|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
41-528 |
4.46e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 4.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 41 LRQAQMSKELIELNKALALKEALAKKMTQNDNQLQpiqfQYQDNIKNLESEVLSLQREKEELVLELQTAKKDANQAKlsE 120
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELE----ELRLELEELELELEEAQAEEYELLAELARLEQDIARLE--E 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 121 RRRKRLQELEGQIADLKKKLQEQSKLLKLKESTEHTVSKLNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQQKDKEVIQLK 200
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 201 ERDRKRQyELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQKEVAEKRKETQSRGMESTAARMKNWLGNEIEVMVS 280
Cdd:COG1196 390 EALRAAA-ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 281 TEEAKRHLNGLLEERKILAQDVAQLK-----EKRESGENPPLKLRRRTFSYDEIHGQDSGAEDSIAKQIESLETELELRS 355
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLllleaEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAL 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 356 AQIADLQQKLLdAESEDRPKQRWESIATILEAKcAIKYLVGELVSSKILVSKLESSLNQSKASCIDVQKMLFEEQNHFAK 435
Cdd:COG1196 549 QNIVVEDDEVA-AAAIEYLKAAKAGRATFLPLD-KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRT 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 436 IETELKE----ELVKVEQQHQEKVLYLLSQLQQSQMTEKQLEESVSEKEQQLLSTLKCQEEELRKMQEVCEQNQQLLQEN 511
Cdd:COG1196 627 LVAARLEaalrRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEE 706
|
490
....*....|....*..
gi 1039796408 512 SAIKQKLTLLQVASKQK 528
Cdd:COG1196 707 RELAEAEEERLEEELEE 723
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
95-371 |
6.61e-10 |
|
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: 62.78 E-value: 6.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 95 LQREKEELVLELQTAKKDANQAKLsERRRKRLQELEGQIADLKKKLQEQSKLL------------KLKESTEHTVSKLNQ 162
Cdd:TIGR02169 216 LLKEKREYEGYELLKEKEALERQK-EAIERQLASLEEELEKLTEEISELEKRLeeieqlleelnkKIKDLGEEEQLRVKE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 163 EIRMMKNQRVQLMRQMKEDAEKFrqwkQQKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDAL 242
Cdd:TIGR02169 295 KIGELEAEIASLERSIAEKEREL----EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLR 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 243 QKQKEVAEKRKETQSRGMEstAARMKNWLGNEIevmvstEEAKRHLNGLLEERKILAQDVAQLKEKRESGENPPLKLRRR 322
Cdd:TIGR02169 371 AELEEVDKEFAETRDELKD--YREKLEKLKREI------NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEE 442
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1039796408 323 TFSYDEIHGQDSGAEDSIAKQIESLETELELRSAQIADLQQKLLDAESE 371
Cdd:TIGR02169 443 KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
35-516 |
6.12e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 6.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 35 FSTQHALRQAQMSKELIELNKALALKEALAKKMTQNDNQLQPIQFQYQDNIKNLEsevlsLQREKEELVLELQTAKKDAN 114
Cdd:PTZ00121 1265 FARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADE-----AKKKAEEAKKKADAAKKKAE 1339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 115 QAKLSERRRKRLQELEGQIADLKKKLQEQSKLLKLKESTEHTVSKLNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQQKDK 194
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKK 1419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 195 EVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQKEVAEKRKETQSRGMESTAARMKnwlgne 274
Cdd:PTZ00121 1420 ADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE------ 1493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 275 iEVMVSTEEAKRHlngllEERKILAQDVAQLKEKRESGENPPLKLRRRTfsyDEIHGQDSGAEDSIAKQIESLETELELR 354
Cdd:PTZ00121 1494 -EAKKKADEAKKA-----AEAKKKADEAKKAEEAKKADEAKKAEEAKKA---DEAKKAEEKKKADELKKAEELKKAEEKK 1564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 355 SAqiadlQQKLLDAESEDRPKQRWESIATILEAKcaIKYLVGELVSSKILVSKLESSLNQSKASCIDVQKMLfEEQNHFA 434
Cdd:PTZ00121 1565 KA-----EEAKKAEEDKNMALRKAEEAKKAEEAR--IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE-EEKKKVE 1636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 435 KIETELKEELVKVEQQHQEKVLYLLSQLQQSQMTE---KQLEES--VSEKEQQLLSTLKCQEEELRKMQEVCEQNQQLLQ 509
Cdd:PTZ00121 1637 QLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEedkKKAEEAkkAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK 1716
|
....*..
gi 1039796408 510 ENSAIKQ 516
Cdd:PTZ00121 1717 KAEELKK 1723
|
|
| Pre-SET |
pfam05033 |
Pre-SET motif; This protein motif is a zinc binding motif. It contains 9 conserved cysteines ... |
605-643 |
9.10e-05 |
|
Pre-SET motif; This protein motif is a zinc binding motif. It contains 9 conserved cysteines that coordinate three zinc ions. It is thought that this region plays a structural role in stabilising SET domains.
Pssm-ID: 461530 [Multi-domain] Cd Length: 99 Bit Score: 42.02 E-value: 9.10e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039796408 605 SIQGCSCKGwCGNKQCGC-RKQKSD---------------------CNVSCSCDPTkCRNR 643
Cdd:pfam05033 41 IPQGCDCGD-CSSEKCSCaQLNGGEfrfpydkdgllvpeskppiyeCNPLCGCPPS-CPNR 99
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
49-382 |
1.19e-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: 45.60 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 49 ELIELNKALALKEALAKKMTQNDNQLQpiqfQYQDNIKNLESEVLSLQREKEELVLELQTAKKDANQAklserrRKRLQE 128
Cdd:pfam12128 588 KRIDVPEWAASEEELRERLDKAEEALQ----SAREKQAAAEEQLVQANGELEKASREETFARTALKNA------RLDLRR 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 129 LEGQIADLKKKLQEQSKllKLKESTEHTVSKLNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQQKDKEVI----------- 197
Cdd:pfam12128 658 LFDEKQSEKDKKNKALA--ERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEgaldaqlallk 735
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 198 ------------QLKERDRKRQYELLKLERNFQKQSNV------LRRKTEEAA---AANKRLKDALQKQKEVAEKRKETQ 256
Cdd:pfam12128 736 aaiaarrsgakaELKALETWYKRDLASLGVDPDVIAKLkreirtLERKIERIAvrrQEVLRYFDWYQETWLQRRPRLATQ 815
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 257 SRGMESTAARMKNWLGNEIevmvstEEAKRHLNGLLEERKilAQDVAQLkekRESGENPPLKLRRRTFSYDEIHGQDSGA 336
Cdd:pfam12128 816 LSNIERAISELQQQLARLI------ADTKLRRAKLEMERK--ASEKQQV---RLSENLRGLRCEMSKLATLKEDANSEQA 884
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1039796408 337 EDSIAKQIESLETELELRSAQIADLQQKLLD------AESEDRPKQRWESIA 382
Cdd:pfam12128 885 QGSIGERLAQLEDLKLKRDYLSESVKKYVEHfknviaDHSGSGLAETWESLR 936
|
|
| SET_SETDB-like |
cd10538 |
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ... |
603-644 |
1.37e-04 |
|
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) and 2 (SETDB2), suppressor of variegation 3-9 homologs, SUV39H1 and SUV39H2, euchromatic histone-lysine N-methyltransferase EHMT1 and EHMT2, and similar proteins; The family includes SET domain bifurcated 1 (SETDB1) and 2 (SETDB2), suppressor of variegation 3-9 homologs, SUV39H1 and SUV39H2, euchromatic histone-lysine N-methyltransferase EHMT1 and EHMT2. SETDB1 (EC 2.1.1.43; also termed ERG-associated protein with SET domain (ESET), histone H3-K9 methyltransferase 4, H3-K9-HMTase 4, or lysine N-methyltransferase 1E (KMT1E)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. SETDB2 (EC 2.1.1.43; also termed chronic lymphocytic leukemia deletion region gene 8 protein (CLLD8), or lysine N-methyltransferase 1F (KMT1F)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It is involved in left-right axis specification in early development and mitosis. SUV39H1 (also termed histone H3-K9 methyltransferase 1, H3-K9-HMTase 1, lysine N-methyltransferase 1A, KMT1A, position-effect variegation 3-9 homolog, SUV39H, or Su(var)3-9 homolog 1) and SUV39H2 (also termed histone H3-K9 methyltransferase 2, H3-K9-HMTase 2, lysine N-methyltransferase 1B, KMT1B, or Su(var)3-9 homolog 2), both act as histone-lysine N-methyltransferases that specifically trimethylate 'Lys-9' of histone H3 (H3K9me3) using monomethylated H3 'Lys-9' as substrate. They mainly function in heterochromatin regions, thereby playing central roles in the establishment of constitutive heterochromatin at pericentric and telomere regions. EHMT1 (also termed Eu-HMTase1, G9a-like protein 1, GLP, GLP1, histone H3-K9 methyltransferase 5, H3-K9-HMTase 5, lysine N-methyltransferase 1D, or KMT1D) and EHMT2 (also termed Eu-HMTase2, HLA-B-associated transcript 8, histone H3-K9 methyltransferase 3, H3-K9-HMTase 3, lysine N-methyltransferase 1C, KMT1C, or protein G9a), both act as histone-lysine N-methyltransferases that specifically mono- and dimethylate 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. This family also includes the pre-SET domain, which is found in a number of histone methyltransferases (HMTase), N-terminal to the SET domain. Pre-SET domain is a zinc binding motif which contains 9 conserved cysteines that coordinate three zinc ions. It is thought that this region plays a structural role in stabilizing SET domains. Most family members, except for Arabidopsis thaliana SUVH9, contain a post-SET domain which harbors a zinc-binding site.
