|
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 ... |
996-1061 |
4.31e-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: 4.31e-43
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564332108 996 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLRRL 1061
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 ... |
909-979 |
8.93e-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: 8.93e-43
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564332108 909 FAQWDGPTVVVWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEIMSLT 979
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 ... |
1081-1152 |
8.37e-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: 147.08 E-value: 8.37e-42
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564332108 1081 DVLVWSNDRVIRWILSIGLKEFANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLL 1152
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 ... |
1000-1059 |
4.36e-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: 4.36e-29
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 1000 WIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLR 1059
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 ... |
916-974 |
1.28e-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: 1.28e-26
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 564332108 916 TVVVWLELWVGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 974
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 ... |
1089-1150 |
1.20e-23 |
|
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: 95.30 E-value: 1.20e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564332108 1089 RVIRWILSIGLKEFANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNN 1150
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 ... |
1081-1152 |
2.30e-21 |
|
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: 89.04 E-value: 2.30e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564332108 1081 DVLVWSNDRVIRWILSIGLKEFANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLL 1152
Cdd:cd09570 1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
246-545 |
3.63e-17 |
|
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: 87.42 E-value: 3.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 246 EDLAKVLELQ-EVIDRQAREQSQMKE--------RLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKED 316
Cdd:TIGR02168 192 EDILNELERQlKSLERQAEKAERYKElkaelrelELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 317 MEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQ 396
Cdd:TIGR02168 272 LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 397 RVAALSKSGplssgssAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVD 476
Cdd:TIGR02168 352 ELESLEAEL-------EELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIE 424
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564332108 477 KLLSESNE----RLQLHLKERMAALEDKNSLLREVENAKKQLEEtqhDKDQLVLNIEALKAELEQMRLRGSSL 545
Cdd:TIGR02168 425 ELLKKLEEaelkELQAELEELEEELEELQEELERLEEALEELRE---ELEEAEQALDAAERELAQLQARLDSL 494
|
|
| SAM_kazrin_repeat1 |
cd09564 |
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ... |
910-974 |
2.55e-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: 74.41 E-value: 2.55e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564332108 910 AQWDGPTVVVWLELWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 974
Cdd:cd09564 2 SRWKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
|
|
| SAM_liprin-beta1,2_repeat2 |
cd09566 |
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ... |
995-1059 |
2.99e-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: 2.99e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564332108 995 DMNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRNSFQCGIMCLR 1059
Cdd:cd09566 1 KLDTHWV-LRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDLL-HLKVTSALHHASIRRGIQVLR 63
|
|
| SAM_kazrin_repeat2 |
cd09567 |
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ... |
995-1059 |
3.13e-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: 3.13e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564332108 995 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLR 1059
Cdd:cd09567 1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
|
|
| SAM_liprin-beta1,2_repeat3 |
cd09569 |
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ... |
1081-1152 |
3.60e-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: 71.33 E-value: 3.60e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564332108 1081 DVLVWSNDRVIRWILSIGLKEFANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLL 1152
Cdd:cd09569 1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
236-541 |
1.97e-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: 78.57 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 236 KRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKE 315
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 316 DMEERITTLEKRYlaAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELA 395
Cdd:TIGR02169 776 KLEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE 853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 396 QRVAALSksgplssGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQL---EEKNQELQRARQREKMN-------- 464
Cdd:TIGR02169 854 KEIENLN-------GKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLrelERKIEELEAQIEKKRKRlselkakl 926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 465 ---EEHNKRLSDTVDKLLSESNERLQLH-LKERMAALEDKNSLLREVEN-AKKQLEETQHDKDQLVLNIEALKAELEQMR 539
Cdd:TIGR02169 927 ealEEELSEIEDPKGEDEEIPEEELSLEdVQAELQRVEEEIRALEPVNMlAIQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
..
gi 564332108 540 LR 541
Cdd:TIGR02169 1007 ER 1008
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
244-541 |
4.87e-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: 4.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 244 SHEDLAKVLE-LQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERIT 322
Cdd:TIGR02168 706 ELEELEEELEqLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 323 TLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALS 402
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE 865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 403 KSGPLSSGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSES 482
Cdd:TIGR02168 866 ELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 483 NERLQLHLkerMAALEDKNSLLREVENAKKQLEETQHDKDQL-VLNIEALkAELEQMRLR 541
Cdd:TIGR02168 946 SEEYSLTL---EEAEALENKIEDDEEEARRRLKRLENKIKELgPVNLAAI-EEYEELKER 1001
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
155-687 |
5.44e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.82 E-value: 5.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 155 SSEVEVLKALKSL--FEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNSQKKALTEGMLDGNHEQENAps 232
Cdd:COG1196 219 KEELKELEAELLLlkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE-- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 233 tngKRSSDGSLSHEdLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMA 312
Cdd:COG1196 297 ---LARLEQDIARL-EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 313 QKEDMEERITTLEKRYLAAQREATsvhdlndKLENEIANKdsmhRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEA 392
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAA-------ELAAQLEEL----EEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 393 ELAQrvaalsksgplssgssaAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLS 472
Cdd:COG1196 442 EALE-----------------EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 473 DtvdkllsESNERLQLHLKERMAALEDKNSLLREVENAKKQLEET------QHDKDQLVLNIEALKAELEQMRLRGSSLH 546
Cdd:COG1196 505 G-------FLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAalaaalQNIVVEDDEVAAAAIEYLKAAKAGRATFL 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 547 HGRPHLGSVPDFRFSVADGHVDAYSTSAVLRRPQKGRLAALRDEpSKVQTLNEQDWERAQQASVLANVAQAFES---DVD 623
Cdd:COG1196 578 PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDT-LLGRTLVAARLEAALRRAVTLAGRLREVTlegEGG 656
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564332108 624 VSDGEDDRDTLLSSVDLLSPSGQADAQTLAMMLQEQLDAINKEIRLIQEEKENTEQRAEEIESR 687
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEE 720
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
995-1059 |
5.86e-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: 64.60 E-value: 5.86e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564332108 995 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRNSFQCGIMCLR 1059
Cdd:pfam00536 1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
304-541 |
8.60e-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: 73.17 E-value: 8.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 304 QREVREAMAQKEDMEERITTLEKrylaaqrEATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRK 383
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEK-------ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 384 AETLPEVEAELAQRVAALSKSGPLSSGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKM 463
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 464 NEEHNKRLSDTVDKL------------------------LSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQH 519
Cdd:TIGR02168 829 LERRIAATERRLEDLeeqieelsedieslaaeieeleelIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
250 260
....*....|....*....|..
