|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
3-158 |
2.95e-102 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 301.10 E-value: 2.95e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 3 IKQVIIQGFRSYRDQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHEGTGPRVISAFVEIIF 82
Cdd:cd03272 1 IKQVIIQGFKSYKDQTVIEPFSPKHNVVVGRNGSGKSNFFAAIRFVLSDEYTHLREEQRQALLHEGSGPSVMSAYVEIIF 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74216698 83 DNSDNRLPIDKEEVSLRRVIGAKKDQYFLDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKINQMATAPDSQRLKL 158
Cdd:cd03272 81 DNSDNRFPIDKEEVRLRRTIGLKKDEYFLDKKNVTKNDVMNLLESAGFSRSNPYYIVPQGKINSLTNMKQDEQQEM 156
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2-351 |
1.69e-58 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 204.05 E-value: 1.69e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 2 YIKQVIIQGFRSYRdQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSD-EFSHLRPEQRLALLHEGTGPRVISAFVEI 80
Cdd:pfam02463 1 YLKRIEIEGFKSYA-KTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGErSAKSLRSERLSDLIHSKSGAFVNSAEVEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 81 IFDNSDNRLPIDKEEVSLRRVIGAKKD-QYFLDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKINQMATAPDSQRLKLL 159
Cdd:pfam02463 80 TFDNEDHELPIDKEEVSIRRRVYRGGDsEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 160 REVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKL 239
Cdd:pfam02463 160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 240 DELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGN 319
Cdd:pfam02463 240 DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKES 319
|
330 340 350
....*....|....*....|....*....|..
gi 74216698 320 SEQRKRLLKERQKLLEKIEEKQKELAETEPKF 351
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEELEKELKELEIKR 351
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-350 |
7.85e-39 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 147.01 E-value: 7.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 1 MYIKQVIIQGFRSYRDQTIVdPFSSKHNVIVGRNGSGKSNFFYAIQFVL---SdeFSHLRPEQRLALLHEGTGPR--VIS 75
Cdd:COG1196 1 MRLKRLELAGFKSFADPTTI-PFEPGITAIVGPNGSGKSNIVDAIRWVLgeqS--AKSLRGGKMEDVIFAGSSSRkpLGR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 76 AFVEIIFDNSDNRLPIDKEEVSLRRVIGAKKD-QYFLDKKMVTKNDVMNLLESAGFSRsNPYYIVKQGKINQMATAPDSQ 154
Cdd:COG1196 78 AEVSLTFDNSDGTLPIDYDEVTITRRLYRSGEsEYYINGKPCRLKDIQDLFLDTGLGP-ESYSIIGQGMIDRIIEAKPEE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 155 RLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNE 234
Cdd:COG1196 157 RRAIIEEAAGISKYKERKEEAERKLEATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 235 TRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQD 314
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
|
330 340 350
....*....|....*....|....*....|....*.
gi 74216698 315 ELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPK 350
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEE 352
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-346 |
2.09e-32 |
|
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: 128.26 E-value: 2.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 2 YIKQVIIQGFRSYRDQTIVdPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSH-LRPEQRLALLHEG-TGPRVISAFVE 79
Cdd:TIGR02169 1 YIERIELENFKSFGKKKVI-PFSKGFTVISGPNGSGKSNIGDAILFALGLSSSKaMRAERLSDLISNGkNGQSGNEAYVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 80 IIFDNSDNRLPiDKEEVSLRRVIG--AKKDQYFLDKKMVTKNDVMNLLESAGFSrSNPYYIVKQGKINQMATAPDSQRLK 157
Cdd:TIGR02169 80 VTFKNDDGKFP-DELEVVRRLKVTddGKYSYYYLNGQRVRLSEIHDFLAAAGIY-PEGYNVVLQGDVTDFISMSPVERRK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 158 LLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRA 237
Cdd:TIGR02169 158 IIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALER 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 238 KLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIK-QRTKLELKAKDLQDEL 316
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEaEIASLERSIAEKEREL 317
|
330 340 350
....*....|....*....|....*....|
gi 74216698 317 AGNSEQRKRLLKERQKLLEKIEEKQKELAE 346
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIEE 347
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
3-85 |
2.34e-32 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 119.34 E-value: 2.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 3 IKQVIIQGFRSYRDQTIVdPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHEGTGPRVISAFVEIIF 82
Cdd:cd03239 1 IKQITLKNFKSYRDETVV-GGSNSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFLAGGGVKAGINSASVEITF 79
|
...
gi 74216698 83 DNS 85
Cdd:cd03239 80 DKS 82
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-348 |
2.86e-32 |
|
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: 127.87 E-value: 2.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 2 YIKQVIIQGFRSYRDQTIVDpFSSKHNVIVGRNGSGKSNFFYAIQFVLSdefshlrpEQRLALLHEGTGPRVI------- 74
Cdd:TIGR02168 1 RLKKLELAGFKSFADPTTIN-FDKGITGIVGPNGCGKSNIVDAIRWVLG--------EQSAKALRGGKMEDVIfngsetr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 75 ----SAFVEIIFDNSDNRLP-IDKEEVSLRRVIGAKKD-QYFLDKKMVTKNDVMNLLESAGFSRSNpYYIVKQGKINQMA 148
Cdd:TIGR02168 72 kplsLAEVELVFDNSDGLLPgADYSEISITRRLYRDGEsEYFINGQPCRLKDIQDLFLDTGLGKRS-YSIIEQGKISEII 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 149 TAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIY 228
Cdd:TIGR02168 151 EAKPEERRAIFEEAAGISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 229 --------------NQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAE 294
Cdd:TIGR02168 231 vlrleelreeleelQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74216698 295 RQEQIK-------QRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETE 348
Cdd:TIGR02168 311 LANLERqleeleaQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1-144 |
1.23e-25 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 103.15 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 1 MYIKQVIIQGFRSYRDQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLS-DEFSHLRPEQRLALLHEGTGPRVISAFVE 79
Cdd:cd03273 1 MHIKEIILDGFKSYATRTVISGFDPQFNAITGLNGSGKSNILDAICFVLGiTNLSTVRASNLQDLIYKRGQAGITKASVT 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 80 IIFDNSD-NRLPIDKE---EVSLRRVIG-AKKDQYFLDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKI 144
Cdd:cd03273 81 IVFDNSDkSQSPIGFEnypEITVTRQIVlGGTNKYLINGHRAQQQRVQDLFQSVQLNVNNPHFLIMQGRI 150
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
3-129 |
1.45e-16 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 78.00 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 3 IKQVIIQGFRSYRDQTIVDPFSSkHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHEG--TGPRVISAFVEI 80
Cdd:cd03275 1 LKRLELENFKSYKGRHVIGPFDR-FTCIIGPNGSGKSNLMDAISFVLGEKSSHLRSKNLKDLIYRArvGKPDSNSAYVTA 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 74216698 81 IFDNSDNrlpidkEEVSLRRVIGAKKDQYFLDKKMVTKNDVMNLLESAG 129
Cdd:cd03275 80 VYEDDDG------EEKTFRRIITGGSSSYRINGKVVSLKEYNEELEKIN 122
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
5-82 |
1.69e-16 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 75.86 E-value: 1.69e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74216698 5 QVIIQGFRSYRDQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPeqrlallHEGTGPRVISAFVEIIF 82
Cdd:cd03227 1 KIVLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRR-------RSGVKAGCIVAAVSAEL 71
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
3-205 |
1.62e-14 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 71.58 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 3 IKQVIIQGFRSYRDQTIVDpFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHlRPEQRLALLHEGTGprviSAFVEIIF 82
Cdd:COG0419 2 LLRLRLENFRSYRDTETID-FDDGLNLIVGPNGAGKSTILEAIRYALYGKARS-RSKLRSDLINVGSE----EASVELEF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 83 DNSDNRlpidkeevslrrvigakkdqyfldkkmvtkndvmnllesagfsrsnpYYIVK-QGKINQMATAPDSQRLKLLRE 161
Cdd:COG0419 76 EHGGKR-----------------------------------------------YRIERrQGEFAEFLEAKPSERKEALKR 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 74216698 162 VAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEE 205
Cdd:COG0419 109 LLGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQLSG 152
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
3-159 |
1.96e-13 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 68.26 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 3 IKQVIIQGFRSYRDQTIVdPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSH-LRPEQRLALLHEGTGPR--VISAFVE 79
Cdd:cd03278 1 LKKLELKGFKSFADKTTI-PFPPGLTAIVGPNGSGKSNIIDAIRWVLGEQSAKsLRGEKMSDVIFAGSETRkpANFAEVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 80 IIFDNSDNRlpidkeevslrrvigakkdqyfldkkmvtkndvmnllesagfsrsnpYYIVKQGKINQMATAPD--SQRLK 157
Cdd:cd03278 80 LTFDNSDGR-----------------------------------------------YSIISQGDVSEIIEAPGkkVQRLS 112
|
..
