|
Name |
Accession |
Description |
Interval |
E-value |
| UBAN |
cd09803 |
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ... |
270-356 |
4.53e-20 |
|
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: 84.32 E-value: 4.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 270 MQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVERKELLQEQLEQLQ 349
Cdd:cd09803 1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80
|
....*..
gi 672088856 350 REFNKLK 356
Cdd:cd09803 81 RENQELK 87
|
|
| CC2-LZ |
pfam16516 |
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ... |
271-356 |
2.45e-18 |
|
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: 79.64 E-value: 2.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 271 QLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVERKELLQEQLEQLQR 350
Cdd:pfam16516 15 EIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEYLQR 94
|
....*.
gi 672088856 351 EFNKLK 356
Cdd:pfam16516 95 QNQQLK 100
|
|
| NEMO |
pfam11577 |
NF-kappa-B essential modulator NEMO; NEMO is a regulatory protein which is part of the IKK ... |
62-128 |
5.93e-18 |
|
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: 77.52 E-value: 5.93e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672088856 62 EQGTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLE 128
Cdd:pfam11577 1 DEETLEQMKELLTENHQLKEAMKQSNQAMKERCEELSAWQEKQKEEREFLECRFREARELLRRLSLE 67
|
|
| zf_C2H2_10 |
pfam18414 |
C2H2 type zinc-finger; This is a zinc finger domain C2H2 which can be found in optineurin ... |
405-430 |
2.66e-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: 57.99 E-value: 2.66e-11
10 20
....*....|....*....|....*.
gi 672088856 405 PDFCCPKCQYQAPDMDTLQIHVMECI 430
Cdd:pfam18414 1 PKHCCPKCQEQLPDIDTLQIHVMDCI 26
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
67-302 |
2.17e-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: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 67 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQALEDLEHL 146
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 147 KKcQQVQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQ---QHSVQVDQLRM 223
Cdd:COG1196 350 EE-ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLErleRLEEELEELEE 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672088856 224 QNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQ 302
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA--LLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
116-291 |
5.64e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 5.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 116 QEARKLVERLSLEKLDLRRQREQALEDLEHLKKCQQVQMAEDK-ASVKAQVTSLL---GELQESQSRLEAATKERQTLEG 191
Cdd:COG4913 627 AEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREiAELEAELERLDassDDLAALEEQLEELEAELEELEE 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 192 RIRAVSEQVRQLESEREVLQQqhsvQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDShiksskgmQ 271
Cdd:COG4913 707 ELDELKGEIGRLEKELEQAEE----ELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEE--------R 774
|
170 180
....*....|....*....|
gi 672088856 272 LEDLRQQLQQAEEALVAKQE 291
Cdd:COG4913 775 IDALRARLNRAEEELERAMR 794
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
131-337 |
2.16e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.01 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 131 DLRRQREQALEDLEHlkkcQQVQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVL 210
Cdd:COG4942 20 DAAAEAEAELEQLQQ----EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 211 QQQHSVQVDQLRMQnqsVEAALRMERQAASEEkrklaqlqaayhqLFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVAKQ 290
Cdd:COG4942 96 RAELEAQKEELAEL---LRALYRLGRQPPLAL-------------LLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 672088856 291 ELIDKLKEEAEQHKIVMETvpvLKAQADIYKADFQAERHAREKLVER 337
Cdd:COG4942 160 AELAALRAELEAERAELEA---LLAELEEERAALEALKAERQKLLAR 203
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
67-333 |
4.61e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 4.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 67 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQALEDLEHL 146
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 147 KkcqqvqmaedkasvkAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSvqvdQLRMQNQ 226
Cdd:TIGR02168 760 E---------------AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT----LLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 227 SVEAALRMERQAASEEKRKLAQLQAayhqlfqdydshiksskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIV 306
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEE-------------------QIEELSEDIESLAAEIEELEELIEELESELEALLNE 881
|
250 260
....*....|....*....|....*..
gi 672088856 307 METVPVLKAQADIYKADFQAERHAREK 333
Cdd:TIGR02168 882 RASLEEALALLRSELEELSEELRELES 908
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
114-304 |
1.24e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 114 KFQEARKLVERLSLEKLDLRRQREQALEDLEHLKkcqqvqmaEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRI 193
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELE--------AELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 194 RAVSEQVRQLESEREVLQQQHSvQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGMQLE 273
Cdd:COG1196 291 YELLAELARLEQDIARLEERRR-ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
170 180 190
....*....|....*....|....*....|.
gi 672088856 274 DLRQQLQQAEEALVAKQELIDKLKEEAEQHK 304
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAA 400
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
67-327 |
1.48e-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: 57.00 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 67 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFlmcKFQEarklverLSLEKLDLRRQREQALEDLEHL 146
Cdd:TIGR02169 180 EEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREY---EGYE-------LLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 147 KkcqqvqmaEDKASVKAQVTSLLGELQESQSRLEAATKERQTL-EGRIRAVSEQVRQLESEREVLQQQHSVQVDQLR-MQ 224
Cdd:TIGR02169 250 E--------EELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEdAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 225 NQSVEAALRMERQAASEE--KRKLAQLQAAYHQLFQDYDShikssKGMQLEDLRQQLQQAE-------EALVAKQELIDK 295
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEelEREIEEERKRRDKLTEEYAE-----LKEELEDLRAELEEVDkefaetrDELKDYREKLEK 396
|
250 260 270
....*....|....*....|....*....|..