Pssm-ID: 380936 [Multi-domain] Cd Length: 217 Bit Score: 43.90 E-value: 1.37e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039796408 603 KKSIQGCSCKGWCGNKQCGCRKQKS---------------------DCNVSCSCDPTkCRNRH 644
Cdd:cd10538 21 IIDSVGCKCKDDCLDSKCACAAESDgifaytkngllrlnnspppifECNSKCSCDDD-CKNRV 82
|
|
| MUTSd |
smart00533 |
DNA-binding domain of DNA mismatch repair MUTS family; |
48-226 |
3.67e-03 |
|
DNA-binding domain of DNA mismatch repair MUTS family;
Pssm-ID: 214710 [Multi-domain] Cd Length: 308 Bit Score: 39.97 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 48 KELIELNKALALKEALAKKMTQNDNQLQ-PIQFQYQDNIKNLESEVLSLQREKEELVLELQTAKKDANQAKLSERRRKrL 126
Cdd:smart00533 79 RDLLRLYDSLEGLKEIRQLLESLDGPLLgLLLKVILEPLLELLELLLELLNDDDPLEVNDGGLIKDGFDPELDELREK-L 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 127 QELEGQIADLKKKLQEQSKLLKLKEStehTVSKLNQEIRMMKNQRVQL-----MRQMKEDAEKFRQWK-QQKDKEVIQLK 200
Cdd:smart00533 158 EELEEELEELLKKEREELGIDSLKLG---YNKVHGYYIEVTKSEAKKVpkdfiRRSSLKNTERFTTPElKELENELLEAK 234
|
170 180
....*....|....*....|....*..
gi 1039796408 201 ERDRKRQYELLK-LERNFQKQSNVLRR 226
Cdd:smart00533 235 EEIERLEKEILReLLEKVLEYLEELRA 261
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
41-528 |
4.46e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 4.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 41 LRQAQMSKELIELNKALALKEALAKKMTQNDNQLQpiqfQYQDNIKNLESEVLSLQREKEELVLELQTAKKDANQAKlsE 120
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELE----ELRLELEELELELEEAQAEEYELLAELARLEQDIARLE--E 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 121 RRRKRLQELEGQIADLKKKLQEQSKLLKLKESTEHTVSKLNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQQKDKEVIQLK 200
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 201 ERDRKRQyELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQKEVAEKRKETQSRGMESTAARMKNWLGNEIEVMVS 280
Cdd:COG1196 390 EALRAAA-ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 281 TEEAKRHLNGLLEERKILAQDVAQLK-----EKRESGENPPLKLRRRTFSYDEIHGQDSGAEDSIAKQIESLETELELRS 355
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLllleaEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAL 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 356 AQIADLQQKLLdAESEDRPKQRWESIATILEAKcAIKYLVGELVSSKILVSKLESSLNQSKASCIDVQKMLFEEQNHFAK 435
Cdd:COG1196 549 QNIVVEDDEVA-AAAIEYLKAAKAGRATFLPLD-KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRT 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 436 IETELKE----ELVKVEQQHQEKVLYLLSQLQQSQMTEKQLEESVSEKEQQLLSTLKCQEEELRKMQEVCEQNQQLLQEN 511
Cdd:COG1196 627 LVAARLEaalrRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEE 706
|
490
....*....|....*..
gi 1039796408 512 SAIKQKLTLLQVASKQK 528
Cdd:COG1196 707 RELAEAEEERLEEELEE 723
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
95-371 |
6.61e-10 |
|
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: 62.78 E-value: 6.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 95 LQREKEELVLELQTAKKDANQAKLsERRRKRLQELEGQIADLKKKLQEQSKLL------------KLKESTEHTVSKLNQ 162
Cdd:TIGR02169 216 LLKEKREYEGYELLKEKEALERQK-EAIERQLASLEEELEKLTEEISELEKRLeeieqlleelnkKIKDLGEEEQLRVKE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 163 EIRMMKNQRVQLMRQMKEDAEKFrqwkQQKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDAL 242
Cdd:TIGR02169 295 KIGELEAEIASLERSIAEKEREL----EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLR 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 243 QKQKEVAEKRKETQSRGMEstAARMKNWLGNEIevmvstEEAKRHLNGLLEERKILAQDVAQLKEKRESGENPPLKLRRR 322
Cdd:TIGR02169 371 AELEEVDKEFAETRDELKD--YREKLEKLKREI------NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEE 442
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1039796408 323 TFSYDEIHGQDSGAEDSIAKQIESLETELELRSAQIADLQQKLLDAESE 371
Cdd:TIGR02169 443 KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
86-371 |
9.35e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 9.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 86 KNLESevLSLQREKEELVLELQTAKKDanqaKLSERRRKRLQELEGQIADLKKKLQEQSKLLklkESTEHTVSKLNQEIR 165
Cdd:COG1196 200 RQLEP--LERQAEKAERYRELKEELKE----LEAELLLLKLRELEAELEELEAELEELEAEL---EELEAELAELEAELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 166 MMKNQRVQLMRQMKEDAEKFRQWKQQKDK----------EVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAAN 235
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELLAELARleqdiarleeRRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 236 KRLKDALQKQKEVAEKRKETQSRGMESTAARMKNW------LGNEIEVMVSTEEAKRHLNGLLEERKILAQDVAQLKEKR 309
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAeelleaLRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039796408 310 ESGENPPLKLRRRTFSYDEIHGQDSGAEDSIAKQIESLETELELRSAQIADLQQKLLDAESE 371
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
38-493 |
4.77e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 4.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 38 QHALRQAQMSKELIELNKALALKEALAKKMTQNDNQLQPIQFQYQDNIKNLESEVLSLQREKEELVLELQTAKKDANQAK 117
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 118 LSERRRKRLQELEGQIADLKKKLQEQSKLLKLKESTEhtvsklnqeirmmknqrvqlmrqmkedaekfRQWKQQKDKEVI 197
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEA-------------------------------AEEEAELEEEEE 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 198 QLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQKEVAEKRKETQSRGMESTAARMkNWLGNEIEV 277
Cdd:COG1196 460 ALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL-IGVEAAYEA 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 278 MVSTEEAKRHLNGLLEERKILAQDVAQLKEKRESGEN--PPLKLRRRTFSYDEIhgqDSGAEDSIAKQIESLETELELRS 355
Cdd:COG1196 539 ALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATflPLDKIRARAALAAAL---ARGAIGAAVDLVASDLREADARY 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 356 AQIADLqqkLLDAESEDRPKQRWESIATILEAKCAIKYLVGELVSSKILVSKLESSLNQSKASCIDVQKMLFEEQNHFAK 435
Cdd:COG1196 616 YVLGDT---LLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE 692
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039796408 436 IETELKEELVKVEQQHQEKVLYLLSQLQQSQMTEKQLEESVSEKEQQLLSTLKCQEEE 493
Cdd:COG1196 693 LELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE 750
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
85-377 |
2.91e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 85 IKNLESEVLSLQREKEELVLELQtakkdaNQAKLSERRRKRLQELEGQIADL--KKKLQEQSKLLKLK---ESTEHTVSK 159
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEIS------ELEKRLEEIEQLLEELNKKIKDLgeEEQLRVKEKIGELEaeiASLERSIAE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 160 LNQEIRMMKNQRVQL---MRQMKEDAEKFRQWKQQKDKEVIQLKERDRKRQYELlklernfqkqsNVLRRKTEEAAAANK 236
Cdd:TIGR02169 313 KERELEDAEERLAKLeaeIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL-----------EDLRAELEEVDKEFA 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 237 RLKDALQKQKEVAEKrketqsrgmestaarmknwLGNEIEvmvsteEAKRHLNGLLEERKILAQDVAQLKEKRESGENPP 316
Cdd:TIGR02169 382 ETRDELKDYREKLEK-------------------LKREIN------ELKRELDRLQEELQRLSEELADLNAAIAGIEAKI 436
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039796408 317 LKLRRRTFSYDEIHGQDSGAEDSIAKQIESLETELElrsaqiaDLQQKLLDAESEDRPKQR 377
Cdd:TIGR02169 437 NELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELY-------DLKEEYDRVEKELSKLQR 490
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
42-313 |
3.90e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 42 RQAQMSKELIELNKALALKEALAKKMTQNDNQLQPIQFQYQDNIKNLESEVLSLQREKEElvLELQTAKKDANQAKLSER 121
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE--LEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 122 RRkRLQELEGQIADLKKKLQE-QSKLLKLKESTEHtvskLNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQQKDKEVIQLK 200
Cdd:COG1196 294 LA-ELARLEQDIARLEERRRElEERLEELEEELAE----LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 201 ERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQKEVAEKRKETQSRGMESTAARMKnwlgnEIEVMVS 280
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE-----EEEEEEA 443
|
250 260 270
....*....|....*....|....*....|...
