----PVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLKVGCHESARIEDM 355
Cdd:TIGR00618 540 LETSEEDVyhqlTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDM 609
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
61-209 |
6.99e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 6.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 61 LEENQELRDAIR-----QSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLD--------LRSQREQA 127
Cdd:COG4913 271 LAELEYLRAALRlwfaqRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdrleqLEREIERL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 128 LKELEQLKKCQQQMAE-----------DKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREV 196
Cdd:COG4913 351 ERELEERERRRARLEAllaalglplpaSAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
170
....*....|....*.
gi 569009763 197 LQQQHSV---QVDQLR 209
Cdd:COG4913 431 LERRKSNipaRLLALR 446
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
145-292 |
8.96e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.10 E-value: 8.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 145 KASVKAQVTSLLGELQESQSrLEAATKdrQALEGRIRAVSEQVRQLESEREVLQQQH---SVQVDQLRMQNQSVEAALRM 221
Cdd:PRK09039 51 KDSALDRLNSQIAELADLLS-LERQGN--QDLQDSVANLRASLSAAEAERSRLQALLaelAGAGAAAEGRAGELAQELDS 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569009763 222 ERQAASEEKRKLAQLQAayhqlfqdydshiksskgmQLEDLRQQLQQAEEALVAKQElidklKEEAEQHKI 292
Cdd:PRK09039 128 EKQVSARALAQVELLNQ-------------------QIAALRRQLAALEAALDASEK-----RDRESQAKI 174
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
57-343 |
1.13e-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: 41.21 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 57 LQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKldlrSQREQALKELEqlkk 136
Cdd:TIGR02169 714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL----HKLEEALNDLE---- 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 137 cqqqmAEDKASVKAQVTSLLGELQESQSRLEAATkdrQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVE 216
Cdd:TIGR02169 786 -----ARLSHSRIPEIQAELSKLEEEVSRIEARL---REIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 217 AALRMERQAASEEKRK---LAQLQAAYHQLFQDYDSHIKSSKGMQ---------LEDLRQQLQQAEEALVAKQELIDKLK 284
Cdd:TIGR02169 858 NLNGKKEELEEELEELeaaLRDLESRLGDLKKERDELEAQLRELErkieeleaqIEKKRKRLSELKAKLEALEEELSEIE 937
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569009763 285 EEAEQHKIVMETVPVL--------KAQADIYK---------ADFQAERHAREKLVEKKEYLQEQLEQLQR---EFNKLK 343
Cdd:TIGR02169 938 DPKGEDEEIPEEELSLedvqaelqRVEEEIRAlepvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILErieEYEKKK 1016
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
55-234 |
1.35e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 55 ETLQRCLEENQELRDAIRQSNQMLRERCEELL--HFQVSQREEKEFLMcKFQEARKLVERLSLEKLDLRSQREQAlKELE 132
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQKEELAELLraLYRLGRQPPLALLL-SPEDFLDAVRRLQYLKYLAPARREQA-EELR 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 133 QLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQA----LEGRIRAVSEQVRQLESEREVLQQQHSvqvdql 208
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKllarLEKELAELAAELAELQQEAEELEALIA------ 230
|
170 180
....*....|....*....|....*.