gi 74216698 158 LL 159
Cdd:cd03278 113 LL 114
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-89 |
5.20e-13 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 69.26 E-value: 5.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 1 MYIKQVIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFS-HLRPEQrlalLHEGTGPRVISAFVE 79
Cdd:COG3593 1 MKLEKIKIKNFRSIKDLSI--ELSDDLTVLVGENNSGKSSILEALRLLLGPSSSrKFDEED----FYLGDDPDLPEIEIE 74
|
90
....*....|
gi 74216698 80 IIFDNSDNRL 89
Cdd:COG3593 75 LTFGSLLSRL 84
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1-151 |
6.44e-11 |
|
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213241 [Multi-domain] Cd Length: 212 Bit Score: 61.16 E-value: 6.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 1 MYIKQVIIQGFRSYRDQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHEGTG-PRVISAFVE 79
Cdd:cd03274 1 LIITKLVLENFKSYAGEQVIGPFHKSFSAIVGPNGSGKSNVIDSMLFVFGFRASKMRQKKLSDLIHNSAGhPNLDSCSVE 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74216698 80 IIFdnsdnrlpidkeevslrrvigakkdQYFLDKKmvtkndvmnLLESAGFSRSNPYYIVKQGKINQMATAP 151
Cdd:cd03274 81 VHF-------------------------QEIIDKP---------LLKSKGIDLDHNRFLILQGEVEQIAQMP 118
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
3-171 |
1.15e-10 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 62.26 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 3 IKQVIIQGFRSYRDQTI-VDPFsskhNVIVGRNGSGKSNFFYAIQF---------------------VLSDEFSHLRPEQ 60
Cdd:COG4637 2 ITRIRIKNFKSLRDLELpLGPL----TVLIGANGSGKSNLLDALRFlsdaargglqdalarrggleeLLWRGPRTITEPI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 61 RLALLHEGTGPRVISAFVEIIFDNSDNRLPIDKEEVSLRRviGAKKDQYFLDKKMVTknDVMNLLESAGFSRSnpyyivk 140
Cdd:COG4637 78 RLELEFAEEDERDLRYELELGLPEPGGRPEVKEERLWLKR--GSGGRPFLDFRPKGR--AVGGEPERLDSPES------- 146
|
170 180 190
....*....|....*....|....*....|..
gi 74216698 141 qgKINQMATAPDSQRLKLLRE-VAGTRVYDER 171
Cdd:COG4637 147 --LLSQLGDPERFPELRALREaLRSWRFYDFH 176
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-350 |
1.99e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 1 MYIKQVIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQFVL-SDEFSHLRPEQRLALLHEGTGPRVISAFVE 79
Cdd:PRK03918 1 MKIEELKIKNFRSHKSSVV--EFDDGINLIIGQNGSGKSSILEAILVGLyWGHGSKPKGLKKDDFTRIGGSGTEIELKFE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 80 iiFDNSDNRL--PIDKEEVSLRRVIGAKKdqyfLDKKMVTKNDVMNLLESAGFSRSNPYyiVKQGKINQMATApDSQRLK 157
Cdd:PRK03918 79 --KNGRKYRIvrSFNRGESYLKYLDGSEV----LEEGDSSVREWVERLIPYHVFLNAIY--IRQGEIDAILES-DESREK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 158 LLREVAGTRVYDERKEESISLMKETEGKREKINELLKY---IEERLHTLEEEKEELAQ------------YQKWDKMRRA 222
Cdd:PRK03918 150 VVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRtenIEELIKEKEKELEEVLReineisselpelREELEKLEKE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 223 L-EYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKtKISAMKEEKEQLSAERQEQIKQ 301
Cdd:PRK03918 230 VkELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDE 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 74216698 302 RTKLELKAKDLQDELAGNSEQRKRL---LKERQKLLEKIEEKQKELAETEPK 350
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKELeekEERLEELKKKLKELEKRLEELEER 360
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-191 |
2.53e-09 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 56.35 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 6 VIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLH---EGTGPRVISAFVEIIF 82
Cdd:pfam13476 1 LTIENFRSFRDQTI--DFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKgdiRIGLEGKGKAYVEITF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 83 DNSDNR-LPIDKEEVSLRRVIGAKKDQYFLDKKMVTKNDVMNLLESAGFSRSNPYYI-VKQGKINQMATAPDSQRLKLLR 160
Cdd:pfam13476 79 ENNDGRyTYAIERSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKIILPLLVfLGQEREEEFERKEKKERLEELE 158
|
170 180 190
....*....|....*....|....*....|.
gi 74216698 161 EVAGTRVYDERKEESISLMKETEGKREKINE 191
Cdd:pfam13476 159 KALEEKEDEKKLLEKLLQLKEKKKELEELKE 189
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
1-65 |
9.37e-09 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 55.77 E-value: 9.37e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74216698 1 MYIKQVIIQGFRSYRDQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALL 65
Cdd:COG3950 1 MRIKSLTIENFRGFEDLEIDFDNPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLL 65
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
1-57 |
1.46e-08 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 55.55 E-value: 1.46e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 74216698 1 MYIKQVIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQFvlsdeFSHLR 57
Cdd:PRK00064 1 MYLTRLSLTDFRNYEELDL--ELSPGVNVLVGENGQGKTNLLEAIYL-----LAPGR 50
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1-296 |
1.86e-08 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 55.30 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 1 MYIKQVIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHEGTGPRVISA--FV 78
Cdd:pfam13175 1 MKIKSIIIKNFRCLKDTEI--DLDEDLTVLIGKNNSGKSSILEALDIFLNNKEKFFEDDFLVLYLKDVIKIDKEDLniFE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 79 EIIFD-----------NSDNRLPIDKEEVSLRRVIGAKKDQYFLDKKMVTKNDVMNLLESAGFsrsnpYYIVKQGKINQM 147
Cdd:pfam13175 79 NISFSidieidvefllILFGYLEIKKKYLCLASKGKAKEYEKTLHPKGANKADLLLELKISDL-----KKYLKQFKIYIY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 148 ATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTI 227
Cdd:pfam13175 154 NNYYLDEKKNVFDKKSKYELPSLKEEFLNSEKEEIKVDKEDLKKLINELEKSINYHENVLENLQIKKLLISADRNASDED 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74216698 228 YNQELN----ETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQ 296
Cdd:pfam13175 234 SEKINSllgaLKQRIFEEALQEELELTEKLKETQNKLKEIDKTLAEELKNILFKKIDKLKDFGYPPFLNPEIE 306
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
230-348 |
5.33e-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: 54.68 E-value: 5.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 230 QELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKA 309
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
90 100 110
....*....|....*....|....*....|....*....
gi 74216698 310 KDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETE 348
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
3-214 |
1.29e-07 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 52.74 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 3 IKQVIIQGFRSYRDQTIVDPFSSKH-----NVIVGRNGSGKSNFFYAIQFVLS-DEFSHLRPEQRLALLHEGTGPRVISA 76
Cdd:COG1106 2 LISFSIENFRSFKDELTLSMVASGLrllrvNLIYGANASGKSNLLEALYFLRNlVLNSSQPGDKLVEPFLLDSESKNEPS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 77 FVEIIFDNSDNRLPIdKEEVSLRRVIgaKKDQYFLdkkmvtkndvmnlleSAGFSRSNPYYIvkqgkinqmatapdsqrl 156
Cdd:COG1106 82 EFEILFLLDGVRYEY-GFELDKERII--SEWLYFL---------------STAAQLNVPLLS------------------ 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74216698 157 KLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIE---ERLHTLEEEKEELAQYQ 214
Cdd:COG1106 126 PLYDWFDNNISLDTSSDGLTLLLKEDESLKEELLELLKIADpgiEDIEVEEEEIEDLVERK 186
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
180-353 |
1.91e-07 |
|
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: 52.46 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 180 KETEGKREKINELLKYIEERLHTLEEEKEELA-QYQKWDKMRRALEYTI--YNQELNETRAKLDELSAKRETSGEK---- 252
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLkQLAALERRIAALARRIraLEQELAALEAELAELEKEIAELRAEleaq 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 253 ----SRQLRDAQQDAR----------DKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAG 318
Cdd:COG4942 103 keelAELLRALYRLGRqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190
....*....|....*....|....*....|....*
gi 74216698 319 NSEQRKRLLKERQkllekieEKQKELAETEPKFNS 353
Cdd:COG4942 183 LEEERAALEALKA-------ERQKLLARLEKELAE 210
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
169-346 |
2.74e-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: 52.37 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 169 DERKEESISLMKETEGKREKINELlkyiEERLHTLEEEKEELAQYQKwdkmRRALEYTIYNQELNETRAKLDELSAKRET 248
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISAL----RKDLARLEAEVEQLEERIA----QLSKELTELEAEIEELEERLEEAEEELAE 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 249 SGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLK 328
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
170
....*....|....*...