gi 564332108 520 DKDQLVLNIEALKAELEQMRLR 541
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELR 930
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
253-537 |
2.30e-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: 72.01 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 253 ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQ 332
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 333 REATSVHDLNDKLENEIAnkdsmhrQTEDKNRQLQERLELAEQKLQQTlrkAETLPEVEAELAQrvaalsksgplSSGSS 412
Cdd:TIGR02168 761 AEIEELEERLEEAEEELA-------EAEAEIEELEAQIEQLKEELKAL---REALDELRAELTL-----------LNEEA 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 413 AAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRAR-QREKMNEEHNKrlsdtVDKLLSESNERLQLHLK 491
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEeLIEELESELEA-----LLNERASLEEALALLRS 894
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 564332108 492 ERMAALEDKNSLLREVENAKKQLEETQHDKDQLVLNIEALKAELEQ 537
Cdd:TIGR02168 895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
192-489 |
3.98e-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: 71.24 E-value: 3.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 192 LEEELGATHKELMI--LKEQNSQKKALTEGMLDGNHEQENApsTNGKRSSDGSLS------HEDLAKVLELQEVIDRQAR 263
Cdd:TIGR02168 218 LKAELRELELALLVlrLEELREELEELQEELKEAEEELEEL--TAELQELEEKLEelrlevSELEEEIEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 264 EQSQM-------KERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREAT 336
Cdd:TIGR02168 296 EISRLeqqkqilRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 337 SVHDLNDKLENEIAnkdsmhrQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSgpLSSGSSAAKE 416
Cdd:TIGR02168 376 ELEEQLETLRSKVA-------QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK--ELQAELEELE 446
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564332108 417 AKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLH 489
Cdd:TIGR02168 447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
74-487 |
2.68e-11 |
|
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: 68.54 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 74 ERDSLQRQLNtALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLLLEHLECLVSRHERSLRmTVVKRQAQSPAG 153
Cdd:TIGR02168 678 EIEELEEKIE-ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE-QLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 154 VSS----EVEVLKALKSLFEHHKALDEK---VRERLRVALERCSLLEEELGATHKELMILKEqNSQKKALTEGMLDGNHE 226
Cdd:TIGR02168 756 LTEleaeIEELEERLEEAEEELAEAEAEieeLEAQIEQLKEELKALREALDELRAELTLLNE-EAANLRERLESLERRIA 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 227 qenapstngkrssdgslshedlakvlELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQRE 306
Cdd:TIGR02168 835 --------------------------ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 307 VREAMAQKEDMEERITTLEKRYLAAQREAtsvHDLNDKLEneiankdsmhrqtedknrQLQERLELAEQKLQQTLRKAET 386
Cdd:TIGR02168 889 LALLRSELEELSEELRELESKRSELRREL---EELREKLA------------------QLELRLEGLEVRIDNLQERLSE 947
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 387 LPEVEAELAQRVAALSKSgplssgSSAAKEAKLLELTSKLRK-------AEERHGNIEERLRQMEAQLEeknqELQRARQ 459
Cdd:TIGR02168 948 EYSLTLEEAEALENKIED------DEEEARRRLKRLENKIKElgpvnlaAIEEYEELKERYDFLTAQKE----DLTEAKE 1017
|
410 420 430
....*....|....*....|....*....|...
gi 564332108 460 R-----EKMNEEHNKRLSDTVDKLlsesNERLQ 487
Cdd:TIGR02168 1018 TleeaiEEIDREARERFKDTFDQV----NENFQ 1046
|
|
| SAM_liprin-beta1,2_repeat1 |
cd09563 |
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
909-973 |
3.79e-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: 59.55 E-value: 3.79e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564332108 909 FAQWDGPTVVVWL-ELWVGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQ 973
Cdd:cd09563 1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
54-401 |
3.79e-11 |
|
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: 67.77 E-value: 3.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 54 LRETQETLALTQGKLHEVGHERDSLQRQLNTAlpQEFAALTKELNvcREQLLEREEEIAELKAERNNTRLLLEHLECLVS 133
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKSLERQAEKA--ERYKELKAELR--ELELALLVLRLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 134 RHERSlrmtvvkrqaqspagvssevevLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNSQk 213
Cdd:TIGR02168 257 ELTAE----------------------LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 214 kaltegmLDGNHEQENAPSTNGKRSSDgsLSHEDLA----KVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTA 289
Cdd:TIGR02168 314 -------LERQLEELEAQLEELESKLD--ELAEELAeleeKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 290 RKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHdlNDKLENEIANKDSMHRQTEDKNRQLQER 369
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEA 462
|
330 340 350
....*....|....*....|....*....|..
