|
Name |
Accession |
Description |
Interval |
E-value |
| SAM_liprin-alpha1,2,3,4_repeat2 |
cd09565 |
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ... |
961-1026 |
3.72e-43 |
|
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.
Pssm-ID: 188964 Cd Length: 66 Bit Score: 150.70 E-value: 3.72e-43
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568952890 961 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLRRL 1026
Cdd:cd09565 1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
|
|
| SAM_liprin-alpha1,2,3,4_repeat1 |
cd09562 |
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 ... |
874-944 |
8.59e-43 |
|
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.
Pssm-ID: 188961 Cd Length: 71 Bit Score: 150.02 E-value: 8.59e-43
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952890 874 FAQWDGPTVVVWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEIMSLT 944
Cdd:cd09562 1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
|
|
| SAM_liprin-alpha1,2,3,4_repeat3 |
cd09568 |
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ... |
1046-1117 |
2.74e-42 |
|
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.
Pssm-ID: 188967 Cd Length: 72 Bit Score: 148.62 E-value: 2.74e-42
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568952890 1046 DVLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLL 1117
Cdd:cd09568 1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
|
|
| SAM_liprin-kazrin_repeat2 |
cd09495 |
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ... |
965-1024 |
3.88e-29 |
|
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and in adheren junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188894 Cd Length: 60 Bit Score: 110.70 E-value: 3.88e-29
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 965 WIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLR 1024
Cdd:cd09495 1 WWVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLVHLKVTSQLHHLSLKCGIHVLH 60
|
|
| SAM_liprin-kazrin_repeat1 |
cd09494 |
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
881-939 |
1.09e-26 |
|
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of the SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and adherens junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188893 Cd Length: 58 Bit Score: 103.46 E-value: 1.09e-26
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 568952890 881 TVVVWLELWVGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 939
Cdd:cd09494 1 RVCAWLEDFGLMP-MYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
|
|
| SAM_liprin-kazrin_repeat3 |
cd09496 |
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of ... |
1054-1115 |
2.42e-24 |
|
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and in adherens junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188895 Cd Length: 62 Bit Score: 97.23 E-value: 2.42e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568952890 1054 RVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNN 1115
Cdd:cd09496 1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETEFNN 62
|
|
| SAM_kazrin_repeat3 |
cd09570 |
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin ... |
1046-1117 |
6.36e-22 |
|
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188969 Cd Length: 72 Bit Score: 90.58 E-value: 6.36e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568952890 1046 DVLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLL 1117
Cdd:cd09570 1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
260-512 |
8.67e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.14 E-value: 8.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 260 RQARE-QSQMKERLASLSSHA-AELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATS 337
Cdd:COG1196 213 ERYRElKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 338 VHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKL----QQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEE 413
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELeeleEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 414 RLRQMEAQLEEKNQELQRARQREKMNEEHNKRLsdtvDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQ 493
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEEL----EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250
....*....|....*....
gi 568952890 494 HDKDQLVVTIEALKAELEQ 512
Cdd:COG1196 449 EEEAELEEEEEALLELLAE 467
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
248-517 |
9.36e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.14 E-value: 9.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 248 LAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKR 327
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 328 YLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQT----LRKAETLPEVEAELAQRVAALSK 403
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAeealLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 404 AEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKL---LSESNERLQLHLKERMAALEDKNSLLR 480
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEeeaLEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270
....*....|....*....|....*....|....*..
gi 568952890 481 EVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRG 517
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL 507
|
|
| SAM_kazrin_repeat1 |
cd09564 |
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ... |
875-939 |
2.08e-16 |
|
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrin contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved into interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188963 Cd Length: 70 Bit Score: 74.80 E-value: 2.08e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568952890 875 AQWDGPTVVVWLELWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 939
Cdd:cd09564 2 SRWKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
|
|
| SAM_liprin-beta1,2_repeat3 |
cd09569 |
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ... |
1046-1117 |
1.05e-15 |
|
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.
Pssm-ID: 188968 Cd Length: 72 Bit Score: 72.87 E-value: 1.05e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568952890 1046 DVLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLL 1117
Cdd:cd09569 1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
|
|
| SAM_kazrin_repeat2 |
cd09567 |
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ... |
960-1024 |
2.70e-15 |
|
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188966 Cd Length: 65 Bit Score: 71.29 E-value: 2.70e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568952890 960 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLR 1024
Cdd:cd09567 1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
246-516 |
2.87e-15 |
|
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: 81.26 E-value: 2.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 246 EDLAKVLELQ-EVIDRQAREQSQMKE--------RLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKED 316
Cdd:TIGR02168 192 EDILNELERQlKSLERQAEKAERYKElkaelrelELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 317 MEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQ 396
Cdd:TIGR02168 272 LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 397 RVAALSKAEERHG----NIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVdKLLSESNERLQLHLKERMAAL 472
Cdd:TIGR02168 352 ELESLEAELEELEaeleELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL-ERLEDRRERLQQEIEELLKKL 430
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 568952890 473 E--DKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLR 516
Cdd:TIGR02168 431 EeaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
|
| SAM_liprin-beta1,2_repeat2 |
cd09566 |
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ... |
960-1024 |
2.91e-15 |
|
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta potentially is able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.
Pssm-ID: 188965 Cd Length: 63 Bit Score: 71.19 E-value: 2.91e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568952890 960 DMNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRNSFQCGIMCLR 1024
Cdd:cd09566 1 KLDTHWV-LRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDLL-HLKVTSALHHASIRRGIQVLR 63
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
192-516 |
2.97e-14 |
|
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: 77.80 E-value: 2.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 192 LEEELGATHKELMILKEQNNQKKTLTDGLLDgnhEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIdrqAREQSQMKER 271
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQ---ELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL---EEDLSSLEQE 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 272 LASLSSHAAELEEDLDTARKDLIKSEEMNTKLQRE-----VREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLE 346
Cdd:TIGR02169 753 IENVKSELKELEARIEELEEDLHKLEEALNDLEARlshsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 347 NEIANKDSMHRQTEDKNRQLQERLELAEQKLQqtlrkaetlpEVEAELAQRVAALSKAEERHGNIEERLRQMEAQL---E 423
Cdd:TIGR02169 833 KEIQELQEQRIDLKEQIKSIEKEIENLNGKKE----------ELEEELEELEAALRDLESRLGDLKKERDELEAQLrelE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 424 EKNQELQRARQREKMN-----------EEHNKRLSDTVDKLLSESNERLQLH-LKERMAALEDKNSLLREVEN-AKKQLE 490
Cdd:TIGR02169 903 RKIEELEAQIEKKRKRlselkaklealEEELSEIEDPKGEDEEIPEEELSLEdVQAELQRVEEEIRALEPVNMlAIQEYE 982
|
330 340
....*....|....*....|....*.
gi 568952890 491 ETQHDKDQLVVTIEALKAELEQMRLR 516
Cdd:TIGR02169 983 EVLKRLDELKEKRAKLEEERKAILER 1008
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
253-516 |
5.00e-14 |
|
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: 77.40 E-value: 5.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 253 ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQ 332
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 333 REATSVHDLNDKLENEIAnkdsmhrQTEDKNRQLQERLELAEQKLQQTlrkAETLPEVEAELAQRVAALSKAEERHGNIE 412
Cdd:TIGR02168 761 AEIEELEERLEEAEEELA-------EAEAEIEELEAQIEQLKEELKAL---REALDELRAELTLLNEEAANLRERLESLE 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 413 ERLRQMEAQLEEKNQELQRAR-QREKMNEEHNKrlsdtVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEE 491
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSeDIESLAAEIEE-----LEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905
|
250 260
....*....|....*....|....*
gi 568952890 492 TQHDKDQLVVTIEALKAELEQMRLR 516
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELR 930
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
245-474 |
1.19e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 75.74 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 245 HEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTL 324
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 325 EKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKA 404
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 405 EErhgniEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLsdtvDKLLSESNERLQLHLKERMAALED 474
Cdd:COG1196 444 LE-----EAAEEEAELEEEEEALLELLAELLEEAALLEAALA----ELLEELAEAAARLLLLLEAEADYE 504
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
960-1024 |
5.11e-13 |
|
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.
Pssm-ID: 425739 Cd Length: 64 Bit Score: 64.98 E-value: 5.11e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568952890 960 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRNSFQCGIMCLR 1024
Cdd:pfam00536 1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
187-516 |
5.60e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.94 E-value: 5.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 187 ERCSLLEEELGATHKELMILKEQNNQKKTLTDGLLDGNHEQESapstngkrssdgsLSHEDLAKVLELQEVIDRQAREQS 266
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR-------------QISALRKDLARLEAEVEQLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 267 QMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLE 346
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 347 NEIANKDSMHRQTEDKNRQLQERLELAEQ---KLQQTLRKAET-LPEVEAELAQRVAALSKAEERHGNIEERLRQMEaql 422
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAeieELEELIEELESeLEALLNERASLEEALALLRSELEELSEELRELE--- 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 423 eEKNQELQRARQ--REKMNEEHNK--RLSDTVDKLLSESNERLQLHLkerMAALEDKNSLLREVENAKKQLEETQHDKDQ 498
Cdd:TIGR02168 908 -SKRSELRRELEelREKLAQLELRleGLEVRIDNLQERLSEEYSLTL---EEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
330
....*....|....*....
gi 568952890 499 L-VVTIEALkAELEQMRLR 516
Cdd:TIGR02168 984 LgPVNLAAI-EEYEELKER 1001
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
192-464 |
5.65e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.94 E-value: 5.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 192 LEEELGATHKELMI--LKEQNNQKKTLTDGLLDGNHEQESApsTNGKRSSDGSLS------HEDLAKVLELQEVIDRQAR 263
Cdd:TIGR02168 218 LKAELRELELALLVlrLEELREELEELQEELKEAEEELEEL--TAELQELEEKLEelrlevSELEEEIEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 264 EQSQM-------KERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITT-------LEKRYL 329
Cdd:TIGR02168 296 EISRLeqqkqilRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEleaeleeLESRLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 330 AAQREATSVHDLNDKLENEIA--------NKDSMHRQTEDKNRQLQERLELAEQKLQQTLRK-AETLPEVEAELAQRVAA 400
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIAslnneierLEARLERLEDRRERLQQEIEELLKKLEEAELKElQAELEELEEELEELQEE 455
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568952890 401 LSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLH 464
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
74-462 |
1.11e-12 |
|
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: 72.78 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 74 ERDSLQRQLNtALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLLLEHLECLVSRHERSLRmTVVKRQAQSPAG 153
Cdd:TIGR02168 678 EIEELEEKIE-ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE-QLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 154 VSS----EVEVLKALKSLFEHHKALDEK---VRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGLLDGNHE 226
Cdd:TIGR02168 756 LTEleaeIEELEERLEEAEEELAEAEAEieeLEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 227 QESAPSTNGKRSSDGSLSHEDLAKVLE-LQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQR 305
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEeLEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 306 EVREAMAQKEDMEERITTLEkrylaaQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQtlrkae 385
Cdd:TIGR02168 916 ELEELREKLAQLELRLEGLE------VRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE------ 983
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 386 tLPEVEAElaqrvaalskAEERHGNIEERLRQMEAQLEeknqELQRARQR-----EKMNEEHNKRLSDTVDKLlsesNER 460
Cdd:TIGR02168 984 -LGPVNLA----------AIEEYEELKERYDFLTAQKE----DLTEAKETleeaiEEIDREARERFKDTFDQV----NEN 1044
|
..
gi 568952890 461 LQ 462
Cdd:TIGR02168 1045 FQ 1046
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
54-432 |
1.13e-12 |
|
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: 72.78 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 54 LRETQETLALTQGKLHEVGHERDSLQRQLNTAlpQEFAALTKELNvcREQLLEREEEIAELKAERNNTRLLLEHLECLVS 133
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKSLERQAEKA--ERYKELKAELR--ELELALLVLRLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 134 RHERSLrmtvvkrqaqspagvssevevlKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQk 213
Cdd:TIGR02168 257 ELTAEL----------------------QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 214 ktltdglLDGNHEQESAPSTNGKRSSDgsLSHEDLA----KVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTA 289
Cdd:TIGR02168 314 -------LERQLEELEAQLEELESKLD--ELAEELAeleeKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 290 RKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHdlNDKLENEIANKDSMHRQTEDKNRQLQER 369
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEA 462
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568952890 370 LELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRA 432
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVL 525
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
221-512 |
2.59e-12 |
|
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: 71.64 E-value: 2.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 221 LDGNHEQESAPSTNGKRSSDG--SLSHEDLAKVLELQEVIDrqareqsQMKERLASLSSHAAELEEDLDTARKDLIKSEE 298
Cdd:TIGR02169 644 LEGELFEKSGAMTGGSRAPRGgiLFSRSEPAELQRLRERLE-------GLKRELSSLQSELRRIENRLDELSQELSDASR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 299 MNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIAnkdsmhRQTEDKNrQLQERLELAEQKLQ 378
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE------ELEEDLH-KLEEALNDLEARLS 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 379 QtlrkaETLPEVEAElaqrvaaLSKAEERHGNIEERLRQMEAQLEEKNQELQRArqREKMNEEHNKRLS-----DTVDKL 453
Cdd:TIGR02169 790 H-----SRIPEIQAE-------LSKLEEEVSRIEARLREIEQKLNRLTLEKEYL--EKEIQELQEQRIDlkeqiKSIEKE 855
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568952890 454 LSESN---ERLQLHLKERMAALED----KNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQ 512
Cdd:TIGR02169 856 IENLNgkkEELEEELEELEAALRDlesrLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
245-441 |
6.64e-12 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 66.87 E-value: 6.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 245 HEDLAKVLELQEvIDRQAReqsQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTL 324
Cdd:COG1579 3 PEDLRALLDLQE-LDSELD---RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 325 EKRylaaQREATSVHDLNDkLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQqtlrkaetlpEVEAELAQRVAALSKA 404
Cdd:COG1579 79 EEQ----LGNVRNNKEYEA-LQKEIESLKRRISDLEDEILELMERIEELEEELA----------ELEAELAELEAELEEK 143
|
170 180 190
....*....|....*....|....*....|....*..
gi 568952890 405 EERhgnIEERLRQMEAQLEEKNQElqRARQREKMNEE 441
Cdd:COG1579 144 KAE---LDEELAELEAELEELEAE--REELAAKIPPE 175
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
155-672 |
1.40e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 155 SSEVEVLKALKSL--FEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGLLDGNHEQESAps 232
Cdd:COG1196 219 KEELKELEAELLLlkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE-- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 233 tngKRSSDGSLSHEdLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMA 312
Cdd:COG1196 297 ---LARLEQDIARL-EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 313 QKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAEtlpEVEA 392
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE---EAAE 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 393 ELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDtvdkllsESNERLQLHLKERMAAL 472
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG-------FLEGVKAALLLAGLRGL 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 473 EDKNSLLREVENAKKQLEET----------QHDKDQLVVTIEALKAE---------LEQMRLRGPSLHHGRPHLGS---- 529
Cdd:COG1196 523 AGAVAVLIGVEAAYEAALEAalaaalqnivVEDDEVAAAAIEYLKAAkagratflpLDKIRARAALAAALARGAIGaavd 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 530 ------VPDFRFSVADGHVDAYSTSAVLRRPQKGRLAALRDEPSKVQTL------------------NEQDWERAQQASV 585
Cdd:COG1196 603 lvasdlREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLegeggsaggsltggsrreLLAALLEAEAELE 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 586 LANVAQAFESDVDVSDGEDDRDTLLSSVDLLSPSGQADAQTLAMMLQEQLDAINKEIRLIQEEKENTEQ---------RA 656
Cdd:COG1196 683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEaleelpeppDL 762
|
570
....*....|....*...
gi 568952890 657 EEIESRVGS--GSLDNLG 672
Cdd:COG1196 763 EELERELERleREIEALG 780
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
158-514 |
1.76e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.91 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 158 VEVLKALKSLFEHHkaldEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGLLDGNHEQESAPSTNGKR 237
Cdd:PRK02224 233 RETRDEADEVLEEH----EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDAD 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 238 SSDGSLSHEDLAKVL-ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKED 316
Cdd:PRK02224 309 AEAVEARREELEDRDeELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 317 MEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQklqqtLRKAETLPEVEAEL-- 394
Cdd:PRK02224 389 LEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA-----LLEAGKCPECGQPVeg 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 395 AQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLS--DTVDKLLSESNERLQ------LHLK 466
Cdd:PRK02224 464 SPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIEekreraEELR 543
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 568952890 467 ERMAALEDKNSLLREVenAKKQLEETQhDKDQLVVTIEALKAELEQMR 514
Cdd:PRK02224 544 ERAAELEAEAEEKREA--AAEAEEEAE-EAREEVAELNSKLAELKERI 588
|
|
| SAM_liprin-beta1,2_repeat1 |
cd09563 |
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
874-938 |
3.03e-11 |
|
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta protein contain three copies (repeats) of SAM domain. They may form heterodimers with liprins-alpha through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta is potentially able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.