gi 74216698 329 ERQKLLEKIEEKQKELAE 346
Cdd:TIGR02168 860 EIEELEELIEELESELEA 877
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
186-348 |
2.90e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 186 REKInELLKYIEERLHTLEEEKEELAQyqkWDKMRRALEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARD 265
Cdd:COG4913 248 REQI-ELLEPIRELAERYAAARERLAE---LEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALRE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 266 KMEDIERQVR--------ELKTKISAMKEEKEQLSAERQEQIKQRTKLELKA------------------KDLQDELAGN 319
Cdd:COG4913 324 ELDELEAQIRgnggdrleQLEREIERLERELEERERRRARLEALLAALGLPLpasaeefaalraeaaallEALEEELEAL 403
|
170 180
....*....|....*....|....*....
gi 74216698 320 SEQRKRLLKERQKLLEKIEEKQKELAETE 348
Cdd:COG4913 404 EEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
170-349 |
4.14e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 170 ERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELA---------QYQKWDKMRRALEYTIYNQE--LNETRAK 238
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNdlearlshsRIPEIQAELSKLEEEVSRIEarLREIEQK 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 239 LDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKE-------QLSAERQEQIKQRTKLELKAKD 311
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEeleaalrDLESRLGDLKKERDELEAQLRE 900
|
170 180 190
....*....|....*....|....*....|....*...
gi 74216698 312 LQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEP 349
Cdd:TIGR02169 901 LERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIED 938
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
180-348 |
4.81e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 4.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 180 KETEGKREKINELLKYIEERLHTLEEEKEELAQyqKWDKMRRALEYTiyNQELNETRAKLDELSAKRETSGEK-SRQLRD 258
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNE--EYNELQAELEAL--QAEIDKLQAEIAEAEAEIEERREElGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 259 AQQ------------------DARDKMEDIER-------QVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQ 313
Cdd:COG3883 95 LYRsggsvsyldvllgsesfsDFLDRLSALSKiadadadLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190
....*....|....*....|....*....|....*
gi 74216698 314 DELAGNSEQRKRLLKERQKLLEKIEEKQKELAETE 348
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
2-47 |
5.01e-07 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 50.92 E-value: 5.01e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 74216698 2 YIKQVIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQF 47
Cdd:COG1195 1 RLKRLSLTNFRNYESLEL--EFSPGINVLVGPNGQGKTNLLEAIYL 44
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
234-348 |
5.54e-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: 51.60 E-value: 5.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 234 ETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKIsamkEEKEQLSAERQEQIKqrtKLELKAKDLQ 313
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL----EELSRQISALRKDLA---RLEAEVEQLE 746
|
90 100 110
....*....|....*....|....*....|....*
gi 74216698 314 DELAGNSEQRKRLLKERQKLLEKIEEKQKELAETE 348
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAE 781
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
170-343 |
6.22e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 6.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 170 ERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQyqKWDKMRRALEYTIYNQELNETRAKLDELSAKRETS 249
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELRE--ELEKLEKLLQLLPLYQELEALEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 250 GEKSRQLRDAQQDardkMEDIERQVRELKTKISAMKEEKEQLSAER-QEQIKQRTKLELKAKDLQDELAGNSEQRKRLLK 328
Cdd:COG4717 152 EERLEELRELEEE----LEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170
....*....|....*
gi 74216698 329 ERQKLLEKIEEKQKE 343
Cdd:COG4717 228 ELEQLENELEAAALE 242
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
143-350 |
6.74e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 6.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 143 KINQMATAPDSQRLKLLREVAGTRVYDE-RKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRR 221
Cdd:PTZ00121 1535 KADEAKKAEEKKKADELKKAEELKKAEEkKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK 1614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 222 ALEYTIYNQEL---NETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQlSAERQEQ 298
Cdd:PTZ00121 1615 AEEAKIKAEELkkaEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED-EKKAAEA 1693
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 74216698 299 IKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPK 350
Cdd:PTZ00121 1694 LKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK 1745
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1-346 |
1.02e-06 |
|
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: 50.74 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 1 MYIKQVIIQGFRSYRDQTIVDPFSSKHN-VIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHEGTGPRVISAFVE 79
Cdd:TIGR00618 1 MKPLRLTLKNFGSYKGTHTIDFTALGPIfLICGKTGAGKTTLLDAITYALYGKLPRRSEVIRSLNSLYAAPSEAAFAELE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 80 IIFDNSDNRLPI---------DKEEVSLRRVIGAKKDQYFLDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKINQMATA 150
Cdd:TIGR00618 81 FSLGTKIYRVHRtlrctrshrKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKTFTRVVLLPQGEFAQFLKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 151 PDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKI-----------NELLKYIEERLHTLEEEKEELAQYQKwdKM 219
Cdd:TIGR00618 161 KSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLtlrsqlltlctPCMPDTYHERKQVLEKELKHLREALQ--QT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 220 RRALEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKME----------------DIERQVRELKTKISA 283
Cdd:TIGR00618 239 QQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINrarkaaplaahikavtQIEQQAQRIHTELQS 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74216698 284 MKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAgnSEQRKRLLKERQKLLEKIEEKQKELAE 346
Cdd:TIGR00618 319 KMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHS--QEIHIRDAHEVATSIREISCQQHTLTQ 379
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
3-58 |
1.22e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 48.37 E-value: 1.22e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 74216698 3 IKQVIIQGFRSYRDQTIVDpFSSKHNVIVGRNGSGKSNFFYAIQFVLsdeFSHLRP 58
Cdd:cd03240 1 IDKLSIRNIRSFHERSEIE-FFSPLTLIVGQNGAGKTTIIEALKYAL---TGELPP 52
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
186-353 |
1.24e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 186 REKINEL---LKYIEERLHTLEEEKEEL-AQYQKWDKMRRAL----EYTIYNQELNETRAKLDELSAKR---ETSGEKSR 254
Cdd:COG4913 609 RAKLAALeaeLAELEEELAEAEERLEALeAELDALQERREALqrlaEYSWDEIDVASAEREIAELEAELerlDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 255 QLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQE---------QIKQRTKLELKAKDLQDELAGNSEQ--R 323
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDElqdrleaaeDLARLELRALLEERFAAALGDAVERelR 768
|
170 180 190
....*....|....*....|....*....|
gi 74216698 324 KRLLKERQKLLEKIEEKQKELAETEPKFNS 353
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
179-349 |
1.54e-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: 49.38 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 179 MKETEGKREKINELLKYIEERLHTLEEEKEEL-AQYQKWDKMRRALEYTIY-------------NQELNETRAKLDELSA 244
Cdd:COG4942 64 IAALARRIRALEQELAALEAELAELEKEIAELrAELEAQKEELAELLRALYrlgrqpplalllsPEDFLDAVRRLQYLKY 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 245 KRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRK 324
Cdd:COG4942 144 LAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
170 180
....*....|....*....|....*
gi 74216698 325 RLlkerQKLLEKIEEKQKELAETEP 349
Cdd:COG4942 224 EL----EALIARLEAEAAAAAERTP 244
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
140-348 |
1.65e-06 |
|
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: 50.06 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 140 KQGKINQMATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQyqkwdkm 219
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEA------- 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 220 rralEYTIYNQELNETRAKLDELSAKretsgekSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQI 299
Cdd:TIGR02168 790 ----QIEQLKEELKALREALDELRAE-------LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 74216698 300 KQRTKLELKAKDLQDELagnseqrKRLLKERQKLLEKIEEKQKELAETE 348
Cdd:TIGR02168 859 AEIEELEELIEELESEL-------EALLNERASLEEALALLRSELEELS 900
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
258-346 |
1.84e-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: 49.38 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 258 DAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKI 337
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
....*....
gi 74216698 338 EEKQKELAE 346
Cdd:COG4942 100 EAQKEELAE 108
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
172-348 |
3.04e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 172 KEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQkwdkmrraleytiynQELNETRAKLDELSAKRETSGE 251
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQ---------------EELEELEEELEELEAELEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 252 KSRQLRDAQQ---------DARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDL----QDELAG 318
Cdd:COG4717 117 ELEKLEKLLQllplyqeleALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLslatEEELQD 196
|
170 180 190
....*....|....*....|....*....|
gi 74216698 319 NSEQRKRLLKERQKLLEKIEEKQKELAETE 348
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELE 226
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
150-343 |
3.37e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 150 APDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEytiyn 229
Cdd:PTZ00121 1583 AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE----- 1657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 230 qelnETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQ------VRELKTKISAMKEEKEQLSAERQE---QIK 300
Cdd:PTZ00121 1658 ----ENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEaeeakkAEELKKKEAEEKKKAEELKKAEEEnkiKAE 1733
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 74216698 301 QRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKE 343
Cdd:PTZ00121 1734 EAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
267-348 |
3.66e-06 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 48.92 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 267 MEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRtklELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAE 346
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKEQDEASFERLAELRDE---LAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPE 489
|
..