gi 1039796408 281 TEEAKRHLNGLLEERKILAQDVAQLKEKRESGE 313
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
126-417 |
4.39e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 4.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 126 LQELEGQIADLKK---------KLQEQSKLLKLkESTEHTVSKLNQEIRMMKNQRVQLmrqmKEDAEKFRQWKQQKDKEV 196
Cdd:COG1196 195 LGELERQLEPLERqaekaeryrELKEELKELEA-ELLLLKLRELEAELEELEAELEEL----EAELEELEAELAELEAEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 197 IQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQKEVAEKRKETQSRgMESTAARMKNWLGNEIE 276
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE-LEELEEELEELEEELEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 277 VMVSTEEAKRHLNGLLEERKILAQDVAQLKEKRESGENPPLKLRRRTFSYDEIHGQDSGAEDSIAKQIESLETELELRSA 356
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039796408 357 QIADLQQKLLDAESEDRPKQRW--ESIATILEAKCAIKYLVGELVSSKILVSKLESSLNQSKA 417
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEeaELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
35-516 |
6.12e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 6.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 35 FSTQHALRQAQMSKELIELNKALALKEALAKKMTQNDNQLQPIQFQYQDNIKNLEsevlsLQREKEELVLELQTAKKDAN 114
Cdd:PTZ00121 1265 FARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADE-----AKKKAEEAKKKADAAKKKAE 1339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 115 QAKLSERRRKRLQELEGQIADLKKKLQEQSKLLKLKESTEHTVSKLNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQQKDK 194
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKK 1419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 195 EVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQKEVAEKRKETQSRGMESTAARMKnwlgne 274
Cdd:PTZ00121 1420 ADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE------ 1493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 275 iEVMVSTEEAKRHlngllEERKILAQDVAQLKEKRESGENPPLKLRRRTfsyDEIHGQDSGAEDSIAKQIESLETELELR 354
Cdd:PTZ00121 1494 -EAKKKADEAKKA-----AEAKKKADEAKKAEEAKKADEAKKAEEAKKA---DEAKKAEEKKKADELKKAEELKKAEEKK 1564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 355 SAqiadlQQKLLDAESEDRPKQRWESIATILEAKcaIKYLVGELVSSKILVSKLESSLNQSKASCIDVQKMLfEEQNHFA 434
Cdd:PTZ00121 1565 KA-----EEAKKAEEDKNMALRKAEEAKKAEEAR--IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE-EEKKKVE 1636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 435 KIETELKEELVKVEQQHQEKVLYLLSQLQQSQMTE---KQLEES--VSEKEQQLLSTLKCQEEELRKMQEVCEQNQQLLQ 509
Cdd:PTZ00121 1637 QLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEedkKKAEEAkkAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK 1716
|
....*..
gi 1039796408 510 ENSAIKQ 516
Cdd:PTZ00121 1717 KAEELKK 1723
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
21-518 |
6.38e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 6.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 21 QVQSSPDTSRSSDVFSTQHALRQAQMSKELIELNK----ALALKEALAKKMTQNDNQLQPIQFQYQ---DNIKNLESEVL 93
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKkaeeAKKKADAAKKKAEEAKKAAEAAKAEAEaaaDEAEAAEEKAE 1367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 94 SLQREKEELVLELQTAKKDANQAKLSERRRKRLQELEGQIADLKKKLQEQSKLLKLKESTEhtvsklnqEIRmmKNQRVQ 173
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAE--------EKK--KADEAK 1437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 174 LMRQMKEDAEKFRQWKQQKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQKEVAEKRK 253
Cdd:PTZ00121 1438 KKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKK 1517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 254 ETQSRGMESTAARMKNWLGNEIEvmvSTEEAKRHLNGLLEERKILAQDVAQLKEKRESGENPPLKLRRRtfsydEIHGQD 333
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKADEAK---KAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKA-----EEAKKA 1589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 334 SGAEDSIAKQIESLETEL---ELRSAQIADLQQKLLDAESEDRPKQRWESIATILEAKCAiKYLVGELVSSKILVSKLES 410
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEKKMkaeEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA-EELKKAEEENKIKAAEEAK 1668
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 411 SLNQSKASCIDVQKMLFEEQN---HFAKIETELK--EELVKVEQQHQEKVLYLLSQLQQSQMTEKQLEESvSEKEQQLLS 485
Cdd:PTZ00121 1669 KAEEDKKKAEEAKKAEEDEKKaaeALKKEAEEAKkaEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE-AEEDKKKAE 1747
|
490 500 510
....*....|....*....|....*....|...
gi 1039796408 486 TLKCQEEELRKMQEVCEQNQQLLQENSAIKQKL 518
Cdd:PTZ00121 1748 EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
89-311 |
5.84e-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: 53.14 E-value: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 89 ESEVLSLQREKEELVLELQTAKKDANQAKLS-ERRRKRLQELEGQIADLKKKLQEQSKLLKLkesTEHTVSKLNQEIRMM 167
Cdd:TIGR02168 669 NSSILERRREIEELEEKIEELEEKIAELEKAlAELRKELEELEEELEQLRKELEELSRQISA---LRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 168 KNQRVQLMRQMKEDAEKFRQWKQQKDKEVIQLKERDRKRQY----------ELLKLERNFQKQSNVLRRKTEEAAAANKR 237
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEleaqieqlkeELKALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039796408 238 LKDaLQKQKEVAEKRKETQSRGMESTAARMKNWLGNEIEVMVSTEEAKRHLNGLLEERKILAQDVAQLKEKRES 311
Cdd:TIGR02168 826 LES-LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
47-258 |
2.07e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 47 SKELIELNKALALKE-ALAKKMTQND-NQLQPIQFQYQDNIKNLESEVLSLQREKEELVLELQTAKKDANQAKLSERRRK 124
Cdd:COG3206 181 EEQLPELRKELEEAEaALEEFRQKNGlVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 125 ---RLQELEGQIADLKKKLQEQSKLLklkeSTEH-TVSKLNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQQKDKEVIQLK 200
Cdd:COG3206 261 qspVIQQLRAQLAELEAELAELSARY----TPNHpDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQL 336
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039796408 201 ERDRKRQYELLKLERNfqkqsnvLRRKTEEAAAANKRLKDALQKQKEVAEKRKETQSR 258
Cdd:COG3206 337 AQLEARLAELPELEAE-------LRRLEREVEVARELYESLLQRLEEARLAEALTVGN 387
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
42-499 |
3.71e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 42 RQAQMSKELIELNKALALKEALAKKMTQNDNQLQPIQFQYQDNIKNLEsevlsLQREKEELVLELQTAKKDANQAKLSER 121
Cdd:PTZ00121 1348 AKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE-----AKKKAEEDKKKADELKKAAAAKKKADE 1422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 122 RRKRLQELEgQIADLKKKLQEQSKLLKLKESTEHTVSKLNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQQ-----KDKEV 196
Cdd:PTZ00121 1423 AKKKAEEKK-KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKaeeakKKADE 1501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 197 IQLKERDRKRQYELLKLERnfQKQSNVLR-----RKTEEA-AAANKRLKDALQKQKEV---AEKRKETQSRGMESTaarm 267
Cdd:PTZ00121 1502 AKKAAEAKKKADEAKKAEE--AKKADEAKkaeeaKKADEAkKAEEKKKADELKKAEELkkaEEKKKAEEAKKAEED---- 1575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 268 KNWLGNEIEVMVSTEEAKRHLNGLL--EERKILAQDVAQLKEKRESGENppLKLRRRTFSYDEIHGQDSGAEDSIAKQIE 345
Cdd:PTZ00121 1576 KNMALRKAEEAKKAEEARIEEVMKLyeEEKKMKAEEAKKAEEAKIKAEE--LKKAEEEKKKVEQLKKKEAEEKKKAEELK 1653
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 346 SLETELELRSAQIADLQQKLLDAESEDRPKQRWESIATILEAKCAIKYLVGELVSSKIL--VSKLESSLNQSKASCIDVQ 423
Cdd:PTZ00121 1654 KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAeeKKKAEELKKAEEENKIKAE 1733
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039796408 424 KMLFEEQnhfakiETELKEELVKVEQQHQEKVlyllsqLQQSQMTEKQLEESVSEKEQQLLSTLKCQEEELRKMQE 499
Cdd:PTZ00121 1734 EAKKEAE------EDKKKAEEAKKDEEEKKKI------AHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
82-388 |
9.52e-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: 49.28 E-value: 9.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 82 QDNIKNLESEV--LSLQREKEELVLELQTAKKDANQAKLSerrrKRLQELEGQIADLKKKLQEQSKLLKLKESTEHTVSK 159
Cdd:TIGR02168 192 EDILNELERQLksLERQAEKAERYKELKAELRELELALLV----LRLEELREELEELQEELKEAEEELEELTAELQELEE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 160 LNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQQKDKEVIQLKERDRKRQYELLKLERNFQKqsnvLRRKTEEAAAAnkrlK 239
Cdd:TIGR02168 268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE----LESKLDELAEE----L 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 240 DALQKQKEVAEKRKETQSRGMESTAARMKNWLGNEIEVMVSTEEAKRHLNGLLEERKILAQDVAQLKEK---------RE 310
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARlerledrreRL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 311 SGENPPLKLRRRTFSYDEIHGQDSGAEDSIAKQIESLET---ELELRSAQIADLQQKLLDAESE-DRPKQRWESIATILE 386
Cdd:TIGR02168 420 QQEIEELLKKLEEAELKELQAELEELEEELEELQEELERleeALEELREELEEAEQALDAAERElAQLQARLDSLERLQE 499
|
..