Pssm-ID: 188962 Cd Length: 64 Bit Score: 59.93 E-value: 3.03e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568952890 874 FAQWDGPTVVVWL-ELWVGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQ 938
Cdd:cd09563 1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
179-508 |
6.20e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 67.29 E-value: 6.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 179 RERLRVALERCSLLEEELGATHKELmiLKEQnnQKKTLTDGLLDGNHEQESAPSTNGKRSSDgslsHedLAKVLE---LQ 255
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTSRRQL--AAEQ--YRLVEMARELAELNEAESDLEQDYQAASD----H--LNLVQTalrQQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 256 EVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEmntklqrEVREAMAQKEDMEERITTLEKR---YLAAQ 332
Cdd:PRK04863 348 EKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEE-------EVDELKSQLADYQQALDVQQTRaiqYQQAV 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 333 REATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQ-------------QTLRKAetLPEVEAELAQRVA 399
Cdd:PRK04863 421 QALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSvaqaahsqfeqayQLVRKI--AGEVSRSEAWDVA 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 400 --ALSKAEErHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDkllseSNERLQLHLKERMAALEDKNS 477
Cdd:PRK04863 499 reLLRRLRE-QRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLD-----DEDELEQLQEELEARLESLSE 572
|
330 340 350
....*....|....*....|....*....|.
gi 568952890 478 llrEVENAKKQLEETQHDKDQLVVTIEALKA 508
Cdd:PRK04863 573 ---SVSEARERRMALRQQLEQLQARIQRLAA 600
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
205-511 |
7.27e-11 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 66.68 E-value: 7.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 205 ILKEQNNQKKTLTDGLLDGNHEQESAPSTNGKRSSDGSLSHEDLAKVL---------------ELQEVIDRQAREQSQMK 269
Cdd:pfam15921 132 IRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMlshegvlqeirsilvDFEEASGKKIYEHDSMS 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 270 E-RLASLSSHAAELEEDLDTARKDLI--------KSEEMNTKLQREVREAMAQKEDMEER--------ITTLEKRYLAAQ 332
Cdd:pfam15921 212 TmHFRSLGSAISKILRELDTEISYLKgrifpvedQLEALKSESQNKIELLLQQHQDRIEQliseheveITGLTEKASSAR 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 333 REATSVHDLNDKLENEIANKDSMHRqtedknRQLQErLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAE------- 405
Cdd:pfam15921 292 SQANSIQSQLEIIQEQARNQNSMYM------RQLSD-LESTVSQLRSELREAKRMYEDKIEELEKQLVLANSEltearte 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 406 -----ERHGNIEERLRQMEAQLEEKNQELQrarqrekMNEEHNKRLSD-------TVDKLLSESNER------------- 460
Cdd:pfam15921 365 rdqfsQESGNLDDQLQKLLADLHKREKELS-------LEKEQNKRLWDrdtgnsiTIDHLRRELDDRnmevqrleallka 437
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 568952890 461 ----LQLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELE 511
Cdd:pfam15921 438 mkseCQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLE 492
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
44-513 |
1.31e-10 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 66.15 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 44 LEERDRLLDTLR-ETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTR 122
Cdd:TIGR00618 417 SAFRDLQGQLAHaKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARL 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 123 LLLEHLECLVSRHERSLRMTVVkrQAQSPAGVSSEVEvlkALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKE 202
Cdd:TIGR00618 497 LELQEEPCPLCGSCIHPNPARQ--DIDNPGPLTRRMQ---RGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQS 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 203 LMILKEQNNQKKTLTDGLLdgNHEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQ--AREQSQMKERLASLSSHAA 280
Cdd:TIGR00618 572 FSILTQCDNRSKEDIPNLQ--NITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQdvRLHLQQCSQELALKLTALH 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 281 ELEEDL------DTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDlNDKLENEIANKDS 354
Cdd:TIGR00618 650 ALQLTLtqervrEHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEE-YDREFNEIENASS 728
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 355 MHRQTedknrqLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGnieERLRQMEAQLEEKNQELQRARQ 434
Cdd:TIGR00618 729 SLGSD------LAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTG---AELSHLAAEIQFFNRLREEDTH 799
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568952890 435 REKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQM 513
Cdd:TIGR00618 800 LLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
45-491 |
1.46e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLL 124
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 125 LEHLEcLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELM 204
Cdd:COG1196 417 ERLEE-ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 205 ILKEQNNQKKTLTDGLLDGNHEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEE 284
Cdd:COG1196 496 LLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAT 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 285 DLdtaRKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEdKNR 364
Cdd:COG1196 576 FL---PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLRE-VTL 651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 365 QLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNK 444
Cdd:COG1196 652 EGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLE 731
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 568952890 445 RLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEE 491
Cdd:COG1196 732 AEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
152-660 |
2.76e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 2.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 152 AGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGLLDGNHEQ---- 227
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERleel 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 228 -ESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQRE 306
Cdd:COG1196 322 eEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 307 VREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIankdsmhRQTEDKNRQLQERLELAEQKLQQTLRKAEt 386
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL-------EEAAEEEAELEEEEEALLELLAELLEEAA- 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 387 lpEVEAELAQRVAALSKAEERhgniEERLRQMEAQLEEKNQELQRARQREKMNEEHNK--RLSDTVDKLLSESNERLQLH 464
Cdd:COG1196 474 --LLEAALAELLEELAEAAAR----LLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAvaVLIGVEAAYEAALEAALAAA 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 465 LKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRGPSLHHGRPHLGSVPDFRFsvadGHVDA 544
Cdd:COG1196 548 LQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVL----GDTLL 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 545 YSTSAVLRRPQKGRLAALRDEPSKVQTLNEQDWERAQQASVLANVAQAFESDVDVSDGEDDRDTLLSSVDLLSPSGQADA 624
Cdd:COG1196 624 GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE 703
|
490 500 510
....*....|....*....|....*....|....*.
gi 568952890 625 QTLAMMLQEQLDAINKEIRLIQEEKENTEQRAEEIE 660
Cdd:COG1196 704 EEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
267-514 |
3.24e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 267 QMKERLASLSSHAAELEEDLDtarkdlikseemntKLQREVREAmAQKEDMEERITTLEKRYLAAQREAtsVHDLNDKLE 346
Cdd:COG1196 183 ATEENLERLEDILGELERQLE--------------PLERQAEKA-ERYRELKEELKELEAELLLLKLRE--LEAELEELE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 347 NEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHgniEERLRQMEAQLEEKN 426
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL---EERRRELEERLEELE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 427 QELQRARQREKMNEEHNKRLSDTVDKL----------LSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQHDK 496
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAeeeleeaeaeLAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
250
....*....|....*...
gi 568952890 497 DQLVVTIEALKAELEQMR 514
Cdd:COG1196 403 EELEEAEEALLERLERLE 420
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
272-519 |
4.67e-10 |
|
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: 62.86 E-value: 4.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 272 LASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYlaaqreatsvhdlnDKLENEIAN 351
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI--------------RALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 352 KDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETL---PEVEAELAQR-VAALSKAEERHGNIEERLRQMEAQLEEKNQ 427
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAELLRALYRLgrqPPLALLLSPEdFLDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 428 ELQRARQREkmnEEHNKRLSDTVDKlLSESNERLQLHLKERMAALedkNSLLREVENAKKQLEETQHDKDQLVVTIEALK 507
Cdd:COG4942 161 ELAALRAEL---EAERAELEALLAE-LEEERAALEALKAERQKLL---ARLEKELAELAAELAELQQEAEELEALIARLE 233
|
250
....*....|..
gi 568952890 508 AELEQMRLRGPS 519
Cdd:COG4942 234 AEAAAAAERTPA 245
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
284-516 |
6.26e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.54 E-value: 6.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 284 EDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREAtsvhdlndkleNEIankdsmhrqtEDKN 363
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREI-----------NEI----------SSEL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 364 RQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQ---LEEKNQELQRARQREKMNE 440
Cdd:PRK03918 217 PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEieeLEEKVKELKELKEKAEEYI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 441 EHNKRLSDTVDKL------LSESNERLQlHLKERMAALEDKNSLLREVENAKKQLE---ETQHDKDQLVVTIEALKAELE 511
Cdd:PRK03918 297 KLSEFYEEYLDELreiekrLSRLEEEIN-GIEERIKELEEKEERLEELKKKLKELEkrlEELEERHELYEEAKAKKEELE 375
|
....*
gi 568952890 512 QMRLR 516
Cdd:PRK03918 376 RLKKR 380
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
246-511 |
7.44e-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: 63.55 E-value: 7.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 246 EDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNtKLQREVREA-----MAQKEDMEER 320
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQ-ALLKEKREYegyelLKEKEALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 321 ITTLEKRYLAAQREATSVHDLNDKLENEIAnkdsmhrQTEDKNRQLQERLELAEQKLQQTLRkaETLPEVEAELAQRVAA 400
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLE-------EIEQLLEELNKKIKDLGEEEQLRVK--EKIGELEAEIASLERS 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 401 LSKAEERHGNIEERLRQMEAQLEEKNQEL--------QRARQREKMNEEHnKRLSDTVDKLLSE------SNERLQLHLK 466
Cdd:TIGR02169 310 IAEKERELEDAEERLAKLEAEIDKLLAEIeelereieEERKRRDKLTEEY-AELKEELEDLRAEleevdkEFAETRDELK 388
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 568952890 467 ERMAALED----KNSLLREVE---NAKKQLEETQHDKDQLVVTIEALKAELE 511
Cdd:TIGR02169 389 DYREKLEKlkreINELKRELDrlqEELQRLSEELADLNAAIAGIEAKINELE 440
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
152-491 |
8.08e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 8.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 152 AGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLtDGLLDGNHEQESAP 231
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKEL-KEKAEEYIKLSEFY 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 232 STNGKRSSDGSlshEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQR----EV 307
Cdd:PRK03918 303 EEYLDELREIE---KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEElerlKK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 308 REAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIAN-KDSMHRQTEDKNRQLQERLELAEQKLQQTLRK-AE 385
Cdd:PRK03918 380 RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKElKKAIEELKKAKGKCPVCGRELTEEHRKELLEEyTA 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 386 TLPEVEAELAQRVAALSKAEERHGNIEE---------RLRQMEAQLEEKNQELqrarqrEKMNEEHNKRLSDTVDKLLSE 456
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKvlkkeseliKLKELAEQLKELEEKL------KKYNLEELEKKAEEYEKLKEK 533
|
330 340 350
....*....|....*....|....*....|....*..
gi 568952890 457 SN--ERLQLHLKERMAALEDKNSLLREVENAKKQLEE 491
Cdd:PRK03918 534 LIklKGEIKSLKKELEKLEELKKKLAELEKKLDELEE 570
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
236-498 |
9.15e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.62 E-value: 9.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 236 KRSSDGSLSHEDLAKVLELQEVID--RQAREQSQMKE-RLASLSSHAAELEEDLDTARKD-LIKSEEMntKLQREVREAM 311
Cdd:PTZ00121 1490 KKAEEAKKKADEAKKAAEAKKKADeaKKAEEAKKADEaKKAEEAKKADEAKKAEEKKKADeLKKAEEL--KKAEEKKKAE 1567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 312 AQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTED---------KNRQLQERLELAEQKLQQTLR 382
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikaeelkKAEEEKKKVEQLKKKEAEEKK 1647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 383 KAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLlsesnERLQ 462
Cdd:PTZ00121 1648 KAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA-----EELK 1722
|
250 260 270
....*....|....*....|....*....|....*.
gi 568952890 463 LHLKERMAALEDknsLLREVENAKKQLEETQHDKDQ 498
Cdd:PTZ00121 1723 KAEEENKIKAEE---AKKEAEEDKKKAEEAKKDEEE 1755
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
110-512 |
1.85e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.38 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 110 EIAELKAErnntrlllehleclvsrherslrmtvVKRQAqspagvSSEVEVLKALKSLFEHHKALDEKVRERLRVALErc 189
Cdd:TIGR02168 678 EIEELEEK--------------------------IEELE------EKIAELEKALAELRKELEELEEELEQLRKELEE-- 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 190 slLEEELGATHKELMIL-KEQNNQKKTLTDGLLDGNHEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQM 268
Cdd:TIGR02168 724 --LSRQISALRKDLARLeAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 269 KERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENE 348
Cdd:TIGR02168 802 REALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE 881
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 349 IAnkdsmhrqtedknrQLQERLELAEQKLQQtlrKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKnqe 428
Cdd:TIGR02168 882 RA--------------SLEEALALLRSELEE---LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL--- 941
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 429 LQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKER-------MAALEDKNSLLREVENAKKQLEETQHDKDQLVV 501
Cdd:TIGR02168 942 QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIkelgpvnLAAIEEYEELKERYDFLTAQKEDLTEAKETLEE 1021
|
410
....*....|.
gi 568952890 502 TIEALKAELEQ 512
Cdd:TIGR02168 1022 AIEEIDREARE 1032
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
38-529 |
1.85e-09 |
|
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: 62.37 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 38 QLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHER--DSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELK 115
Cdd:TIGR00606 353 QLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERqiKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIR 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 116 AERNNTRLLLEHLECLVSRHERSLRMtvVKRQAQSPAGVSSEV-----EVLKALK--SLFEHHKALDEKVRERLRVALER 188
Cdd:TIGR00606 433 DEKKGLGRTIELKKEILEKKQEELKF--VIKELQQLEGSSDRIleldqELRKAERelSKAEKNSLTETLKKEVKSLQNEK 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 189 CSLLEEElgatHKELMILKEQNNQKKTLTDGLL---DGNHEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQ 265
Cdd:TIGR00606 511 ADLDRKL----RKLDQEMEQLNHHTTTRTQMEMltkDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEI 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 266 SQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQkEDMEERITTLEKRYLAAQREA---TSVHDLN 342
Cdd:TIGR00606 587 NQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS-QDEESDLERLKEEIEKSSKQRamlAGATAVY 665
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 343 DKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAET-LPEVEAELA----QRVAALSKAEERHGNIEERLRQ 417
Cdd:TIGR00606 666 SQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDkLKSTESELKkkekRRDEMLGLAPGRQSIIDLKEKE 745
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 418 MEaQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESN---------ERLQLHLKE------RMAALEDKNSLLREV 482
Cdd:TIGR00606 746 IP-ELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKvcltdvtimERFQMELKDverkiaQQAAKLQGSDLDRTV 824
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 568952890 483 ENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRGPSLHHGRPHLGS 529
Cdd:TIGR00606 825 QQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKS 871
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
249-516 |
4.93e-09 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 60.08 E-value: 4.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 249 AKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRY 328
Cdd:pfam19220 48 SRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 329 LAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERH 408
Cdd:pfam19220 128 AAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDAT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 409 gniEERLRQMEAQLEEKNQELQRA-RQREKMNEEHNKRLSdTVDKLLSESNERL----QLhLKERMAALEDKNSLLREVE 483
Cdd:pfam19220 208 ---RARLRALEGQLAAEQAERERAeAQLEEAVEAHRAERA-SLRMKLEALTARAaateQL-LAEARNQLRDRDEAIRAAE 282
|
250 260 270
....*....|....*....|....*....|...
gi 568952890 484 NAkkqLEETQHDKDQLVVTIEALKAELEQMRLR 516
Cdd:pfam19220 283 RR---LKEASIERDTLERRLAGLEADLERRTQQ 312
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
254-520 |
4.94e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 4.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 254 LQEVIdrqaREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRylaaQR 333
Cdd:PRK03918 167 LGEVI----KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL----KE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 334 EATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQK---LQQTLRKAETLPEVEAELAQRVAALSKAEERHGN 410
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkeLKELKEKAEEYIKLSEFYEEYLDELREIEKRLSR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 411 IEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDtvdklLSESNERLQ--LHLKERMAALEDKNSLLrEVENAKKQ 488
Cdd:PRK03918 319 LEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEE-----LEERHELYEeaKAKKEELERLKKRLTGL-TPEKLEKE 392
|
250 260 270
....*....|....*....|....*....|..
gi 568952890 489 LEETQHDKDQLVVTIEALKAELEQMRLRGPSL 520
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKEL 424
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
258-441 |
6.87e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.46 E-value: 6.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 258 IDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREV----REAMAQKEDMEERITTLEKRYLAAQR 333
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIdklqAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 334 ------------EATSVHDLNDKLE--NEI--ANKDSMHRQTEDKNR--QLQERLELAEQKLQQTLRKAET-LPEVEAEL 394
Cdd:COG3883 98 sggsvsyldvllGSESFSDFLDRLSalSKIadADADLLEELKADKAEleAKKAELEAKLAELEALKAELEAaKAELEAQQ 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568952890 395 AQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEE 441
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
253-435 |
8.61e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.01 E-value: 8.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 253 ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYlAAQ 332
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL-AEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 333 REATSVHDLNDKLENEIANKD------------SMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAA 400
Cdd:COG4942 110 LRALYRLGRQPPLALLLSPEDfldavrrlqylkYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189
|
170 180 190
....*....|....*....|....*....|....*
gi 568952890 401 LSKAEERHGNIEERLRQMEAQLEEKNQELQRARQR 435
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
302-493 |
9.86e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.69 E-value: 9.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 302 KLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIankDSMHRQTEDKNRQLQERLELAEQKLQQTL 381
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI---DKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 382 RKAETLPEVEA--------ELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKL 453
Cdd:COG3883 97 RSGGSVSYLDVllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568952890 454 LSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQ 493
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
37-452 |
1.00e-08 |
|
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: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 37 EQLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELnvcreqllEREEEIAELKA 116
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA--------LLEAALAELLE 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 117 ERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKslfehhKALDEKVRERLRVALERCSLLEEEL 196
Cdd:COG1196 485 ELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVE------AAYEAALEAALAAALQNIVVEDDEV 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 197 GATHKELmiLKEQNNQKKTLTDGLLDGNHEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASLS 276
Cdd:COG1196 559 AAAAIEY--LKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAAL 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 277 SHAAELEEDLDTARKDL-----------IKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKL 345
Cdd:COG1196 637 RRAVTLAGRLREVTLEGeggsaggsltgGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER 716
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 346 ENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNI-----------EER 414
Cdd:COG1196 717 LEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPVnllaieeyeelEER 796
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 568952890 415 LRQMEAQLEeknqELQRARQR-----EKMNEEHNKRLSDTVDK 452
Cdd:COG1196 797 YDFLSEQRE----DLEEARETleeaiEEIDRETRERFLETFDA 835
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
315-582 |
1.36e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 315 EDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQ-TLRKAETLPEVEAE 393
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQlEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 394 LAQRVAALSKAEErhgnieerLRQMEAQLEEKNQELQraRQREKMNEEHNkrlsdTVDKLLSESNERLQLHLKERMAALE 473
Cdd:TIGR02168 760 EAEIEELEERLEE--------AEEELAEAEAEIEELE--AQIEQLKEELK-----ALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 474 DKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRGPSLHHGRPHLGSVPDFRFSVADGHVDAYSTSAVLRR 553
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
250 260 270
....*....|....*....|....*....|..