gi 74216698 347 TE 348
Cdd:COG0542 490 LE 491
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1-310 |
5.73e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 5.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 1 MYIKQVIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFshlrpEQRLALLHEGTGPRVISAFVEI 80
Cdd:COG4717 1 MKIKELEIYGFGKFRDRTI--EFSPGLNVIYGPNEAGKSTLLAFIRAMLLERL-----EKEADELFKPQGRKPELNLKEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 81 ifdnsdnrlpidKEEVSLRRVIGAKKDQYfldkkmvtkndvmnllesagfsrsnpyyivkQGKINQMATApdSQRLKLLR 160
Cdd:COG4717 74 ------------KELEEELKEAEEKEEEY-------------------------------AELQEELEEL--EEELEELE 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 161 EVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKwdkmrralEYTIYNQELNETRAKLD 240
Cdd:COG4717 109 AELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEE--------ELEELEAELAELQEELE 180
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 241 ELsaKRETSGEKSRQLRDAQQDArdkmEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAK 310
Cdd:COG4717 181 EL--LEQLSLATEEELQDLAEEL----EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
169-339 |
6.16e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 169 DERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEelaqYQKWDKMRRALEYTiyNQELNETRAKLDELSAKRET 248
Cdd:COG4913 630 EERLEALEAELDALQERREALQRLAEYSWDEIDVASAERE----IAELEAELERLDAS--SDDLAALEEQLEELEAELEE 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 249 SGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAM----KEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRK 324
Cdd:COG4913 704 LEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAedlaRLELRALLEERFAAALGDAVERELRENLEERIDALRARLN 783
|
170
....*....|....*
gi 74216698 325 RLlkeRQKLLEKIEE 339
Cdd:COG4913 784 RA---EEELERAMRA 795
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
183-350 |
1.06e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 183 EGKREKINELLKYIEERLHTLEEEKEE----LAQY-QKWDKMRRALEYTIYNQELNETRAKLDELSAKRETSGEKSRQLR 257
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEaeaaLEEFrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 258 DAQQDARDKMEDIER--QVRELKTKISAMKEEKEQLSA-------ERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLK 328
Cdd:COG3206 247 AQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQRILASLEAELEALQ 326
|
170 180
....*....|....*....|..
gi 74216698 329 ERQKLLEKIEEKQKELAETEPK 350
Cdd:COG3206 327 AREASLQAQLAQLEARLAELPE 348
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
143-346 |
1.72e-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: 46.59 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 143 KINQMATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEEL------------ 210
Cdd:TIGR02168 741 EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELraeltllneeaa 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 211 ----------AQYQKWDKMRRALEYTI---------YNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIE 271
Cdd:TIGR02168 821 nlrerlesleRRIAATERRLEDLEEQIeelsediesLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74216698 272 RQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELagnSEQRKRLLKERQKLLEKIEEKQKELAE 346
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL---SEEYSLTLEEAEALENKIEDDEEEARR 972
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
181-350 |
2.25e-05 |
|
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: 45.30 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 181 ETEGKREKINELLKYIEERLHTLEEEKEELAQyqkwdkmrralEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQ 260
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEA-----------RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 261 QDARD--KMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIE 338
Cdd:COG1579 83 GNVRNnkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
170
....*....|..
gi 74216698 339 EKQKELAETEPK 350
Cdd:COG1579 163 AEREELAAKIPP 174
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
263-348 |
3.94e-05 |
|
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: 45.14 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 263 ARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQK 342
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
....*.
gi 74216698 343 ELAETE 348
Cdd:COG4942 98 ELEAQK 103
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
154-351 |
4.56e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 154 QRLKLLREVAGTRVYDERKEESISLmketEGKREKINELLKYIEERLHTLEEEKEELAQyqkwdkMRRALEYTIYN---- 229
Cdd:COG4913 269 ERLAELEYLRAALRLWFAQRRLELL----EAELEELRAELARLEAELERLEARLDALRE------ELDELEAQIRGnggd 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 230 ------QELNETRAKLDELSAKREtsgEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRT 303
Cdd:COG4913 339 rleqleREIERLERELEERERRRA---RLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR 415
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 74216698 304 KLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKeLAETEPKF 351
Cdd:COG4913 416 DLRRELRELEAEIASLERRKSNIPARLLALRDALAEALG-LDEAELPF 462
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
186-346 |
5.65e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 186 REKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTI-YNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDAR 264
Cdd:COG1340 115 RKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKKALeKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELH 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 265 DKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKllEKIEEKQKEL 344
Cdd:COG1340 195 EEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEK--EELEEKAEEI 272
|
..
gi 74216698 345 AE 346
Cdd:COG1340 273 FE 274
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
139-348 |
5.85e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 139 VKQGKINQMATAPDSQR------------LKLLREVAGT------RVYDERKEESISLMKETEGKREK-INELLKYIEER 199
Cdd:PRK02224 135 VRQGEVNKLINATPSDRqdmiddllqlgkLEEYRERASDarlgveRVLSDQRGSLDQLKAQIEEKEEKdLHERLNGLESE 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 200 LHTLEEEKEEL-AQYQKWDKMRRALEYTIynQELNETRAKLDELSA--------------KRETSGEKSRQLRDAQQDAR 264
Cdd:PRK02224 215 LAELDEEIERYeEQREQARETRDEADEVL--EEHEERREELETLEAeiedlretiaeterEREELAEEVRDLRERLEELE 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 265 DKMED--------------IERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKER 330
Cdd:PRK02224 293 EERDDllaeaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESEL 372
|
250
....*....|....*...
gi 74216698 331 QKLLEKIEEKQKELAETE 348
Cdd:PRK02224 373 EEAREAVEDRREEIEELE 390
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
1-100 |
7.16e-05 |
|
recF protein; All proteins in this family for which functions are known are DNA binding proteins that assist the filamentation of RecA onto DNA for the initiation of recombination or recombinational repair. 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: 273173 [Multi-domain] Cd Length: 365 Bit Score: 44.27 E-value: 7.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 1 MYIKQVIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIqFVLSDEFSHlRPEQRLALLHEGTgPRvisAFVEI 80
Cdd:TIGR00611 1 MYLSRLELTDFRNYDAVDL--ELSPGVNVIVGPNGQGKTNLLEAI-YYLALGRSH-RTSRDKPLIRFGA-EA---FVIEG 72
|
90 100
....*....|....*....|
gi 74216698 81 IFDNSDNRLPIDKEEVSLRR 100
Cdd:TIGR00611 73 RVSKGDREVTIPLEGLLKKK 92
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
11-79 |
7.88e-05 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases with a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213209 [Multi-domain] Cd Length: 270 Bit Score: 43.83 E-value: 7.88e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74216698 11 FRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQFvLSDEFSHLRPEQRlALLHEGTGPRVISAFVE 79
Cdd:cd03242 9 FRNYAELEL--EFEPGVTVLVGENAQGKTNLLEAISL-LATGKSHRTSRDK-ELIRWGAEEAKISAVLE 73
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
8-346 |
8.28e-05 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 44.34 E-value: 8.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 8 IQGFRSYRDQTIVDPFSSKhNVIVGRNGSGK---SNFFYAIQfvLSDEFSHLRPEQRLALLHEGTGPRVI---SAFVEII 81
Cdd:COG4694 8 LKNVGAFKDFGWLAFFKKL-NLIYGENGSGKstlSRILRSLE--LGDTSSEVIAEFEIEAGGSAPNPSVRvfnRDFVEEN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 82 FDNSDNRLPI----------DKEEVSLRRVIGAKKDQYF------------LDKKMVTKNDVM-NLLESAGFSRSNPYYI 138
Cdd:COG4694 85 LRSGEEIKGIftlgeenielEEEIEELEKEIEDLKKELDklekelkeakkaLEKLLEDLAKSIkDDLKKLFASSGRNYRK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 139 VK-QGKINQMATAPDSQ---RLKLLREVAGTRVYDERKEESIS---------LMKETEGKREK--------------INE 191
Cdd:COG4694 165 ANlEKKLSALKSSSEDElkeKLKLLKEEEPEPIAPITPLPDLKallseaetlLEKSAVSSAIEelaaliqnpgnsdwVEQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 192 LLKYI----------------EERLHTLEE--------EKEELAQYQKW--------DKMRRALEYTIYNQELNETRAKL 239
Cdd:COG4694 245 GLAYHkeeeddtcpfcqqelaAERIEALEAyfddeyekLLAALKDLLEElesainalSALLLEILRTLLPSAKEDLKAAL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 240 DELSAKRETS----GEKSRQLRDAQQ-DARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELkaKDLQD 314
Cdd:COG4694 325 EALNALLETLlaalEEKIANPSTSIDlDDQELLDELNDLIAALNALIEEHNAKIANLKAEKEEARKKLEAHEL--AELKE 402
|
410 420 430
....*....|....*....|....*....|....*
gi 74216698 315 ELAGNSEQRKRLLKERQ---KLLEKIEEKQKELAE 346
Cdd:COG4694 403 DLSRYKAEVEELIEELKtikALKKALEDLKTEISE 437
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
197-348 |
8.66e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 8.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 197 EERLHTLEEEKEELAQyqkwdkmrraleytiynqELNETRAKLDELSAKRETSGEKSRqLRDAQQDARDKMEDIERQVRE 276
Cdd:PRK02224 474 RERVEELEAELEDLEE------------------EVEEVEERLERAEDLVEAEDRIER-LEERREDLEELIAERRETIEE 534
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74216698 277 LKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAgNSEQRKRLLKERQKLLEKIEEKQKELAETE 348
Cdd:PRK02224 535 KRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVA-ELNSKLAELKERIESLERIRTLLAAIADAE 605
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
168-348 |
8.81e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 8.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 168 YDERKEESISLMKETEGKREKINELLKYIE---ERLHTLEEEKEELAQyqKWDKMRRALEYTIYNQELNETRakLDELSA 244
Cdd:PRK02224 246 HEERREELETLEAEIEDLRETIAETEREREelaEEVRDLRERLEELEE--ERDDLLAEAGLDDADAEAVEAR--REELED 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 245 KRETSGEKSRQLRDAQQDA-------RDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELA 317
Cdd:PRK02224 322 RDEELRDRLEECRVAAQAHneeaeslREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFG 401
|
170 180 190
....*....|....*....|....*....|.