gi 1039796408 387 AK 388
Cdd:TIGR02168 500 NL 501
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
42-258 |
1.08e-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: 49.28 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 42 RQAQMSKELIELNKALALKEALAKKMTQNDNQLQPIQFQYQDNIKNLESEVLSLQREKEELVLELQTAKKDAN--QAKLS 119
Cdd:TIGR02168 282 EIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELEslEAELE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 120 ERRRKrLQELEGQIADLKKKLQEQSKLlklkestehtVSKLNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQQKDKEVIQL 199
Cdd:TIGR02168 362 ELEAE-LEELESRLEELEEQLETLRSK----------VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 200 KERDRKR-QYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQKEVAEKRKETQSR 258
Cdd:TIGR02168 431 EEAELKElQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
122-464 |
1.46e-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: 48.51 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 122 RRKRLQELEGQIADLKKKLQEQSKLLKlkestehtvsKLNQEIRMMKNQRVQLMRQMKEDAEKFRQwkQQKDKEVIQLKE 201
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALA----------ELRKELEELEEELEQLRKELEELSRQISA--LRKDLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 202 RDRKRQYELLKLER-NFQKQSNVLRRKTEEAAAANKRLKDALQKQKEVAEKRKEtqsrgmestaarmknwlgneievmvS 280
Cdd:TIGR02168 743 EQLEERIAQLSKELtELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE-------------------------E 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 281 TEEAKRHLNGLLEERKILAQDVAQLKEKRESGENPPLKLRRRTFSYDEIHGQDSGAEDSIAKQIESLETELELRSAQIAD 360
Cdd:TIGR02168 798 LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 361 LQQKL--LDAESEDRPKQRWESIATILEAKCAIKYLVGELVSSKILVSKLESSLNQSKASCIDVQKMLFEEQNHFAKIET 438
Cdd:TIGR02168 878 LLNERasLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAE 957
|
330 340
....*....|....*....|....*.
gi 1039796408 439 ELKEELVKVEQQHQEKVLYLLSQLQQ 464
Cdd:TIGR02168 958 ALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
115-359 |
2.59e-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: 47.07 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 115 QAKLSERRRKRLQELEGQIADLKKKLQ----EQSKLLKLKESTEHTVSKLNQEIRMMKNQRVQLMRQMKEdaekfrqwkq 190
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAalkkEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE---------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 191 qKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQKEVAEKRKEtQSRGMESTAARMKnw 270
Cdd:COG4942 88 -LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARRE-QAEELRADLAELA-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 271 lgneiEVMVSTEEAKRHLNGLLEERKILAQDVAQLKEKRESGENpplKLRRRTFSYDEIHGQDSGAEDSIAKQIESLETE 350
Cdd:COG4942 164 -----ALRAELEAERAELEALLAELEEERAALEALKAERQKLLA---RLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
....*....
gi 1039796408 351 LELRSAQIA 359
Cdd:COG4942 236 AAAAAERTP 244
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
167-527 |
2.65e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 167 MKNQRVQLMRQmKEDAEKFRQwkqqkdkeviqLKERDRKRQYELLKLERNFQKQSnvlRRKTEEAAAANKRLKDALQKQK 246
Cdd:COG1196 198 LERQLEPLERQ-AEKAERYRE-----------LKEELKELEAELLLLKLRELEAE---LEELEAELEELEAELEELEAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 247 EVAEKRKETQSRgmestaarmknwlgneievmvSTEEAKRHLNGLLEERKILAQDVAQLKEKREsgenpPLKLRRRtfsy 326
Cdd:COG1196 263 AELEAELEELRL---------------------ELEELELELEEAQAEEYELLAELARLEQDIA-----RLEERRR---- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 327 deihgQDSGAEDSIAKQIESLETELELRSAQIADLQQKLLDAESEDRpkqrwesiatileakcaikylvgelvSSKILVS 406
Cdd:COG1196 313 -----ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE--------------------------EAEAELA 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 407 KLESSLNQSKASCIDVQKMLFEEQNHFAKIETELKEElvkveqqhQEKVLYLLSQLQQSQMTEKQLEESVSEKEQQLLST 486
Cdd:COG1196 362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL--------AAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1039796408 487 LKCQEEELRKMQEVCEQNQQLLQENSAIKQKLTLLQVASKQ 527
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
62-247 |
5.35e-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: 46.30 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 62 ALAKKMTQNDNQLQpiqfQYQDNIKNLESEVLSLQREKEELVLELQTAKKDANQA-----------KLSERR----RKRL 126
Cdd:COG4942 17 AQADAAAEAEAELE----QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALarriraleqelAALEAElaelEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 127 QELEGQIADLKKKLQEQSKLLKLKESTEHTVSKLNQE-----IRMMK------NQRVQLMRQMKEDAEKFRQWKQQKDKE 195
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEdfldaVRRLQylkylaPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1039796408 196 VIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQKE 247
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
17-269 |
5.49e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 5.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 17 EADTQVQSSPDTSRSSDVFSTQHALRQAQMSKElIELNKALALKEALAKKMTQNDNQLQPiQFQYQDNIKNLESEvLSLQ 96
Cdd:COG3206 54 EASATLLVEPQSSDVLLSGLSSLSASDSPLETQ-IEILKSRPVLERVVDKLNLDEDPLGE-EASREAAIERLRKN-LTVE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 97 REKEELVLEL-------QTAKK----------DANQAKLSERRRKRLQELEGQIADLKKKLQE-QSKLLKLKE-----ST 153
Cdd:COG3206 131 PVKGSNVIEIsytspdpELAAAvanalaeaylEQNLELRREEARKALEFLEEQLPELRKELEEaEAALEEFRQknglvDL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 154 EHTVSKLNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQQ------------KDKEVIQLKERDRKRQYELLKLERNFQKQS 221
Cdd:COG3206 211 SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQlgsgpdalpellQSPVIQQLRAQLAELEAELAELSARYTPNH 290
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1039796408 222 NVLRRKTEEAAAANKRLKDALQK-------QKEVAEKRKETQSRGMESTAARMKN 269
Cdd:COG3206 291 PDVIALRAQIAALRAQLQQEAQRilasleaELEALQAREASLQAQLAQLEARLAE 345
|
|
| Pre-SET |
pfam05033 |
Pre-SET motif; This protein motif is a zinc binding motif. It contains 9 conserved cysteines ... |
605-643 |
9.10e-05 |
|
Pre-SET motif; This protein motif is a zinc binding motif. It contains 9 conserved cysteines that coordinate three zinc ions. It is thought that this region plays a structural role in stabilising SET domains.