gi 672088856 296 LKEEAEQHKIVMETVPVLKAQADIYKADFQAE 327
Cdd:TIGR02169 397 LKREINELKRELDRLQEELQRLSEELADLNAA 428
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
115-302 |
7.08e-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: 7.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 115 FQEARKLVE------RLSLEKLDLRRQREqALEDLEhlKKCQQVQMAEDKASVKAQVTSLLgELQESQSRLEAATKERQT 188
Cdd:COG4913 224 FEAADALVEhfddleRAHEALEDAREQIE-LLEPIR--ELAERYAAARERLAELEYLRAAL-RLWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 189 LEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSK 268
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASA 379
|
170 180 190
....*....|....*....|....*....|....
gi 672088856 269 GmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQ 302
Cdd:COG4913 380 E-EFAALRAEAAALLEALEEELEALEEALAEAEA 412
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
73-295 |
3.80e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 73 LEENQELR-DAIRQSNQMLRERCEELLHfQVSQREEKeflMCKFQEARKLV-----ERLSLEKL-DLRRQREQALEDLEH 145
Cdd:COG3206 162 LEQNLELRrEEARKALEFLEEQLPELRK-ELEEAEAA---LEEFRQKNGLVdlseeAKLLLQQLsELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 146 LKKcQQVQMAEDKASVKAQVTSLLG--ELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRM 223
Cdd:COG3206 238 AEA-RLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILA 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672088856 224 Q-------NQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDshIKSSKGMQLEDLRQQLQQAEEALVAKQELIDK 295
Cdd:COG3206 317 SleaeleaLQAREASLQAQLAQLEARLAELPELEAELRRLEREVE--VARELYESLLQRLEEARLAEALTVGNVRVIDP 393
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
67-301 |
6.22e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 6.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 67 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKL-------DLRRQREQA 139
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQilrerlaNLERQLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 140 LEDLEHLKKcQQVQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQhsvqvd 219
Cdd:TIGR02168 322 EAQLEELES-KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ------ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 220 qlrmqnqsvEAALRMERQAASEEKRklaqlqaayhqlfqdydshiksskgmQLEDLRQQLQQAEEALVAKQELIDKLKEE 299
Cdd:TIGR02168 395 ---------IASLNNEIERLEARLE--------------------------RLEDRRERLQQEIEELLKKLEEAELKELQ 439
|
..
gi 672088856 300 AE 301
Cdd:TIGR02168 440 AE 441
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
173-337 |
7.69e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 7.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 173 QESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSV--QVDQLRMQNQSVEAA------LRMERQAASEEKR 244
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAlqRLAEYSWDEIDVASAereiaeLEAELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 245 KLAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADF 324
Cdd:COG4913 686 DLAALEEQLEELEAELEELEE-----ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALG 760
|
170
....*....|....
gi 672088856 325 QA-ERHAREKLVER 337
Cdd:COG4913 761 DAvERELRENLEER 774
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
150-337 |
4.19e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 150 QQVQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVe 229
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 230 aalrmerQAASEEKRKLAQL-----------QAAYHQLFQDYDSHIKSskgmQLEDLRQQLQQAEEALVAKQELIDKLKE 298
Cdd:COG3883 96 -------YRSGGSVSYLDVLlgsesfsdfldRLSALSKIADADADLLE----ELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 672088856 299 EAEQHKIVMETvpvLKAQADIYKADFQAERHAREKLVER 337
Cdd:COG3883 165 ELEAAKAELEA---QQAEQEALLAQLSAEEAAAEAQLAE 200
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
110-337 |
9.44e-06 |
|
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: 47.45 E-value: 9.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 110 FLMCKFQEARKLVERLSLEKLDLRRQREQALEDLEHLKKcQQVQMAEDKASVKAQVTSLLGELQESQSRLEAatkerqtL 189
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKK-EEKALLKQLAALERRIAALARRIRALEQELAA-------L 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 190 EGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKg 269
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA- 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672088856 270 mQLEDLRQQLQQA----EEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVER 337
Cdd:COG4942 161 -ELAALRAELEAEraelEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
116-337 |
9.64e-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: 48.14 E-value: 9.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 116 QEARKLVERLS-LEKLDlrRQREQALEDLEHLKkcQQVQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEG--- 191
Cdd:TIGR02169 153 VERRKIIDEIAgVAEFD--RKKEKALEELEEVE--ENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGyel 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 192 --RIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKG 269
Cdd:TIGR02169 229 lkEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLER 308
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672088856 270 mQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQadiYKADFQAERHAREKLVER 337
Cdd:TIGR02169 309 -SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK---LTEEYAELKEELEDLRAE 372
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
69-301 |
1.34e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.76 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 69 LQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLrrqrEQALEDLEHLKK 148
Cdd:TIGR02169 714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKL----EEALNDLEARLS 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 149 CQQVQMAEDKAS-VKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRMQNQS 227
Cdd:TIGR02169 790 HSRIPEIQAELSkLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK----EIENLNGKKEE 865
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672088856 228 VEAALRmerqaasEEKRKLAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAE 301
Cdd:TIGR02169 866 LEEELE-------ELEAALRDLESRLGDLKKERDELEA-----QLRELERKIEELEAQIEKKRKRLSELKAKLE 927
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
153-252 |
4.07e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 46.10 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 153 QMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQ--NQSVEA 230
Cdd:PRK11448 146 ALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKrkEITDQA 225
|
90 100
....*....|....*....|....