gi 74216698 318 GNSEQRKRLLKERQKLLEKIEEKQKELAETE 348
Cdd:PRK02224 402 DAPVDLGNAEDFLEELREERDELREREAELE 432
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
169-350 |
9.05e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 9.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 169 DERKEESISLMKETEGKREKINELlkyiEERLHTLEEEKEEL-AQYQKWDKMRRALEY--TIYNQELNETRAKLDELSAK 245
Cdd:PRK02224 359 EELREEAAELESELEEAREAVEDR----REEIEELEEEIEELrERFGDAPVDLGNAEDflEELREERDELREREAELEAT 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 246 RET---SGEKSRQLRDAQQ------------------DARDKMEDIERQVRELKTKISAMKEEKEQLSaERQEQIKQRTK 304
Cdd:PRK02224 435 LRTareRVEEAEALLEAGKcpecgqpvegsphvetieEDRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIER 513
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 74216698 305 LELKAKDLQDELAgnsEQRKRLLKERQKLLEKIEEKQKELAETEPK 350
Cdd:PRK02224 514 LEERREDLEELIA---ERRETIEEKRERAEELRERAAELEAEAEEK 556
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
229-348 |
1.22e-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: 43.60 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 229 NQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELK 308
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74216698 309 AKDLQDELAG-------NSEQR---------------------KRLLKERQKLLEKIEEKQKELAETE 348
Cdd:COG4942 99 LEAQKEELAEllralyrLGRQPplalllspedfldavrrlqylKYLAPARREQAEELRADLAELAALR 166
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
169-346 |
1.41e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 169 DERKEESISLMKETEGKREKINELL----------KYIEERLHTLEEEKEELAqyqkwdkmRRALEYTIYNQELNETRAK 238
Cdd:PRK02224 275 EELAEEVRDLRERLEELEEERDDLLaeaglddadaEAVEARREELEDRDEELR--------DRLEECRVAAQAHNEEAES 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 239 LDELSAKREtsgEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAG 318
Cdd:PRK02224 347 LREDADDLE---ERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDE 423
|
170 180
....*....|....*....|....*...
gi 74216698 319 NSEQRKRLLKERQKLLEKIEEKQKELAE 346
Cdd:PRK02224 424 LREREAELEATLRTARERVEEAEALLEA 451
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
166-346 |
1.55e-04 |
|
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: 43.67 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 166 RVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETR-AKLDELSA 244
Cdd:pfam12128 657 RLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALdAQLALLKA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 245 KREtsgeKSRQLRDAQQDA---------------RDKMEDIERQVRELKTKISAMKEEK-----------EQLSAERQEQ 298
Cdd:pfam12128 737 AIA----ARRSGAKAELKAletwykrdlaslgvdPDVIAKLKREIRTLERKIERIAVRRqevlryfdwyqETWLQRRPRL 812
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 74216698 299 IKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAE 346
Cdd:pfam12128 813 ATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSE 860
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
168-350 |
1.76e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 168 YDERKEESISLMKETEGKREKINELLKYIEErlhtLEEEKEELAQYQKwdkmrraleytiynqELNETRAKLDEL-SAKR 246
Cdd:PRK03918 319 LEEEINGIEERIKELEEKEERLEELKKKLKE----LEKRLEELEERHE---------------LYEEAKAKKEELeRLKK 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 247 ETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDelagnsEQRKRL 326
Cdd:PRK03918 380 RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTE------EHRKEL 453
|
170 180
....*....|....*....|....
gi 74216698 327 LKERQKLLEKIEEKQKELAETEPK 350
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERK 477
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
168-346 |
1.89e-04 |
|
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: 43.40 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 168 YDERKEESISLMKETEGKREKINELLKYIEERLHTLEEE----KEELAQYQKWDKM--RRALEYTIYNQELNETRA--KL 239
Cdd:COG3096 352 YQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEvdslKSQLADYQQALDVqqTRAIQYQQAVQALEKARAlcGL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 240 DELSAKretsgeksrQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSA------------ERQEQIKQRTKLEL 307
Cdd:COG3096 432 PDLTPE---------NAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKayelvckiagevERSQAWQTARELLR 502
|
170 180 190
....*....|....*....|....*....|....*....
gi 74216698 308 KAKDLQdELAGNSEQRKRLLKERQKLLEKIEEKQKELAE 346
Cdd:COG3096 503 RYRSQQ-ALAQRLQQLRAQLAELEQRLRQQQNAERLLEE 540
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
173-344 |
1.91e-04 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 42.29 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 173 EESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIY-----NQELNETRAKLDELSAKRE 247
Cdd:pfam12795 23 QQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQELAALQAKAEAAPKEILASLsleelEQRLLQTSAQLQELQNQLA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 248 TSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIK-QRTKLELKAKDLQDELAGNSEQRKRL 326
Cdd:pfam12795 103 QLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWALQaELAALKAQIDMLEQELLSNNNRQDLL 182
|
170
....*....|....*...
gi 74216698 327 LKERQKLLEKIEEKQKEL 344
Cdd:pfam12795 183 KARRDLLTLRIQRLEQQL 200
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
261-348 |
2.37e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 261 QDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKL---------ELKAKDLQDELAGNSEQRKRLLK--- 328
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALqrlaeyswdEIDVASAEREIAELEAELERLDAssd 685
|
90 100
....*....|....*....|
gi 74216698 329 ERQKLLEKIEEKQKELAETE 348
Cdd:COG4913 686 DLAALEEQLEELEAELEELE 705
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
170-348 |
2.41e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 170 ERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAqyqkwdkmrraleytiynqelnETRAKLDELSAKRETS 249
Cdd:PRK02224 499 ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAE----------------------ELRERAAELEAEAEEK 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 250 GEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLsAERQEQIKQRTKLELKAKDLQDElagNSEQRKRL--L 327
Cdd:PRK02224 557 REAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLL-AAIADAEDEIERLREKREALAEL---NDERRERLaeK 632
|
170 180
....*....|....*....|....*..
gi 74216698 328 KERQKLLE------KIEEKQKELAETE 348
Cdd:PRK02224 633 RERKRELEaefdeaRIEEAREDKERAE 659
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
180-350 |
2.91e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 180 KETEGKREKInelLKYIEERLHTLEEEKEeLAQYQKWDKMRRALEytiynQELNETRAKLDELsakretsgeksrqlrda 259
Cdd:PRK12704 34 KEAEEEAKRI---LEEAKKEAEAIKKEAL-LEAKEEIHKLRNEFE-----KELRERRNELQKL----------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 260 QQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDEL---AGNS--EQRKRLLK------ 328
Cdd:PRK12704 88 EKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELeriSGLTaeEAKEILLEkveeea 167
|
170 180
....*....|....*....|....