gi 568952890 554 PQKGRLAALRDEPSKVQTLNEQ---DWERAQQ 582
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQlelRLEGLEV 936
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
360-511 |
1.45e-08 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 58.64 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 360 EDKNRQLQERLELAEQKLQQTLRKAETlpEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMN 439
Cdd:PRK12704 45 EEAKKEAEAIKKEALLEAKEEIHKLRN--EFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQK 122
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568952890 440 EEHNKRLSDTVDKLLSESNERLqlhlkERMAAL---EDKNSLLREVEnakkqlEETQHDKDQLVVTIEAlKAELE 511
Cdd:PRK12704 123 QQELEKKEEELEELIEEQLQEL-----ERISGLtaeEAKEILLEKVE------EEARHEAAVLIKEIEE-EAKEE 185
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
45-441 |
1.48e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.31 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALpqEFAALTKELnvcreqlleREEEIAELKAERNNTRLL 124
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE--RYQALLKEK---------REYEGYELLKEKEALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 125 LEHLECLVSRHERSLRmtvvKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKvrERLRValercsllEEELGATHKELM 204
Cdd:TIGR02169 239 KEAIERQLASLEEELE----KLTEEISELEKRLEEIEQLLEELNKKIKDLGEE--EQLRV--------KEKIGELEAEIA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 205 ILKEQNNQKKtltdglldgnHEQESApstNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLAslsshaaELEE 284
Cdd:TIGR02169 305 SLERSIAEKE----------RELEDA---EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYA-------ELKE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 285 DLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNR 364
Cdd:TIGR02169 365 ELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKE 444
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568952890 365 QLQERLELAEQKLQQTlrkaetlpeveaelaqrVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEE 441
Cdd:TIGR02169 445 DKALEIKKQEWKLEQL-----------------AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
31-514 |
1.65e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 58.98 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 31 DADSHFEQLMVSMLEERDrlldTLRETQETLALTQGKLHEVGHERDSLQ----RQLNTALPQEFAALTKELNVCREQLLE 106
Cdd:pfam15921 167 DSNTQIEQLRKMMLSHEG----VLQEIRSILVDFEEASGKKIYEHDSMStmhfRSLGSAISKILRELDTEISYLKGRIFP 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 107 REEEIAELKAE-RNNTRLLLEH----LECLVSRHERSLR-MTVVKRQAQSPA-GVSSEVEV------------LKALKSL 167
Cdd:pfam15921 243 VEDQLEALKSEsQNKIELLLQQhqdrIEQLISEHEVEITgLTEKASSARSQAnSIQSQLEIiqeqarnqnsmyMRQLSDL 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 168 FEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQ----KKTLTD---GLLDGNHEQESAPSTNGK---- 236
Cdd:pfam15921 323 ESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQfsqeSGNLDDqlqKLLADLHKREKELSLEKEqnkr 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 237 ---RSSDGSLSHEDLAKVL-------------------ELQEVIDRQAREQSQMKERLASLSSHAAELE----------E 284
Cdd:pfam15921 403 lwdRDTGNSITIDHLRRELddrnmevqrleallkamksECQGQMERQMAAIQGKNESLEKVSSLTAQLEstkemlrkvvE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 285 DLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNR 364
Cdd:pfam15921 483 ELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDK 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 365 Q---LQERLELAEQKLQQTLRKAETL----PEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEknQELQRArqreK 437
Cdd:pfam15921 563 VieiLRQQIENMTQLVGQHGRTAGAMqvekAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSD--LELEKV----K 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 438 MNEEHNKRLSDTVDKllseSNERLQLhLKERMAALEDKNSLLREVE----NAKKQLEETQHDKDQLVVTIEALKAELEQM 513
Cdd:pfam15921 637 LVNAGSERLRAVKDI----KQERDQL-LNEVKTSRNELNSLSEDYEvlkrNFRNKSEEMETTTNKLKMQLKSAQSELEQT 711
|
.
gi 568952890 514 R 514
Cdd:pfam15921 712 R 712
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
156-463 |
2.28e-08 |
|
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: 58.60 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 156 SEVEVLKALKSLFEHHKALDEKVR---------ERLRVA-------LERCSLLEEELGATHKEL----MILKEQNNQKkt 215
Cdd:pfam17380 266 TENEFLNQLLHIVQHQKAVSERQQqekfekmeqERLRQEkeekareVERRRKLEEAEKARQAEMdrqaAIYAEQERMA-- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 216 ltdglLDGNHEQESAPSTNGKRSSDgSLSHEDLAKVLELQEVIDRQAREQSQMKERLaslsshaaelEEDLDTARKDLIK 295
Cdd:pfam17380 344 -----MERERELERIRQEERKRELE-RIRQEEIAMEISRMRELERLQMERQQKNERV----------RQELEAARKVKIL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 296 SEEMNTKLQREVREAM--------AQKEDM----EERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKN 363
Cdd:pfam17380 408 EEERQRKIQQQKVEMEqiraeqeeARQREVrrleEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRK 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 364 RQLQERLELAEQKLQQtlRKAETLPE------VEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREK 437
Cdd:pfam17380 488 RAEEQRRKILEKELEE--RKQAMIEEerkrklLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEER 565
|
330 340
....*....|....*....|....*.
gi 568952890 438 MNEEHNKRLSDTVDKLLSESNERLQL 463
Cdd:pfam17380 566 SRLEAMEREREMMRQIVESEKARAEY 591
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
44-468 |
3.11e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 44 LEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTA-LPQEFAALTKELNVCREQLLEREEEIAELKAERNNTR 122
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLpLYQELEALEAELAELPERLEELEERLEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 123 LLLEHLECLVSRHERSLRmtvvkrqaqspagvSSEVEVLKALKSLFEHHKALDEKV---RERLRVALERCSLLEEELGAT 199
Cdd:COG4717 167 ELEAELAELQEELEELLE--------------QLSLATEEELQDLAEELEELQQRLaelEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 200 HKELMILKEQNNQKKTLTDGLLDGnheqeSAPSTNGKRSSDGSLSHEDLAKVLELQEVI-------DRQAREQSQMKERL 272
Cdd:COG4717 233 ENELEAAALEERLKEARLLLLIAA-----ALLALLGLGGSLLSLILTIAGVLFLVLGLLallflllAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 273 ASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANK 352
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 353 DSMHRQTEDKnRQLQERLELAEQKLQQ------TLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLE--E 424
Cdd:COG4717 388 RAALEQAEEY-QELKEELEELEEQLEEllgeleELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEqlE 466
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 568952890 425 KNQELQRARQREKMNEEHNKRLSD--TVDKLLSESNERLQLHLKER 468
Cdd:COG4717 467 EDGELAELLQELEELKAELRELAEewAALKLALELLEEAREEYREE 512
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
37-514 |
5.15e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 5.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 37 EQLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHERDSLqrqlnTALPQEFAALTKELNVCREQLLEREEEIAELKA 116
Cdd:PRK03918 199 EKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEI-----EELEKELESLEGSKRKLEEKIRELEERIEELKK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 117 ERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpagVSSEVEvlKALKSLFEHHKALDEKVRErLRVALERCSLLEEEL 196
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAEEYIKLSEFYEEYLD---ELREIE--KRLSRLEEEINGIEERIKE-LEEKEERLEELKKKL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 197 GATHKELMILKEQN---NQKKTLTDGLldgnheqesapstNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQ-SQMKERL 272
Cdd:PRK03918 348 KELEKRLEELEERHelyEEAKAKKEEL-------------ERLKKRLTGLTPEKLEKELEELEKAKEEIEEEiSKITARI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 273 ASLSSHAAELE---EDLDTA---------------RKDLIK--SEEMNtKLQREVREAMAQKEDMEERITTLEKrYLAAQ 332
Cdd:PRK03918 415 GELKKEIKELKkaiEELKKAkgkcpvcgrelteehRKELLEeyTAELK-RIEKELKEIEEKERKLRKELRELEK-VLKKE 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 333 REATSVHDLNDKLEN-----EIANKDSMHRQTEDKnRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEER 407
Cdd:PRK03918 493 SELIKLKELAEQLKEleeklKKYNLEELEKKAEEY-EKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEE 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 408 HGNIEERLRQM----EAQLEEKNQELQR----------ARQREKMNEEHNKRLSDTVDKL---LSESNERLQlHLKERMA 470
Cdd:PRK03918 572 LAELLKELEELgfesVEELEERLKELEPfyneylelkdAEKELEREEKELKKLEEELDKAfeeLAETEKRLE-ELRKELE 650
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 568952890 471 ALEDKNS-------------LLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMR 514
Cdd:PRK03918 651 ELEKKYSeeeyeelreeyleLSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
314-514 |
7.54e-08 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 56.84 E-value: 7.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 314 KEDMEERITTLEKRYLAAQREATSVHDLNDKLEnEIANKDsmhrQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEA- 392
Cdd:PRK11281 38 EADVQAQLDALNKQKLLEAEDKLVQQDLEQTLA-LLDKID----RQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDe 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 393 ELAQRVAALSkaeerhgnieerLRQMEAQLEEKNQELQRARqrekmneehnKRLSDTVDKLLSESN--ERLQLHLKERMA 470
Cdd:PRK11281 113 ETRETLSTLS------------LRQLESRLAQTLDQLQNAQ----------NDLAEYNSQLVSLQTqpERAQAALYANSQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568952890 471 ALEDKNSLLREVENAKKQLEETQhdKDQLVVTIEALKAELEQMR 514
Cdd:PRK11281 171 RLQQIRNLLKGGKVGGKALRPSQ--RVLLQAEQALLNAQNDLQR 212
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
353-514 |
7.83e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.99 E-value: 7.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 353 DSMHRQTEDKNRQLQERLELAEQKLQQTLRKAEtlpEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQEL-QR 431
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELE---ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 432 ARQREKmneehNKRLSDTVDKLL-SESNERL--QLHLKERMAalEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKA 508
Cdd:COG3883 92 ARALYR-----SGGSVSYLDVLLgSESFSDFldRLSALSKIA--DADADLLEELKADKAELEAKKAELEAKLAELEALKA 164
|
....*.
gi 568952890 509 ELEQMR 514
Cdd:COG3883 165 ELEAAK 170
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
169-514 |
1.33e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 169 EHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDglLDGNHEQESAPSTNGKRSSDGSLSHEDL 248
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE--AKKKAEEDKKKADELKKAAAAKKKADEA 1423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 249 AKVLELQEVIDrQAREQSQMKERLASLSSHAAELE--EDLDTARKDLIKSEEMNTKLQ--REVREAMAQKEDMEERITTL 324
Cdd:PTZ00121 1424 KKKAEEKKKAD-EAKKKAEEAKKADEAKKKAEEAKkaEEAKKKAEEAKKADEAKKKAEeaKKADEAKKKAEEAKKKADEA 1502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 325 EKRYlAAQREATSVHDLNDKLENEIANKDSMHRQTEDKnRQLQERLELAEQKLQQTLRKAETLPEVEA---ELAQRVAAL 401
Cdd:PTZ00121 1503 KKAA-EAKKKADEAKKAEEAKKADEAKKAEEAKKADEA-KKAEEKKKADELKKAEELKKAEEKKKAEEakkAEEDKNMAL 1580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 402 SKAEE----RHGNIEERLRQMEAQLEEKNQELQRARQ-----REKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAAL 472
Cdd:PTZ00121 1581 RKAEEakkaEEARIEEVMKLYEEEKKMKAEEAKKAEEakikaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 568952890 473 EDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMR 514
Cdd:PTZ00121 1661 IKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
246-435 |
1.41e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 246 EDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLdtarkdlikseemntkLQREVREAMAQKEDMEERITTLE 325
Cdd:COG4913 252 ELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL----------------LEAELEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 326 KRYLAAQREATSVHdlNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQkLQQTLRKAE-TLPEVEAELAQRVAAL--- 401
Cdd:COG4913 316 ARLDALREELDELE--AQIRGNGGDRLEQLEREIERLERELEERERRRAR-LEALLAALGlPLPASAEEFAALRAEAaal 392
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568952890 402 --------SKAEERHGNIEERLRQMEAQLEEKNQELQRARQR 435
Cdd:COG4913 393 lealeeelEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
1047-1117 |
1.42e-07 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 49.60 E-value: 1.42e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952890 1047 VLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDfsalaLLLQIPTQNTQARAVLEREFNNLL 1117
Cdd:smart00454 1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEE-----DLKELGITKLGHRKKILKAIQKLK 66
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
331-661 |
1.51e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.82 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 331 AQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGN 410
Cdd:PRK02224 197 EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 411 IEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKL----------LSESNERLQLH------LKERMAALED 474
Cdd:PRK02224 277 LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELedrdeelrdrLEECRVAAQAHneeaesLREDADDLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 475 KNSLLRE-VENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRgpsLHHGRPHLGSVPDFRFSVADGHVDAYSTSAVLRr 553
Cdd:PRK02224 357 RAEELREeAAELESELEEAREAVEDRREEIEELEEEIEELRER---FGDAPVDLGNAEDFLEELREERDELREREAELE- 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 554 pqkGRLAALRDEPSKVQTLNE--------QDWERAQQASVLANVAQAFES-DVDVSDGEDDRDTLLSSVDLLSPSGQADA 624
Cdd:PRK02224 433 ---ATLRTARERVEEAEALLEagkcpecgQPVEGSPHVETIEEDRERVEElEAELEDLEEEVEEVEERLERAEDLVEAED 509
|
330 340 350
....*....|....*....|....*....|....*..
gi 568952890 625 QtlAMMLQEQLDAINKeirLIQEEKENTEQRAEEIES 661
Cdd:PRK02224 510 R--IERLEERREDLEE---LIAERRETIEEKRERAEE 541
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
32-509 |
2.05e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 32 ADSHFEQLMVSMLEER-DRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTA-------LPQEFAALTKELNVCREQ 103
Cdd:COG4913 281 LRLWFAQRRLELLEAElEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrleqLEREIERLERELEERERR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 104 LLEREEEIA-----------ELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSP--AGVSSEVEVLKALKSLFEH 170
Cdd:COG4913 361 RARLEALLAalglplpasaeEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRelRELEAEIASLERRKSNIPA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 171 HkalDEKVRERLRvalERCSLLEEEL---GathkELMILKEQ------------NNQKKTL------------------T 217
Cdd:COG4913 441 R---LLALRDALA---EALGLDEAELpfvG----ELIEVRPEeerwrgaiervlGGFALTLlvppehyaaalrwvnrlhL 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 218 DGLLDGNHEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQareqsqmkerLASLSSHA-AELEEDLDTARKD---- 292
Cdd:COG4913 511 RGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAE----------LGRRFDYVcVDSPEELRRHPRAitra 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 293 -LIKSE----EMNTklQREVRE-------AMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLEN--EIANKDSMHRQ 358
Cdd:COG4913 581 gQVKGNgtrhEKDD--RRRIRSryvlgfdNRAKLAALEAELAELEEELAEAEERLEALEAELDALQErrEALQRLAEYSW 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 359 TEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQRekm 438
Cdd:COG4913 659 DEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR--- 735
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952890 439 neehnkrlsdtVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAE 509
Cdd:COG4913 736 -----------LEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
253-513 |
2.28e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 55.57 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 253 ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREamaqkedmeerittLEKRYLAAQ 332
Cdd:pfam01576 360 ELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQE--------------LQARLSESE 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 333 REATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQ--QTLRKAETLPEVeaelaqrvaalskaeerhgN 410
Cdd:pfam01576 426 RQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQdtQELLQEETRQKL-------------------N 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 411 IEERLRQMEaqlEEKNQELQRARQREKMNEEHNKRLSdTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLE 490
Cdd:pfam01576 487 LSTRLRQLE---DERNSLQEQLEEEEEAKRNVERQLS-TLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLE 562
|
250 260
....*....|....*....|...
gi 568952890 491 ETQHDKDQLVVTIEALKAELEQM 513
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDL 585
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
45-512 |
2.52e-07 |
|
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: 55.03 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTaLPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLL 124
Cdd:TIGR04523 124 VELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYND-LKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 125 LEHLECLVSRHeRSLRMTVVKRQAQSpagvSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKEL- 203
Cdd:TIGR04523 203 LSNLKKKIQKN-KSLESQISELKKQN----NQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELe 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 204 ---MILKEQNNQKKTLTDGLLDGNHEQEsapstngkrssdgslshEDLAKvlELQEVIDRQAREQSQMKERLASLSSHAA 280
Cdd:TIGR04523 278 qnnKKIKELEKQLNQLKSEISDLNNQKE-----------------QDWNK--ELKSELKNQEKKLEEIQNQISQNNKIIS 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 281 ELEEDLDTARKDLIKSEEMNTKLQREVREamaqKEDMEERIttlekrylaaQREATSVHDLNDKLENEIANKDSMHRQTE 360
Cdd:TIGR04523 339 QLNEQISQLKKELTNSESENSEKQRELEE----KQNEIEKL----------KKENQSYKQEIKNLESQINDLESKIQNQE 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 361 DKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMN- 439
Cdd:TIGR04523 405 KLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNl 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 440 EEHNKRLSDTVDKLLSESNERLQlhLKERMAALEDKNSLL----REVENAKKQLE------ETQHDKDQLVVTIEALKAE 509
Cdd:TIGR04523 485 EQKQKELKSKEKELKKLNEEKKE--LEEKVKDLTKKISSLkekiEKLESEKKEKEskisdlEDELNKDDFELKKENLEKE 562
|
...
gi 568952890 510 LEQ 512
Cdd:TIGR04523 563 IDE 565
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
874-940 |
3.53e-07 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 48.45 E-value: 3.53e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568952890 874 FAQWDGPTVVVWLELWvGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEI 940
Cdd:smart00454 1 VSQWSPESVADWLESI-GLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
113-516 |
3.54e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 113 ELKAERNNTRLLLEHLECLVSRHERSLRmtVVKRQAQSPAGVSSEV-EVLKALKSLFEHHKALDEKVR--ERLRVALERC 189
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRLEEEIN--GIEERIKELEEKEERLeELKKKLKELEKRLEELEERHElyEEAKAKKEEL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 190 SLLEEELGATHKELMI--LKEQNNQKKTLTDGLLD-----GNHEQESA---PSTNGKRSSDGS-------LSHEDLAKVL 252
Cdd:PRK03918 375 ERLKKRLTGLTPEKLEkeLEELEKAKEEIEEEISKitariGELKKEIKelkKAIEELKKAKGKcpvcgreLTEEHRKELL 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 253 -ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARK--------DLIKS--EEMNTKLQREVREAMAQKEDMEERI 321
Cdd:PRK03918 455 eEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliklkelaEQLKEleEKLKKYNLEELEKKAEEYEKLKEKL 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 322 TTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQER-------LELAEQKLQQTLRKAETLPEVEAEL 394
Cdd:PRK03918 535 IKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesveeLEERLKELEPFYNEYLELKDAEKEL 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 395 AQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQreKMNEEHNKRLSDTVDKL------LSESNERLQLHLKER 468
Cdd:PRK03918 615 EREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK--KYSEEEYEELREEYLELsrelagLRAELEELEKRREEI 692
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 568952890 469 MAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIE---ALKAELEQMRLR 516
Cdd:PRK03918 693 KKTLEKLKEELEEREKAKKELEKLEKALERVEELREkvkKYKALLKERALS 743
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
249-512 |
3.63e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.66 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 249 AKVLELQEVIDRqAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRy 328
Cdd:PRK02224 489 EEVEEVEERLER-AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEE- 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 329 laAQREATSVHDLNDKLEneiANKDSmhRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSkaeERH 408
Cdd:PRK02224 567 --AEEAREEVAELNSKLA---ELKER--IESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKR---ERK 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 409 GNIEERLRqmEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSE----SNERLQLH-LKERMAALEDKNSLLREVE 483
Cdd:PRK02224 637 RELEAEFD--EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEigavENELEELEeLRERREALENRVEALEALY 714
|
250 260
....*....|....*....|....*....