Pssm-ID: 461530 [Multi-domain] Cd Length: 99 Bit Score: 42.02 E-value: 9.10e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039796408 605 SIQGCSCKGwCGNKQCGC-RKQKSD---------------------CNVSCSCDPTkCRNR 643
Cdd:pfam05033 41 IPQGCDCGD-CSSEKCSCaQLNGGEfrfpydkdgllvpeskppiyeCNPLCGCPPS-CPNR 99
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
94-286 |
9.93e-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: 45.53 E-value: 9.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 94 SLQREKEELVLELQTAKKDANQAKLSERR-RKRLQELEGQIADLKKKLQEQSKLLKLKES----TEHTVSKLNQEIRMMK 168
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKAlLKQLAALERRIAALARRIRALEQELAALEAelaeLEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 169 NQRVQLMRQM-----------------KEDAEKFRQWKQQKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEA 231
Cdd:COG4942 104 EELAELLRALyrlgrqpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039796408 232 AAANKRLKDALQKQKEVAEKRKETQSRGMESTAARMKNW--LGNEIEVMVSTEEAKR 286
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAeeLEALIARLEAEAAAAA 240
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
49-382 |
1.19e-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: 45.60 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 49 ELIELNKALALKEALAKKMTQNDNQLQpiqfQYQDNIKNLESEVLSLQREKEELVLELQTAKKDANQAklserrRKRLQE 128
Cdd:pfam12128 588 KRIDVPEWAASEEELRERLDKAEEALQ----SAREKQAAAEEQLVQANGELEKASREETFARTALKNA------RLDLRR 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 129 LEGQIADLKKKLQEQSKllKLKESTEHTVSKLNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQQKDKEVI----------- 197
Cdd:pfam12128 658 LFDEKQSEKDKKNKALA--ERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEgaldaqlallk 735
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 198 ------------QLKERDRKRQYELLKLERNFQKQSNV------LRRKTEEAA---AANKRLKDALQKQKEVAEKRKETQ 256
Cdd:pfam12128 736 aaiaarrsgakaELKALETWYKRDLASLGVDPDVIAKLkreirtLERKIERIAvrrQEVLRYFDWYQETWLQRRPRLATQ 815
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 257 SRGMESTAARMKNWLGNEIevmvstEEAKRHLNGLLEERKilAQDVAQLkekRESGENPPLKLRRRTFSYDEIHGQDSGA 336
Cdd:pfam12128 816 LSNIERAISELQQQLARLI------ADTKLRRAKLEMERK--ASEKQQV---RLSENLRGLRCEMSKLATLKEDANSEQA 884
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1039796408 337 EDSIAKQIESLETELELRSAQIADLQQKLLD------AESEDRPKQRWESIA 382
Cdd:pfam12128 885 QGSIGERLAQLEDLKLKRDYLSESVKKYVEHfknviaDHSGSGLAETWESLR 936
|
|
| SET_SETDB-like |
cd10538 |
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ... |
603-644 |
1.37e-04 |
|
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) and 2 (SETDB2), suppressor of variegation 3-9 homologs, SUV39H1 and SUV39H2, euchromatic histone-lysine N-methyltransferase EHMT1 and EHMT2, and similar proteins; The family includes SET domain bifurcated 1 (SETDB1) and 2 (SETDB2), suppressor of variegation 3-9 homologs, SUV39H1 and SUV39H2, euchromatic histone-lysine N-methyltransferase EHMT1 and EHMT2. SETDB1 (EC 2.1.1.43; also termed ERG-associated protein with SET domain (ESET), histone H3-K9 methyltransferase 4, H3-K9-HMTase 4, or lysine N-methyltransferase 1E (KMT1E)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. SETDB2 (EC 2.1.1.43; also termed chronic lymphocytic leukemia deletion region gene 8 protein (CLLD8), or lysine N-methyltransferase 1F (KMT1F)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It is involved in left-right axis specification in early development and mitosis. SUV39H1 (also termed histone H3-K9 methyltransferase 1, H3-K9-HMTase 1, lysine N-methyltransferase 1A, KMT1A, position-effect variegation 3-9 homolog, SUV39H, or Su(var)3-9 homolog 1) and SUV39H2 (also termed histone H3-K9 methyltransferase 2, H3-K9-HMTase 2, lysine N-methyltransferase 1B, KMT1B, or Su(var)3-9 homolog 2), both act as histone-lysine N-methyltransferases that specifically trimethylate 'Lys-9' of histone H3 (H3K9me3) using monomethylated H3 'Lys-9' as substrate. They mainly function in heterochromatin regions, thereby playing central roles in the establishment of constitutive heterochromatin at pericentric and telomere regions. EHMT1 (also termed Eu-HMTase1, G9a-like protein 1, GLP, GLP1, histone H3-K9 methyltransferase 5, H3-K9-HMTase 5, lysine N-methyltransferase 1D, or KMT1D) and EHMT2 (also termed Eu-HMTase2, HLA-B-associated transcript 8, histone H3-K9 methyltransferase 3, H3-K9-HMTase 3, lysine N-methyltransferase 1C, KMT1C, or protein G9a), both act as histone-lysine N-methyltransferases that specifically mono- and dimethylate 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. This family also includes the pre-SET domain, which is found in a number of histone methyltransferases (HMTase), N-terminal to the SET domain. Pre-SET domain is a zinc binding motif which contains 9 conserved cysteines that coordinate three zinc ions. It is thought that this region plays a structural role in stabilizing SET domains. Most family members, except for Arabidopsis thaliana SUVH9, contain a post-SET domain which harbors a zinc-binding site.
Pssm-ID: 380936 [Multi-domain] Cd Length: 217 Bit Score: 43.90 E-value: 1.37e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039796408 603 KKSIQGCSCKGWCGNKQCGCRKQKS---------------------DCNVSCSCDPTkCRNRH 644
Cdd:cd10538 21 IIDSVGCKCKDDCLDSKCACAAESDgifaytkngllrlnnspppifECNSKCSCDDD-CKNRV 82
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
42-517 |
2.62e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 42 RQAQMSKELIELNKALALKEALAKKMTQNDNQLQpiQFQYQDNIKNLESEVLSLQREKEELVLELQTAKKDANQAKLSER 121
Cdd:PTZ00121 1170 RKAEDAKKAEAARKAEEVRKAEELRKAEDARKAE--AARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEE 1247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 122 RRK---------------------------------------------RLQELEGQIADLKKKLQEQSKLLKLKESTEHT 156
Cdd:PTZ00121 1248 ERNneeirkfeearmahfarrqaaikaeearkadelkkaeekkkadeaKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA 1327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 157 VSKLNQ-EIRMMKNQRVQLMRQMKEDAEKFRQWKQQKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAAN 235
Cdd:PTZ00121 1328 KKKADAaKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKA 1407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 236 KRLKDALQKQKEVAEKRKETQSRGMESTAARMKNWLGNEIEVMVSTEEAKRHLNGL--------LEERKILAQDVAQLKE 307
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKkkaeeakkADEAKKKAEEAKKADE 1487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 308 KRESGENPPLKLRRRTFSYDEIHGQDSGAEDSIAKQIESLETELELRSAQIADLQQKLLDAESEDRPKQ--RWESIATIL 385
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEElkKAEEKKKAE 1567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 386 EAKCAIKYLVGELVSSKILVSKLESSLNQSKASCIDVQKMLFEEQNhfAKIETELKEELVKVEQQHQEKVLYLLSQLQQS 465
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK--KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE 1645
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1039796408 466 QMTEKQLEESVSEKEQQLLSTLKCQEEELRKMQEVCEQNQQLLQENSAIKQK 517
Cdd:PTZ00121 1646 KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE 1697
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
83-499 |
3.18e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 83 DNIKNLESEVLSLQREKEEL--------VLELQTAKKDANQAKLSER---RRKRLQELEGQIADLKKKL----------Q 141
Cdd:PRK03918 214 SELPELREELEKLEKEVKELeelkeeieELEKELESLEGSKRKLEEKireLEERIEELKKEIEELEEKVkelkelkekaE 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 142 EQSKLLKLKESTEHTVSKLNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQQKDKEVIQLKERDRKRQYELLkLERNFQKQS 221
Cdd:PRK03918 294 EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHEL-YEEAKAKKE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 222 NVLRRKTEEAA----AANKRLKDALQKQKEVAEKRKETQSR--GMESTAARMKNWLgNEIEVM----------VSTEEAK 285
Cdd:PRK03918 373 ELERLKKRLTGltpeKLEKELEELEKAKEEIEEEISKITARigELKKEIKELKKAI-EELKKAkgkcpvcgreLTEEHRK 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 286 RHLNGLLEERKILAQDVAQLKEKRESGENPPLKLRRRTFSYDEIHgqdsgAEDSIAKQIESLETELElrsaqiaDLQQKL 365
Cdd:PRK03918 452 ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELI-----KLKELAEQLKELEEKLK-------KYNLEE 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 366 LDAESEDRPKQRWESIatilEAKCAIKYLVGELVSSKILVSKLESSLNQSKASCIDVQKMLFEEQNHFAKIETELKEELV 445
Cdd:PRK03918 520 LEKKAEEYEKLKEKLI----KLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLK 595
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039796408 446 KVEQQHQE--KVLYLLSQLQQSQMTEKQLEESVSEKEQQLLSTLKCQEEELRKMQE 499
Cdd:PRK03918 596 ELEPFYNEylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE 651
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
86-252 |
3.76e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 86 KNLESEVLSLQREKEELV----LELQTAKKDA-NQAKlsERRRKRLQELEGQIADLKKKLQEQSKLLKLKESTEhtvskl 160
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILeeakKEAEAIKKEAlLEAK--EEIHKLRNEFEKELRERRNELQKLEKRLLQKEENL------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 161 nqeirmmkNQRVQLMRQMKEDAEKFRQWKQQKDKEVIQLKER-DRKRQYELLKLER--NFQKQS--NVLRRKTEEAAA-- 233
Cdd:PRK12704 99 --------DRKLELLEKREEELEKKEKELEQKQQELEKKEEElEELIEEQLQELERisGLTAEEakEILLEKVEEEARhe 170
|
170
....*....|....*....