gi 564332108 370 LELAEQKLQQTLRKAETLPEVEAELAQRVAAL 401
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQARLDSL 494
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
304-544 |
4.38e-11 |
|
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: 66.33 E-value: 4.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 304 QREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRK 383
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 384 AETLpevEAELAQRVAALSKSGP------LSSGSSAAKEAKLLELTSKLrkAEERHGNIEErLRQMEAQLEEKNQELQRA 457
Cdd:COG4942 99 LEAQ---KEELAELLRALYRLGRqpplalLLSPEDFLDAVRRLQYLKYL--APARREQAEE-LRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 458 RQREKMNEEHNKRLSDTVDKLLSESNERLQlhlkermaaledknSLLREVENAKKQLEETQHDKDQLVLNIEALKAELEQ 537
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLA--------------RLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
....*..
gi 564332108 538 MRLRGSS 544
Cdd:COG4942 239 AAERTPA 245
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
158-524 |
1.16e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.22 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 158 VEVLKALKSLFEHHkaldEKVRERLRVALERCSLLEEELGATHKELMILKEQNSQKKALTEGMLDGNHEQENAPSTNGKR 237
Cdd:PRK02224 233 RETRDEADEVLEEH----EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDAD 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 238 SSDGSLSHEDLAKVL-ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKED 316
Cdd:PRK02224 309 AEAVEARREELEDRDeELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 317 MEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQ--------QTLRK---AE 385
Cdd:PRK02224 389 LEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEagkcpecgQPVEGsphVE 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 386 TLPEVE---AELAQRVAAL-SKSGPLSSGSSAAKEAKllELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRAR--- 458
Cdd:PRK02224 469 TIEEDRervEELEAELEDLeEEVEEVEERLERAEDLV--EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRera 546
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564332108 459 ---------QREKMNEEHNKrlSDTVDKLLSESNERLQlHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQL 524
Cdd:PRK02224 547 aeleaeaeeKREAAAEAEEE--AEEAREEVAELNSKLA-ELKERIESLERIRTLLAAIADAEDEIERLREKREAL 618
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
169-539 |
1.19e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.32 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 169 EHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNSQKKALTEGMLDGNHEQENA-----PSTNGKRSSDGSL 243
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAdelkkAAAAKKKADEAKK 1425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 244 SHEDLAKVLELQ---------EVIDRQAREQSQMKE--RLASLSSHAAELEEDLDTARK--DLIKSEEMNTKLQREVREA 310
Cdd:PTZ00121 1426 KAEEKKKADEAKkkaeeakkaDEAKKKAEEAKKAEEakKKAEEAKKADEAKKKAEEAKKadEAKKKAEEAKKKADEAKKA 1505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 311 MAQKEDMEERITTLEKRYLAAQREATSVHDLND-KLENEIANKDSMHRQTEDKNRQLQERLE---LAEQKLQQTLRKAET 386
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEaKKAEEKKKADELKKAEELKKAEEKKKAEeakKAEEDKNMALRKAEE 1585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 387 LPEVEAELAQRVAALSKSGPLSSGSSAAKEAKLLELTSKLRKAEERHGNIEErLRQMEAQLEEKNQELQRARQREKMNEE 466
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQ-LKKKEAEEKKKAEELKKAEEENKIKAA 1664
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564332108 467 HNKRLSDTvDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVLNIEALKAELEQMR 539
Cdd:PTZ00121 1665 EEAKKAEE-DKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAK 1736
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
248-533 |
3.97e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 64.59 E-value: 3.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 248 LAKVLE---LQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEmntklqrEVREAMAQKEDMEERITTL 324
Cdd:PRK04863 337 LNLVQTalrQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEE-------EVDELKSQLADYQQALDVQ 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 325 EKR---YLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKlqqtLRKAETLPEVEAELAQRVAAL 401
Cdd:PRK04863 410 QTRaiqYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQK----LSVAQAAHSQFEQAYQLVRKI 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 402 SKSGPLSSGSSAAKEAklleltskLRKAEErHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDkllse 481
Cdd:PRK04863 486 AGEVSRSEAWDVAREL--------LRRLRE-QRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLD----- 551
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 564332108 482 SNERLQLHLKERMAALEDKNSllrEVENAKKQLEETQHDKDQLVLNIEALKA 533
Cdd:PRK04863 552 DEDELEQLQEELEARLESLSE---SVSEARERRMALRQQLEQLQARIQRLAA 600
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
152-536 |
6.28e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.54 E-value: 6.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 152 AGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNS-----QKKALTEGMLDGNHE 226
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKelkelKEKAEEYIKLSEFYE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 227 QENAPSTNGKrssdgslshEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQR- 305
Cdd:PRK03918 304 EYLDELREIE---------KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEl 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 306 ---EVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIAN-KDSMHRQTEDK------NRQLQE--RLELA 373
Cdd:PRK03918 375 erlKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKElKKAIEELKKAKgkcpvcGRELTEehRKELL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 374 EQ------KLQQTLRKA-ETLPEVEAELAQRVAALSKSGPLSSGSSAAKEAKLLE------LTSKLRKAEERHGNIEERL 440
Cdd:PRK03918 455 EEytaelkRIEKELKEIeEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEeklkkyNLEELEKKAEEYEKLKEKL 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 441 RQMEAQLEEKNQELQRARQREKMNEEHNKRLsDTVDKLLSESNERLQL-------HLKERMAALEDKNSLLREVENAKKQ 513
Cdd:PRK03918 535 IKLKGEIKSLKKELEKLEELKKKLAELEKKL-DELEEELAELLKELEElgfesveELEERLKELEPFYNEYLELKDAEKE 613
|
410 420
....*....|....*....|...