gi 672088856 231 ALRMErqAASEEKRKL--AQLQAA 252
Cdd:PRK11448 226 AKRLE--LSEEETRILidQQLRKA 247
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
67-222 |
5.24e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 5.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 67 ETLQRCLEENQELRDAIRQSNQMLRERCEELL--HFQVSQREEkeflmckfQEARKLVERLSLEKLDLRRQREQALEDLE 144
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEaqIRGNGGDRL--------EQLEREIERLERELEERERRRARLEALLA 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 145 HLKkcqqVQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSV---QVDQL 221
Cdd:COG4913 370 ALG----LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNipaRLLAL 445
|
.
gi 672088856 222 R 222
Cdd:COG4913 446 R 446
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
121-309 |
7.14e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 7.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 121 LVERLSLEKLDLRRQREQALE-DLEHLKKC-QQVQMAEDKasvKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSE 198
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPElNLKELKELeEELKEAEEK---EEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 199 QVRQLESEREVLQQQHSV-----QVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGmQLE 273
Cdd:COG4717 124 LLQLLPLYQELEALEAELaelpeRLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE-ELE 202
|
170 180 190
....*....|....*....|....*....|....*.
gi 672088856 274 DLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMET 309
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
63-251 |
7.74e-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: 7.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 63 QGTPETLQRCLEENQELRDAIRQSNQMLRERCEELlhfqvsqREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQALED 142
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEEL-------KEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 143 LEHLKKCQQVQMAEdKASVKAQVTSLLGELQESQSRLEAATKERQtlEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLR 222
Cdd:TIGR02168 388 VAQLELQIASLNNE-IERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQEELERLEEALE 464
|
170 180
....*....|....*....|....*....
gi 672088856 223 MQNQSVEAALRMERQAASEEKRKLAQLQA 251
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQLQARLDS 493
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
66-302 |
8.50e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 8.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 66 PETLQRCLEENQELRDAIRQSNQMLRERC----EELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQaLE 141
Cdd:TIGR02169 261 SELEKRLEEIEQLLEELNKKIKDLGEEEQlrvkEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAE-IE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 142 DLEHlkkcQQVQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQhsvqVDQL 221
Cdd:TIGR02169 340 ELER----EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRE----LDRL 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 222 RMQNQSVEAALRMERQAASEEKRKLAQLQAAyhqlfqdydshiKSSKGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAE 301
Cdd:TIGR02169 412 QEELQRLSEELADLNAAIAGIEAKINELEEE------------KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYD 479
|
.
gi 672088856 302 Q 302
Cdd:TIGR02169 480 R 480
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
88-343 |
8.57e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 8.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 88 QMLRERCEEL---LHFQVSQREEKEFLM----CKFQEARKLVERLSLEKLDLRRQREQALEDLEHLKKCQQvQMAEDKAS 160
Cdd:TIGR02169 677 QRLRERLEGLkreLSSLQSELRRIENRLdelsQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS-SLEQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 161 VKAQVTSLLGELQESQSRLEAATKERQTLEGRIRavSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAAS 240
Cdd:TIGR02169 756 VKSELKELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEK 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 241 EEKRKLAQLQAAYHQlfqdydshiKSSKGMQLEDLRQQL----QQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQ 316
Cdd:TIGR02169 834 EIQELQEQRIDLKEQ---------IKSIEKEIENLNGKKeeleEELEELEAALRDLESRLGDLKKERDELEAQLRELERK 904
|
250 260
....*....|....*....|....*..
gi 672088856 317 ADIYKADFQAERHAREKLVERKELLQE 343
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEALEE 931
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
132-356 |
1.76e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 132 LRRQREQAL------EDLEHLkkcqqvqmaeDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLES 205
Cdd:TIGR02168 205 LERQAEKAErykelkAELREL----------ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 206 EREVLQQQhsVQVDQLRMQNQSVEAAlRMERQAAsEEKRKLAQLQAAYHQLfQDYDSHIKSSKGMQLEDLRQQLQQAEEA 285
Cdd:TIGR02168 275 EVSELEEE--IEELQKELYALANEIS-RLEQQKQ-ILRERLANLERQLEEL-EAQLEELESKLDELAEELAELEEKLEEL 349
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672088856 286 LVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVERKELLQEQLEQLQREFNKLK 356
Cdd:TIGR02168 350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQ 420
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
98-337 |
2.05e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 98 LHFQVSQREEKEfLMCKFQEARKLVERLSLEKLDLRRQREQALEDLEHLKkcqqvQMAEDKASVKAQVTSLLGELQESQS 177
Cdd:PRK02224 192 LKAQIEEKEEKD-LHERLNGLESELAELDEEIERYEEQREQARETRDEAD-----EVLEEHEERREELETLEAEIEDLRE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 178 RLEAATKERQTLEGRIRAVSEQVRQLESEREVL----------QQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLA 247
Cdd:PRK02224 266 TIAETEREREELAEEVRDLRERLEELEEERDDLlaeaglddadAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 248 QLQAAYHQLFQDYDshiksSKGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAE 327
Cdd:PRK02224 346 SLREDADDLEERAE-----ELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREE 420
|
250
....*....|.