gi 74216698 329 --ERQKLLEKIEEKQKELAETEPK 350
Cdd:PRK12704 168 rhEAAVLIKEIEEEAKEEADKKAK 191
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
172-353 |
3.00e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 172 KEESISLMKEtegKREKINELLKYIEERLHTLEEEKEELAQ--------YQKWDKMRRALEYTiyNQELNETrakLDELS 243
Cdd:pfam01576 10 KEEELQKVKE---RQQKAESELKELEKKHQQLCEEKNALQEqlqaetelCAEAEEMRARLAAR--KQELEEI---LHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 244 AKRETSGEKSRQLRDAQQDARDKMEDIERQVRElktkisamkEEkeqlsAERQEQIKQRTKLELKAKDLQDELAGNSEQR 323
Cdd:pfam01576 82 SRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDE---------EE-----AARQKLQLEKVTTEAKIKKLEEDILLLEDQN 147
|
170 180 190
....*....|....*....|....*....|
gi 74216698 324 KRLLKERQKLLEKIEEKQKELAETEPKFNS 353
Cdd:pfam01576 148 SKLSKERKLLEERISEFTSNLAEEEEKAKS 177
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
227-326 |
3.35e-04 |
|
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: 42.80 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 227 IYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLE 306
Cdd:pfam15921 304 IQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLL 383
|
90 100
....*....|....*....|
gi 74216698 307 LKAKDLQDELAGNSEQRKRL 326
Cdd:pfam15921 384 ADLHKREKELSLEKEQNKRL 403
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
28-94 |
3.68e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 41.99 E-value: 3.68e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74216698 28 NVIVGRNGSGKSNFFYAIQFvLSDEFSHLRPEQRLALLHEGTGprvisaFVEIIFDNSDNRLPIDKE 94
Cdd:pfam13304 2 NVLIGPNGSGKSNLLEALRF-LADFDALVIGLTDERSRNGGIG------GIPSLLNGIDPKEPIEFE 61
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
187-347 |
4.51e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 187 EKINELLKYIEERLHTLEEEKEELAQyqkwdkmrraleytiynqELNETRAKLDELSAKREtsgeksrqlrdAQQDARDK 266
Cdd:PRK00409 516 EKLNELIASLEELERELEQKAEEAEA------------------LLKEAEKLKEELEEKKE-----------KLQEEEDK 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 267 MedIERQVRELKTKISAMKEEKEQLSAERQEQIKQrTKLELKAKDLQDElagnseqrKRLLKERQKLLEKIEEKQKELAE 346
Cdd:PRK00409 567 L--LEEAEKEAQQAIKEAKKEADEIIKELRQLQKG-GYASVKAHELIEA--------RKRLNKANEKKEKKKKKQKEKQE 635
|
.
gi 74216698 347 T 347
Cdd:PRK00409 636 E 636
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
170-343 |
4.76e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.36 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 170 ERKEESISLMKE-TEGKREKINELLKYIEERLHTLEEEKEELaQYQKWDKMRRALEYtiyNQELNETRAKLDELSAKRET 248
Cdd:TIGR02169 818 EQKLNRLTLEKEyLEKEIQELQEQRIDLKEQIKSIEKEIENL-NGKKEELEEELEEL---EAALRDLESRLGDLKKERDE 893
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 249 SGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEE---------------KEQLSAERQEQIKQRTKLELKA---- 309
Cdd:TIGR02169 894 LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEElseiedpkgedeeipEEELSLEDVQAELQRVEEEIRAlepv 973
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 74216698 310 --------KDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKE 343
Cdd:TIGR02169 974 nmlaiqeyEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
179-322 |
4.80e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 179 MKETEGKREKINELLKYIEERLHTLEEEKEELAQYQ------------------------KWDKMRRALEYTiyNQELNE 234
Cdd:COG3883 60 LEALQAEIDKLQAEIAEAEAEIEERREELGERARALyrsggsvsyldvllgsesfsdfldRLSALSKIADAD--ADLLEE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 235 TRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQD 314
Cdd:COG3883 138 LKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
....*...
gi 74216698 315 ELAGNSEQ 322
Cdd:COG3883 218 AAAAAAAA 225
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
205-353 |
4.88e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 205 EEKEELAQYQ-KWDKMRRALEYTIynQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISA 283
Cdd:TIGR02169 671 SEPAELQRLReRLEGLKRELSSLQ--SELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74216698 284 MKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAG-----NSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNS 353
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDlearlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR 823
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
148-346 |
5.48e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.96 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 148 ATAPDSQRLKL-LREVAGTRVYDERK-----EESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQyqKWDKMRR 221
Cdd:PRK10929 20 ATAPDEKQITQeLEQAKAAKTPAQAEivealQSALNWLEERKGSLERAKQYQQVIDNFPKLSAELRQQLNN--ERDEPRS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 222 A---LEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDA-------QQDARDKMEDIERQVRELKTKISAMKE----- 286
Cdd:PRK10929 98 VppnMSTDALEQEILQVSSQLLEKSRQAQQEQDRAREISDSlsqlpqqQTEARRQLNEIERRLQTLGTPNTPLAQaqlta 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74216698 287 ---------------EKEQLSAE-RQEQIKQRTKL-ELKAKDLQDELagnSEQRKRLLKERQKLLEKIEEKQKELAE 346
Cdd:PRK10929 178 lqaesaalkalvdelELAQLSANnRQELARLRSELaKKRSQQLDAYL---QALRNQLNSQRQREAERALESTELLAE 251
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1-262 |
5.74e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 1 MYIKQVIIQGFRSYRDQTIVdpFSSKHNVIVGRNGSGKSNFFYAIQFVLsdeFSHLRPEQRLALLHEGTGPRVISAFVEI 80
Cdd:PRK01156 1 MIIKRIRLKNFLSHDDSEIE--FDTGINIITGKNGAGKSSIVDAIRFAL---FTDKRTEKIEDMIKKGKNNLEVELEFRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 81 IFDNSDNRLPIDKEEVSLRRVIGAKKDQYFLDKKMvtkNDVMNLLESAGFSRSNPYYI----VKQGKINQMATAPDSQRL 156
Cdd:PRK01156 76 GGHVYQIRRSIERRGKGSRREAYIKKDGSIIAEGF---DDTTKYIEKNILGISKDVFLnsifVGQGEMDSLISGDPAQRK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 157 KLLREVAG----TRVYDERKEESISLMKETEGKREKINELLKYIEErlhtLEEEKEELAQYQKW------DKMRRALEYT 226
Cdd:PRK01156 153 KILDEILEinslERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLE----LENIKKQIADDEKShsitlkEIERLSIEYN 228
|
250 260 270
....*....|....*....|....*....|....*.
gi 74216698 227 IYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQD 262
Cdd:PRK01156 229 NAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESD 264
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
170-350 |
5.98e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 170 ERKEESISLMKETEGKReKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKLDELSAKRETS 249
Cdd:PTZ00121 1454 EEAKKAEEAKKKAEEAK-KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE 1532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 250 GEKSRQLRDAQQ----DARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQ--RTKLELKAKDLQDELAGNSEQR 323
Cdd:PTZ00121 1533 AKKADEAKKAEEkkkaDELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaeEARIEEVMKLYEEEKKMKAEEA 1612
|
170 180
....*....|....*....|....*....
gi 74216698 324 KRLLKERQKL--LEKIEEKQKELAETEPK 350
Cdd:PTZ00121 1613 KKAEEAKIKAeeLKKAEEEKKKVEQLKKK 1641
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
171-343 |
7.62e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.58 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 171 RKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEEL-AQYQKWDKMRRALEytiynQELNETRAKLDELSAKRETS 249
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELeSELEALLNERASLE-----EALALLRSELEELSEELREL 906
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 250 GEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEE-KEQLSAERQEQIKQRTKLELKAKDLQDELA---------GN 319
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARRRLKrlenkikelGP 986
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 74216698 320 -------------------SEQRKRLLKERQKLLEKIEEKQKE 343
Cdd:TIGR02168 987 vnlaaieeyeelkerydflTAQKEDLTEAKETLEEAIEEIDRE 1029
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
183-344 |
8.16e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.03 E-value: 8.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 183 EGKREKINELLKYIEERLHTLEEEKEELAQY-QKWDKMRRALEYTI---------YNQELNETRAKLDELSAKRETSGEK 252
Cdd:pfam07888 37 EECLQERAELLQAQEAANRQREKEKERYKRDrEQWERQRRELESRVaelkeelrqSREKHEELEEKYKELSASSEELSEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 253 SRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQK 332
Cdd:pfam07888 117 KDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQE 196
|
170
....*....|..