gi 564332108 514 LEETQHDKDQLVLNIEALKAELE 536
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELA 636
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
284-545 |
6.83e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.54 E-value: 6.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 284 EDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTED-- 361
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElk 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 362 --------KNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSGPLSSGSSAAKEAKLlELTSKLRKAEERH 433
Cdd:PRK03918 238 eeieelekELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYE-EYLDELREIEKRL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 434 GNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDtvdklLSESNERLQ--LHLKERMAALEDKNSLLrEVENAK 511
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEE-----LEERHELYEeaKAKKEELERLKKRLTGL-TPEKLE 390
|
250 260 270
....*....|....*....|....*....|....
gi 564332108 512 KQLEETQHDKDQLVLNIEALKAELEQMRLRGSSL 545
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKEL 424
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
246-536 |
7.33e-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: 7.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 246 EDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNtKLQREVREA-----MAQKEDMEER 320
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQ-ALLKEKREYegyelLKEKEALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 321 ITTLEKRYLAAQREATSVHDLNDKLENEIAnkdsmhrQTEDKNRQLQERLELAEQKLQQTLRkaETLPEVEAELAQRVAA 400
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLE-------EIEQLLEELNKKIKDLGEEEQLRVK--EKIGELEAEIASLERS 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 401 LsksgplssgssAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKnqelqrARQREKMNEEHnKRLSDTVDKLLS 480
Cdd:TIGR02169 310 I-----------AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEE------RKRRDKLTEEY-AELKEELEDLRA 371
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564332108 481 E------SNERLQLHLKERMAALED----KNSLLREVE---NAKKQLEETQHDKDQLVLNIEALKAELE 536
Cdd:TIGR02169 372 EleevdkEFAETRDELKDYREKLEKlkreINELKRELDrlqEELQRLSEELADLNAAIAGIEAKINELE 440
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
175-536 |
8.74e-10 |
|
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: 63.21 E-value: 8.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 175 DEKVRERLRVALERcSLLEEELGATHKELMiLKEQNSQKKALTEGMLdgnheqenapstngkrSSDGSLsHEDLAKVLEL 254
Cdd:pfam15921 136 ESQSQEDLRNQLQN-TVHELEAAKCLKEDM-LEDSNTQIEQLRKMML----------------SHEGVL-QEIRSILVDF 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 255 QEVIDRQAREQSQMKE-RLASLSSHAAELEEDLDTARKDLI--------KSEEMNTKLQREVREAMAQKEDMEER----- 320
Cdd:pfam15921 197 EEASGKKIYEHDSMSTmHFRSLGSAISKILRELDTEISYLKgrifpvedQLEALKSESQNKIELLLQQHQDRIEQliseh 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 321 ---ITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRqtedknRQLQErLELAEQKLQQTLRKAETLPEVEAELAQR 397
Cdd:pfam15921 277 eveITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYM------RQLSD-LESTVSQLRSELREAKRMYEDKIEELEK 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 398 VAALSKSgplssgssaakeaKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQrarqrekMNEEHNKRLSD---- 473
Cdd:pfam15921 350 QLVLANS-------------ELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELS-------LEKEQNKRLWDrdtg 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 474 ---TVDKLLSESNER-----------------LQLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVLNIEALKA 533
Cdd:pfam15921 410 nsiTIDHLRRELDDRnmevqrleallkamkseCQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKM 489
|
...