gi 569009763 209 RMQNQSVEAALRMERQAASEEKRKLA 234
Cdd:COG4942 231 RLEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
31-336 |
1.57e-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: 40.98 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 31 DMLGEESSLGKPAMLHLPSEQGTPETLQRCLEENQELRDAIRQS-NQMLRERCEELLHFQVSQREEKEFLMCKFQEARKL 109
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAElNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 110 VERLSLEKLDLRSQR-EQALKELEQLKKCQQQMAEDKASVKAQVTSLlGELQESQSRLEAATKDRQAL------EGRIRA 182
Cdd:pfam12128 324 LEALEDQHGAFLDADiETAAADQEQLPSWQSELENLEERLKALTGKH-QDVTAKYNRRRSKIKEQNNRdiagikDKLAKI 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 183 VSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAyhqlfqdydshiksskgmqlEDL 262
Cdd:pfam12128 403 REARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATAT--------------------PEL 462
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569009763 263 RQQLQQaeealvaKQELIDKLKEEAEQhkivmETVPVLKAQADIYKADFQAERhAREKLVEKKEYLQEQLEQLQ 336
Cdd:pfam12128 463 LLQLEN-------FDERIERAREEQEA-----ANAEVERLQSELRQARKRRDQ-ASEALRQASRRLEERQSALD 523
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
112-358 |
1.81e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 112 RLSLEKLDLRSQREQALKELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRL---EAATKDRQALEGRIRAVSEQVR 188
Cdd:PRK04863 283 VHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLnlvQTALRQQEKIERYQADLEELEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 189 QLESEREVLQQQHSVQ-------------VDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAyHQLFQDYDSHIKSSK 255
Cdd:PRK04863 363 RLEEQNEVVEEADEQQeenearaeaaeeeVDELKSQLADYQQALDVQQTRAIQYQQAVQALERA-KQLCGLPDLTADNAE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 256 GMqLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVpvLKAQADIYKADfqAERHAREKL--VEKKEYLQEQLE 333
Cdd:PRK04863 442 DW-LEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLV--RKIAGEVSRSE--AWDVARELLrrLREQRHLAEQLQ 516
|
250 260
....*....|....*....|....*
gi 569009763 334 QLQREFNKLKVGCHESARIEDMRKR 358
Cdd:PRK04863 517 QLRMRLSELEQRLRQQQRAERLLAE 541
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
91-275 |
1.84e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 91 SQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKCQQ--QMAEDKASVKAQVTSLLGELQESQSRLEA 168
Cdd:COG4717 78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEERLEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 169 ATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLfqdyd 248
Cdd:COG4717 158 LRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL----- 232
|
170 180
....*....|....*....|....*..
gi 569009763 249 shiksSKGMQLEDLRQQLQQAEEALVA 275
Cdd:COG4717 233 -----ENELEAAALEERLKEARLLLLI 254
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
55-344 |
1.84e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.83 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 55 ETLQRCLEENQELRDAIRQSNQMlreRCEELLHFQVSQREEKEF------LMCKFQEARKLVERLSLEKLDlrSQREQAL 128
Cdd:COG5022 800 QPLLSLLGSRKEYRSYLACIIKL---QKTIKREKKLRETEEVEFslkaevLIQKFGRSLKAKKRFSLLKKE--TIYLQSA 874
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 129 KELEQLKKCQQQMAEDKASVKaqvtsllgELQESQSRLEAatkdrQALEgriraVSEQVRQLESEREVLQQQHSVQVDQL 208
Cdd:COG5022 875 QRVELAERQLQELKIDVKSIS--------SLKLVNLELES-----EIIE-----LKKSLSSDLIENLEFKTELIARLKKL 936
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 209 RMQNQSVEAALRMERQaaSEEKRKLAQLQAAYHQLFQDYDSHIKSSKGM--QLEDLRQQLQQAEEALVAKQELIDKLKEE 286
Cdd:COG5022 937 LNNIDLEEGPSIEYVK--LPELNKLHEVESKLKETSEEYEDLLKKSTILvrEGNKANSELKNFKKELAELSKQYGALQES 1014
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 569009763 287 AEQHKIVMETVPVLKAQADIYKADfQAERHAREKLVEKKEYLQEQLEQLQREFNKLKV 344
Cdd:COG5022 1015 TKQLKELPVEVAELQSASKIISSE-STELSILKPLQKLKGLLLLENNQLQARYKALKL 1071
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
149-301 |
2.00e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.23 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 149 KAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRMQNQSVEAALRMERQAASE 228
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEA----ELEEKDERIERLERELSEARSEERR 459
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569009763 229 EKRKlaqlqaayhqlfqdyDSHIKSSKGMqLEDLRQQLQQAEEALvakQELIDKLKEEAEQHKIVM--ETVPVLK 301
Cdd:COG2433 460 EIRK---------------DREISRLDRE-IERLERELEEERERI---EELKRKLERLKELWKLEHsgELVPVKV 515
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
49-290 |
2.36e-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: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 49 SEQGTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVE-RLSLEKLDLRSQREQA 127
Cdd:TIGR00618 567 EIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDvRLHLQQCSQELALKLT 646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 128 LKELEQLKKCQQQMAEDKASVKAQ----VTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSV 203
Cdd:TIGR00618 647 ALHALQLTLTQERVREHALSIRVLpkelLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENA 726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 204 QVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSskGMQLEDLRQQLQQAEEALVAKQELIDKL 283
Cdd:TIGR00618 727 SSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQT--GAELSHLAAEIQFFNRLREEDTHLLKTL 804
|
....*..