gi 568952890 484 NAKKQLEETQHDkdqlvvtieaLKAELEQ 512
Cdd:PRK02224 715 DEAEELESMYGD----------LRAELRQ 733
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
969-1024 |
3.64e-07 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 48.45 E-value: 3.64e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 568952890 969 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLR 1024
Cdd:smart00454 11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
280-473 |
3.71e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 3.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 280 AELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQT 359
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 360 ED--KNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLR-QMEAQLEEKNQELQRARQRE 436
Cdd:COG4717 129 PLyqELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRL 208
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568952890 437 KMNEEHNKRLSDTVDKLLSE----SNERLQLHLKERMAALE 473
Cdd:COG4717 209 AELEEELEEAQEELEELEEEleqlENELEAAALEERLKEAR 249
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
47-512 |
5.04e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 5.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 47 RDRLLDTLRETQETLALTQGKLHEVG-HERDSLQRQLNTA--LPQEFAALTKELNvcreqllEREEEIAELKAERNNTRL 123
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNlKELKELEEELKEAeeKEEEYAELQEELE-------ELEEELEELEAELEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 124 LLEHLECLVSRHERSLRMTVVKRQAQSPAGV-------------------SSEVEVLKALKSLFEHHKALDEKVRERLRV 184
Cdd:COG4717 117 ELEKLEKLLQLLPLYQELEALEAELAELPERleeleerleelreleeeleELEAELAELQEELEELLEQLSLATEEELQD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 185 ALERCSLLEEELGATHKELMILKEQNNQKKTLTDGLldgnhEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQARE 264
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQL-----ENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 265 QSQMKERLASLSSHAAeleedldTARKDLIKSEEMNTKLQREVREAMAQKE-DMEERITTLEKRYLAAQREATSVHDLND 343
Cdd:COG4717 272 ILTIAGVLFLVLGLLA-------LLFLLLAREKASLGKEAEELQALPALEElEEEELEELLAALGLPPDLSPEELLELLD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 344 KleneIANKDSMHRQTEDKNRQLQerLELAEQKLQQTLRKAETlpEVEAELAQRVAALSKAEErhgnIEERLRQMEAQLE 423
Cdd:COG4717 345 R----IEELQELLREAEELEEELQ--LEELEQEIAALLAEAGV--EDEEELRAALEQAEEYQE----LKEELEELEEQLE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 424 EKNQELQRARQREKmNEEHNKRLSDTVDKLLSESNERLQLH-----LKERMAALEDKNSL---LREVENAKKQLEETQHD 495
Cdd:COG4717 413 ELLGELEELLEALD-EEELEEELEELEEELEELEEELEELReelaeLEAELEQLEEDGELaelLQELEELKAELRELAEE 491
|
490
....*....|....*..
gi 568952890 496 KDQLVVTIEALKAELEQ 512
Cdd:COG4717 492 WAALKLALELLEEAREE 508
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
236-507 |
5.67e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 5.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 236 KRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKE 315
Cdd:PTZ00121 1230 KKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKK 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 316 DMEE--RITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAE 393
Cdd:PTZ00121 1310 KAEEakKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE 1389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 394 LAQRVAALSKAEERHGNIEERLRQMEA-----QLEEKNQELQRARQREKMNEEhnKRLSDTVDKLLSESN--ERLQLHLK 466
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADELKKAAAAkkkadEAKKKAEEKKKADEAKKKAEE--AKKADEAKKKAEEAKkaEEAKKKAE 1467
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 568952890 467 ERMAA--LEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALK 507
Cdd:PTZ00121 1468 EAKKAdeAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKK 1510
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
307-516 |
5.81e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 5.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 307 VREAMAQKEDMEERITTLE---KRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKN--RQLQERLELAEQKLQQTL 381
Cdd:COG4913 213 VREYMLEEPDTFEAADALVehfDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAelEYLRAALRLWFAQRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 382 RKAEtLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQ-----------LEEKNQELQRARQREKMNEEHNKRLSDTV 450
Cdd:COG4913 293 LEAE-LEELRAELARLEAELERLEARLDALREELDELEAQirgnggdrleqLEREIERLERELEERERRRARLEALLAAL 371
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568952890 451 DKLLSESNERLQLHLKERMAALEDKNSLLREVEN----AKKQLEETQHDKDQLVVTIEALK-------AELEQMRLR 516
Cdd:COG4913 372 GLPLPASAEEFAALRAEAAALLEALEEELEALEEalaeAEAALRDLRRELRELEAEIASLErrksnipARLLALRDA 448
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
44-514 |
7.80e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 7.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 44 LEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTaLPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRL 123
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEE-LEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRD 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 124 LLEhleclvsrhERSLRMTVVKRQAQSPAGVSSEVEvlKALKSLFEHHKALD---EKVRERLRVALERCSLLEEELGATH 200
Cdd:PRK02224 329 RLE---------ECRVAAQAHNEEAESLREDADDLE--ERAEELREEAAELEselEEAREAVEDRREEIEELEEEIEELR 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 201 KELMILKEQNNQKKTLTDGLLDgnhEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVID----RQAREQSQMKERLASLS 276
Cdd:PRK02224 398 ERFGDAPVDLGNAEDFLEELRE---ERDELREREAELEATLRTARERVEEAEALLEAGKcpecGQPVEGSPHVETIEEDR 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 277 SHAAELEEDLDTARKDLiksEEMNTKLQR--EVREAMAQKEDMEERITTLEKRylAAQREATsVHDLNDKLENEIANKDS 354
Cdd:PRK02224 475 ERVEELEAELEDLEEEV---EEVEERLERaeDLVEAEDRIERLEERREDLEEL--IAERRET-IEEKRERAEELRERAAE 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 355 MHRQTEDKNRQLQERLELAEQKLqqtlrkaetlpEVEAELAQRVAALSKAEERHGNIEERLrqmeAQLEEKNQELQRARQ 434
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEAR-----------EEVAELNSKLAELKERIESLERIRTLL----AAIADAEDEIERLRE 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 435 REK----MNEEHNKRLS---DTVDKLLSESNE-RLQlhlkermAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEAL 506
Cdd:PRK02224 614 KREalaeLNDERRERLAekrERKRELEAEFDEaRIE-------EAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAV 686
|
....*...
gi 568952890 507 KAELEQMR 514
Cdd:PRK02224 687 ENELEELE 694
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
145-504 |
7.95e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 7.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 145 KRQAQSPAGVSSEVEVLKALKSLFEHHKALDE--KVRERLRVALERCSLLEEElgatHKELMILKEQNNQKKTLTDGLLD 222
Cdd:PTZ00121 1456 AKKAEEAKKKAEEAKKADEAKKKAEEAKKADEakKKAEEAKKKADEAKKAAEA----KKKADEAKKAEEAKKADEAKKAE 1531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 223 GNHEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVID-RQAREQSQMKERLASLSSHAAE---------LEEDLDTARKD 292
Cdd:PTZ00121 1532 EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEaKKAEEDKNMALRKAEEAKKAEEarieevmklYEEEKKMKAEE 1611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 293 LIKSEEMNTKLQrEVREAmaqkEDMEERITTLEKRYLAAQREATSVHDLNDklENEIANKDSMHRQTEDKNR--QLQERL 370
Cdd:PTZ00121 1612 AKKAEEAKIKAE-ELKKA----EEEKKKVEQLKKKEAEEKKKAEELKKAEE--ENKIKAAEEAKKAEEDKKKaeEAKKAE 1684
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 371 ELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKrlsdtV 450
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKK-----I 1759
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 568952890 451 DKLLSESNERLQLHLKERMAALEDKnsLLREVENAKKQLEETQHD-KDQLVVTIE 504
Cdd:PTZ00121 1760 AHLKKEEEKKAEEIRKEKEAVIEEE--LDEEDEKRRMEVDKKIKDiFDNFANIIE 1812
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
260-663 |
8.08e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 8.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 260 RQAREQSQMKERLASLSSHAAELEEDLDTARK---DLIKSEEMNTKLQREVREAMAQKEDMEERittlEKRYLAAQREAT 336
Cdd:PTZ00121 1278 RKADELKKAEEKKKADEAKKAEEKKKADEAKKkaeEAKKADEAKKKAEEAKKKADAAKKKAEEA----KKAAEAAKAEAE 1353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 337 SVhdlNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQ--KLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEER 414
Cdd:PTZ00121 1354 AA---ADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkkKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEK 1430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 415 LRQMEAQleEKNQELQRARQREKMNEEhnKRLSDTVDKLLSEsnerlqlhlKERMAALEDKNSLLREVENAKKQLEETQH 494
Cdd:PTZ00121 1431 KKADEAK--KKAEEAKKADEAKKKAEE--AKKAEEAKKKAEE---------AKKADEAKKKAEEAKKADEAKKKAEEAKK 1497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 495 DKDQLVVTIEAlKAELEQMRlrgpslhhgrphlgsvpdfrfsvadgHVDAYSTSAVLRRPQKGRLAalrDEPSKVQTLNE 574
Cdd:PTZ00121 1498 KADEAKKAAEA-KKKADEAK--------------------------KAEEAKKADEAKKAEEAKKA---DEAKKAEEKKK 1547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 575 QD-WERAQQASVLANVAQAFESdvdvSDGEDDRDTLLSSVDLLSPSGQADAQTLAMMLQEQLDAINKEIRLIQEEKENTE 653
Cdd:PTZ00121 1548 ADeLKKAEELKKAEEKKKAEEA----KKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE 1623
|
410
....*....|..
gi 568952890 654 Q--RAEEIESRV 663
Cdd:PTZ00121 1624 ElkKAEEEKKKV 1635
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
302-474 |
9.51e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.46 E-value: 9.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 302 KLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLElaeqklqqTL 381
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG--------NV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 382 RKAETLPEVEAELAQrvaalskAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERL 461
Cdd:COG1579 86 RNNKEYEALQKEIES-------LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
170
....*....|...
gi 568952890 462 QLHLKERMAALED 474
Cdd:COG1579 159 EELEAEREELAAK 171
|
|
| SAM_superfamily |
cd09487 |
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
969-1020 |
1.37e-06 |
|
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.
Pssm-ID: 188886 [Multi-domain] Cd Length: 56 Bit Score: 46.46 E-value: 1.37e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 568952890 969 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRNSFQCGI 1020
Cdd:cd09487 4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
38-513 |
1.69e-06 |
|
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: 52.53 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 38 QLMVSMLEERDR--LLDTLRETQETLALTQGKLHE--VGHERDSLQRQ-----LNTALPQEFAALTKELNvcreqlLERE 108
Cdd:pfam12128 231 QAIAGIMKIRPEftKLQQEFNTLESAELRLSHLHFgyKSDETLIASRQeerqeTSAELNQLLRTLDDQWK------EKRD 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 109 EEIAELKAERNNTRLLLEHLECLVSRHERSLRMTVVKR---QAQSPAgVSSEVEVL-KALKSLFEHHKALDEKVRERLRV 184
Cdd:pfam12128 305 ELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAaadQEQLPS-WQSELENLeERLKALTGKHQDVTAKYNRRRSK 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 185 ALERCSlleEELGATHKELMILKEQNNQKKTLTDGLLDGnheQESApstngkrssdgsLSHEDLAKVLELQEVIDRQARE 264
Cdd:pfam12128 384 IKEQNN---RDIAGIKDKLAKIREARDRQLAVAEDDLQA---LESE------------LREQLEAGKLEFNEEEYRLKSR 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 265 QSQMKERLASLSSHAAELE------EDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSV 338
Cdd:pfam12128 446 LGELKLRLNQATATPELLLqlenfdERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDEL 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 339 --------HDLNDKLENEIAN-KDS---------MHR----------QTEDKNRQLQERLELAEQKLQQTLRKAETLpev 390
Cdd:pfam12128 526 elqlfpqaGTLLHFLRKEAPDwEQSigkvispelLHRtdldpevwdgSVGGELNLYGVKLDLKRIDVPEWAASEEEL--- 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 391 EAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLK---E 467
Cdd:pfam12128 603 RERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDsanE 682
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 568952890 468 RMAALE-DKNSLLREVENAKKQ-----LEETQHDKDQLVVTIEALKAELEQM 513
Cdd:pfam12128 683 RLNSLEaQLKQLDKKHQAWLEEqkeqkREARTEKQAYWQVVEGALDAQLALL 734
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
160-513 |
1.69e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 160 VLKALKSLFEhhKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGLLDGNHEQESApstnGKRSS 239
Cdd:COG4717 39 LLAFIRAMLL--ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEEL----EAELE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 240 DGSLSHEDLAKVLELQEVIDRQAREQSQMK---ERLASLSSHAA---ELEEDLDTARKDLIKSEEMNTKLQREVREAMAQ 313
Cdd:COG4717 113 ELREELEKLEKLLQLLPLYQELEALEAELAelpERLEELEERLEelrELEEELEELEAELAELQEELEELLEQLSLATEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 314 K-EDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELA------------------- 373
Cdd:COG4717 193 ElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLiaaallallglggsllsli 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 374 ------------------------EQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIE-----------ERLRQM 418
Cdd:COG4717 273 ltiagvlflvlgllallflllareKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSpeellelldriEELQEL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 419 EAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKL----------------LSESNERLQLHLKERMAALE--DKNSLLR 480
Cdd:COG4717 353 LREAEELEEELQLEELEQEIAALLAEAGVEDEEELraaleqaeeyqelkeeLEELEEQLEELLGELEELLEalDEEELEE 432
|
410 420 430
....*....|....*....|....*....|...
gi 568952890 481 EVENAKKQLEETQHDKDQLVVTIEALKAELEQM 513
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQL 465
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
161-475 |
1.71e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.76 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 161 LKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGLLDGNHEQESAPSTNGKRSSD 240
Cdd:TIGR02169 690 LSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 241 GSLSHEDLAKVLE------LQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQK 314
Cdd:TIGR02169 770 LEEDLHKLEEALNdlearlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 315 EDMEERITTLEKRYLAAQREA----TSVHDLNDKLEN---EIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETL 387
Cdd:TIGR02169 850 KSIEKEIENLNGKKEELEEELeeleAALRDLESRLGDlkkERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAL 929
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 388 PEVEAELAQRVAA----------LSKAEERHGNIEERLRQMEAQLEEKNQELqrarqrekmnEEHNKRLSDTVDKLLSES 457
Cdd:TIGR02169 930 EEELSEIEDPKGEdeeipeeelsLEDVQAELQRVEEEIRALEPVNMLAIQEY----------EEVLKRLDELKEKRAKLE 999
|
330
....*....|....*...
gi 568952890 458 NERLQlhLKERMAALEDK 475
Cdd:TIGR02169 1000 EERKA--ILERIEEYEKK 1015
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
269-511 |
2.12e-06 |
|
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: 51.94 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 269 KERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEK-------RYLAAQREATSVHDL 341
Cdd:TIGR04523 95 KDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKeleklnnKYNDLKKQKEELENE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 342 NDKLENEIANKDSMHRQTEDKNRQLQERL---------------ELAEQKLQQTLRKaETLPEVEAELAQRVAALSKAEE 406
Cdd:TIGR04523 175 LNLLEKEKLNIQKNIDKIKNKLLKLELLLsnlkkkiqknkslesQISELKKQNNQLK-DNIEKKQQEINEKTTEISNTQT 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 407 RHGNIEERLRQMEAQLEEKNQELQRArqrEKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENak 486
Cdd:TIGR04523 254 QLNQLKDEQNKIKKQLSEKQKELEQN---NKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQN-- 328
|
250 260
....*....|....*....|....*
gi 568952890 487 kQLEETQHDKDQLVVTIEALKAELE 511
Cdd:TIGR04523 329 -QISQNNKIISQLNEQISQLKKELT 352
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
246-509 |
2.38e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 246 EDLAKVLELQEVID-RQAREQSQMKERLASLSSHAAELEEDLDTARK-DLIKSEEMNTKLQREVREAMAQKEDMEERITT 323
Cdd:PTZ00121 1185 EEVRKAEELRKAEDaRKAEAARKAEEERKAEEARKAEDAKKAEAVKKaEEAKKDAEEAKKAEEERNNEEIRKFEEARMAH 1264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 324 LEKRYLAAQ----REATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQE--RLELAEQKLQQTLRKAETLPEvEAELAQR 397
Cdd:PTZ00121 1265 FARRQAAIKaeeaRKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEakKADEAKKKAEEAKKKADAAKK-KAEEAKK 1343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 398 VAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQlHLKERMAA------ 471
Cdd:PTZ00121 1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD-ELKKAAAAkkkade 1422
|
250 260 270
....*....|....*....|....*....|....*...
gi 568952890 472 LEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAE 509
Cdd:PTZ00121 1423 AKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAE 1460
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
224-498 |
4.44e-06 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 50.19 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 224 NHEQESAPSTNGKRSSDGSL------SHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSE 297
Cdd:pfam15905 42 NNSKDASTPATARKVKSLELkkksqkNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 298 EMNTKLQREVREAMAQKEDMEE-----------RITTLEKRYLAAQREAT--SVHDLNDKLENEIANKDSMHRQTEDKNR 364
Cdd:pfam15905 122 ASVASLEKQLLELTRVNELLKAkfsedgtqkkmSSLSMELMKLRNKLEAKmkEVMAKQEGMEGKLQVTQKNLEHSKGKVA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 365 QLQERLELAEQKLQQTlrKAETLpeveaELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNK 444
Cdd:pfam15905 202 QLEEKLVSTEKEKIEE--KSETE-----KLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELS 274
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 568952890 445 RLSDTVD---KLLSESNERLQLHLKERmaaledKNSLLREVENAKKQL--EETQHDKDQ 498
Cdd:pfam15905 275 KQIKDLNekcKLLESEKEELLREYEEK------EQTLNAELEELKEKLtlEEQEHQKLQ 327
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
129-515 |
4.92e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 50.66 E-value: 4.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 129 ECLVSRHErslrmtVVKRQAQSPAGVSSEVEVLKALKSLFEH-HKALDEKVrERLRVALERCSLLEEELGATHKELMILK 207
Cdd:pfam07888 38 ECLQERAE------LLQAQEAANRQREKEKERYKRDREQWERqRRELESRV-AELKEELRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 208 EQNNQKKtltDGLLDGNHEQEsapstngkrssdgslshedlAKVLELQEVIdRQAREQSQMKErlaslsshaAELEEDLD 287
Cdd:pfam07888 111 EELSEEK---DALLAQRAAHE--------------------ARIRELEEDI-KTLTQRVLERE---------TELERMKE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 288 TARKDLIKSEE-------MNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLeNEIANKDSMHRQTE 360
Cdd:pfam07888 158 RAKKAGAQRKEeeaerkqLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKL-TTAHRKEAENEALL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 361 DKNRQLQERLELAEQKLqQTLRkaETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKN----QELQRARQRE 436
Cdd:pfam07888 237 EELRSLQERLNASERKV-EGLG--EELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRarwaQERETLQQSA 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568952890 437 KMNEEHNKRLSDTVDKLlsesNERLQlhlKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRL 515
Cdd:pfam07888 314 EADKDRIEKLSAELQRL----EERLQ---EERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQA 385
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
258-435 |
5.92e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 5.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 258 IDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATS 337
Cdd:COG4913 666 AEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 338 VH--DLNDKLENEIANK--DSMHRQTEDKNRQLQERLELAEQKLQQTLRKA-ETLPEVEAELAQRVAALSKAEERHGNIE 412
Cdd:COG4913 746 ELraLLEERFAAALGDAveRELRENLEERIDALRARLNRAEEELERAMRAFnREWPAETADLDADLESLPEYLALLDRLE 825
|
170 180
....*....|....*....|...