gi 1039796408 234 ANKRLKDALQKQKEVAEKR 252
Cdd:PRK12704 171 AAVLIKEIEEEAKEEADKK 189
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
42-310 |
3.86e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.96 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 42 RQAQMSKELIELNKALALKEALAKKMtQNDNQLQPIQFQYQDNIKN-----LESEVLSLQREKEELVLELQTAKKDANQA 116
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEEKAREV-ERRRKLEEAEKARQAEMDRqaaiyAEQERMAMERERELERIRQEERKRELERI 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 117 KLSE--------RRRKRLQ------------ELEgqiADLKKKLQEQSKLLKLKESTEHT--VSKLNQEIRMMKNQRVQL 174
Cdd:pfam17380 366 RQEEiameisrmRELERLQmerqqknervrqELE---AARKVKILEEERQRKIQQQKVEMeqIRAEQEEARQREVRRLEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 175 MRQMKEDAEKFRQWKQQKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKT-EEAAAANKRL------------KDA 241
Cdd:pfam17380 443 ERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIlEKELEERKQAmieeerkrklleKEM 522
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039796408 242 LQKQKEVAEKRKETQSRGMESTAARMKNWLGNEIEVMVSTEEAKRhLNGLLEERKILAQDVAQLKEKRE 310
Cdd:pfam17380 523 EERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSR-LEAMEREREMMRQIVESEKARAE 590
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
250-528 |
3.98e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 250 EKRKETQSRgMESTAARMknwlgNEIEVMvsTEEAKRHLNGLLEERKIlAQDVAQLKEKRESgenppLKLRRRTFSYDEI 329
Cdd:COG1196 172 ERKEEAERK-LEATEENL-----ERLEDI--LGELERQLEPLERQAEK-AERYRELKEELKE-----LEAELLLLKLREL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 330 HGQDSGAEDSIAK---QIESLETELELRSAQIADLQQKLLDAESEDRPKQrwesiATILEAKCAIKYLVGELVSSKILVS 406
Cdd:COG1196 238 EAELEELEAELEEleaELEELEAELAELEAELEELRLELEELELELEEAQ-----AEEYELLAELARLEQDIARLEERRR 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 407 KLESSLNQSKascidvqkmlfEEQNHFAKIETELKEELVKVEQQHQEKVLYLLSQLQQSQMTEKQLEESVSEKEQQLLST 486
Cdd:COG1196 313 ELEERLEELE-----------EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1039796408 487 LKCQEEELRKMQEVCEQNQQLLQENSAIKQKLTLLQVASKQK 528
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
282-510 |
4.98e-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: 43.21 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 282 EEAKRHLNGLLEERKILAQDVAQLKEKRESGENPPLKLRRRTfsydeihgqdsgaeDSIAKQIESLETELELRSAQIADL 361
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI--------------AALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 362 QQKLldAESEDRPKQRWESIATILEAKcaikYLVGELVSSKILVSKleSSLNQSKASCIDVQKMLFEEQNHFAKIETELk 441
Cdd:COG4942 89 EKEI--AELRAELEAQKEELAELLRAL----YRLGRQPPLALLLSP--EDFLDAVRRLQYLKYLAPARREQAEELRADL- 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039796408 442 EELVKVEQQHQEKVLYLLSQLQQSQMTEKQLEESVSEKeQQLLSTLKCQEEELRKMQEVCEQNQQLLQE 510
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAER-QKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
85-196 |
5.02e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 85 IKNLESEVLSLQREKEELVLELQTAKKDanqaklserrrkRLQELEGQIADLKKKLQEQSKLLKLKESTEHTVSKLNQEI 164
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKEQDEASFE------------RLAELRDELAELEEELEALKARWEAEKELIEEIQELKEEL 480
|
90 100 110
....*....|....*....|....*....|..
gi 1039796408 165 RMMKNQRVQLMRQMKEDAEKFRQWKQQKDKEV 196
Cdd:COG0542 481 EQRYGKIPELEKELAELEEELAELAPLLREEV 512
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
72-252 |
5.13e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 5.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 72 NQLQPIQFQYQDNIKNLESEVLSLQREKEELVLELQTAKKDANQ-----AKLSERRRKRLQELEGQIADLKKKLQEQSKL 146
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKlqaeiAEAEAEIEERREELGERARALYRSGGSVSYL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 147 LKLKESTEHT--VSKLNQEIRMMKNQRvQLMRQMKEDAEKFRQWKQQKDKEVIQLKERDRKRQYELLKLERNFQKQSNVL 224
Cdd:COG3883 106 DVLLGSESFSdfLDRLSALSKIADADA-DLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALL 184
|
170 180
....*....|....*....|....*...
gi 1039796408 225 RRKTEEAAAANKRlKDALQKQKEVAEKR 252
Cdd:COG3883 185 AQLSAEEAAAEAQ-LAELEAELAAAEAA 211
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
85-311 |
5.30e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 85 IKNLESEVlslqrEKEELVLELQTAKKDANQAKLSERR--RKRLQELEGQIADLKKKLQEQSKLLKLKESTEHTVSKLNQ 162
Cdd:PRK03918 178 IERLEKFI-----KRTENIEELIKEKEKELEEVLREINeiSSELPELREELEKLEKEVKELEELKEEIEELEKELESLEG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 163 EIRMMKNQRVQLMRQMKEDAEKFR------------QWKQQKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEE 230
Cdd:PRK03918 253 SKRKLEEKIRELEERIEELKKEIEeleekvkelkelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 231 AAAANKRLKDALQKQKEVAEKRKETQSR------------GMESTAARMKNWLGNEIEVMVstEEAKRHLNGLLEERKIL 298
Cdd:PRK03918 333 LEEKEERLEELKKKLKELEKRLEELEERhelyeeakakkeELERLKKRLTGLTPEKLEKEL--EELEKAKEEIEEEISKI 410
|
250
....*....|...