gi 569009763 284 KEEAEQH 290
Cdd:TIGR00618 805 EAEIGQE 811
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
123-360 |
2.51e-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: 40.11 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 123 QREQALKELEQLKKCQQQMAEdkaSVKAQVTSLLGELqESQSRLEAATKDRQALEGRIRAVSEQVRQLESERE-----VL 197
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQE---RLRQEKEEKAREV-ERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERErelerIR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 198 QQQHSVQVDQLRMQNQSVEAA-------LRMERQAASEEKRKlaQLQAAYHQLFQDYDSHIKSSKGM-QLEDLRQQLQQA 269
Cdd:pfam17380 355 QEERKRELERIRQEEIAMEISrmrelerLQMERQQKNERVRQ--ELEAARKVKILEEERQRKIQQQKvEMEQIRAEQEEA 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 270 EEALVAKQElidklKEEAEQHKIVMETVPVLKAQADIYKADfQAERHAREKLVEKKEYLQEQLEQLQREFNKLKVGCHES 349
Cdd:pfam17380 433 RQREVRRLE-----EERAREMERVRLEEQERQQQVERLRQQ-EEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQ 506
|
250
....*....|.
gi 569009763 350 ARIEDMRKRHV 360
Cdd:pfam17380 507 AMIEEERKRKL 517
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
120-344 |
2.76e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.32 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 120 LRSQREQALKELEQLKKCQQQMAEDKASVKAQVtSLLGELQESQSRLEAATkdrqaLEGRIRAVSEQVRQLESEREVLQQ 199
Cdd:COG3096 841 LRQRRSELERELAQHRAQEQQLRQQLDQLKEQL-QLLNKLLPQANLLADET-----LADRLEELREELDAAQEAQAFIQQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 200 QHSV------QVDQLRMQNQSVEaALRMERQAASEEKRKLAQLQAAYHQLFQDYdSHIKSSKGMQL--------EDLRQQ 265
Cdd:COG3096 915 HGKAlaqlepLVAVLQSDPEQFE-QLQADYLQAKEQQRRLKQQIFALSEVVQRR-PHFSYEDAVGLlgensdlnEKLRAR 992
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569009763 266 LQQAEEALvakqeliDKLKEEAEQHkivmetvpvlKAQADIYKADFQAERHAREKlvekkeyLQEQLEQLQREFNKLKV 344
Cdd:COG3096 993 LEQAEEAR-------REAREQLRQA----------QAQYSQYNQVLASLKSSRDA-------KQQTLQELEQELEELGV 1047
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
160-343 |
2.90e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.04 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 160 QESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQ-----------QHSVQVDQLRMQNQSVEAALRMERQAASE 228
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERykelkaelrelELALLVLRLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 229 EKRKLAQLQAAYHQLfqdydshikSSKGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKivmETVPVLKAQADIYK 308
Cdd:TIGR02168 255 LEELTAELQELEEKL---------EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR---ERLANLERQLEELE 322
|
170 180 190
....*....|....*....|....*....|....*
gi 569009763 309 ADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLK 343
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
118-277 |
3.15e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.89 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 118 LDLRSQREQALKELEQLKKcqqqmaedkasvkaQVTSLLGELQESQSRLEAATKDRQAlEGRIRAVSEQVRQLESE-REV 196
Cdd:PRK11281 69 LALLDKIDRQKEETEQLKQ--------------QLAQAPAKLRQAQAELEALKDDNDE-ETRETLSTLSLRQLESRlAQT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 197 LQQQHSVQVDQLRMQNQSVEAALRMERqAASEEKRKLAQLQAAYHQLFQDYDShiksskGMQLEDLRQQLQQAEEALVAK 276
Cdd:PRK11281 134 LDQLQNAQNDLAEYNSQLVSLQTQPER-AQAALYANSQRLQQIRNLLKGGKVG------GKALRPSQRVLLQAEQALLNA 206
|
.