gi 74216698 333 LLEKIEEKQKEL 344
Cdd:pfam07888 197 LRNSLAQRDTQV 208
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
169-342 |
9.64e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 9.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 169 DERKEESISLMKETEGKReKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELN---ETRAKLDEL--- 242
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKK-KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKkkaEEAKKADEAkkk 1452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 243 ---SAKRETSGEKSRQLRDAQQ------------DARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLEL 307
Cdd:PTZ00121 1453 aeeAKKAEEAKKKAEEAKKADEakkkaeeakkadEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE 1532
|
170 180 190
....*....|....*....|....*....|....*
gi 74216698 308 KAKdlQDELAGNSEQRKRLLKERQKLLEKIEEKQK 342
Cdd:PTZ00121 1533 AKK--ADEAKKAEEKKKADELKKAEELKKAEEKKK 1565
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
158-347 |
1.23e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 40.61 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 158 LLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKW-DKMRRALE------------ 224
Cdd:pfam06160 279 LEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYTLNENELERVRGLEKQlEELEKRYDeiverleekeva 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 225 YTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKIsamkeEKEQLSAERQEQIKQRTK 304
Cdd:pfam06160 359 YSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLV-----EKSNLPGLPESYLDYFFD 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 74216698 305 LELKAKDLQDELAG---NSEQRKRLLKERQKLLEKIEEKQKELAET 347
Cdd:pfam06160 434 VSDEIEDLADELNEvplNMDEVNRLLDEAQDDVDTLYEKTEELIDN 479
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
171-342 |
1.33e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 171 RKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKM-RRALEYTIYNQELNETRAKLDELSAK---- 245
Cdd:COG3206 203 QKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSgPDALPELLQSPVIQQLRAQLAELEAElael 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 246 RETSGEKS---RQLRDAQQDARDKMED-IERQVRELKTKISAMKEEKEQLSAERQE---QIKQRTKLELKAKDLQDELAG 318
Cdd:COG3206 283 SARYTPNHpdvIALRAQIAALRAQLQQeAQRILASLEAELEALQAREASLQAQLAQleaRLAELPELEAELRRLEREVEV 362
|
170 180
....*....|....*....|....
gi 74216698 319 NSEQRKRLLKERQKLleKIEEKQK 342
Cdd:COG3206 363 ARELYESLLQRLEEA--RLAEALT 384
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
181-343 |
1.35e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 40.32 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 181 ETEGKREKINELLKYIEERLHTLEEEKEELAQYQKwdkmRRALEYTIYNQELNETRAKLDELSAKREtsgeksRQLRDAQ 260
Cdd:pfam15709 349 EVERKRREQEEQRRLQQEQLERAEKMREELELEQQ----RRFEEIRLRKQRLEEERQRQEEEERKQR------LQLQAAQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 261 QDARDKMEDIERQVRELKTKisamkeeKEQLSAERQEQIKQRTKlelkakdlqdelagnsEQRKRLLKERQKLLEKIEEK 340
Cdd:pfam15709 419 ERARQQQEEFRRKLQELQRK-------KQQEEAERAEAEKQRQK----------------ELEMQLAEEQKRLMEMAEEE 475
|
...
gi 74216698 341 QKE 343
Cdd:pfam15709 476 RLE 478
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
146-350 |
1.36e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 146 QMATAPDSQRLKLLREVAGTRVYDERKEESISL----MKETEGKREKINELLKYIEERLHTLEEEK--EELAQYQKWDKM 219
Cdd:PTZ00121 1588 KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIkaeeLKKAEEEKKKVEQLKKKEAEEKKKAEELKkaEEENKIKAAEEA 1667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 220 RRALEYTIYNQEL---NETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQ 296
Cdd:PTZ00121 1668 KKAEEDKKKAEEAkkaEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 74216698 297 EQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPK 350
Cdd:PTZ00121 1748 EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIK 1801
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
239-348 |
1.42e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.61 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 239 LDELSAKRETSGEKSRQLRDAQQDARDKMEdiERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAG 318
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTEE--EEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERR 459
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 74216698 319 NSEQRK----------RLLKERQKLLEKIEEKQKELAETE 348
Cdd:COG2433 460 EIRKDReisrldreieRLERELEEERERIEELKRKLERLK 499
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
229-346 |
1.44e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 39.70 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 229 NQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSA---ERQEQIKQRTKL 305
Cdd:pfam06008 53 AQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSsdlSRMLAEAQRMLG 132
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 74216698 306 ELKAKDLQDELAGNSEQRK---RLLKERQKLLEKIEEKQKELAE 346
Cdd:pfam06008 133 EIRSRDFGTQLQNAEAELKaaqDLLSRIQTWFQSPQEENKALAN 176
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
157-348 |
1.55e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 157 KLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETR 236
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELK 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 237 AKLDELSAKRetsgEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMK-----EEKEQLSAERQEQIKQRTKLELK--- 308
Cdd:PRK03918 609 DAEKELEREE----KELKKLEEELDKAFEELAETEKRLEELRKELEELEkkyseEEYEELREEYLELSRELAGLRAElee 684
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 74216698 309 AKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETE 348
Cdd:PRK03918 685 LEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVE 724
|
|
| MAT1 |
pfam06391 |
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ... |
227-352 |
1.94e-03 |
|
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for cyclin-dependent kinase-activating kinase (CAK), which interacts with the transcription factor TFIIH. The domain found to the N-terminal side of this domain is a C3HC4 RING finger.
Pssm-ID: 461894 [Multi-domain] Cd Length: 202 Bit Score: 39.15 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 227 IYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQ--IKQRTK 304
Cdd:pfam06391 58 TNGIDVEETEKKIEQYEKENKDLILKNKMKLSQEEEELEELLELEKREKEERRKEEKQEEEEEKEKKEKAKQelIDELMT 137
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 74216698 305 LELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFN 352
Cdd:pfam06391 138 SNKDAEEIIAQHKKTAKKRKSERRRKLEELNRVLEQKPTQFSTGIKFG 185
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
173-346 |
2.31e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.89 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 173 EESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYN-----QELNETrakLDELSAKRE 247
Cdd:PRK11281 66 EQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTLSlrqleSRLAQT---LDQLQNAQN 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 248 TSGEKSRQLRDAQ-QDARDKMEDIERQVR--ELKTKISAMKEEKEQLSAERQEQIK-QRTKLELKAKDLQDELAGNS--- 320
Cdd:PRK11281 143 DLAEYNSQLVSLQtQPERAQAALYANSQRlqQIRNLLKGGKVGGKALRPSQRVLLQaEQALLNAQNDLQRKSLEGNTqlq 222
|
170 180 190
....*....|....*....|....*....|....*..
gi 74216698 321 ---EQRKRLLKERQKLLEK--------IEEKQKELAE 346
Cdd:PRK11281 223 dllQKQRDYLTARIQRLEHqlqllqeaINSKRLTLSE 259
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
191-299 |
2.39e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 39.68 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 191 ELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEytiYNQELNETRAKLDELSAKretsGEKSRQLRDAQQDARDKMEDI 270
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKEQDEASFERLAE---LRDELAELEEELEALKAR----WEAEKELIEEIQELKEELEQR 483
|
90 100
....*....|....*....|....*....
gi 74216698 271 ERQVRELKTKISAMKEEKEQLSAERQEQI 299
Cdd:COG0542 484 YGKIPELEKELAELEEELAELAPLLREEV 512
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
143-346 |
2.41e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 143 KINQMATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRA 222
Cdd:PTZ00121 1213 KAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKA 1292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 223 LEYtiynqELNETRAKLDELSAKRETSgEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQR 302
Cdd:PTZ00121 1293 DEA-----KKAEEKKKADEAKKKAEEA-KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 74216698 303 TKLELK---AKDLQDELAGNSEQRKR---LLKERQKLLEKIEEKQKELAE 346
Cdd:PTZ00121 1367 EAAEKKkeeAKKKADAAKKKAEEKKKadeAKKKAEEDKKKADELKKAAAA 1416
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
254-335 |
2.76e-03 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 39.59 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 254 RQLRDAQQDARDKMED------IERQVRELKtkiSAMKEEKEQLsAERQEQIKQRTK-------LELKAKDLQD------ 314
Cdd:pfam13779 489 RRLRAAQERLSEALERgasdeeIAKLMQELR---EALDDYMQAL-AEQAQQNPQDLQqpddpnaQEMTQQDLQRmldrie 564
|
90 100
....*....|....*....|...
gi 74216698 315 ELA--GNSEQRKRLLKERQKLLE 335
Cdd:pfam13779 565 ELArsGRRAEAQQMLSQLQQMLE 587
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
193-297 |
3.08e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 39.28 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 193 LKYIEERLHTLEE------EKEELAQYQKWDKMRRALEytiynqelnetrAKLDELSAKRETSGEKSRQLRDAQQDARDK 266
Cdd:PRK05431 4 IKLIRENPEAVKEalakrgFPLDVDELLELDEERRELQ------------TELEELQAERNALSKEIGQAKRKGEDAEAL 71
|
90 100 110
....*....|....*....|....*....|.
gi 74216698 267 MEdierQVRELKTKISAMKEEKEQLSAERQE 297
Cdd:PRK05431 72 IA----EVKELKEEIKALEAELDELEAELEE 98
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
230-316 |
3.50e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 39.55 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 230 QELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKA 309
Cdd:PRK11448 149 QEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKEITDQAAKR 228
|
....*..