gi 568952890 413 ERlrqmeaQLEEKNQELQRARQR 435
Cdd:COG4913 826 ED------GLPEYEERFKELLNE 842
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
253-456 |
6.70e-06 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 50.07 E-value: 6.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 253 ELQEVIDRQAREQSQMKERLASLSSHAAELE---------EDLDTARKDLIKSEEMNTKLQrEVREAMAQKED-MEERIT 322
Cdd:COG0497 169 ALKKELEELRADEAERARELDLLRFQLEELEaaalqpgeeEELEEERRRLSNAEKLREALQ-EALEALSGGEGgALDLLG 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 323 tlekrylAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQ----------ERLELAEQKLQ---QTLRK----AE 385
Cdd:COG0497 248 -------QALRALERLAEYDPSLAELAERLESALIELEEAASELRryldslefdpERLEEVEERLAllrRLARKygvtVE 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952890 386 TLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQrekmneEHNKRLSDTVDKLLSE 456
Cdd:COG0497 321 ELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARK------KAAKKLEKAVTAELAD 385
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
318-534 |
7.44e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 7.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 318 EERITTLEKRYLAAQREATSVHDLNDKLENEIankdsmhrqtedknRQLQERLElAEQKLQQTLRKAETLPEVEAELA-- 395
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAEL--------------DALQERRE-ALQRLAEYSWDEIDVASAEREIAel 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 396 -QRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALED 474
Cdd:COG4913 674 eAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE 753
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568952890 475 KNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLR-----GPSLHHGRPHLGSVPDFR 534
Cdd:COG4913 754 RFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAfnrewPAETADLDADLESLPEYL 818
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
341-524 |
9.26e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 9.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 341 LNDKLENEianKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQME- 419
Cdd:COG4717 47 LLERLEKE---ADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEk 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 420 ---------------AQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVEN 484
Cdd:COG4717 124 llqllplyqelealeAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568952890 485 AKKQLEETQHDKDQLVVTIEALKAELEQMRLRGPSLHHGR 524
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
399-516 |
9.49e-06 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 47.90 E-value: 9.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 399 AALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLlsesNERLQLHLK---ERMA--ALE 473
Cdd:COG1842 16 ALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKW----EEKARLALEkgrEDLAreALE 91
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 568952890 474 DKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLR 516
Cdd:COG1842 92 RKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAK 134
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
36-438 |
1.11e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 49.30 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 36 FEQLMVSMLEERDRL--LDTLRE---------TQETLALTQGKLHEVGHERD-SLQRQLNTALPQEFAALTKELNVCREQ 103
Cdd:pfam19220 5 NELLRVRLGEMADRLedLRSLKAdfsqliepiEAILRELPQAKSRLLELEALlAQERAAYGKLRRELAGLTRRLSAAEGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 104 LLEREEEIAELKAERNNTRLLLEHLECLVSrhERSLRMTVVKRQAqspagvSSEVEVLKALKslfEHHKALdekvRERLR 183
Cdd:pfam19220 85 LEELVARLAKLEAALREAEAAKEELRIELR--DKTAQAEALERQL------AAETEQNRALE---EENKAL----REEAQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 184 VALERCSLLEEELGATHKELMILKEQNNQKKTLTDglldgnhEQESAPSTNGKRSSDGSLSHEDLAKVLELQEV--IDRQ 261
Cdd:pfam19220 150 AAEKALQRAEGELATARERLALLEQENRRLQALSE-------EQAAELAELTRRLAELETQLDATRARLRALEGqlAAEQ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 262 AREQSQMKERLASLSSHAAE---LEEDLDTARKDLIKSEEMNTklqrevrEAMAQKEDMEERITTLEKRYLAAQREATSV 338
Cdd:pfam19220 223 AERERAEAQLEEAVEAHRAErasLRMKLEALTARAAATEQLLA-------EARNQLRDRDEAIRAAERRLKEASIERDTL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 339 HDLNDKLENEIANKDSMHRQTEDKNRQLQERLElaeqklqqTLRKAetlpeveaeLAQRVAALSKAEERHGNIEERLRQM 418
Cdd:pfam19220 296 ERRLAGLEADLERRTQQFQEMQRARAELEERAE--------MLTKA---------LAAKDAALERAEERIASLSDRIAEL 358
|
410 420
....*....|....*....|....*..
gi 568952890 419 E-------AQLEEKNQELQRARQREKM 438
Cdd:pfam19220 359 TkrfeverAALEQANRRLKEELQRERA 385
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
365-514 |
1.12e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 365 QLQERLELAE--QKLQQTLRKAETLPEVEAELAQRVAALskaEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEh 442
Cdd:COG1579 5 DLRALLDLQEldSELDRLEHRLKELPAELAELEDELAAL---EARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE- 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568952890 443 nkrlsdtvdKLLSESNERLQLHLKERMAALEDKNSLLREVE-NAKKQLEETQHDKDQLVVTIEALKAELEQMR 514
Cdd:COG1579 81 ---------QLGNVRNNKEYEALQKEIESLKRRISDLEDEIlELMERIEELEEELAELEAELAELEAELEEKK 144
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
251-516 |
1.20e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.79 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 251 VLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEkryla 330
Cdd:pfam01576 140 ILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLE----- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 331 aqREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLE---LAEQKLQQTLRKAET-LPEVEAELAQRVAALSKAEE 406
Cdd:pfam01576 215 --GESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEeetAQKNNALKKIRELEAqISELQEDLESERAARNKAEK 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 407 RHGNIEERLRQMEAQLEEK------NQELQRARQRE-----KMNEEHNKRLsdtvDKLLSESNERLQLHLKERMAALEDK 475
Cdd:pfam01576 293 QRRDLGEELEALKTELEDTldttaaQQELRSKREQEvtelkKALEEETRSH----EAQLQEMRQKHTQALEELTEQLEQA 368
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 568952890 476 NSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLR 516
Cdd:pfam01576 369 KRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKK 409
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
175-485 |
1.29e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.51 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 175 DEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDgLLDGNHEQESAPSTNGKRSSDGSLShEDLAKVLEL 254
Cdd:PRK01156 464 EEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKE-YLESEEINKSINEYNKIESARADLE-DIKIKINEL 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 255 QEVIDRQareqSQMKERLASLSShaaeleEDLDTARKDLIKSEEMNTKLqrEVREAMAQKEDMEERITTLEKRylaAQRE 334
Cdd:PRK01156 542 KDKHDKY----EEIKNRYKSLKL------EDLDSKRTSWLNALAVISLI--DIETNRSRSNEIKKQLNDLESR---LQEI 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 335 ATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQErLELAEQKLQQTLrkaETLPEVEAELAQRVAALSKAEERHGNIEER 414
Cdd:PRK01156 607 EIGFPDDKSYIDKSIREIENEANNLNNKYNEIQE-NKILIEKLRGKI---DNYKKQIAEIDSIIPDLKEITSRINDIEDN 682
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952890 415 LRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVdkllSESNERLqlhlkERMAALEDKNSLLREVENA 485
Cdd:PRK01156 683 LKKSRKALDDAKANRARLESTIEILRTRINELSDRI----NDINETL-----ESMKKIKKAIGDLKRLREA 744
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
254-514 |
1.29e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 254 LQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQR 333
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 334 EATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEE 413
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 414 RLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQ 493
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260
....*....|....*....|.
gi 568952890 494 HDKDQLVVTIEALKAELEQMR 514
Cdd:COG4372 269 VEKDTEEEELEIAALELEALE 289
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
221-508 |
1.34e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.57 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 221 LDGNHEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDR--QAREQ----SQMKERLASLSSHAAELEEDLDTARKDli 294
Cdd:PRK04863 856 HESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLADRveEIREQldeaEEAKRFVQQHGNALAQLEPIVSVLQSD-- 933
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 295 ksEEMNTKLQREVREAMAQKEDMEERITTLEkrYLAAQREATSVHDLNDKLEneiankdsmhrQTEDKNRQLQERLELAE 374
Cdd:PRK04863 934 --PEQFEQLKQDYQQAQQTQRDAKQQAFALT--EVVQRRAHFSYEDAAEMLA-----------KNSDLNEKLRQRLEQAE 998
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 375 QklqQTLRKAETLPEVEAELAQRVAALSKAEERHgnieERLRQMEAQLEEKNQEL---------QRARQREkmnEEHNKR 445
Cdd:PRK04863 999 Q---ERTRAREQLRQAQAQLAQYNQVLASLKSSY----DAKRQMLQELKQELQDLgvpadsgaeERARARR---DELHAR 1068
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568952890 446 LSDTvdkllsesnerlqlhlKERMAALEDKNSLL-REVENAKKQLEETQHDKDQLVVTIEALKA 508
Cdd:PRK04863 1069 LSAN----------------RSRRNQLEKQLTFCeAEMDNLTKKLRKLERDYHEMREQVVNAKA 1116
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
249-484 |
1.49e-05 |
|
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: 49.66 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 249 AKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRY 328
Cdd:TIGR00606 843 SKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQ 922
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 329 LAAQREATSVHDLNDKLENEIankdsmhRQTEDKNRQLQERLELAEQKLQQTlrKAETLPEVEAELAQRVAALSKAEERH 408
Cdd:TIGR00606 923 QEKEELISSKETSNKKAQDKV-------NDIKEKVKNIHGYMKDIENKIQDG--KDDYLKQKETELNTVNAQLEECEKHQ 993
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568952890 409 GNIEERLRQMEAQLEEKNQE---LQRARQREKMNEEHnKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVEN 484
Cdd:TIGR00606 994 EKINEDMRLMRQDIDTQKIQerwLQDNLTLRKRENEL-KEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHV 1071
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
127-485 |
2.24e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.81 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 127 HLECLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMIL 206
Cdd:pfam02463 676 LEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKS 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 207 KEQNNQKKTLTDGLLDGNHEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDL 286
Cdd:pfam02463 756 RLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEEL 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 287 DTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQL 366
Cdd:pfam02463 836 EELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEK 915
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 367 QERLELAEQKLQQTLRKAETLPEVEaeLAQRVAALSKAEERHGNIEERLRQMEAQLEEK-----NQELQRARQREKMNEE 441
Cdd:pfam02463 916 ENEIEERIKEEAEILLKYEEEPEEL--LLEEADEKEKEENNKEEEEERNKRLLLAKEELgkvnlMAIEEFEEKEERYNKD 993
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 568952890 442 H--NKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENA 485
Cdd:pfam02463 994 EleKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFY 1039
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
44-434 |
2.27e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 44 LEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRL 123
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 124 LLEHLECLVSRHERSLRmtvVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKEL 203
Cdd:COG4717 228 ELEQLENELEAAALEER---LKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 204 MILKEQNNQKKTltdglldgnhEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLAsLSSHAAELE 283
Cdd:COG4717 305 EELQALPALEEL----------EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ-LEELEQEIA 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 284 EDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSvhdlnDKLENEIANKDSMHRQTEDKN 363
Cdd:COG4717 374 ALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE-----EELEEELEELEEELEELEEEL 448
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952890 364 RQLQERLELAEQKLQQtLRKAETLPEVEAELAQRVAALSKAEERHGnieeRLRQMEAQLEEKNQELQRARQ 434
Cdd:COG4717 449 EELREELAELEAELEQ-LEEDGELAELLQELEELKAELRELAEEWA----ALKLALELLEEAREEYREERL 514
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
253-436 |
2.99e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 253 ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAmaqKEDMEERITTLEKRYLAAQ 332
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA---EAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 333 R------------EATSVHDLNDKLEN--------------------EIANKDSMHRQTEDKNRQLQERLELAEQKLQQT 380
Cdd:COG3883 97 RsggsvsyldvllGSESFSDFLDRLSAlskiadadadlleelkadkaELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 381 LRKAE----TLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQRE 436
Cdd:COG3883 177 QAEQEallaQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
253-383 |
3.67e-05 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 46.05 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 253 ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREA-MAQKEDMEERITTLEKRYLAA 331
Cdd:pfam15619 57 ELPQLIARHNEEVRVLRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKnLAEREELQKKLEQLEAKLEDK 136
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 568952890 332 QREatsVHDLNDKLEN-------EIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRK 383
Cdd:pfam15619 137 DEK---IQDLERKLELenksfrrQLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKERE 192
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
1047-1117 |
4.42e-05 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 42.64 E-value: 4.42e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952890 1047 VLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFsalalLLQIPTQNTQARAVLEREFNNLL 1117
Cdd:pfam07647 1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLRLTLED-----LKRLGITSVGHRRKILKKIQELK 66
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
379-512 |
4.79e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 379 QTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNE----EHNKRLSDTVDKLL 454
Cdd:COG1579 4 EDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLEleieEVEARIKKYEEQLG 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568952890 455 SESNER----LQL---HLKERMAALEDK-NSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQ 512
Cdd:COG1579 84 NVRNNKeyeaLQKeieSLKRRISDLEDEiLELMERIEELEEELAELEAELAELEAELEEKKAELDE 149
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
259-434 |
5.01e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 259 DRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIK----------SEEMNTKLQR------EVREAMAQKEDMEERIT 322
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdlSEEAKLLLQQlselesQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 323 TLEKR------YLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKN---RQLQERLELAEQKLQQTLRKAETLPEVEAE 393
Cdd:COG3206 244 ALRAQlgsgpdALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHpdvIALRAQIAALRAQLQQEAQRILASLEAELE 323
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568952890 394 -LAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQ 434
Cdd:COG3206 324 aLQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARE 365
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
364-505 |
6.47e-05 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 45.26 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 364 RQLQERLELAEQKLQQTLRKAETLP----------------EVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQ 427
Cdd:pfam12072 27 AKIGSAEELAKRIIEEAKKEAETKKkealleakeeihklraEAERELKERRNELQRQERRLLQKEETLDRKDESLEKKEE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 428 ELQRARQREKMNEEHNKRLSDTVDKLLSESNERLqlhlkERMAAL---EDKNSLLREVEnakkqlEETQHDKDQLVVTIE 504
Cdd:pfam12072 107 SLEKKEKELEAQQQQLEEKEEELEELIEEQRQEL-----ERISGLtseEAKEILLDEVE------EELRHEAAVMIKEIE 175
|
.
gi 568952890 505 A 505
Cdd:pfam12072 176 E 176
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
253-507 |
8.73e-05 |
|
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: 46.94 E-value: 8.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 253 ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKS-------EEMNTKLQREVREAMAQKEDMEERITTLE 325
Cdd:TIGR04523 395 DLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNnseikdlTNQDSVKELIIKNLDNTRESLETQLKVLS 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 326 KRYLAAQREAtsvhdlnDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLpevEAELAQRVAALSKAE 405
Cdd:TIGR04523 475 RSINKIKQNL-------EQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKL---ESEKKEKESKISDLE 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 406 ERHGNIEERLR--QMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNE-RLQLHLKERMAA-LED------- 474
Cdd:TIGR04523 545 DELNKDDFELKkeNLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDlIKEIEEKEKKISsLEKelekakk 624
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 568952890 475 ---------------KNSLLREVENAKKQLEETQHDKDQLVVTIEALK 507
Cdd:TIGR04523 625 eneklssiiknikskKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESK 672
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
363-502 |
1.15e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 45.81 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 363 NRQLQERLELAEQKLQQtlrkaetlpeVEAELAqRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQ-------- 434
Cdd:COG1566 78 PTDLQAALAQAEAQLAA----------AEAQLA-RLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQAlykkgavs 146
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568952890 435 REKMNEEHNKRlsDTVDKLLSESNERLQLhLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVT 502
Cdd:COG1566 147 QQELDEARAAL--DAAQAQLEAAQAQLAQ-AQAGLREEEELAAAQAQVAQAEAALAQAELNLARTTIR 211
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
164-658 |
1.30e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 46.25 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 164 LKSLFEHHKALDEKVrERLRVALERC----SLLEEELGATHKELMILKEQnnqkktltdglldgnhEQESAPSTNGKRSS 239
Cdd:pfam05483 284 LKELIEKKDHLTKEL-EDIKMSLQRSmstqKALEEDLQIATKTICQLTEE----------------KEAQMEELNKAKAA 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 240 DGSLSHEDLAKVLELQEVI----DRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKL--QREVREAMAQ 313
Cdd:pfam05483 347 HSFVVTEFEATTCSLEELLrteqQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILaeDEKLLDEKKQ 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 314 KEDMEERITTLEKR--YLAAQREaTSVHDLNDKLENEIANKDSMHRQTEDKNRQLQ-ERLELAEQKLQQTLRKAETlPEV 390
Cdd:pfam05483 427 FEKIAEELKGKEQEliFLLQARE-KEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEkEKLKNIELTAHCDKLLLEN-KEL 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 391 EAELAQRVAALSKAEERHGNIEERLRQMEAQLEE-KNQELQRARQREKMNEEHnKRLSDTVDKLLSESNERLQLHLKERM 469
Cdd:pfam05483 505 TQEASDMTLELKKHQEDIINCKKQEERMLKQIENlEEKEMNLRDELESVREEF-IQKGDEVKCKLDKSEENARSIEYEVL 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 470 AALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALK----AELEQMRLRGPSLHHGRPHLGSVPDFRFSVADGH---- 541
Cdd:pfam05483 584 KKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKkkgsAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYqkei 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 542 -VDAYSTSAVLRRPQKGRLAAlrDEPSKVQtlNEQDWERAQQASVLANVAQAFESDVD-VSDGEDDRDTLLSSVDLLSPS 619
Cdd:pfam05483 664 eDKKISEEKLLEEVEKAKAIA--DEAVKLQ--KEIDKRCQHKIAEMVALMEKHKHQYDkIIEERDSELGLYKNKEQEQSS 739
|
490 500 510
....*....|....*....|....*....|....*....