gi 569009763 277 Q 277
Cdd:PRK11281 207 Q 207
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
119-288 |
4.11e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.12 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 119 DLRSQREQALKELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQ 198
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 199 QQHSV---QVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVA 275
Cdd:COG4372 122 KERQDleqQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEE 201
|
170
....*....|...
gi 569009763 276 KQELIDKLKEEAE 288
Cdd:COG4372 202 LAEAEKLIESLPR 214
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
80-330 |
4.13e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 80 ERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKCQQQMAEDKASVKAQVTSLLGEL 159
Cdd:PRK02224 223 ERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 160 QESQSRLEAATKDRQALEGRIravsEQVRQLESEREVLQQQHSVQVDQLRmqnqsvEAALRMERQAasEEKRKLAqlqaa 239
Cdd:PRK02224 303 GLDDADAEAVEARREELEDRD----EELRDRLEECRVAAQAHNEEAESLR------EDADDLEERA--EELREEA----- 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 240 yhqlfqdydshiksskgmqlEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAER-HAR 318
Cdd:PRK02224 366 --------------------AELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERdELR 425
|
250
....*....|..
gi 569009763 319 EKLVEKKEYLQE 330
Cdd:PRK02224 426 EREAELEATLRT 437
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
129-239 |
4.27e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 38.79 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 129 KELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQV-----------RQLESER--- 194
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGaaaegragelaQELDSEKqvs 132
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 569009763 195 -------EVLQQqhsvQVDQLRMQNQSVEAALRmerqaASEEKRKLAQLQAA 239
Cdd:PRK09039 133 aralaqvELLNQ----QIAALRRQLAALEAALD-----ASEKRDRESQAKIA 175
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
112-342 |
4.40e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.53 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 112 RLSLEKLDLRSQREQALKELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLE 191
Cdd:COG1196 592 LARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 192 SEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQlfqdydshiksskgmQLEDLRQQLQQAEE 271
Cdd:COG1196 672 AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELE---------------EEALEEQLEAEREE 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 272 ALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQA---------ERHAREKlvEKKEYLQEQLEQLQREFNKL 342
Cdd:COG1196 737 LLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvnllaiEEYEELE--ERYDFLSEQREDLEEARETL 814
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
119-344 |
4.58e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.56 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 119 DLRSQREQALKELEQLKKCQQQMAEDKASVKAQVtSLLGELQES---------QSRLEAATKDRQALEGRIRAVSEQ--- 186
Cdd:PRK04863 841 QLNRRRVELERALADHESQEQQQRSQLEQAKEGL-SALNRLLPRlnlladetlADRVEEIREQLDEAEEAKRFVQQHgna 919
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 187 VRQLESEREVLQQQHSvQVDQLRMQNQSVEAALRMERQAAseekRKLAQL-QAAYHQLFQDYDSHIKSSKGMQlEDLRQQ 265
Cdd:PRK04863 920 LAQLEPIVSVLQSDPE-QFEQLKQDYQQAQQTQRDAKQQA----FALTEVvQRRAHFSYEDAAEMLAKNSDLN-EKLRQR 993
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569009763 266 LQQAEEALvakqeliDKLKEEAEQHkivmetvpvlKAQADIYKADFQAERHAREKlvekkeyLQEQLEQLQREFNKLKV 344
Cdd:PRK04863 994 LEQAEQER-------TRAREQLRQA----------QAQLAQYNQVLASLKSSYDA-------KRQMLQELKQELQDLGV 1048
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
93-358 |
4.63e-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: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 93 REEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKkcqQQMAEDKASVKAQVT------SLLGELQESQSRL 166
Cdd:COG3096 353 QEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLK---SQLADYQQALDVQQTraiqyqQAVQALEKARALC 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 167 EAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRM----ERQAASEEKRKLAQlQAAYHQ 242
Cdd:COG3096 430 GLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIagevERSQAWQTARELLR-RYRSQQ 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 243 LFQDYDSHIKsskgMQLEDLRQQLQQAEEAlvakQELIDKLKEEAEQHKIVMETVPVLKAQADIykadfqaerhAREKLV 322
Cdd:COG3096 509 ALAQRLQQLR----AQLAELEQRLRQQQNA----ERLLEEFCQRIGQQLDAAEELEELLAELEA----------QLEELE 570
|
250 260 270
....*....|....*....|....*....|....*.