gi 1039796408 299 AQDVAQLKEKRES 311
Cdd:PRK03918 411 TARIGELKKEIKE 423
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
45-258 |
7.39e-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: 43.13 E-value: 7.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 45 QMSKELIELNKALALKEALAKKMTQNDNQLQPIQFQYQDNIKNLESEVLSLQREKEEL--VLELQTAKKDANQAKLsERR 122
Cdd:TIGR02169 795 EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIekEIENLNGKKEELEEEL-EEL 873
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 123 RKRLQELEGQIADLKKKLQE-QSKLLKLKESTEHTVSKLNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQqkDKEVIQLKE 201
Cdd:TIGR02169 874 EAALRDLESRLGDLKKERDElEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE--DEEIPEEEL 951
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039796408 202 RDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQKEVAEKRKETQSR 258
Cdd:TIGR02169 952 SLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILER 1008
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
173-377 |
7.49e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 173 QLMRQMKEDAEKFRQWKQQKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQKEVAEKR 252
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 253 KETQSRGMESTAARMKNWLGNEIEVMVSTEEAKRHLNGLLEERKILAQDVAQLKEKRESGEnpplKLRRRTFSYDEIHGQ 332
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA----ELAALRAELEAERAE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1039796408 333 DSGAEDSIAKQIESLETELELRSAQIADLQQKLLDAESEDRPKQR 377
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
336-551 |
8.34e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 8.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 336 AEDSIAK-----QIESLETELELRSAQIADLQQKLLDAESE-DRPKQRWESIATILEAKCAIkylVGELVSSKILvSKLE 409
Cdd:COG3206 194 AEAALEEfrqknGLVDLSEEAKLLLQQLSELESQLAEARAElAEAEARLAALRAQLGSGPDA---LPELLQSPVI-QQLR 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 410 SSLNQSKASCIDVQKMLFEEQNHFAKIETELKEELVKVEQQHQEKVLYLLSQLQQSQMTEKQLEESVSEKEQQLLSTLKc 489
Cdd:COG3206 270 AQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPE- 348
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039796408 490 QEEELRKMQEVCEQNQQLLQEnsaIKQKLTLLQVASKQKPHLTRnIFQSPDSSFEYIPPKPK 551
Cdd:COG3206 349 LEAELRRLEREVEVARELYES---LLQRLEEARLAEALTVGNVR-VIDPAVVPLKPVSPKKL 406
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
79-234 |
8.60e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 8.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 79 FQYQDNIKNLESEVLSLQREKEELVLELQTAKKDANQAKLSERRRK---RLQELEGQIADLKKKLQEQSKLLKLKESTEH 155
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAleaELAELPERLEELEERLEELRELEEELEELEA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 156 TVSKLNQEIRMMKNQR----VQLMRQMKEDAEKFRQWKQQKDKEVIQLKER--DRKRQYELLKLERNFQKQSNVLRRKTE 229
Cdd:COG4717 171 ELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQEEleELEEELEQLENELEAAALEERLKEARL 250
|
....*
gi 1039796408 230 EAAAA 234
Cdd:COG4717 251 LLLIA 255
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
77-386 |
8.70e-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: 8.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 77 IQFQYQDNIKNLESEVLSLQREKEELVLELQTAKKDANQakLSERRR------------KRLQELEGQIADLKKKLQE-- 142
Cdd:COG4913 604 LGFDNRAKLAALEAELAELEEELAEAEERLEALEAELDA--LQERREalqrlaeyswdeIDVASAEREIAELEAELERld 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 143 --QSKLLKLKEstehTVSKLNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQQKDKEVIQLKER-DRKRQYELLKLERnfqk 219
Cdd:COG4913 682 asSDDLAALEE----QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAeDLARLELRALLEE---- 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 220 qsnvlRRKTEEAAAANKRLKDALQKQKEVAEKRKETQSRGMESTAARMKN-WLGNEIEVMVSTEEAKRHLNGLleeRKIL 298
Cdd:COG4913 754 -----RFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNReWPAETADLDADLESLPEYLALL---DRLE 825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 299 AQDVAQLKEKresgenppLKLRRRTFSYDEI---HGQDSGAEDSIAKQIESLETELE----------------LRSAQIA 359
Cdd:COG4913 826 EDGLPEYEER--------FKELLNENSIEFVadlLSKLRRAIREIKERIDPLNDSLKripfgpgrylrlearpRPDPEVR 897
|
330 340 350
....*....|....*....|....*....|...
gi 1039796408 360 DLQQKLLDA------ESEDRPKQRWESIATILE 386
Cdd:COG4913 898 EFRQELRAVtsgaslFDEELSEARFAALKRLIE 930
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
160-550 |
1.19e-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: 42.42 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 160 LNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQQKDKEViQLKERDRKRQYELLKLERN--FQKQSNVLRRKTEEAAAANKR 237
Cdd:pfam17380 271 LNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEE-KAREVERRRKLEEAEKARQaeMDRQAAIYAEQERMAMERERE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 238 LKDALQKQKEVAEKRKETQSRGMEstAARMKNWLGNEIEVMVSTEEAKRHLNG-----LLEE---RKILAQDVAQLKEKR 309
Cdd:pfam17380 350 LERIRQEERKRELERIRQEEIAME--ISRMRELERLQMERQQKNERVRQELEAarkvkILEEerqRKIQQQKVEMEQIRA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 310 ESGENPPLKLRRrtfsydeihgqdsgAEDSIAKQIESLETELELRSAQIADLQQklldaESEDRPKQRWEsiatiLEAKC 389
Cdd:pfam17380 428 EQEEARQREVRR--------------LEEERAREMERVRLEEQERQQQVERLRQ-----QEEERKRKKLE-----LEKEK 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 390 AIKYLVGELvSSKILVSKLESSlnqskascidvQKMLFEEQNHFAKIETELKEELVKVEQQHQEKVLYLLSQLQQSQMTE 469
Cdd:pfam17380 484 RDRKRAEEQ-RRKILEKELEER-----------KQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEER 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 470 KQLEESV--SEKEQQLLSTLKCQEEELRKMQEVCEQNQQLLQENSAIKQKLTLLQVASKQKP-----HLTRNIFQSPdss 542
Cdd:pfam17380 552 RRIQEQMrkATEERSRLEAMEREREMMRQIVESEKARAEYEATTPITTIKPIYRPRISEYQPpdvesHMIRFTTQSP--- 628
|
....*...
gi 1039796408 543 fEYIPPKP 550
Cdd:pfam17380 629 -EWATPSP 635
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
40-371 |
1.21e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 40 ALRQAQMSKELIELNKALALKEALAKKMTQndnQLQPIQFQYQDnIKNLESEVLSLQREKEELVLELQTAKKDANQAKLS 119
Cdd:PRK03918 292 AEEYIKLSEFYEEYLDELREIEKRLSRLEE---EINGIEERIKE-LEEKEERLEELKKKLKELEKRLEELEERHELYEEA 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 120 ERRRKRLQELEGQIA-----DLKKKLQEqskLLKLKESTEHTVSKLNQEIRMMKNQRVQLMRQM---------------- 178
Cdd:PRK03918 368 KAKKEELERLKKRLTgltpeKLEKELEE---LEKAKEEIEEEISKITARIGELKKEIKELKKAIeelkkakgkcpvcgre 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 179 ------KEDAEKFRQWKQQKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKT--EEAAAANKRLK----DALQKQK 246
Cdd:PRK03918 445 lteehrKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKkynlEELEKKA 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 247 EVAEKRKEtQSRGMESTAARMKNWLGNEIEVMVSTEEAKRHLNGLLEERKILaqdvaqLKEKRESGENPPLKLRRRTFSY 326
Cdd:PRK03918 525 EEYEKLKE-KLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAEL------LKELEELGFESVEELEERLKEL 597
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1039796408 327 DEIHGQDSGAEDS------IAKQIESLETELELRSAQIADLQQKLLDAESE 371
Cdd:PRK03918 598 EPFYNEYLELKDAekelerEEKELKKLEEELDKAFEELAETEKRLEELRKE 648
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
341-535 |
1.89e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 341 AKQIESLETELELRSAQIADLQQKLLDAESEDRPKQrwESIAT----ILEAKCAIKYLVGELVSSKILVSKLESS---LN 413
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELE--EKLEElrleVSELEEEIEELQKELYALANEISRLEQQkqiLR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 414 QSKASCIDVQKMLFEEQNHFAKIETELKEELVKVEQQhqekvlyLLSQLQQSQMTEKQLEESVSEKEQQLLSTLKCQEEE 493
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEK-------LEELKEELESLEAELEELEAELEELESRLEELEEQL 381
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1039796408 494 LRKMQEVCEQNQQLLQENSAIKQKLTLLQVASKQKPHLTRNI 535
Cdd:TIGR02168 382 ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI 423
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
85-254 |
2.46e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 85 IKNLESEVLSLQREKEELVLELQTAKKDaNQAKLSErrrkrLQELEGQIADLKKKLQEQSKLLKLKESTEHTV----SKL 160
Cdd:TIGR04523 351 LTNSESENSEKQRELEEKQNEIEKLKKE-NQSYKQE-----IKNLESQINDLESKIQNQEKLNQQKDEQIKKLqqekELL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 161 NQEIRMMKNQRVQLMRQMKEDAEKfrqwKQQKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKD 240
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQ----DSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKK 500
|
170
....*....|....