gi 568952890 620 GQADAQTLAMMLQEQLDAINKEIRLIQEEKENTEQRAEE 658
Cdd:pfam05483 740 AKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
281-521 |
1.33e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.50 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 281 ELEEDLDTARKDLIKSEEMNTKlqREVREAMAQKEDMEERI----TTLEKRYLAAQREATSVHDLNDKLENEIANKDSMH 356
Cdd:pfam02463 157 EIEEEAAGSRLKRKKKEALKKL--IEETENLAELIIDLEELklqeLKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 357 RQTEDKNRQLQERLELAEQKLQQTLRKAEtlpevEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQRE 436
Cdd:pfam02463 235 NEERIDLLQELLRDEQEEIESSKQEIEKE-----EEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRK 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 437 KMNEEhNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLR 516
Cdd:pfam02463 310 VDDEE-KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSS 388
|
....*
gi 568952890 517 GPSLH 521
Cdd:pfam02463 389 AAKLK 393
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
320-516 |
1.45e-04 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 44.60 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 320 RITTLEKRYLAAQREATSVHDLNDKLENeIANKDSmhrqTEDKNRQLQERLELAEQKLQQTLRKAETL------------ 387
Cdd:pfam12795 1 KLDELEKAKLDEAAKKKLLQDLQQALSL-LDKIDA----SKQRAAAYQKALDDAPAELRELRQELAALqakaeaapkeil 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 388 -----PEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTvDKLLSESnerLQ 462
Cdd:pfam12795 76 aslslEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPP-GEPLSEA---QR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568952890 463 LHLKERMAALEDKNSLLR-EVENA-------KKQLEETQHDKDQLVVTIEALKAELEQMRLR 516
Cdd:pfam12795 152 WALQAELAALKAQIDMLEqELLSNnnrqdllKARRDLLTLRIQRLEQQLQALQELLNEKRLQ 213
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
246-494 |
1.55e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.12 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 246 EDLAKVLELQevidRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLE 325
Cdd:TIGR00618 273 RAQEAVLEET----QERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 326 KRYLAAQReatsvhdLNDKLENEIANKDSMHRQTEDKN--RQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALS- 402
Cdd:TIGR00618 349 TLHSQEIH-------IRDAHEVATSIREISCQQHTLTQhiHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRd 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 403 -KAEERHGNIEERLRQMEAQLEEknQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLRE 481
Cdd:TIGR00618 422 lQGQLAHAKKQQELQQRYAELCA--AAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLEL 499
|
250
....*....|...
gi 568952890 482 VENAKKQLEETQH 494
Cdd:TIGR00618 500 QEEPCPLCGSCIH 512
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
249-513 |
1.59e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.94 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 249 AKVLELQEVIDRQAR-EQSQMKERLASLSSHAAELEEDLDTARK---DLIKS----EEMNTKLQREVREAMAQKEDMEER 320
Cdd:pfam01576 327 QEVTELKKALEEETRsHEAQLQEMRQKHTQALEELTEQLEQAKRnkaNLEKAkqalESENAELQAELRTLQQAKQDSEHK 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 321 -------ITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKN-----------RQLQERLELAEQKLQQTLR 382
Cdd:pfam01576 407 rkklegqLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNiklskdvssleSQLQDTQELLQEETRQKLN 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 383 KAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKL--------- 453
Cdd:pfam01576 487 LSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALtqqleekaa 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 454 ----LSESNERLQLHLKERMAALEDKNSLLREVENAKKQ---------------------------------------LE 490
Cdd:pfam01576 567 aydkLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKfdqmlaeekaisaryaeerdraeaeareketralslaraLE 646
|
330 340
....*....|....*....|...
gi 568952890 491 ETQHDKDQLVVTIEALKAELEQM 513
Cdd:pfam01576 647 EALEAKEELERTNKQLRAEMEDL 669
|
|
| SAM_STIM-1,2-like |
cd09504 |
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ... |
877-935 |
1.88e-04 |
|
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like (Stromal interaction molecule) proteins is a putative protein-protein interaction domain. STIM1 and STIM2 human proteins are type I transmembrane proteins. The N-terminal part of them includes "hidden" EF-hand and SAM domains. This region is responsible for sensing changes in store-operated and basal cytoplasmic Ca2+ levels and initiates oligomerization. "Hidden" EF hand and SAM domains have a stable intramolecular association, and the SAM domain is a component that regulates stability within STIM proteins. Destabilization of the EF-SAM association during Ca2+ depletion leads to partial unfolding and aggregation (homooligomerization), thus activating the store-operated Ca2+ entry. Immunoprecipitation analysis indicates that STIM1 and STIM2 can form co-precipitable oligomeric associations in vivo. It was suggested that STIM1 and STIM2 are involved in opposite regulation of store operated channels in plasma membrane.
Pssm-ID: 188903 Cd Length: 74 Bit Score: 41.16 E-value: 1.88e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568952890 877 WDGPTVVVWLELWVGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNPLHRLKLRL 935
Cdd:cd09504 5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
969-1024 |
1.93e-04 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 40.72 E-value: 1.93e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 568952890 969 EWLPSLGLPQYRSYFMECLVD-ARMLDHLTKKDLrGQLKMVDSFHRNSFQCGIMCLR 1024
Cdd:pfam07647 11 DWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDL-KRLGITSVGHRRKILKKIQELK 66
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
248-514 |
2.05e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.71 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 248 LAKVLELQEVIDR--QAREQ-SQMKERLASLSSH---AAELEEDLDTARKDLIKSEEmntkLQREVREAMAQKEDMEERI 321
Cdd:COG3096 882 QANLLADETLADRleELREElDAAQEAQAFIQQHgkaLAQLEPLVAVLQSDPEQFEQ----LQADYLQAKEQQRRLKQQI 957
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 322 TTLEkrYLAAQREATSVHDLNDKLEneiankdsmhrQTEDKNRQLQERLELAEQklqqtlrkaetlpeveaelaqrvaAL 401
Cdd:COG3096 958 FALS--EVVQRRPHFSYEDAVGLLG-----------ENSDLNEKLRARLEQAEE------------------------AR 1000
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 402 SKAEERhgnieerLRQMEAQLEEKNQELQ----RARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNS 477
Cdd:COG3096 1001 REAREQ-------LRQAQAQYSQYNQVLAslksSRDAKQQTLQELEQELEELGVQADAEAEERARIRRDELHEELSQNRS 1073
|
250 260 270
....*....|....*....|....*....|....*..
gi 568952890 478 LLREVEnakKQLEETQHDKDQLVVTIEALKAELEQMR 514
Cdd:COG3096 1074 RRSQLE---KQLTRCEAEMDSLQKRLRKAERDYKQER 1107
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
250-421 |
2.30e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 250 KVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQR--EVREAMAQKEDMEERITTLEKR 327
Cdd:COG3206 206 GLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSAR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 328 YLAAQREATSVHDLNDKLENEIAN-KDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEE 406
Cdd:COG3206 286 YTPNHPDVIALRAQIAALRAQLQQeAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARE 365
|
170
....*....|....*
gi 568952890 407 RHGNIEERLRQMEAQ 421
Cdd:COG3206 366 LYESLLQRLEEARLA 380
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
342-446 |
2.60e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.20 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 342 NDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRV-----AALSKAEERHGNIEERLR 416
Cdd:PRK00409 515 KEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAekeaqQAIKEAKKEADEIIKELR 594
|
90 100 110
....*....|....*....|....*....|...
gi 568952890 417 QMEAQL--EEKNQELQRARQR-EKMNEEHNKRL 446
Cdd:PRK00409 595 QLQKGGyaSVKAHELIEARKRlNKANEKKEKKK 627
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
36-497 |
2.70e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.34 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 36 FEQLMVSMLEERDRLLDTLRETQ--ETLALTQGKLHEVGH-ERDSLQRQ---LNTALPQEFAALTKELNVCREQLLEREE 109
Cdd:TIGR00618 154 FAQFLKAKSKEKKELLMNLFPLDqyTQLALMEFAKKKSLHgKAELLTLRsqlLTLCTPCMPDTYHERKQVLEKELKHLRE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 110 EIAELKAERNNTRLLLEHLECLVSRHE--RSLRMTVVKRQAQSPAGVSSEVEVLKALKS--LFEHHKALDEKVRERLRVA 185
Cdd:TIGR00618 234 ALQQTQQSHAYLTQKREAQEEQLKKQQllKQLRARIEELRAQEAVLEETQERINRARKAapLAAHIKAVTQIEQQAQRIH 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 186 LERCSLLEEELGATHKELMILKEQNN--QKKTLTDGLLDGNHEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDrQAR 263
Cdd:TIGR00618 314 TELQSKMRSRAKLLMKRAAHVKQQSSieEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKT-TLT 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 264 EQSQMKERLASLSSHAAELEEDLDTARKDL---IKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATsvhd 340
Cdd:TIGR00618 393 QKLQSLCKELDILQREQATIDTRTSAFRDLqgqLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSL---- 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 341 lnDKLENEIANKDSMHRQTEDKNRQLQERLELaEQKLQQTLRKAETLPEVEAELAQRVAALS----KAEERHGNIEERLR 416
Cdd:TIGR00618 469 --KEREQQLQTKEQIHLQETRKKAVVLARLLE-LQEEPCPLCGSCIHPNPARQDIDNPGPLTrrmqRGEQTYAQLETSEE 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 417 QMEAQL-EEKNQ------ELQRARQREKMNEEHNKRLSDTVDKLLSEsnerLQLHLKERMAALEDKNSLLREVENAKKQL 489
Cdd:TIGR00618 546 DVYHQLtSERKQraslkeQMQEIQQSFSILTQCDNRSKEDIPNLQNI----TVRLQDLTEKLSEAEDMLACEQHALLRKL 621
|
....*...
gi 568952890 490 EETQHDKD 497
Cdd:TIGR00618 622 QPEQDLQD 629
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
267-430 |
2.96e-04 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 43.02 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 267 QMKERLASLSSHAAELEEDLDTARKDLIK---------SEEMNTKLQrEVREAMAQK-EDMEERIT-TLEKrylAAQREA 335
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGPVAQELVDrleketealRERLQKDLE-EVRAKLEPYlEELQAKLGqNVEE---LRQRLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 336 TSVHDLNDKLENEIankDSMHRQTEDKNRQLQERLELAEQKLQQTLrkAETLPEVEAELAQRVAALSK-----AEERHGN 410
Cdd:pfam01442 77 PYTEELRKRLNADA---EELQEKLAPYGEELRERLEQNVDALRARL--APYAEELRQKLAERLEELKEslapyAEEVQAQ 151
|
170 180
....*....|....*....|
gi 568952890 411 IEERLRQMEAQLEEKNQELQ 430
Cdd:pfam01442 152 LSQRLQELREKLEPQAEDLR 171
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
163-441 |
3.28e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.81 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 163 ALKSLFEhhkALDEKVR--ERLRVALER-CSLLEEELGATHKELMILKEQ-NNQKKTLTD---GLLD-GNHEQESAPSTN 234
Cdd:pfam10174 437 ALTTLEE---ALSEKERiiERLKEQREReDRERLEELESLKKENKDLKEKvSALQPELTEkesSLIDlKEHASSLASSGL 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 235 GKRSSDGSL-----SHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHaaeLEEDLDTARKDLIKSEEMNTKLQREVRE 309
Cdd:pfam10174 514 KKDSKLKSLeiaveQKKEECSKLENQLKKAHNAEEAVRTNPEINDRIRL---LEQEVARYKEESGKAQAEVERLLGILRE 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 310 AMAQKEDMEERITTLEKRYLAAQREATSvhdlndklenEIANKDSMhrQTEDKNRQLQErlelaeqkLQQTLRKAETLPE 389
Cdd:pfam10174 591 VENEKNDKDKKIAELESLTLRQMKEQNK----------KVANIKHG--QQEMKKKGAQL--------LEEARRREDNLAD 650
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 568952890 390 VEAE--LAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQ-REKMNEE 441
Cdd:pfam10174 651 NSQQlqLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAeRRKQLEE 705
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
295-512 |
3.56e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 295 KSEEMNTKLQREVREAMAQKED---MEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKnRQLQERLE 371
Cdd:PTZ00121 1105 KTETGKAEEARKAEEAKKKAEDarkAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDA-KKAEAARK 1183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 372 LAEQKLQQTLRKAETLPEVEA----------------ELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRAR-- 433
Cdd:PTZ00121 1184 AEEVRKAEELRKAEDARKAEAarkaeeerkaeearkaEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARma 1263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 434 ---QREKMNEEHNKRLSDTVDKL--------LSESNERLQL-HLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVV 501
Cdd:PTZ00121 1264 hfaRRQAAIKAEEARKADELKKAeekkkadeAKKAEEKKKAdEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKK 1343
|
250
....*....|.
gi 568952890 502 TIEALKAELEQ 512
Cdd:PTZ00121 1344 AAEAAKAEAEA 1354
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
45-427 |
3.70e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.94 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 45 EERDRLLD-------TLRETQETLALTQGKLHEVGHERDSLQRQlNTALPQEFAALTKELNVCREQLLER------EEEI 111
Cdd:COG3096 278 NERRELSEralelrrELFGARRQLAEEQYRLVEMARELEELSAR-ESDLEQDYQAASDHLNLVQTALRQQekieryQEDL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 112 AELkAERnntrlLLEHLECLVSRHERSLRmtvvkRQAQSPAgvsSEVEVlKALKS-LFEHHKALDE---------KVRER 181
Cdd:COG3096 357 EEL-TER-----LEEQEEVVEEAAEQLAE-----AEARLEA---AEEEV-DSLKSqLADYQQALDVqqtraiqyqQAVQA 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 182 LRVALERCSLLEEELGATHKELMILKEQNNQkktLTDGLLDGNHeqesapstngkRSSDGSLSHEDLAKVLELQEVID-- 259
Cdd:COG3096 422 LEKARALCGLPDLTPENAEDYLAAFRAKEQQ---ATEEVLELEQ-----------KLSVADAARRQFEKAYELVCKIAge 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 260 --------------RQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAmaqkEDMEERITTLE 325
Cdd:COG3096 488 versqawqtarellRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAA----EELEELLAELE 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 326 krylaAQREatsvhDLNDKLENEIANKDSMHRQTEDKNRQ-------------LQERLE-LAEQkLQQTLrkaETLPEVE 391
Cdd:COG3096 564 -----AQLE-----ELEEQAAEAVEQRSELRQQLEQLRARikelaarapawlaAQDALErLREQ-SGEAL---ADSQEVT 629
|
410 420 430
....*....|....*....|....*....|....*.
gi 568952890 392 AELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQ 427
Cdd:COG3096 630 AAMQQLLEREREATVERDELAARKQALESQIERLSQ 665
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
176-517 |
3.96e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 44.73 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 176 EKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGLldGNHEQESAPSTNgkrssdgslSHEDLAKVLELQ 255
Cdd:pfam05557 135 EELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEI--QSQEQDSEIVKN---------SKSELARIPELE 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 256 EVIDRQAREQSQ---MKERLASLSSHAAELEEDLDT---ARKDLIKSEEMNTKLQREVRE----------AMAQKEDMEE 319
Cdd:pfam05557 204 KELERLREHNKHlneNIENKLLLKEEVEDLKRKLEReekYREEAATLELEKEKLEQELQSwvklaqdtglNLRSPEDLSR 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 320 RITTLEKRYLAAQREATSVhdlndkleneiankDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVA 399
Cdd:pfam05557 284 RIEQLQQREIVLKEENSSL--------------TSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVL 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 400 ALSKaeERHGnIEERLRQMEAQLEEKN---QELQRARQREKMNEE---HNKRLSDTVDKLLSE--------SNERLQLHL 465
Cdd:pfam05557 350 LLTK--ERDG-YRAILESYDKELTMSNyspQLLERIEEAEDMTQKmqaHNEEMEAQLSVAEEElggykqqaQTLERELQA 426
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 568952890 466 KERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRG 517
Cdd:pfam05557 427 LRQQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQG 478
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
281-500 |
4.30e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 281 ELEEDLDT--ARKDLIKSE-EMNTKLQREVREAMAQkedmeeRITTLEKRYLAAQREATSVHDLNDKLENEIANKD-SMH 356
Cdd:PHA02562 178 ELNQQIQTldMKIDHIQQQiKTYNKNIEEQRKKNGE------NIARKQNKYDELVEEAKTIKAEIEELTDELLNLVmDIE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 357 RQTEDKNRQLQERLELAEQ-----KLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQ-MEAQLEEKNQELQ 430
Cdd:PHA02562 252 DPSAALNKLNTAAAKIKSKieqfqKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKlDTAIDELEEIMDE 331
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952890 431 RARQREKMNEEHNK-RLSDTVDKLLSESNERLQLHLKERMAALEDKNSllrEVENAKKQLEETQHDKDQLV 500
Cdd:PHA02562 332 FNEQSKKLLELKNKiSTNKQSLITLVDKAKKVKAAIEELQAEFVDNAE---ELAKLQDELDKIVKTKSELV 399
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
193-514 |
4.65e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.40 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 193 EEELGATHKELMILKEQNNQ-KKTLTDglLDGNHEQESAPST--NGKRSSDGSLSHED-------LAKVLELQEVI---- 258
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKaESELKE--LEKKHQQLCEEKNalQEQLQAETELCAEAeemrarlAARKQELEEILhele 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 259 ----DRQAREQSQMKERlASLSSHAAELEEDLD---TARK------------------DLIKSEEMNTKLQREvreamaq 313
Cdd:pfam01576 82 srleEEEERSQQLQNEK-KKMQQHIQDLEEQLDeeeAARQklqlekvtteakikkleeDILLLEDQNSKLSKE------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 314 KEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQtEDKNRQLQERL---------ELAEQKLQQTLRKA 384
Cdd:pfam01576 154 RKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKK-EEKGRQELEKAkrklegestDLQEQIAELQAQIA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 385 ETLPEVEAELAQRVAALSKAEE---RHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSEsnerL 461
Cdd:pfam01576 233 ELRAQLAKKEEELQAALARLEEetaQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTE----L 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952890 462 QLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLV--------VTIEALKAELEQMR 514
Cdd:pfam01576 309 EDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLqemrqkhtQALEELTEQLEQAK 369
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
264-428 |
5.25e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 42.59 E-value: 5.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 264 EQSQMKERLASLSSHAAELEEDLDTARKD---LIKSEEMNTKLQREVREAMAQKEDMEERIttlekrylaaqreatsvhd 340
Cdd:pfam13851 55 ENKRLTEPLQKAQEEVEELRKQLENYEKDkqsLKNLKARLKVLEKELKDLKWEHEVLEQRF------------------- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 341 lnDKLENEianKDSMHRQTEDKNRQLQERLELAEQKLQQTLRK-AETLPEVEAELAQRVAALSKAEERHGNIEERLRQMe 419
Cdd:pfam13851 116 --EKVERE---RDELYDKFEAAIQDVQQKTGLKNLLLEKKLQAlGETLEKKEAQLNEVLAAANLDPDALQAVTEKLEDV- 189
|
....*....