gi 672088856 328 R-HAREKLVER 337
Cdd:PRK02224 421 RdELREREAEL 431
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
70-292 |
2.25e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.80 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 70 QRCLEENQELRDAIRQSNQMLRERCEELLhfQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQALEDLEHLKKC 149
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRAKLLMKRAAHVK--QQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 150 QQ-VQMAEDKASVKAQVTSllgELQESQSRLEAATKERQTLEGRIrAVSEQVRQLESEREVLQQQHSVQVDQLRMQNqsv 228
Cdd:TIGR00618 385 QQqKTTLTQKLQSLCKELD---ILQREQATIDTRTSAFRDLQGQL-AHAKKQQELQQRYAELCAAAITCTAQCEKLE--- 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672088856 229 EAALRMERQAASEEKRKLAQLQAAyhqlfqdydsHIKSSKGMQLEDLRQQLQQAEEALVAKQEL 292
Cdd:TIGR00618 458 KIHLQESAQSLKEREQQLQTKEQI----------HLQETRKKAVVLARLLELQEEPCPLCGSCI 511
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
59-322 |
2.79e-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: 43.02 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 59 LPSEQGTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREE-KEFLMCKFQEARKLVERLSLEKLDLRRQRE 137
Cdd:COG5185 245 LEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENtKEKIAEYTKSIDIKKATESLEEQLAAAEAE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 138 QALEDlehlkkcqqvQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEG--RIRAVSEQVR----QLESEREVLQ 211
Cdd:COG5185 325 QELEE----------SKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGevELSKSSEELDsfkdTIESTKESLD 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 212 QQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKS-SKGMQLEDLRQQLQQAEEALVAKQ 290
Cdd:COG5185 395 EIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISElNKVMREADEESQSRLEEAYDEINR 474
|
250 260 270
....*....|....*....|....*....|..
gi 672088856 291 ELIDKLKEEAEQHKIVMETVPVLKAQADIYKA 322
Cdd:COG5185 475 SVRSKKEDLNEELTQIESRVSTLKATLEKLRA 506
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
158-305 |
2.82e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.65 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 158 KASVKAQVTSLLGELQESQSrLEAATKerQTLEGRIRAVSEQVRQLESEREVLQQQH---SVQVDQLRMQNQSVEAALRM 234
Cdd:PRK09039 51 KDSALDRLNSQIAELADLLS-LERQGN--QDLQDSVANLRASLSAAEAERSRLQALLaelAGAGAAAEGRAGELAQELDS 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672088856 235 ERQAASEEKRKLAQLQAayhqlfqdydshiksskgmQLEDLRQQLQQAEEALVAKQElidklKEEAEQHKI 305
Cdd:PRK09039 128 EKQVSARALAQVELLNQ-------------------QIAALRRQLAALEAALDASEK-----RDRESQAKI 174
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
67-252 |
4.45e-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: 42.74 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 67 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQ-------REQA 139
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQiaslnneIERL 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 140 LEDLEHLKKCQQVQMAEDKASVKAQVTSllgELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSVQVD 219
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIEELLKKLEEA---ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
|
170 180 190
....*....|....*....|....*....|...