gi 569009763 323 EKKEYLQEQLEQLQREFNKLKvgchesARIEDMRKR 358
Cdd:COG3096 571 EQAAEAVEQRSELRQQLEQLR------ARIKELAAR 600
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
102-343 |
4.87e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 102 KFQEARKLVERLSLEKLDLRSQREQALKELEQLKKcqqqMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIR 181
Cdd:PRK03918 201 ELEEVLREINEISSELPELREELEKLEKEVKELEE----LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 182 AVSEQVRQLESEREVLQQQhsvqvdqlrmqnqsveAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKsskgmQLED 261
Cdd:PRK03918 277 ELEEKVKELKELKEKAEEY----------------IKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-----ELEE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 262 LRQQLQQAEEALVAKQELIDKLKEEAEQHkivmETVPVLKAQADIYKADFQAErhAREKLVEKKEYLQEQLEQLQREFNK 341
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLEELEERHELY----EEAKAKKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIEEEISK 409
|
..
gi 569009763 342 LK 343
Cdd:PRK03918 410 IT 411
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
253-360 |
6.90e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 38.91 E-value: 6.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 253 SSKGMQLEDLRQQLQQAE---EALVAKQ-----ELIDKLKEEAEQhkivmetvpvLKAQADIYKADFQAERHAREKLVEK 324
Cdd:COG0542 407 DSKPEELDELERRLEQLEiekEALKKEQdeasfERLAELRDELAE----------LEEELEALKARWEAEKELIEEIQEL 476
|
90 100 110
....*....|....*....|....*....|....*.
gi 569009763 325 KEYLQEQLEQLQREFNKLKVGCHESARIEDMRKRHV 360
Cdd:COG0542 477 KEELEQRYGKIPELEKELAELEEELAELAPLLREEV 512
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
55-342 |
8.07e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 38.51 E-value: 8.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 55 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQRE-----EKEFLMCKFQEARKLVERLSLEKLDLRSQREQALK 129
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEalndlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ 819
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 130 ELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLR 209
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 210 MQNQSVEaalrmERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKG---------MQLEDLRQQLQQAEEALVAKQELI 280
Cdd:TIGR02169 900 ELERKIE-----ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGedeeipeeeLSLEDVQAELQRVEEEIRALEPVN 974
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569009763 281 DKLKEEAEqhkIVMETVPVLKAQadiyKADFQAERHAREKLVE-----KKEYLQEQLEQLQREFNKL 342
Cdd:TIGR02169 975 MLAIQEYE---EVLKRLDELKEK----RAKLEEERKAILERIEeyekkKREVFMEAFEAINENFNEI 1034
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
159-294 |
9.27e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.22 E-value: 9.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009763 159 LQESQSRLEAATKDRqalegrIRAVSEQVRQL--ESEREVLQQQHSVQVDQLRMQNQsvEAALRMERQAASEEKRKLAQL 236
Cdd:PRK12704 44 LEEAKKEAEAIKKEA------LLEAKEEIHKLrnEFEKELRERRNELQKLEKRLLQK--EENLDRKLELLEKREEELEKK 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569009763 237 QAAYHQLFQDYDSHIKSSKGMQLEdLRQQLQQ-----AEEAlvaKQELIDKLKEEAEQHKIVM 294
Cdd:PRK12704 116 EKELEQKQQELEKKEEELEELIEE-QLQELERisgltAEEA---KEILLEKVEEEARHEAAVL 174
|
|
| |