gi 568952890 420 aqLEEKNQE 428
Cdd:pfam13851 190 --LESKNQL 196
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
260-519 |
5.33e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.56 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 260 RQAREQsqmkeRLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQ--KEDMEERITTLEKRylaaQREats 337
Cdd:COG3096 780 RAAREK-----RLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVafAPDPEAELAALRQR----RSE--- 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 338 vhdlndkLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQT-LRKAETLPEVEAELAQRVAALSKAE---ERHGNIEE 413
Cdd:COG3096 848 -------LERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQAnLLADETLADRLEELREELDAAQEAQafiQQHGKALA 920
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 414 RLR--------------QMEAQLEEKNQELQRARQR-EKMNEEHNKRL----SDTVDkLLSESNErLQLHLKERMAALED 474
Cdd:COG3096 921 QLEplvavlqsdpeqfeQLQADYLQAKEQQRRLKQQiFALSEVVQRRPhfsyEDAVG-LLGENSD-LNEKLRARLEQAEE 998
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 568952890 475 KNSLLRE-VENAKKQLEE---------TQHD-KDQlvvTIEALKAELEQMRLRGPS 519
Cdd:COG3096 999 ARREAREqLRQAQAQYSQynqvlaslkSSRDaKQQ---TLQELEQELEELGVQADA 1051
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
344-510 |
7.27e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.50 E-value: 7.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 344 KLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRK---------AETLPEVEAELAQRVAALSKAEERHGNIEER 414
Cdd:COG1842 41 EARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKgredlareaLERKAELEAQAEALEAQLAQLEEQVEKLKEA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 415 LRQMEAQLEEKNQELQRARQREKMNeEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAK---KQLEE 491
Cdd:COG1842 121 LRQLESKLEELKAKKDTLKARAKAA-KAQEKVNEALSGIDSDDATSALERMEEKIEEMEARAEAAAELAAGDsldDELAE 199
|
170 180
....*....|....*....|..
gi 568952890 492 TQHDK---DQLvvtiEALKAEL 510
Cdd:COG1842 200 LEADSeveDEL----AALKAKM 217
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
154-512 |
7.35e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 7.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 154 VSSEVEVLKALKSLFEHHKALDEKVRErLRVALERcslLEEELGATH------------------KELMILKEQNNQKKT 215
Cdd:pfam01576 670 VSSKDDVGKNVHELERSKRALEQQVEE-MKTQLEE---LEDELQATEdaklrlevnmqalkaqfeRDLQARDEQGEEKRR 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 216 LtdgLLDGNHEQESAPSTNGKRSSDGSLSHEDLA---KVLELQEVIDRQAREQS--QMKERLASLSSHAAELEEDLDTAR 290
Cdd:pfam01576 746 Q---LVKQVRELEAELEDERKQRAQAVAAKKKLEldlKELEAQIDAANKGREEAvkQLKKLQAQMKDLQRELEEARASRD 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 291 KDLIKSEEMNTKLQREVREAMAQKEDMEerittlekrylAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERL 370
Cdd:pfam01576 823 EILAQSKESEKKLKNLEAELLQLQEDLA-----------ASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARI 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 371 ELAEQKLQQTLRKAETLPEVEAELAQRVAALS---KAEERHGNIEERLRQmeaQLEEKNQELQ-RARQREKMNEEHNKRL 446
Cdd:pfam01576 892 AQLEEELEEEQSNTELLNDRLRKSTLQVEQLTtelAAERSTSQKSESARQ---QLERQNKELKaKLQEMEGTVKSKFKSS 968
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568952890 447 SDTVDKLLSESNERLQLHLKERMAA---LEDKNSLLRE----VENAKKQLEETQHDKDQLVVTIEALKAELEQ 512
Cdd:pfam01576 969 IAALEAKIAQLEEQLEQESRERQAAnklVRRTEKKLKEvllqVEDERRHADQYKDQAEKGNSRMKQLKRQLEE 1041
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
162-352 |
8.01e-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: 8.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 162 KALKSLFEHHKALDEKV---RERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGLLDGNHEQESAPSTNGKRS 238
Cdd:COG4942 48 KEEKALLKQLAALERRIaalARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLS 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 239 SDGSLsheDLAKVLE-LQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDM 317
Cdd:COG4942 128 PEDFL---DAVRRLQyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARL 204
|
170 180 190
....*....|....*....|....*....|....*
gi 568952890 318 EERITTLEKRYLAAQREATSVHDLNDKLENEIANK 352
Cdd:COG4942 205 EKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
343-508 |
8.03e-04 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 42.36 E-value: 8.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 343 DKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAE----------------TLPEVEAELAQRVAALSKAEE 406
Cdd:pfam04012 39 VKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNeelarealaekkslekQAEALETQLAQQRSAVEQLRK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 407 RHGNIEERLRQMEAQLEEKNQELQRARQREKMNEehnkrlsdTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENA- 485
Cdd:pfam04012 119 QLAALETKIQQLKAKKNLLKARLKAAKAQEAVQT--------SLGSLSTSSATDSFERIEEKIEEREARADAAAELASAv 190
|
170 180
....*....|....*....|....*
gi 568952890 486 --KKQLEETQHDKDQLVVTIEALKA 508
Cdd:pfam04012 191 dlDAKLEQAGIQMEVSEDVLARLKA 215
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
246-459 |
8.77e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.38 E-value: 8.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 246 EDLAKVLElQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARK-------DLIKSEEMNT-KLQREVREAMAQKEDM 317
Cdd:PRK05771 34 EDLKEELS-NERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKvsvksleELIKDVEEELeKIEKEIKELEEEISEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 318 EERITTLEKRylaaQREATSVHDLNDKLENEIANKdSMHRQTEDKNRQLQERLELAEQKLQQTLRK-------------A 384
Cdd:PRK05771 113 ENEIKELEQE----IERLEPWGNFDLDLSLLLGFK-YVSVFVGTVPEDKLEELKLESDVENVEYIStdkgyvyvvvvvlK 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568952890 385 ETLPEVEAELAQrvAALSKAE-ERHGNIEERLRQMEAQLEEKNQELQRARQR-EKMNEEHNKRLSDTVDKLLSESNE 459
Cdd:PRK05771 188 ELSDEVEEELKK--LGFERLElEEEGTPSELIREIKEELEEIEKERESLLEElKELAKKYLEELLALYEYLEIELER 262
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
139-662 |
1.08e-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: 43.50 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 139 LRMTVVKRQAQspagVSSEVEVLKALKSLFEHHKALDEKVRERLRVALErcslLEEELGATHKELMILKEQNNQKKTLTD 218
Cdd:TIGR00606 222 IRDQITSKEAQ----LESSREIVKSYENELDPLKNRLKEIEHNLSKIMK----LDNEIKALKSRKKQMEKDNSELELKME 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 219 GLLDGNHEQESAPSTNgkRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERL---ASLSSHAAELEEDLDTARKDLIK 295
Cdd:TIGR00606 294 KVFQGTDEQLNDLYHN--HQRTVREKERELVDCQRELEKLNKERRLLNQEKTELlveQGRLQLQADRHQEHIRARDSLIQ 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 296 SEEMNTKL---------QREVREAMA-QKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQ 365
Cdd:TIGR00606 372 SLATRLELdgfergpfsERQIKNFHTlVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEK 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 366 LQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEErHGNIEERLRQMEAQLEEKNQELQRARQREKMNEE--HN 443
Cdd:TIGR00606 452 KQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEK-NSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQlnHH 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 444 KRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENaKKQLEETQHDK-DQLVVTIEALK------AELEQMRlr 516
Cdd:TIGR00606 531 TTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPN-KKQLEDWLHSKsKEINQTRDRLAklnkelASLEQNK-- 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 517 gpslHHGRPHLGSVPDFRFSVADGHVDAYSTsavlrrpqkgrlaalRDEPSKVQTLNEQDWERAQQASVLANVAQAFESD 596
Cdd:TIGR00606 608 ----NHINNELESKEEQLSSYEDKLFDVCGS---------------QDEESDLERLKEEIEKSSKQRAMLAGATAVYSQF 668
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568952890 597 VDVSDGEDDRdtllssvdlLSPSGQADAQTLAmMLQEQLDAINKEIRLIQEEKENTEQRAEEIESR 662
Cdd:TIGR00606 669 ITQLTDENQS---------CCPVCQRVFQTEA-ELQEFISDLQSKLRLAPDKLKSTESELKKKEKR 724
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
31-473 |
1.09e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.57 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 31 DADSHFEQLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQ---LNTALPQEFAAL---TKELNVCREQL 104
Cdd:pfam15921 321 DLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQEsgnLDDQLQKLLADLhkrEKELSLEKEQN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 105 LE-------REEEIAELKAERNNTRLLLEHLECLVsRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEK 177
Cdd:pfam15921 401 KRlwdrdtgNSITIDHLRRELDDRNMEVQRLEALL-KAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRK 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 178 VRERL---RVALER---------CSLLEEE--LGATHKELMILKEQNNQK-KTLTDGLLDGNHEQESAPSTNGKRssdgs 242
Cdd:pfam15921 480 VVEELtakKMTLESsertvsdltASLQEKEraIEATNAEITKLRSRVDLKlQELQHLKNEGDHLRNVQTECEALK----- 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 243 LSHEDLAKVLE-LQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEeri 321
Cdd:pfam15921 555 LQMAEKDKVIEiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLE--- 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 322 ttLEKRYL--AAQREATSVHDLN---DKLENEIAN-KDSMHRQTEDKN------RQLQERLELAEQKLQQTLRKAET--- 386
Cdd:pfam15921 632 --LEKVKLvnAGSERLRAVKDIKqerDQLLNEVKTsRNELNSLSEDYEvlkrnfRNKSEEMETTTNKLKMQLKSAQSele 709
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 387 ---------------------------------------------------------LPEVEAELAQRVAALSKAEERHG 409
Cdd:pfam15921 710 qtrntlksmegsdghamkvamgmqkqitakrgqidalqskiqfleeamtnankekhfLKEEKNKLSQELSTVATEKNKMA 789
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568952890 410 NIEERLRQMEAQLEEKNQELQRARQREKMneehnkRLSDTVDKLLSESNERLQLHLKERMAALE 473
Cdd:pfam15921 790 GELEVLRSQERRLKEKVANMEVALDKASL------QFAECQDIIQRQEQESVRLKLQHTLDVKE 847
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
113-524 |
1.15e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 113 ELKAERNNTRLLLEH-LECLVSRHERSLRmTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKvrERLRVALERCSL 191
Cdd:pfam01576 320 ELRSKREQEVTELKKaLEEETRSHEAQLQ-EMRQKHTQALEELTEQLEQAKRNKANLEKAKQALES--ENAELQAELRTL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 192 LEEELGATHK---------ELMI-LKEQNNQKKTLTDGLLDGNHEQESAPSTNGKRSSDGSLSHEDLAKV-LELQeviDR 260
Cdd:pfam01576 397 QQAKQDSEHKrkklegqlqELQArLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLeSQLQ---DT 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 261 QAREQSQMKERLaSLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQ----KEDMEERITTLEKRYLAAQREAT 336
Cdd:pfam01576 474 QELLQEETRQKL-NLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQlsdmKKKLEEDAGTLEALEEGKKRLQR 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 337 SVHDLNDKLENEIANKDSMHRQTE-------------DKNRQLQERLELAEQKLQQTL--------RKAETLPEVEAELA 395
Cdd:pfam01576 553 ELEALTQQLEEKAAAYDKLEKTKNrlqqelddllvdlDHQRQLVSNLEKKQKKFDQMLaeekaisaRYAEERDRAEAEAR 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 396 QRVA-------ALSKAEERHGNIEERLRQMEAQLEE---------KN-QELQRA-RQREKMNEEHNKRLSDTVDKLLSES 457
Cdd:pfam01576 633 EKETralslarALEEALEAKEELERTNKQLRAEMEDlvsskddvgKNvHELERSkRALEQQVEEMKTQLEELEDELQATE 712
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 458 NERLQLHLKerMAAL----------------EDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRGPSLH 521
Cdd:pfam01576 713 DAKLRLEVN--MQALkaqferdlqardeqgeEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAAN 790
|
...
gi 568952890 522 HGR 524
Cdd:pfam01576 791 KGR 793
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
357-513 |
1.17e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.40 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 357 RQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALskaEERHGNIEERLRQMEAQLEEKNQELQRARQRE 436
Cdd:COG3096 525 EQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEEL---EEQAAEAVEQRSELRQQLEQLRARIKELAARA 601
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568952890 437 KMNEEHNKRLsdtvdkllsesnERLQLHLKErmaALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQM 513
Cdd:COG3096 602 PAWLAAQDAL------------ERLREQSGE---ALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERL 663
|
|
| F-BAR_PACSIN1 |
cd07680 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ... |
323-444 |
1.28e-03 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSIN 1 or Syndapin I is expressed specifically in the brain and is localized in neurites and synaptic boutons. It binds the brain-specific proteins dynamin I, synaptojanin, synapsin I, and neural Wiskott-Aldrich syndrome protein (nWASP), and functions as a link between the cytoskeletal machinery and synaptic vesicle endocytosis. PACSIN 1 interacts with huntingtin and may be implicated in the neuropathology of Huntington's disease. It contains an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153364 [Multi-domain] Cd Length: 258 Bit Score: 41.96 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 323 TLEKRYLAAQREATSVHDLNDKLENEIAN----------KDSMHRQTE---DKNRQLQERLELAEQKLQQTLRKAETLPE 389
Cdd:cd07680 61 SLERAWGAIMTEADKVSELHQEVKNNLLNedlekvknwqKDAYHKQIMggfKETKEAEDGFRKAQKPWAKKMKELEAAKK 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568952890 390 V------EAELAQRVAALSKAEErhGNIEERLRQMEAQLEEKNQELQRARQR-EKMNEEHNK 444
Cdd:cd07680 141 AyhlackEEKLAMTREANSKAEQ--SVTPEQQKKLQDKVDKCKQDVQKTQEKyEKVLDDVGK 200
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
253-521 |
1.44e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 253 ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQ 332
Cdd:COG4372 70 QARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAERE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 333 REATSVHDLNDKLENEIAN--KDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALS--KAEERH 408
Cdd:COG4372 150 EELKELEEQLESLQEELAAleQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLeaKDSLEA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 409 GNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQ 488
Cdd:COG4372 230 KLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSL 309
|
250 260 270
....*....|....*....|....*....|...
gi 568952890 489 LEETQHDKDQLVVTIEALKAELEQMRLRGPSLH 521
Cdd:COG4372 310 IGALEDALLAALLELAKKLELALAILLAELADL 342
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
876-938 |
1.63e-03 |
|
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.
Pssm-ID: 425739 Cd Length: 64 Bit Score: 38.02 E-value: 1.63e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568952890 876 QWDGPTVVVWLElWVGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQ 938
Cdd:pfam00536 2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQ 61
|
|
| SAM_Neurabin-like |
cd09512 |
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ... |
1045-1111 |
1.72e-03 |
|
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like (Neural actin-binding) subfamily is a putative protein-protein interaction domain. This group currently includes the SAM domains of neurobin-I, SAMD14 and neurobin-I/SAMD14-like proteins. Most are multidomain proteins and in addition to SAM domain they contain other protein-binding domains such as PDZ and actin-binding domains. Members of this subfamily participate in signal transduction. Neurabin-I is involved in the regulation of Ca signaling intensity in alpha-adrenergic receptors; it forms a functional pair of opposing regulators with neurabin-II. Neurabins are expressed almost exclusively in neuronal cells. They are known to interact with protein phosphatase 1 and inhibit its activity; they also can bind actin filaments; however, the exact role of the SAM domain is unclear, since SAM doesn't participate in these interactions.
Pssm-ID: 188911 [Multi-domain] Cd Length: 70 Bit Score: 38.02 E-value: 1.72e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568952890 1045 RDVLVWSNDRVIRWILSIGLKEYANNLIESGVHG-ALLALDETfDFSALALllqiptQNTQARAVLER 1111
Cdd:cd09512 2 RPVSEWSVQQVCQWLMGLGLEQYIPEFTANNIDGqQLLQLDSS-KLKALGI------TSSSDRSLLKK 62
|
|
| SAM_SARM1-like_repeat1 |
cd09501 |
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
969-1016 |
1.72e-03 |
|
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of SARM1-like adaptor proteins is a protein-protein interaction domain. SARM1-like proteins contain two tandem SAM domains. SARM1-like proteins are involved in TLR (Toll-like receptor) signaling. They are responsible for targeted localization of the whole protein to post-synaptic regions of axons. In humans SARM1 expression is detected in kidney and liver.