gi 672088856 220 QLRMQNQSVEAALRMERQAASEEKRKLAQLQAA 252
Cdd:TIGR02168 483 ELAQLQARLDSLERLQENLEGFSEGVKALLKNQ 515
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
74-308 |
4.70e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 74 EENQELRDAiRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQALEDLEHLKKCQQVQ 153
Cdd:PTZ00121 1575 DKNMALRKA-EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELK 1653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 154 MAEDKASVKAQvtSLLGELQESQSRLEAATKErqtlEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQsVEAALR 233
Cdd:PTZ00121 1654 KAEEENKIKAA--EEAKKAEEDKKKAEEAKKA----EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE-LKKAEE 1726
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672088856 234 MERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVAKQElidkLKEEAEQHKIVME 308
Cdd:PTZ00121 1727 ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE----LDEEDEKRRMEVD 1797
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
162-314 |
4.97e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 162 KAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRMQNQSVEAALRMERQAASE 241
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEA----ELEEKDERIERLERELSEARSEERR 459
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672088856 242 EKRKlaqlqaayhqlfqdyDSHIKSSKGMqLEDLRQQLQQAEEALvakQELIDKLKEEAEQHKIVM--ETVPVLK 314
Cdd:COG2433 460 EIRK---------------DREISRLDRE-IERLERELEEERERI---EELKRKLERLKELWKLEHsgELVPVKV 515
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
64-302 |
5.78e-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: 42.25 E-value: 5.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 64 GTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFlmcKFQEARKLVERLSLEkldlrrqREQALEDL 143
Cdd:COG5185 272 ENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQL---AAAEAEQELEESKRE-------TETGIQNL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 144 EHLKKCQQVQMAEDKASVKAQVTSLLGELQESQSRlEAATKERQTLEGRIRAVSEQVR-QLESEREVLQ----------Q 212
Cdd:COG5185 342 TAEIEQGQESLTENLEAIKEEIENIVGEVELSKSS-EELDSFKDTIESTKESLDEIPQnQRGYAQEILAtledtlkaadR 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 213 QHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVAKQEL 292
Cdd:COG5185 421 QIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKAT 500
|
250
....*....|
gi 672088856 293 IDKLKEEAEQ 302
Cdd:COG5185 501 LEKLRAKLER 510
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
67-284 |
6.28e-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: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 67 ETLQRCLEENQELRDAIRQSNQMLRErceelLHFQVSQREEKeflmckFQEARKLVERLSLEKLDLRRQREQALEDLEHL 146
Cdd:COG4913 664 ASAEREIAELEAELERLDASSDDLAA-----LEEQLEELEAE------LEELEEELDELKGEIGRLEKELEQAEEELDEL 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 147 KkcQQVQMAEDKASVkaQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHsVQVDQLRMQNQ 226
Cdd:COG4913 733 Q--DRLEAAEDLARL--ELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAF-NREWPAETADL 807
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672088856 227 SVEAAlrmerqAASEEKRKLAQLQA----AYHQLFQDYdshIKSSKGMQLEDLRQQLQQAEE 284
Cdd:COG4913 808 DADLE------SLPEYLALLDRLEEdglpEYEERFKEL---LNENSIEFVADLLSKLRRAIR 860
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
67-247 |
6.59e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 6.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 67 ETLQRCLEENQELRDAIRQSNQMLRERCEELL--HFQVSQREEKEFLMcKFQEARKLVERLSLEKLDLRRQREQALEDLE 144
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQKEELAELLraLYRLGRQPPLALLL-SPEDFLDAVRRLQYLKYLAPARREQAEELRA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 145 HLKKCQQVQMAEDKAsvKAQVTSLLGELQESQSRLEAATKERQT----LEGRIRAVSEQVRQLESEREVLQQQHSvqvdq 220
Cdd:COG4942 158 DLAELAALRAELEAE--RAELEALLAELEEERAALEALKAERQKllarLEKELAELAAELAELQQEAEELEALIA----- 230
|
170 180
....*....|....*....|....*..
gi 672088856 221 lRMQNQSVEAALRMERQAASEEKRKLA 247
Cdd:COG4942 231 -RLEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
105-370 |
9.91e-04 |
|
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: 41.65 E-value: 9.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 105 REEKEFLMCKFQEARKLVERLSLEKLDLRRQR----EQALEDLEHLKKCQQVQMAEDKASVKAQVTSLLGELQESQSRLE 180
Cdd:pfam17380 302 RQEKEEKAREVERRRKLEEAEKARQAEMDRQAaiyaEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRELE 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 181 AATKERQTLEGRIRAVSEQVRQ---LESEREVLQQQHSVQVDQLRMQNQSV--EAALRMERQAASEEKRKLAQLQAAYHQ 255
Cdd:pfam17380 382 RLQMERQQKNERVRQELEAARKvkiLEEERQRKIQQQKVEMEQIRAEQEEArqREVRRLEEERAREMERVRLEEQERQQQ 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 256 ---LFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVAKQELID---KLKEEAEQHKIVMetvpvlKAQADIYKADFQAERH 329
Cdd:pfam17380 462 verLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEErkqAMIEEERKRKLLE------KEMEERQKAIYEEERR 535
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 672088856 330 aREKLVERKELLQEQLEQLQREfnKLKVGCHESARIEDMRK 370
Cdd:pfam17380 536 -REAEEERRKQQEMEERRRIQE--QMRKATEERSRLEAMER 573
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
69-306 |
1.13e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 69 LQRCLEENQELRDAIRQsnqmLRERCEELlhfqvsqREEKEFLMCKFQEARKLVE--RLSLEKLD-----LRRQREQALE 141
Cdd:PRK02224 337 AQAHNEEAESLREDADD----LEERAEEL-------REEAAELESELEEAREAVEdrREEIEELEeeieeLRERFGDAPV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 142 DLEHLKKCQQvQMAEDKASVKAQVTSLLGELQESQSRLEAATKER---------QTLEG-----RIRAVSEQVRQLESER 207
Cdd:PRK02224 406 DLGNAEDFLE-ELREERDELREREAELEATLRTARERVEEAEALLeagkcpecgQPVEGsphveTIEEDRERVEELEAEL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 208 EVLQQQHSVQVDQLRMQNQSVEAALRMERqaaSEEKRKLAQlqaayhQLFQDYDSHIKsSKGMQLEDLRQQLQQAEEALV 287
Cdd:PRK02224 485 EDLEEEVEEVEERLERAEDLVEAEDRIER---LEERREDLE------ELIAERRETIE-EKRERAEELRERAAELEAEAE 554
|
250
....*....|....*....