gi 1039796408 241 ALQKQKEVAEKRKE 254
Cdd:TIGR04523 501 LNEEKKELEEKVKD 514
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
174-521 |
2.93e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 174 LMRQMKEDAEKFRQWKQQKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDAlqkQKEVAEKRK 253
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEEL---REELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 254 ETQSRGMESTAARMKNWLGNEIEVMVSTEEAKRHLNGLLEERKILAQDVAQLKEKRES-GENPPLKLRRRTFSYDEIHGQ 332
Cdd:COG4717 124 LLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEElLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 333 DSGAEDSIAKQIESLETELELRSAQIADLQQKLLDAESEDRPKQrWESIATILEAKCAIKYLVGELVSSKILVSK----- 407
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE-ARLLLLIAAALLALLGLGGSLLSLILTIAGvlflv 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 408 -----LESSLNQSKASCIDVQKMLFEEQNHFAKIETELKEELVKV----EQQHQEKVLYLLSQLQQSQ-------MTEKQ 471
Cdd:COG4717 283 lgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAlglpPDLSPEELLELLDRIEELQellreaeELEEE 362
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1039796408 472 LEESVSEKE-QQLLSTLKCQ-EEELRKMQEVCEQNQQLLQENSAIKQKLTLL 521
Cdd:COG4717 363 LQLEELEQEiAALLAEAGVEdEEELRAALEQAEEYQELKEELEELEEQLEEL 414
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
40-242 |
3.04e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 40 ALRQAQMSKELIELNKALalkEALAKKMTQNDNQLQPIQ-FQYQDNIKNLESEVLSLQREKEELVLELQTAKKDANQAK- 117
Cdd:COG4913 247 AREQIELLEPIRELAERY---AAARERLAELEYLRAALRlWFAQRRLELLEAELEELRAELARLEAELERLEARLDALRe 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 118 ----LSERRR----KRLQELEGQIADLKKKLQEQS-KLLKLKESTEHTVSKLNQEIRMMKNQRVQLmRQMKEDAEKFRQW 188
Cdd:COG4913 324 eldeLEAQIRgnggDRLEQLEREIERLERELEERErRRARLEALLAALGLPLPASAEEFAALRAEA-AALLEALEEELEA 402
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039796408 189 KQQKDKEVIQLKERDRKRQYELLKlERNF--QKQSNVlrrkTEEAAAANKRLKDAL 242
Cdd:COG4913 403 LEEALAEAEAALRDLRRELRELEA-EIASleRRKSNI----PARLLALRDALAEAL 453
|
|
| MUTSd |
smart00533 |
DNA-binding domain of DNA mismatch repair MUTS family; |
48-226 |
3.67e-03 |
|
DNA-binding domain of DNA mismatch repair MUTS family;
Pssm-ID: 214710 [Multi-domain] Cd Length: 308 Bit Score: 39.97 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 48 KELIELNKALALKEALAKKMTQNDNQLQ-PIQFQYQDNIKNLESEVLSLQREKEELVLELQTAKKDANQAKLSERRRKrL 126
Cdd:smart00533 79 RDLLRLYDSLEGLKEIRQLLESLDGPLLgLLLKVILEPLLELLELLLELLNDDDPLEVNDGGLIKDGFDPELDELREK-L 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 127 QELEGQIADLKKKLQEQSKLLKLKEStehTVSKLNQEIRMMKNQRVQL-----MRQMKEDAEKFRQWK-QQKDKEVIQLK 200
Cdd:smart00533 158 EELEEELEELLKKEREELGIDSLKLG---YNKVHGYYIEVTKSEAKKVpkdfiRRSSLKNTERFTTPElKELENELLEAK 234
|
170 180
....*....|....*....|....*..
gi 1039796408 201 ERDRKRQYELLK-LERNFQKQSNVLRR 226
Cdd:smart00533 235 EEIERLEKEILReLLEKVLEYLEELRA 261
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
35-506 |
4.72e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.42 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 35 FSTQHALRQAQMSKELIELNKALALKEALAKKMTQNDNQLQPIQFQYQdNIKNLESEVLSLQREKEELVLELQTAKKDAN 114
Cdd:TIGR00606 417 LQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQ-QLEGSSDRILELDQELRKAERELSKAEKNSL 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 115 qaklSERRRKRLQELEGQIADLKKKLQEQSKllKLKESTEHTVSKLNQEI----RMMKNQRVQLMRQMKEDA-------- 182
Cdd:TIGR00606 496 ----TETLKKEVKSLQNEKADLDRKLRKLDQ--EMEQLNHHTTTRTQMEMltkdKMDKDEQIRKIKSRHSDEltsllgyf 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 183 ---EKFRQWKQQKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQKEVA-------EKR 252
Cdd:TIGR00606 570 pnkKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESdlerlkeEIE 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 253 KETQSRGMESTAARMKNWLGNEIEVMVS-----------TEEAKRHLNGLLEERKILAQDvaqlkeKRESGENPPLKLRR 321
Cdd:TIGR00606 650 KSSKQRAMLAGATAVYSQFITQLTDENQsccpvcqrvfqTEAELQEFISDLQSKLRLAPD------KLKSTESELKKKEK 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 322 RTfsyDEIHGQDSGAE---DSIAKQIESLETELELRSAQIADLQQKLLDAESEDRPKQRWESIATILEAKCAIK---YLV 395
Cdd:TIGR00606 724 RR---DEMLGLAPGRQsiiDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMerfQME 800
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 396 GELVSSKILVSKLESSLNQSKASCIDVQKMLFEEQNHFAKIETELkEELVKVEQQHQEKVLYLLSQ-------------- 461
Cdd:TIGR00606 801 LKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKI-ELNRKLIQDQQEQIQHLKSKtnelkseklqigtn 879
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1039796408 462 LQQSQMTEKQLEESVSEKeQQLLSTLKCQEEELRKMQEVCEQNQQ 506
Cdd:TIGR00606 880 LQRRQQFEEQLVELSTEV-QSLIREIKDAKEQDSPLETFLEKDQQ 923
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
110-300 |
4.88e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 110 KKDANQAKLSERRRKR-LQELEGQIADLKKK--LQEQSKLLKLKESTEHTVSKLNQEIrmmknqrvqlmrqmkedaekfr 186
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRiLEEAKKEAEAIKKEalLEAKEEIHKLRNEFEKELRERRNEL---------------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 187 qwkQQKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQKEVAEK-----RKETQSRGME 261
Cdd:PRK12704 85 ---QKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisgltAEEAKEILLE 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 1039796408 262 STAARMKnwlgNEIEVMVSTEEAKRHLNGLLEERKILAQ 300
Cdd:PRK12704 162 KVEEEAR----HEAAVLIKEIEEEAKEEADKKAKEILAQ 196
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
42-371 |
5.56e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 42 RQAQMSKELIELNKALALKEaLAKKMTQNDNQLQPIQFQYqDNIKNLESEVLSLQREKEELVLELQTAKKDANQAK--LS 119
Cdd:COG4717 110 ELEELREELEKLEKLLQLLP-LYQELEALEAELAELPERL-EELEERLEELRELEEELEELEAELAELQEELEELLeqLS 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 120 ERRRKRLQELEGQIADLKKKLQEQSKLLKLKESTehtVSKLNQEIRMMKNQRVQLMRQMKEDAEK--------------- 184
Cdd:COG4717 188 LATEEELQDLAEELEELQQRLAELEEELEEAQEE---LEELEEELEQLENELEAAALEERLKEARlllliaaallallgl 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 185 ----------------------------FRQWKQQKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANK 236
Cdd:COG4717 265 ggsllsliltiagvlflvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 237 RLKDALQKQKEVAEKRKETQsrgMESTAARMKNWLGneiEVMVSTEEAkrhlnglLEERKILAQDVAQLKEKRESgenpp 316
Cdd:COG4717 345 RIEELQELLREAEELEEELQ---LEELEQEIAALLA---EAGVEDEEE-------LRAALEQAEEYQELKEELEE----- 406
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1039796408 317 LKLRRRTFSYDEIHGQDSGAEDSIAKQIESLETELELRSAQIADLQQKLLDAESE 371
Cdd:COG4717 407 LEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAE 461
|
|
| PLN02678 |
PLN02678 |
seryl-tRNA synthetase |
172-284 |
5.72e-03 |
|
seryl-tRNA synthetase
Pssm-ID: 215364 [Multi-domain] Cd Length: 448 Bit Score: 39.69 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796408 172 VQLMRQMK-EDAEKFRQWKQQKDK------EVIQLKERDRKRQYELLKLERNF---QKQSNVLRRKTEEAAaankrlkDA 241
Cdd:PLN02678 4 INLFREEKgGDPELIRESQRRRFAsvelvdEVIALDKEWRQRQFELDSLRKEFnklNKEVAKLKIAKEDAT-------EL 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1039796408 242 LQKQKEVAEKRKETQSRGMESTAARMK--NWLGNEI--EVMVSTEEA 284
Cdd:PLN02678 77 IAETKELKKEITEKEAEVQEAKAALDAklKTIGNLVhdSVPVSNDEA 123
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