gi 74216698 310 KDLQDEL 316
Cdd:PRK11448 229 LELSEEE 235
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
141-349 |
3.65e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 39.50 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 141 QGKINqmATAPDSQRLKLLREVAGTRVYDER------------KEESISLMKETEGKREKINELlKYIEERLHTLEEEKE 208
Cdd:PLN02939 191 QEKIH--VEILEEQLEKLRNELLIRGATEGLcvhslskeldvlKEENMLLKDDIQFLKAELIEV-AETEERVFKLEKERS 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 209 ELaqyqkwDKMRRALEYT-IYNQE--LNETRAKLDELSAKRETSG----------EKSRQLRDAQQDARDKMEDIERQVR 275
Cdd:PLN02939 268 LL------DASLRELESKfIVAQEdvSKLSPLQYDCWWEKVENLQdlldratnqvEKAALVLDQNQDLRDKVDKLEASLK 341
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74216698 276 ELKTKisamkeekeQLSAERQEQIKQRTK-LELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEP 349
Cdd:PLN02939 342 EANVS---------KFSSYKVELLQQKLKlLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKEESKKRSLEHP 407
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
251-350 |
3.80e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 39.02 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 251 EKSRQlRDAQQDARDKMEDI----ERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRL 326
Cdd:PRK09510 78 EEQRK-KKEQQQAEELQQKQaaeqERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRA 156
|
90 100
....*....|....*....|....
gi 74216698 327 LKERQKLLEkiEEKQKELAETEPK 350
Cdd:PRK09510 157 AAAAKKAAA--EAKKKAEAEAAKK 178
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
13-49 |
4.01e-03 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 37.61 E-value: 4.01e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 74216698 13 SYRDQTIVDPFS-----SKHNVIVGRNGSGKSNFFYAIQFVL 49
Cdd:cd00267 8 RYGGRTALDNVSltlkaGEIVALVGPNGSGKSTLLRAIAGLL 49
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
230-353 |
4.48e-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: 37.98 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 230 QELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSaERQEQI---KQRTKLE 306
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE-EQLGNVrnnKEYEALQ 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 74216698 307 LKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNS 353
Cdd:COG1579 96 KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEE 142
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
143-342 |
4.66e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.97 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 143 KINQMATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKinELLKYIEERLHTLEEEKEELAQYQKWDKMRRA 222
Cdd:PTZ00121 1279 KADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKA--EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAA 1356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 223 LEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQdARDKMEDIERQVRELKTKISAMKEEKEqlSAERQEQIKQR 302
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE-AKKKAEEDKKKADELKKAAAAKKKADE--AKKKAEEKKKA 1433
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 74216698 303 TKLELKAKDLQ--DELAGNSEQRKRllkeRQKLLEKIEEKQK 342
Cdd:PTZ00121 1434 DEAKKKAEEAKkaDEAKKKAEEAKK----AEEAKKKAEEAKK 1471
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
3-59 |
5.85e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 38.03 E-value: 5.85e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 74216698 3 IKQVIIQGFRSYRDQTIvdPFSsKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPE 59
Cdd:COG4938 1 IKSISIKNFGPFKEAEL--ELK-PLTLLIGPNGSGKSTLIQALLLLLQSNFIYLPAE 54
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
146-350 |
7.01e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 38.18 E-value: 7.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 146 QMATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKRE--KINELlkyieerlhtleeEKEELAQYQKWDKMRRAL 223
Cdd:pfam17380 332 QAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEisRMREL-------------ERLQMERQQKNERVRQEL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 224 EYTIYNQELNETRAKldelsaKRETSGEKSRQLRDAQQDARDKMEDI--ERQVRELKTKISAMKEEKEQLSAERQEQIKQ 301
Cdd:pfam17380 399 EAARKVKILEEERQR------KIQQQKVEMEQIRAEQEEARQREVRRleEERAREMERVRLEEQERQQQVERLRQQEEER 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74216698 302 RTKLELKAKDLQDELAGNSEQRKRLLKE-------------RQKLLEK-IEEKQKELAETEPK 350
Cdd:pfam17380 473 KRKKLELEKEKRDRKRAEEQRRKILEKEleerkqamieeerKRKLLEKeMEERQKAIYEEERR 535
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
166-341 |
7.08e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 38.18 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 166 RVYDERKEESISLMKETEGKRE-KINEllkyiEERLHTLEEEKEELAQYQKWDKMRRALEYtiynQELNETRAKldELSA 244
Cdd:pfam17380 382 RLQMERQQKNERVRQELEAARKvKILE-----EERQRKIQQQKVEMEQIRAEQEEARQREV----RRLEEERAR--EMER 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 245 KRETSGEKSRQ---LRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQ-LSAERQEQIKQRTKLELKAKDLQDELAG-- 318
Cdd:pfam17380 451 VRLEEQERQQQverLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKeLEERKQAMIEEERKRKLLEKEMEERQKAiy 530
|
170 180
....*....|....*....|...
gi 74216698 319 NSEQRKRLLKERQKLLEKIEEKQ 341
Cdd:pfam17380 531 EEERRREAEEERRKQQEMEERRR 553
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
155-346 |
7.09e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 38.37 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 155 RLKLLREVAGTRVYDE---RKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELaqyqkwDKMRRALEYtiynqe 231
Cdd:PRK05771 61 KLRSYLPKLNPLREEKkkvSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKEL------EQEIERLEP------ 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 232 LNETRAKLDELSAKRETSGEKSRqlRDAQQDARDKMEDIERQVRELKTK-------ISAMKEEKEQLSAERQEQIKQRTK 304
Cdd:PRK05771 129 WGNFDLDLSLLLGFKYVSVFVGT--VPEDKLEELKLESDVENVEYISTDkgyvyvvVVVLKELSDEVEEELKKLGFERLE 206
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 74216698 305 LELKaKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAE 346
Cdd:PRK05771 207 LEEE-GTPSELIREIKEELEEIEKERESLLEELKELAKKYLE 247
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
271-346 |
7.16e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 37.89 E-value: 7.16e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74216698 271 ERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAE 346
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
170-317 |
8.50e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 37.84 E-value: 8.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 170 ERKEESISLMKETEG----KREKINELLKYIEERLHTLEEEKEELaqyqkwDKMRRALEytiynqelnetrAKLDELSAK 245
Cdd:PRK12704 61 EAKEEIHKLRNEFEKelreRRNELQKLEKRLLQKEENLDRKLELL------EKREEELE------------KKEKELEQK 122
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74216698 246 RETSGEKSRQLRDAQQDARDKMEDIERQVRElKTKISAMKEEKEQLSAERQEQIKQrtkLELKAKDLQDELA 317
Cdd:PRK12704 123 QQELEKKEEELEELIEEQLQELERISGLTAE-EAKEILLEKVEEEARHEAAVLIKE---IEEEAKEEADKKA 190
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
214-349 |
8.75e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 38.01 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 214 QKWDKMRRALEytiynqELNETRAKLDELSAKRetsgeksRQLRDAQQDARdKMEDIERQVRELKTKISAMKEEKEQLSA 293
Cdd:COG3096 492 QAWQTARELLR------RYRSQQALAQRLQQLR-------AQLAELEQRLR-QQQNAERLLEEFCQRIGQQLDAAEELEE 557
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 74216698 294 ERQEQikqrtklELKAKDLQDELAGNSEQRKRLlkeRQKlLEKIEEKQKELAETEP 349
Cdd:COG3096 558 LLAEL-------EAQLEELEEQAAEAVEQRSEL---RQQ-LEQLRARIKELAARAP 602
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
247-345 |
9.21e-03 |
|
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 36.72 E-value: 9.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 247 ETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKD-------LQDELAGN 319
Cdd:pfam06785 79 ELDAEGFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRLESEEqlaekqlLINEYQQT 158
|
90 100
....*....|....*....|....*.
gi 74216698 320 SEQRKRLLKERQKLLEKIEEKQKELA 345
Cdd:pfam06785 159 IEEQRSVLEKRQDQIENLESKVRDLN 184
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
1-49 |
9.32e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 36.86 E-value: 9.32e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 74216698 1 MYIKQVIIQGFRSYRDQTIVDpFSSKHN----VIVGRNGSGKSNFFYAIQFVL 49
Cdd:cd03279 1 MKPLKLELKNFGPFREEQVID-FTGLDNnglfLICGPTGAGKSTILDAITYAL 52
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
229-346 |
9.66e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 37.57 E-value: 9.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216698 229 NQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELK 308
Cdd:COG4372 44 QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE 123
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 74216698 309 AKDLQDE---LAGNSEQRKRLLKERQKLLEKIEEKQKELAE 346
Cdd:COG4372 124 RQDLEQQrkqLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
|
| |