gi 672088856 288 AKQELIDKLKEEAEQHKIV 306
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREE 573
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
235-304 |
1.17e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 1.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 235 ERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHK 304
Cdd:PRK12704 48 KKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRN-ELQKLEKRLLQKEENLDRKLELLEKREEELEKKE 116
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
40-244 |
1.20e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 40 EDQDMLGEESSLGKPAMLHLPSEQGTPETLQRCLEENQELRDAIRQSNQM-LRERCEELLH-FQVSQREEKEFLMCKFQE 117
Cdd:COG4717 317 EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEeLEQEIAALLAeAGVEDEEELRAALEQAEE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 118 ARKLVERLSLEKLDLRRQREQALEDLEhlkkcqqvqmAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAV- 196
Cdd:COG4717 397 YQELKEELEELEEQLEELLGELEELLE----------ALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLe 466
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 672088856 197 -SEQVRQLESEREVLQQQHSVQVDQlRMQNQSVEAALRMERQAASEEKR 244
Cdd:COG4717 467 eDGELAELLQELEELKAELRELAEE-WAALKLALELLEEAREEYREERL 514
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
172-307 |
1.30e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 172 LQESQSRLEAATKERqtlegrIRAVSEQVRQL--ESEREVLQQQHSVQVDQLRMQNQsvEAALRMERQAASEEKRKLAQL 249
Cdd:PRK12704 44 LEEAKKEAEAIKKEA------LLEAKEEIHKLrnEFEKELRERRNELQKLEKRLLQK--EENLDRKLELLEKREEELEKK 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672088856 250 QAAYHQLFQDYDSHIKSSKGMQLEdLRQQLQQ-----AEEAlvaKQELIDKLKEEAEQHKIVM 307
Cdd:PRK12704 116 EKELEQKQQELEKKEEELEELIEE-QLQELERisgltAEEA---KEILLEKVEEEARHEAAVL 174
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
83-288 |
1.39e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 83 IRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERlslekldLRRQREQALEDLEHLKKCQQVQMAEDKasvK 162
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEE-------LEAELEELREELEKLEKLLQLLPLYQE---L 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 163 AQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSV----QVDQLRMQNQSVEAALRMERQA 238
Cdd:COG4717 135 EALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLateeELQDLAEELEELQQRLAELEEE 214
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 672088856 239 ASEEKRKLAQLQAAYHQLfqdydshiksSKGMQLEDLRQQLQQAEEALVA 288
Cdd:COG4717 215 LEEAQEELEELEEELEQL----------ENELEAAALEERLKEARLLLLI 254
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
77-374 |
1.59e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 77 QELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVErlslekldLRRQREQALEDLEHLKKCQQVQMAE 156
Cdd:PTZ00121 1428 EEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE--------AKKKAEEAKKADEAKKKAEEAKKKA 1499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 157 DKASVKAQVTSLLGELQESQSRLEA-----ATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAA 231
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAKKAEEAKKAdeakkAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMA 1579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 232 LRMERQAASEEKRKLAQLQAAYHQlfqdyDSHIKSSKGMQLEDLR---QQLQQAEEALVAKQELIDKLKEE---AEQHKI 305
Cdd:PTZ00121 1580 LRKAEEAKKAEEARIEEVMKLYEE-----EKKMKAEEAKKAEEAKikaEELKKAEEEKKKVEQLKKKEAEEkkkAEELKK 1654
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672088856 306 VMETVPVLKAQadIYKADFQAERHAREKLVERKELLQEQLeqlqrefnKLKVGCHESARIEDMRKRHVE 374
Cdd:PTZ00121 1655 AEEENKIKAAE--EAKKAEEDKKKAEEAKKAEEDEKKAAE--------ALKKEAEEAKKAEELKKKEAE 1713
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
67-302 |
1.87e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 67 ETLQRCLEENQELRDAirqsnqmlrERCEEllhfqVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQALEDLEHL 146
Cdd:PRK02224 436 RTARERVEEAEALLEA---------GKCPE-----CGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERA 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 147 KkcqqvqmaedkasvkaqvtsllgELQESQSRLEAATKERQTLEGRIravSEQVRQLESEREVLQQQHSvQVDQLRMQNQ 226
Cdd:PRK02224 502 E-----------------------DLVEAEDRIERLEERREDLEELI---AERRETIEEKRERAEELRE-RAAELEAEAE 554
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 672088856 227 SVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDShiksskgmqLEDLRQQLQQAEEALVAKQELIDKLKEEAEQ 302