gi 564332108 534 ELE 536
Cdd:pfam15921 490 TLE 492
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
245-449 |
1.31e-09 |
|
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: 59.94 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 245 HEDLAKVLELQEvIDRQAReqsQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTL 324
Cdd:COG1579 3 PEDLRALLDLQE-LDSELD---RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 325 EKRylaaQREATSVHDLNDkLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQqtlrkaetlpEVEAELAQRVAALsks 404
Cdd:COG1579 79 EEQ----LGNVRNNKEYEA-LQKEIESLKRRISDLEDEILELMERIEELEEELA----------ELEAELAELEAEL--- 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 564332108 405 gplssgssAAKEAKLLELTSKLRKAEERhgnIEERLRQMEAQLEE 449
Cdd:COG1579 141 --------EEKKAELDEELAELEAELEE---LEAEREELAAKIPP 174
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
255-485 |
2.73e-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: 60.55 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 255 QEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQRE 334
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 335 AtsvhdlnDKLENEIANkdsMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSGPLSSGSSAA 414
Cdd:COG4942 99 L-------EAQKEELAE---LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564332108 415 KEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNER 485
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
45-538 |
3.44e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 3.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNtALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLL 124
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRR-ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 125 LEHLECLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELM 204
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 205 ILKEQNSQKKALTEGMLDGNHEQEnapstngKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEE 284
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEE-------EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 285 DLDTARKDLIKS----------------EEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENE 348
Cdd:COG1196 506 FLEGVKAALLLAglrglagavavligveAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRAR 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 349 IANKDSMHRQTEDKNR----QLQERLELAEQKLQQTL-------RKAETLPEVEAELAQRVAALSKSGPLSSGSSAAKEA 417
Cdd:COG1196 586 AALAAALARGAIGAAVdlvaSDLREADARYYVLGDTLlgrtlvaARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 418 KLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAAL 497
Cdd:COG1196 666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 564332108 498 EDKNSLLREVENAKKQLEETQHDkdqlvlnIEALKAELEQM 538
Cdd:COG1196 746 ELLEEEALEELPEPPDLEELERE-------LERLEREIEAL 779
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
31-533 |
6.79e-09 |
|
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: 60.52 E-value: 6.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 31 DADSHFEQLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQ---LNTALPQEFAAL---TKELNVCREQL 104
Cdd:pfam15921 321 DLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQEsgnLDDQLQKLLADLhkrEKELSLEKEQN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 105 LE-------REEEIAELKAERNNTRLLLEHLECLVsRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEK 177
Cdd:pfam15921 401 KRlwdrdtgNSITIDHLRRELDDRNMEVQRLEALL-KAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRK 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 178 VRERL---RVALER---------CSLLEEE--LGATHKELMILKEQNSQK-KALTEGMLDGNHEQENAPSTNGKRssdgs 242
Cdd:pfam15921 480 VVEELtakKMTLESsertvsdltASLQEKEraIEATNAEITKLRSRVDLKlQELQHLKNEGDHLRNVQTECEALK----- 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 243 LSHEDLAKVLE-LQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEeri 321
Cdd:pfam15921 555 LQMAEKDKVIEiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLE--- 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 322 ttLEKRYL--AAQREATSVHDLN---DKLENEIAN-KDSMHRQTEDKN------RQLQERLELAEQKLQQTLRKAET-LP 388
Cdd:pfam15921 632 --LEKVKLvnAGSERLRAVKDIKqerDQLLNEVKTsRNELNSLSEDYEvlkrnfRNKSEEMETTTNKLKMQLKSAQSeLE 709
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 389 EVEAELAQRVAALSKSGPLSSGSS---AAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQR-ARQREKMN 464
Cdd:pfam15921 710 QTRNTLKSMEGSDGHAMKVAMGMQkqiTAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTvATEKNKMA 789
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564332108 465 EEHNkrlsdtvdklLSESNERlqlHLKERMAALE---DKNSL-LREVEN-AKKQLEETQHDKDQLVLNIEALKA 533
Cdd:pfam15921 790 GELE----------VLRSQER---RLKEKVANMEvalDKASLqFAECQDiIQRQEQESVRLKLQHTLDVKELQG 850
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
202-679 |
1.30e-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: 59.36 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 202 ELMILKEQNSQKKALTEGMLDGNHEQENAPSTngkRSSDGSLSHEdlakvlelQEVIDRQAREQSQMKER-LASLSSHAA 280
Cdd:pfam15921 259 ELLLQQHQDRIEQLISEHEVEITGLTEKASSA---RSQANSIQSQ--------LEIIQEQARNQNSMYMRqLSDLESTVS 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 281 ELEEDLDTARKDL-IKSEEMNTKL---QREVREAMAQKEDMEERITTLE---KRYLA----AQREATSVHDLNDKL-ENE 348
Cdd:pfam15921 328 QLRSELREAKRMYeDKIEELEKQLvlaNSELTEARTERDQFSQESGNLDdqlQKLLAdlhkREKELSLEKEQNKRLwDRD 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 349 IANK---DSMHRQTEDKNRQLQeRLELAEQKLqqtlrKAETLPEVEAELAQ---RVAALSKSGPLSSGSSAAKEA--KLL 420
Cdd:pfam15921 408 TGNSitiDHLRRELDDRNMEVQ-RLEALLKAM-----KSECQGQMERQMAAiqgKNESLEKVSSLTAQLESTKEMlrKVV 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 421 E-LTSK---LRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNE----RLQLHLKE 492
Cdd:pfam15921 482 EeLTAKkmtLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTEcealKLQMAEKD 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 493 RM-----------------------AALEDKNSLLREVENAKKQLEETQHDKDQLVLNIEALKAELEQMRLRGSSL-HHG 548
Cdd:pfam15921 562 KVieilrqqienmtqlvgqhgrtagAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLvNAG 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 549 RPHLGSVPDFR-------FSVADGHVDAYSTS---AVLRRpqkgrlaALRDEPSKVQ-TLNEQDWERAQQASVLANVAQA 617