Pssm-ID: 188900 [Multi-domain] Cd Length: 69 Bit Score: 38.05 E-value: 1.72e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 568952890 969 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSF 1016
Cdd:cd09501 11 TWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLRKRF 58
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
174-512 |
1.73e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.64 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 174 LDEKVRERL---RVALERCSLLEEELgaTHKELMILKEqnNQKKTLTDGLLDGNHEQESAPSTNGKRSSDGSLSHEDL-- 248
Cdd:COG5185 143 LDEIADIEAsygEVETGIIKDIFGKL--TQELNQNLKK--LEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGse 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 249 ------AKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTAR-KDLIKSEEMNTKLQREVREAMAQKEDMEERI 321
Cdd:COG5185 219 stllekAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRlEKLGENAESSKRLNENANNLIKQFENTKEKI 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 322 TTLEKrylaaqreatsvhdlndkleneianKDSMHRQTEDKNRQLQERLElaEQKLQQTLRKAET-LPEVEAELAQRVAA 400
Cdd:COG5185 299 AEYTK-------------------------SIDIKKATESLEEQLAAAEA--EQELEESKRETETgIQNLTAEIEQGQES 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 401 LSKAEERHGN-------------IEERLRQMEAQLEEKNQELQRARQ-REKMNEEHNKRLSDTVdKLLSESNERLQlhlk 466
Cdd:COG5185 352 LTENLEAIKEeienivgevelskSSEELDSFKDTIESTKESLDEIPQnQRGYAQEILATLEDTL-KAADRQIEELQ---- 426
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 568952890 467 ermAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQ 512
Cdd:COG5185 427 ---RQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAY 469
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
325-517 |
1.78e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 325 EKRYLAAQREAtsvhdlndkLENEIANKDSMHRQTEDKNRQLQErlelAEQKLQQTLRKAETLPEVEAELAQRVAALSKA 404
Cdd:PRK04863 507 EQRHLAEQLQQ---------LRMRLSELEQRLRQQQRAERLLAE----FCKRLGKNLDDEDELEQLQEELEARLESLSES 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 405 EERHGNIEERLRQMEAQLEEKNQELQRARQrekmnEEHNkrlsdtvdklLSESNERLQLHLKErmaALEDKNSLLREVEN 484
Cdd:PRK04863 574 VSEARERRMALRQQLEQLQARIQRLAARAP-----AWLA----------AQDALARLREQSGE---EFEDSQDVTEYMQQ 635
|
170 180 190
....*....|....*....|....*....|...
gi 568952890 485 AKKQLEETQHDKDQLVVTIEALKAELEQMRLRG 517
Cdd:PRK04863 636 LLERERELTVERDELAARKQALDEEIERLSQPG 668
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
112-487 |
1.81e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 112 AELKAERNNTRLLLEHLECLVSRH---------ERSLRMTVVKRQaqspagvssevEVLKALKSLFEHHKaldeKVRERL 182
Cdd:PRK04863 803 ATLSFDVQKLQRLHQAFSRFIGSHlavafeadpEAELRQLNRRRV-----------ELERALADHESQEQ----QQRSQL 867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 183 RVALERCSLLEEELGathkELMILKEQnnqkkTLTDGLLDgnheqesapstngkrssdgslSHEDLAKVLELQEVIDRQA 262
Cdd:PRK04863 868 EQAKEGLSALNRLLP----RLNLLADE-----TLADRVEE---------------------IREQLDEAEEAKRFVQQHG 917
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 263 REQSQMKERLASLSSHAAELEEdldtarkdlikseemntkLQREVREAMAQKEDMEERITTLEkrYLAAQREATSVHDLN 342
Cdd:PRK04863 918 NALAQLEPIVSVLQSDPEQFEQ------------------LKQDYQQAQQTQRDAKQQAFALT--EVVQRRAHFSYEDAA 977
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 343 DKLEneiankdsmhrQTEDKNRQLQERLELAEqklQQTLRKAETLPEVEAELAQRVAALSKAEERHgnieERLRQMEAQL 422
Cdd:PRK04863 978 EMLA-----------KNSDLNEKLRQRLEQAE---QERTRAREQLRQAQAQLAQYNQVLASLKSSY----DAKRQMLQEL 1039
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 423 EEKNQEL---------QRARQREkmnEEHNKRLSDT------VDKLLSESNERLQlHLKERMAALEDKNSLLRE-VENAK 486
Cdd:PRK04863 1040 KQELQDLgvpadsgaeERARARR---DELHARLSANrsrrnqLEKQLTFCEAEMD-NLTKKLRKLERDYHEMREqVVNAK 1115
|
.
gi 568952890 487 K 487
Cdd:PRK04863 1116 A 1116
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
364-514 |
1.86e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 364 RQLQERLELAEQKLQQTLRKAETlpevEAELAQRVAALSKAEERHgnieERLRQMEAQLEEKNQELQRARQREKMNEEHn 443
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKK----EAEAIKKEALLEAKEEIH----KLRNEFEKELRERRNELQKLEKRLLQKEEN- 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952890 444 krlsdtvdkllsesnerlqlhLKERMAALEDKNSLLREVENAKKQLEETqhdkdqlvvtIEALKAELEQMR 514
Cdd:PRK12704 98 ---------------------LDRKLELLEKREEELEKKEKELEQKQQE----------LEKKEEELEELI 137
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
207-430 |
2.15e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 207 KEQNNQKKTLtDGLLDGNHEQESAPSTNGKRSSdgSLSHEDLAkvlELQEVIDRQAREQSQMKERLASLSSHAAELEEDL 286
Cdd:PHA02562 177 RELNQQIQTL-DMKIDHIQQQIKTYNKNIEEQR--KKNGENIA---RKQNKYDELVEEAKTIKAEIEELTDELLNLVMDI 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 287 DTARKDLIKSEEMNTKLQREV----REA------------MAQKEDMEERITTLEKRYLAAQreaTSVHDLNDKLENEIA 350
Cdd:PHA02562 251 EDPSAALNKLNTAAAKIKSKIeqfqKVIkmyekggvcptcTQQISEGPDRITKIKDKLKELQ---HSLEKLDTAIDELEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 351 NKDSMHRQTEdKNRQLQERLELAEQKLQQTLRKAEtlpEVEAElaqrvaaLSKAEERHGNIEERLRQMEAQLEEKNQELQ 430
Cdd:PHA02562 328 IMDEFNEQSK-KLLELKNKISTNKQSLITLVDKAK---KVKAA-------IEELQAEFVDNAEELAKLQDELDKIVKTKS 396
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
174-470 |
2.21e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.16 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 174 LDEKVRERLRVALERCSLLEEELGATHKELMILKEQNN-------QKKTLTDGLLDGNHEQESapSTNGKRSSDGSLSHE 246
Cdd:pfam02029 71 REERRQKRLQEALERQKEFDPTIADEKESVAERKENNEeeensswEKEEKRDSRLGRYKEEET--EIREKEYQENKWSTE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 247 DLAKVLELQEVIDRQAREQSQMKERlaslssHAAElEEDLDTARKDLIKSEEMNTKLQREVR---EAMAQKEDMEERITT 323
Cdd:pfam02029 149 VRQAEEEGEEEEDKSEEAEEVPTEN------FAKE-EVKDEKIKKEKKVKYESKVFLDQKRGhpeVKSQNGEEEVTKLKV 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 324 LEKRYLAAQREAtsvhdlnDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAEtlpeVEAELAQRvaalsK 403
Cdd:pfam02029 222 TTKRRQGGLSQS-------QEREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLRQKQQEAE----LELEELKK-----K 285
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568952890 404 AEERHGNIEERLRQMEAqlEEKnqelqrarQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMA 470
Cdd:pfam02029 286 REERRKLLEEEEQRRKQ--EEA--------ERKLREEEEKRRMKEEIERRRAEAAEKRQKLPEDSSS 342
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
179-518 |
2.26e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.20 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 179 RERLRVAlerCSLLEEELGATHKELMILKEQNNQKKTLTDGLLDGNHEQE-------SAPSTNGKRSSDGSLSHEDLAKV 251
Cdd:PLN02939 28 RRRLAVS---CRARRRGFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQlentslrTVMELPQKSTSSDDDHNRASMQR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 252 LELQEVIDRQAREQSQMKERLASLssHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRY--- 328
Cdd:PLN02939 105 DEAIAAIDNEQQTNSKDGEQLSDF--QLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLset 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 329 -----LAAQrEATSVHDLNDKLENeiANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRK--AETLPEVEAELAQRVAAL 401
Cdd:PLN02939 183 darikLAAQ-EKIHVEILEEQLEK--LRNELLIRGATEGLCVHSLSKELDVLKEENMLLKddIQFLKAELIEVAETEERV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 402 SKAEERHGNIEERLRQMEAQLE------------------EKNQELQRARQREKMNEEH-------NKRLSDTVDKL--- 453
Cdd:PLN02939 260 FKLEKERSLLDASLRELESKFIvaqedvsklsplqydcwwEKVENLQDLLDRATNQVEKaalvldqNQDLRDKVDKLeas 339
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952890 454 LSESN------ERLQLhLKERMAALEDKnsLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRGP 518
Cdd:PLN02939 340 LKEANvskfssYKVEL-LQQKLKLLEER--LQASDHEIHSYIQLYQESIKEFQDTLSKLKEESKKRSLEHP 407
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
45-276 |
3.15e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNtALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLL 124
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA-ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 125 LEHLECLVSRHERSLRMTVVKRQAQ---SPAGVSSEVEVLKALKSLFEHhkalDEKVRERLRVALERCSLLEEELGATHK 201
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPA----RREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568952890 202 ELM-ILKEQNNQKKTLTDGLLDgnhEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASLS 276
Cdd:COG4942 175 ELEaLLAELEEERAALEALKAE---RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
246-491 |
3.25e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.06 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 246 EDLAKVLELQEVIDRQAREQSQMKERLAslsshAAELEEDLDTARKDLIKSEEMNtKLQREVREAMAQKEDMEERITTLE 325
Cdd:pfam13868 120 EKLEKQRQLREEIDEFNEEQAEWKELEK-----EEEREEDERILEYLKEKAEREE-EREAEREEIEEEKEREIARLRAQQ 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 326 KRYLAAQREATsvhDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETlpeveaelaqrvaalsKAE 405
Cdd:pfam13868 194 EKAQDEKAERD---ELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERR----------------LAE 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 406 ERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVdkllsesNERLQLHLKERMAALEDKNSLLREVENA 485
Cdd:pfam13868 255 EAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQI-------EEREEQRAAEREEELEEGERLREEEAER 327
|
....*.
gi 568952890 486 KKQLEE 491
Cdd:pfam13868 328 RERIEE 333
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
284-512 |
4.11e-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: 41.54 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 284 EDLDTARKDLIKSEEMN----TKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQT 359
Cdd:TIGR04523 78 KILEQQIKDLNDKLKKNkdkiNKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 360 EDKNRQLQERLELAEQKL----QQTLRKAETLPEVEAELAQRVAALSKAEERhgniEERLRQMEAQLEE-KNQELQRARQ 434
Cdd:TIGR04523 158 NNKYNDLKKQKEELENELnlleKEKLNIQKNIDKIKNKLLKLELLLSNLKKK----IQKNKSLESQISElKKQNNQLKDN 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 435 REKMNEEHNKR---LSDTVDKLLSESNErlQLHLKERmaaLEDKNSllrEVENAKKQLEETQHDKDQLVVTIEALKAELE 511
Cdd:TIGR04523 234 IEKKQQEINEKtteISNTQTQLNQLKDE--QNKIKKQ---LSEKQK---ELEQNNKKIKELEKQLNQLKSEISDLNNQKE 305
|
.
gi 568952890 512 Q 512
Cdd:TIGR04523 306 Q 306
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
364-515 |
4.13e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 41.23 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 364 RQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERlrqmeaqlEEKNQELQRARQREKMNEEHN 443
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRER--------EELQREEERLVQKEEQLDARA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 444 KRLSDTVDKLLSESNerlqlHLKERMAALEDKNSLLREV---------ENAKKQL-----EETQHDKDQLVVTIEAlKAE 509
Cdd:PRK12705 98 EKLDNLENQLEEREK-----ALSARELELEELEKQLDNElyrvagltpEQARKLLlklldAELEEEKAQRVKKIEE-EAD 171
|
....*.
gi 568952890 510 LEQMRL 515
Cdd:PRK12705 172 LEAERK 177
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
246-446 |
4.89e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 40.67 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 246 EDLAKVLELQEVIDRQAREQSQMKER--LASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITT 323
Cdd:pfam13868 130 EEIDEFNEEQAEWKELEKEEEREEDEriLEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAK 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 324 LEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSK 403
Cdd:pfam13868 210 LYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRL 289
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568952890 404 A---------EERHgniEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRL 446
Cdd:pfam13868 290 EhrrelekqiEERE---EQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
320-516 |
5.87e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 40.65 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 320 RITTLEKRYLAAQREATSVHDL----NDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPE------ 389
Cdd:pfam07888 28 RAELLQNRLEECLQERAELLQAqeaaNRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEkykels 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 390 -VEAELAQRVAALSKAEERHG----NIEERLRQMEAQLEEKNQELQRARQREKM------NEEHNKRLSDTVDKLLSESN 458
Cdd:pfam07888 108 aSSEELSEEKDALLAQRAAHEarirELEEDIKTLTQRVLERETELERMKERAKKagaqrkEEEAERKQLQAKLQQTEEEL 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568952890 459 ERLQLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLR 516
Cdd:pfam07888 188 RSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQER 245
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
271-514 |
5.95e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 40.61 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 271 RLASLSSHAAELEEDLD------------TARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRY------LAAQ 332
Cdd:pfam06160 61 SLPDIEELLFEAEELNDkyrfkkakkaldEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYrelrktLLAN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 333 REA--TSVHDLNDKLEN--------EIANKDSMHRQTEDKNRQLQERLELAEQKLQQT---LRKAET-LPEVEAELAQRV 398
Cdd:pfam06160 141 RFSygPAIDELEKQLAEieeefsqfEELTESGDYLEAREVLEKLEEETDALEELMEDIpplYEELKTeLPDQLEELKEGY 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 399 AALSKAEER--HGNIEERLRQMEAQLEE-----KNQELQRArqrEKMNEEHNKRLSDTVDKLLSESNERLQLHlkERMAA 471
Cdd:pfam06160 221 REMEEEGYAleHLNVDKEIQQLEEQLEEnlallENLELDEA---EEALEEIEERIDQLYDLLEKEVDAKKYVE--KNLPE 295
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 568952890 472 LEDknsllrEVENAKKQLEETQHDKDQL----------VVTIEALKAELEQMR 514
Cdd:pfam06160 296 IED------YLEHAEEQNKELKEELERVqqsytlneneLERVRGLEKQLEELE 342
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
255-433 |
6.18e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.33 E-value: 6.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 255 QEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRyLAAQRe 334
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQE-LDSEK- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 335 ATSVHDLndkleneiankdsmhRQTEDKNRQLQErlelaeqklqqtLRkaetlpeveAELAQRVAALSKAEERHGNIEER 414
Cdd:PRK09039 130 QVSARAL---------------AQVELLNQQIAA------------LR---------RQLAALEAALDASEKRDRESQAK 173
|
170 180
....*....|....*....|...
gi 568952890 415 L----RQMEAQLEEKNQELQRAR 433
Cdd:PRK09039 174 IadlgRRLNVALAQRVQELNRYR 196
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
389-660 |
6.32e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.82 E-value: 6.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 389 EVEAELAQRVAALSKAEERhgniEERLRQMeaqLEEKNQELQR-ARQREKMNEehnkrlsdtVDKLLSESNE-RLQLHLK 466
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEEN----IERLDLI---IDEKRQQLERlRREREKAER---------YQALLKEKREyEGYELLK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 467 ERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRGPSLHHGRphlgsVPDFRFSVADGHVD--- 543
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEE-----QLRVKEKIGELEAEias 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 544 AYSTSAVLRRPQK---GRLAALRDEPSKVQ-TLNEQDWERAQQASVLANVAQAFESDvdvsdgEDDRDTLLSSVDLLSPS 619
Cdd:TIGR02169 306 LERSIAEKERELEdaeERLAKLEAEIDKLLaEIEELEREIEEERKRRDKLTEEYAEL------KEELEDLRAELEEVDKE 379
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 568952890 620 GQA------DAQTLAMMLQEQLDAINKEIRLIQEEKENTEQRAEEIE 660
Cdd:TIGR02169 380 FAEtrdelkDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN 426
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
260-491 |
6.44e-03 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 40.59 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 260 RQAREQSQMKERLASLSShaaeLEEDLdtARKDLIKseemntKLQREVREAMAQKEDMEERITTLEKRYLAAQREATS-- 337
Cdd:pfam15066 292 QENCKTPDTEQSFESLQP----LEEDM--ALNEVLQ------KLKHTNRKQQMQIQDLQCSNLYLEKKVKELQMKITKqq 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 338 -----VHDLNDKLENEIANKDSMHRQTEDKNRQLQ---ERLELAEQKLQQTLRKAETLpevEAELAQRVAALSKAEERHG 409
Cdd:pfam15066 360 vfvdiINKLKENVEELIEDKYNVILEKNDINKTLQnlqEILANTQKHLQESRKEKETL---QLELKKIKVNYVHLQERYI 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 410 N-IEERLR------QMEAQLEEKNQELQRARQrekMNEEHNKRLSDTVDKLLSESNERLQ--LHLKERMAALEDKNslLR 480
Cdd:pfam15066 437 TeMQQKNKsvsqclEMDKTLSKKEEEVERLQQ---LKGELEKATTSALDLLKREKETREQefLSLQEEFQKHEKEN--LE 511
|
250
....*....|.
gi 568952890 481 EVENAKKQLEE 491
Cdd:pfam15066 512 ERQKLKSRLEK 522
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
249-513 |
6.58e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.49 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 249 AKVLELQEVIDRQAREQSQM----KERLASLSSHAAELEEDLDTARKdliKSEEMNTKLQ----REVREAMAQKEDMEEr 320
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMelehKRARIELEKKASALKRQLDRESD---RNQELQKRIRllekREAEAEEALREQAEL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 321 iTTLEKRYLAAQREA--------TSVHDLNDKLENEIA-------NKDSMHRQTEDKNRQLQERLEL-------AEQKLQ 378
Cdd:pfam05557 78 -NRLKKKYLEALNKKlnekesqlADAREVISCLKNELSelrrqiqRAELELQSTNSELEELQERLDLlkakaseAEQLRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 379 QTLRKAETLPEVEA---ELAQRVAALSKAEERHGNIEERLrqmeAQLEEKNQELQRARqrekmneEHNKRLSDTVDK--L 453
Cdd:pfam05557 157 NLEKQQSSLAEAEQrikELEFEIQSQEQDSEIVKNSKSEL----ARIPELEKELERLR-------EHNKHLNENIENklL 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568952890 454 LSESNERLQLHL------KERMAALEDKNS-LLREVENAKKQLEETQHDkdqlVVTIEALKAELEQM 513
Cdd:pfam05557 226 LKEEVEDLKRKLereekyREEAATLELEKEkLEQELQSWVKLAQDTGLN----LRSPEDLSRRIEQL 288
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
280-396 |
8.67e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.04 E-value: 8.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 280 AELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQ---REATSVHDLNDklENEIANKDSMH 356
Cdd:COG1842 94 AELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKaqeKVNEALSGIDS--DDATSALERME 171
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 568952890 357 RQTEDKNRQLQERLELAEQK-LQQTLRKAETLPEVEAELAQ 396
Cdd:COG1842 172 EKIEEMEARAEAAAELAAGDsLDDELAELEADSEVEDELAA 212
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
296-511 |
9.35e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 9.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 296 SEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQ 375
Cdd:COG4372 1 GDRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 376 KLQQTlrkaetlpevEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTV---DK 452
Cdd:COG4372 81 ELEEL----------NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIaerEE 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568952890 453 LLSESNERLQlHLKERMAALEDKNSLLrEVENAKKQLEETQHDKDQLVVTIEALKAELE 511
Cdd:COG4372 151 ELKELEEQLE-SLQEELAALEQELQAL-SEAEAEQALDELLKEANRNAEKEEELAEAEK 207
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
44-403 |
9.81e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.44 E-value: 9.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 44 LEERDRLLDTLRETQETLaltQGKLHEVGHERDSLQRQLNT------ALPQEFAALTKELNVCREQLLEREEEIAELKAE 117
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRI---ENRLDELSQELSDASRKIGEiekeieQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 118 rnntrllLEHLECLVSRHERSLrmtvvkrqaqspAGVSSEVEVLKA--LKSLFEHHKALDEKVRERLRVALERCSLLEEE 195
Cdd:TIGR02169 760 -------LKELEARIEELEEDL------------HKLEEALNDLEArlSHSRIPEIQAELSKLEEEVSRIEARLREIEQK 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 196 LGATHKELMILKEQNNQKKTLTDGLLDgnheqesapstngKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASL 275
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRIDLKE-------------QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDL 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952890 276 SSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLnDKLENEIANKDSM 355
Cdd:TIGR02169 888 KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL-EDVQAELQRVEEE 966
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 568952890 356 HRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSK 403
Cdd:TIGR02169 967 IRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
|