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREEVAELNSKLAELKERIES---------LERIRTLLAAIADAEDEIERLREKREALAEL 621
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
101-290 |
1.91e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.87 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 101 QVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQALEDLEHL----------KKCQQVQMAEDKASVKAQVTSLLG 170
Cdd:pfam15921 305 QEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQlvlanselteARTERDQFSQESGNLDDQLQKLLA 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 171 ELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESErevlqqqhsvqVDQLRMQNQSVEAALR-MERQAASEEKRKLAQL 249
Cdd:pfam15921 385 DLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRE-----------LDDRNMEVQRLEALLKaMKSECQGQMERQMAAI 453
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 672088856 250 QAAYHQLFQdydshiKSSKGMQLEDLRQQLQQAEEALVAKQ 290
Cdd:pfam15921 454 QGKNESLEK------VSSLTAQLESTKEMLRKVVEELTAKK 488
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
115-313 |
1.96e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 40.22 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 115 FQEARKLVERLSlekldlRRQREQALEDLEhlkkcQQVQMAEDKA-----------------SVKAQVTSLLGELQESQS 177
Cdd:COG3524 160 LAESEELVNQLS------ERAREDAVRFAE-----EEVERAEERLrdareallafrnrngilDPEATAEALLQLIATLEG 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 178 RLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRmqnqsveaalrmERQAASEEKRKLAQLQAAYhqlf 257
Cdd:COG3524 229 QLAELEAELAALRSYLSPNSPQVRQLRRRIAALEK----QIAAER------------ARLTGASGGDSLASLLAEY---- 288
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 672088856 258 qdydshiksskgmqlEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETV--PVL 313
Cdd:COG3524 289 ---------------ERLELEREFAEKAYTSALAALEQARIEAARQQRYLAVIvqPTL 331
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
174-299 |
1.97e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.13 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 174 ESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAY 253
Cdd:pfam09787 44 ALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEEL 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 254 HQLFQD-------YDSHIKSsKGMQLEDLRQQL--------QQAE---------EALVAKQELIDKLKEE 299
Cdd:pfam09787 124 RYLEEElrrskatLQSRIKD-REAEIEKLRNQLtsksqsssSQSElenrlhqltETLIQKQTMLEALSTE 192
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
114-333 |
1.97e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 114 KFQEARKLverlSLEKLDLRRQREQALEDLEHLKKCQQVQMAEDKASVKAQVTSLLGELQESQSRLEAATK--------E 185
Cdd:PTZ00121 1099 KAEEAKKT----ETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKaeearkaeD 1174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 186 RQTLEGRIRAV----------------------SEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEK 243
Cdd:PTZ00121 1175 AKKAEAARKAEevrkaeelrkaedarkaeaarkAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEI 1254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 244 RKLAQLQAAYhqlFQDYDSHIKSSKGMQLEDLR--QQLQQAEEALVAKQ-ELIDKLKEEAEQHKIVMETVPvlKAQADIY 320
Cdd:PTZ00121 1255 RKFEEARMAH---FARRQAAIKAEEARKADELKkaEEKKKADEAKKAEEkKKADEAKKKAEEAKKADEAKK--KAEEAKK 1329
|
250
....*....|...
gi 672088856 321 KADfQAERHAREK 333
Cdd:PTZ00121 1330 KAD-AAKKKAEEA 1341
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
138-252 |
2.00e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.95 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 138 QALEDLEHLKKCQQVQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLE--SER-----EVL 210
Cdd:PRK09039 63 AELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKqvSARalaqvELL 142
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 672088856 211 QQQhsvqVDQLRMQNQSVEAALRmerqaASEEKRKLAQLQAA 252
Cdd:PRK09039 143 NQQ----IAALRRQLAALEAALD-----ASEKRDRESQAKIA 175
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
176-355 |
2.44e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 176 QSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSV-----QVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQ 250
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLvdlseEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 251 AayhQLFQDYDSHIKSSKGMQLEDLRQQLQQAEealvakQELIDKLKEEAEQHKIVMEtvpvLKAQADIYKADFQAE--- 327
Cdd:COG3206 247 A---QLGSGPDALPELLQSPVIQQLRAQLAELE------AELAELSARYTPNHPDVIA----LRAQIAALRAQLQQEaqr 313
|
170 180 190
....*....|....*....|....*....|...