Cdd:pfam15921 642 SERLRAVKDIKqerdqllNEVKTSRNELNSLSedyEVLKR-------NFRNKSEEMEtTTNKLKMQLKSAQSELEQTRNT 714
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564332108 618 FESdVDVSDGEDDRDTLLSSVDLLSPSGQADA-QTLAMMLQEQLDAINKEIRLIQEEKENTEQ 679
Cdd:pfam15921 715 LKS-MEGSDGHAMKVAMGMQKQITAKRGQIDAlQSKIQFLEEAMTNANKEKHFLKEEKNKLSQ 776
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
265-537 |
3.15e-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: 58.16 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 265 QSQMKERLASLSSHAAELEEDLDTARKDLikseemnTKLQREVREAMAQKEDMEERITTLEKRYLAAQREatsvhdlndk 344
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLQSEL-------RRIENRLDELSQELSDASRKIGEIEKEIEQLEQE---------- 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 345 leneiankdsmHRQTEDKNRQLQERLELAEQKLQQtlrKAETLPEVEAELAQRVAALSK-SGPLSSGSSAAKEAKLLELT 423
Cdd:TIGR02169 732 -----------EEKLKERLEELEEDLSSLEQEIEN---VKSELKELEARIEELEEDLHKlEEALNDLEARLSHSRIPEIQ 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 424 SKLRKAEERHGNIEERLRQMEAQLEEKNQELQRArqREKMNEEHNKRLS-----DTVDKLLSESN---ERLQLHLKERMA 495
Cdd:TIGR02169 798 AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL--EKEIQELQEQRIDlkeqiKSIEKEIENLNgkkEELEEELEELEA 875
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 564332108 496 ALED----KNSLLREVENAKKQLEETQHDKDQLVLNIEALKAELEQ 537
Cdd:TIGR02169 876 ALRDlesrLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
144-523 |
4.23e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 144 VKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVR--ERLRVALERCSLLEEelgATHKELMILKEQNSQKKALTEGML 221
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKkaDEAKKKAEEAKKADE---AKKKAEEAKKAEEAKKKAEEAKKA 1472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 222 D---GNHEQENAPSTNGKRSSDGSLSHEDLAKVLELQEVID--RQAREQSQMKE-RLASLSSHAAELEEDLDTARKD-LI 294
Cdd:PTZ00121 1473 DeakKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADeaKKAEEAKKADEaKKAEEAKKADEAKKAEEKKKADeLK 1552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 295 KSEEMntKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTED---------KNRQ 365
Cdd:PTZ00121 1553 KAEEL--KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikaeelkKAEE 1630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 366 LQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSgplssgssaAKEAKlleltsklRKAEERHgNIEERLRQMEA 445
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK---------AEEDK--------KKAEEAK-KAEEDEKKAAE 1692
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564332108 446 QLEEKNQELQRARQREKMNEEHNKRLsdtvdkllsesnERLQLHLKERMAALEDknsLLREVENAKKQLEETQHDKDQ 523
Cdd:PTZ00121 1693 ALKKEAEEAKKAEELKKKEAEEKKKA------------EELKKAEEENKIKAEE---AKKEAEEDKKKAEEAKKDEEE 1755
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
246-460 |
4.78e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 4.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 246 EDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLdtarkdlikseemntkLQREVREAMAQKEDMEERITTLE 325
Cdd:COG4913 252 ELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL----------------LEAELEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 326 KRYLAAQREATSVHdlNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQkLQQTLRKAE-TLPEVEAELAQRVAALsks 404
Cdd:COG4913 316 ARLDALREELDELE--AQIRGNGGDRLEQLEREIERLERELEERERRRAR-LEALLAALGlPLPASAEEFAALRAEA--- 389
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 564332108 405 gplssgssaakEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQR 460
Cdd:COG4913 390 -----------AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
264-461 |
6.63e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 6.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 264 EQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLND 343
Cdd:TIGR02169 288 EQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 344 KLENEIANKDSMHRQTEDKNRQLQERLELA----------EQKLQQTLRKA---------------ETLPEVEAELAQRV 398
Cdd:TIGR02169 368 DLRAELEEVDKEFAETRDELKDYREKLEKLkreinelkreLDRLQEELQRLseeladlnaaiagieAKINELEEEKEDKA 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564332108 399 AALSKS-GPLSSGSS--AAKEAKLLELTSKLRKaeerhgnIEERLRQMEAQLEEKNQELQRARQRE 461
Cdd:TIGR02169 448 LEIKKQeWKLEQLAAdlSKYEQELYDLKEEYDR-------VEKELSKLQRELAEAEAQARASEERV 506
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
44-538 |
6.63e-08 |
|
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: 57.29 E-value: 6.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 44 LEERDRLLDTLR-ETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTR 122
Cdd:TIGR00618 417 SAFRDLQGQLAHaKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARL 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 123 LLLEHLECLVSRHERSLRMTVVkrQAQSPAGVSSEVEvlkALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKE 202
Cdd:TIGR00618 497 LELQEEPCPLCGSCIHPNPARQ--DIDNPGPLTRRMQ---RGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQS 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 203 LMILKEQNSQKKALTEGMLdgNHEQENAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQ--AREQSQMKERLASLSSHAA 280
Cdd:TIGR00618 572 FSILTQCDNRSKEDIPNLQ--NITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQdvRLHLQQCSQELALKLTALH 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 281 ELEEDLdtarkdlikseemntkLQREVREAMAQKEDMEERitTLEKRYLAAQREATSVHDLNDKLEnEIANKDSMHR--- 357
Cdd:TIGR00618 650 ALQLTL----------------TQERVREHALSIRVLPKE--LLASRQLALQKMQSEKEQLTYWKE-MLAQCQTLLRele 710
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 358 QTEDKNRQLQERLELAEQKLQQTLR-KAETLPEVEAEL-AQRVAALSKSgplssgsSAAKEAKLLELTSKLRKAEErhgn 435
Cdd:TIGR00618 711 THIEEYDREFNEIENASSSLGSDLAaREDALNQSLKELmHQARTVLKAR-------TEAHFNNNEEVTAALQTGAE---- 779
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 436 ieerLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLE 515
Cdd:TIGR00618 780 ----LSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYE 855
|
490 500
....*....|....*....|...
gi 564332108 516 ETQHDKDQLVLNIEALKAELEQM 538
Cdd:TIGR00618 856 ECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
302-518 |
6.92e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.38 E-value: 6.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 302 KLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIAnkdsmhrqtedknrQLQERLELAEQKLQQTl 381
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID--------------KLQAEIAEAEAEIEER- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 382 rkaetlpevEAELAQRVAALSKSGPLSSGSSAAKEAK----LLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRA 457
Cdd:COG3883 85 ---------REELGERARALYRSGGSVSYLDVLLGSEsfsdFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564332108 458 RQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQ 518
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
252-533 |
7.23e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.27 E-value: 7.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 252 LELQEVIDRQAREQ-SQMKERLASLSSHAAELeedldtarkDLIKSEEmntkLQREVREAMAQKEDMEErittlEKRYLA 330
Cdd:PRK04863 853 LADHESQEQQQRSQlEQAKEGLSALNRLLPRL---------NLLADET----LADRVEEIREQLDEAEE-----AKRFVQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 331 AQREATSvhdlndKLENEIankdSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLpeveAELAQRVAALSKSgplSSG 410
Cdd:PRK04863 915 QHGNALA------QLEPIV----SVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFAL----TEVVQRRAHFSYE---DAA 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 411 SSAAKEAKLLE-LTSKLRKAEERHGNIEERLRQMEAQLEEKNQ---ELQRARQR-EKMNEEHNKRLSDTVDKLLSESNER 485
Cdd:PRK04863 978 EMLAKNSDLNEkLRQRLEQAEQERTRAREQLRQAQAQLAQYNQvlaSLKSSYDAkRQMLQELKQELQDLGVPADSGAEER 1057
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 564332108 486 LQLHLKERMAAL----EDKNSLLR-------EVENAKKQLEETQHDKDQLVLNIEALKA 533
Cdd:PRK04863 1058 ARARRDELHARLsanrSRRNQLEKqltfceaEMDNLTKKLRKLERDYHEMREQVVNAKA 1116
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
280-474 |
9.29e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 9.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 280 AELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKED-------MEERITTLEKRYLAAQREATSVHDLNDKLENEIANK 352
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEkeeeyaeLQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 353 DSMHRQTEDKNR--QLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKsgpLSSGSSAAKEAKLLELTSKLRKAE 430
Cdd:COG4717 129 PLYQELEALEAElaELPERLEELEERLEELRELEEELEELEAELAELQEELEE---LLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 564332108 431 ERHGNIEERLRQMEAQLEEKNQELQRArQREKMNEEHNKRLSDT 474
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQL-ENELEAAALEERLKEA 248
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
249-540 |
9.89e-08 |
|
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: 55.84 E-value: 9.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 249 AKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRY 328
Cdd:pfam19220 48 SRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 329 LAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSGPLS 408
Cdd:pfam19220 128 AAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDAT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 409 SGSSAAKEAKLLELTSKLRKAEERHGNIEERLRqmeaqleeknqeLQRARQREKMnEEHNKRLSDTvDKLLSESNErlql 488
Cdd:pfam19220 208 RARLRALEGQLAAEQAERERAEAQLEEAVEAHR------------AERASLRMKL-EALTARAAAT-EQLLAEARN---- 269
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 564332108 489 HLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVLNIEALKAELEQMRL 540
Cdd:pfam19220 270 QLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARA 321
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
253-466 |
1.30e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.22 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 253 ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAmaqKEDMEERITTLEKRYLAAQ 332
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA---EAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 333 R------------EATSVHDLNDKLENeianKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAA 400
Cdd:COG3883 97 RsggsvsyldvllGSESFSDFLDRLSA----LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564332108 401 LsksgplssgssaakEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEE 466
Cdd:COG3883 173 L--------------EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
177-554 |
1.62e-07 |
|
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: 56.21 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 177 KVRERLRVALERCSLLEEELGATHKELMILKEQNSQ------KKALTEGMLDGNHEQENAPST----------------N 234
Cdd:TIGR00606 475 ELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKadldrkLRKLDQEMEQLNHHTTTRTQMemltkdkmdkdeqirkI 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 235 GKRSSDGSLSH-EDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQ 313