gi 672088856 328 -----RHAREKLVERKELLQEQLEQLQREFNKL 355
Cdd:COG3206 314 ilaslEAELEALQAREASLQAQLAQLEARLAEL 346
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
151-305 |
2.70e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.20 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 151 QVQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQhsvqvdqlrmQNQSVEA 230
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEE----------AEKEAQQ 577
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672088856 231 ALRMERQAASEEKRKLAQLQAAYHqlfqdydSHIKSSkgmQLEDLRQQLQQAEEALVAKqelidKLKEEAEQHKI 305
Cdd:PRK00409 578 AIKEAKKEADEIIKELRQLQKGGY-------ASVKAH---ELIEARKRLNKANEKKEKK-----KKKQKEKQEEL 637
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
67-303 |
3.31e-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: 39.95 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 67 ETLQRCLEENQELRDAIrQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRR-QREQALEDLEH 145
Cdd:TIGR00618 584 EDIPNLQNITVRLQDLT-EKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHAlQLTLTQERVRE 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 146 LKKCQQVQMAEDKASVKAqvtsllgELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQN 225
Cdd:TIGR00618 663 HALSIRVLPKELLASRQL-------ALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLA 735
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672088856 226 QSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSskGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQH 303
Cdd:TIGR00618 736 AREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQT--GAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQE 811
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
185-304 |
3.52e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 185 ERQTLEGRIRAVSEQVRQLES-EREVLQQQHsvQVDQLRmqnQSVEAALRmeRQAASEEKRKLAQLQAAYHQLFqdyDSH 263
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERaHEALEDARE--QIELLE---PIRELAER--YAAARERLAELEYLRAALRLWF---AQR 288
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 672088856 264 IKSSKGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHK 304
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELE 329
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
77-299 |
3.97e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 77 QELRDAIRQSNQMLRE-RCEEllhfqVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQR---EQALEDLEHLKKCQ-Q 151
Cdd:PRK02224 436 RTARERVEEAEALLEAgKCPE-----CGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVeevEERLERAEDLVEAEdR 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 152 VQMAEDKASV---------------KAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESER----EVLQQ 212
Cdd:PRK02224 511 IERLEERREDleeliaerretieekRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLaelkERIES 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 213 QHSVQVDQLRMQNQSVEAALRMERQAA-----SEEKRKLAQLQAAYHQLFQDYDshiksskGMQLEDLRQQLQQAEEALV 287
Cdd:PRK02224 591 LERIRTLLAAIADAEDEIERLREKREAlaelnDERRERLAEKRERKRELEAEFD-------EARIEEAREDKERAEEYLE 663
|
250
....*....|..
gi 672088856 288 AKQELIDKLKEE 299
Cdd:PRK02224 664 QVEEKLDELREE 675
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
67-303 |
4.55e-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: 39.65 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 67 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEkeflmckFQEARKLVERLSLEKLDLRRQREQALEDLEHL 146
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA-------LDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 147 KKcQQVQMAEDKASVKAQVTSL---LGELQESQSRLEAATKErqtLEGRIRAVSEQVRQLESEREVLQQqhsvqvdqlrm 223
Cdd:TIGR02168 837 ER-RLEDLEEQIEELSEDIESLaaeIEELEELIEELESELEA---LLNERASLEEALALLRSELEELSE----------- 901
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 224 QNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDShiksskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQH 303
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN--------LQERLSEEYSLTLEEAEALENKIEDDEEEARRR 973
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
65-247 |
4.82e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.37 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 65 TPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVsqreekeflmcKFQEARKLVERLSLEKLDLRRQREQALEDLE 144
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELED-----------ELAALEARLEAAKTELEDLEKEIKRLELEIE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 145 HLKKcqqvQMAEDKASVKAQVTSllGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHS---VQVDQL 221
Cdd:COG1579 70 EVEA----RIKKYEEQLGNVRNN--KEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAeleAELEEK 143
|
170 180
....*....|....*....|....*.
gi 672088856 222 RMQNQSVEAALRMERQAASEEKRKLA 247
Cdd:COG1579 144 KAELDEELAELEAELEELEAEREELA 169
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
101-304 |
7.03e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.97 E-value: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 101 QVSQREEKEflmcKFQEARKLVERlslEKLDLRRQREqaLEDLEHLKKCQQVQMAEDKASVKAQVTSLLGELQESQSRLE 180
Cdd:PTZ00121 1556 ELKKAEEKK----KAEEAKKAEED---KNMALRKAEE--AKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK 1626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 181 AATKERQTLEGRIRAVSEQVRQLESEREVlQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAyhqlfQDY 260
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEKKKAEELKKA-EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE-----AEE 1700
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 672088856 261 DSHIKSSKGMQLEDLR--QQLQQAEEALVAKQElidKLKEEAEQHK 304
Cdd:PTZ00121 1701 AKKAEELKKKEAEEKKkaEELKKAEEENKIKAE---EAKKEAEEDK 1743
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
103-316 |
9.87e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 38.46 E-value: 9.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 103 SQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQaLEDLEHLKKCQQVQMAEDKASVKAQVTSLLGELQESQSRLEAA 182
Cdd:TIGR04523 194 NKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQ-LKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 183 TKERQTLEGRIRAVSEQVRQLESEREVLQQQHSV---------------QVDQLRMQ-NQSVEAALRMERQAA------- 239
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwnkelkselknqekKLEEIQNQiSQNNKIISQLNEQISqlkkelt 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088856 240 ------SEEKRKLAQLQAAYHQLFQDYDSHIKSSKGM--QLEDLRQQLQQAEEALVAKQELIDKLKEEAE----QHKIVM 307
Cdd:TIGR04523 353 nsesenSEKQRELEEKQNEIEKLKKENQSYKQEIKNLesQINDLESKIQNQEKLNQQKDEQIKKLQQEKEllekEIERLK 432
|
....*....
gi 672088856 308 ETVPVLKAQ 316
Cdd:TIGR04523 433 ETIIKNNSE 441
|
|
| |