Cdd:TIGR00606 555 KSRHSDELTSLlGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 314 kEDMEERITTLEKRYLAAQRE---ATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAET-LPE 389
Cdd:TIGR00606 635 -QDEESDLERLKEEIEKSSKQramLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDkLKS 713
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 390 VEAELAQrvaalsksgplssgssaaKEAKLLELtskLRKAEERHGNIEERLRQMEaQLEEKNQELQRARQREKMNEEHNK 469
Cdd:TIGR00606 714 TESELKK------------------KEKRRDEM---LGLAPGRQSIIDLKEKEIP-ELRNKLQKVNRDIQRLKNDIEEQE 771
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 470 RLSDTVDKLLSESN---------ERLQLHLKE------RMAALEDKNSLLREVENAKKQLEETQHDKDQLVLNIEALKAE 534
Cdd:TIGR00606 772 TLLGTIMPEEESAKvcltdvtimERFQMELKDverkiaQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKL 851
|
410 420
....*....|....*....|
gi 564332108 535 LEQMRLRGSSLHHGRPHLGS 554
Cdd:TIGR00606 852 IQDQQEQIQHLKSKTNELKS 871
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
45-537 |
1.67e-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: 55.80 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTaLPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLL 124
Cdd:TIGR04523 124 VELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYND-LKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 125 LEHLECLVSRHeRSLRMTVVKRQAQSpagvSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKEL- 203
Cdd:TIGR04523 203 LSNLKKKIQKN-KSLESQISELKKQN----NQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELe 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 204 ---MILKEQNSQKKALTEGMLDGNHEQEnapstngkrssdgslshEDLAKvlELQEVIDRQAREQSQMKERLASLSSHAA 280
Cdd:TIGR04523 278 qnnKKIKELEKQLNQLKSEISDLNNQKE-----------------QDWNK--ELKSELKNQEKKLEEIQNQISQNNKIIS 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 281 ELEEDLDTARKDLIKSEEMNTKLQREVREamaqKEDMEERIttlekrylaaQREATSVHDLNDKLENEIANKDSMHRQTE 360
Cdd:TIGR04523 339 QLNEQISQLKKELTNSESENSEKQRELEE----KQNEIEKL----------KKENQSYKQEIKNLESQINDLESKIQNQE 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 361 DKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKsgplssgSSAAKEAKLLELTS-------KLRKAEERH 433
Cdd:TIGR04523 405 KLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTN-------QDSVKELIIKNLDNtresletQLKVLSRSI 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 434 GNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLsESNERLQLHLKERMAALEDKNSLLREV------ 507
Cdd:TIGR04523 478 NKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLK-EKIEKLESEKKEKESKISDLEDELNKDdfelkk 556
|
490 500 510
....*....|....*....|....*....|
gi 564332108 508 ENAKKQLEETQHDKDQLVLNIEALKAELEQ 537
Cdd:TIGR04523 557 ENLEKEIDEKNKEIEELKQTQKSLKKKQEE 586
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
38-520 |
1.86e-07 |
|
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: 55.61 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 38 QLMVSMLEERDR--LLDTLRETQETLALTQGKLHE--VGHERDSLQRQ-----LNTALPQEFAALTKELNvcreqlLERE 108
Cdd:pfam12128 231 QAIAGIMKIRPEftKLQQEFNTLESAELRLSHLHFgyKSDETLIASRQeerqeTSAELNQLLRTLDDQWK------EKRD 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 109 EEIAELKAERNNTRLLLEHLECLVSRHERSLRMTVVKR---QAQSPAgVSSEVEVL-KALKSLFEHHKALDEKVRERLRV 184
Cdd:pfam12128 305 ELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAaadQEQLPS-WQSELENLeERLKALTGKHQDVTAKYNRRRSK 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 185 ALERCSlleEELGATHKELMILKEQNSQKKALTEGMLDGnheQENApstngkrssdgsLSHEDLAKVLELQEVIDRQARE 264
Cdd:pfam12128 384 IKEQNN---RDIAGIKDKLAKIREARDRQLAVAEDDLQA---LESE------------LREQLEAGKLEFNEEEYRLKSR 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 265 QSQMKERLASLSSHAAELE------EDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSV 338
Cdd:pfam12128 446 LGELKLRLNQATATPELLLqlenfdERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDEL 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 339 --------HDLNDKLENEIAN-KDSMHRQTedkNRQLQERLELAEQKLQQTLRKAETLPEVEAELaQRVAAlsksgPLSS 409
Cdd:pfam12128 526 elqlfpqaGTLLHFLRKEAPDwEQSIGKVI---SPELLHRTDLDPEVWDGSVGGELNLYGVKLDL-KRIDV-----PEWA 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 410 GSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDtvdkllSESNERLQLH 489
Cdd:pfam12128 597 ASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFD------EKQSEKDKKN 670
|
490 500 510
....*....|....*....|....*....|.
gi 564332108 490 lKERMAALEDKNSLLREVENAKKQLEETQHD 520
Cdd:pfam12128 671 -KALAERKDSANERLNSLEAQLKQLDKKHQA 700
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
157-539 |
2.06e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 157 EVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNSQKKALTE---------GMLDGNHEQ 227
Cdd:PRK03918 284 ELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKklkelekrlEELEERHEL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 228 -ENAPST----NGKRSSDGSLSHEDLAKVLELQEVIDRQAREQ-SQMKERLASLSSHAAELE---EDLDTA--------- 289
Cdd:PRK03918 364 yEEAKAKkeelERLKKRLTGLTPEKLEKELEELEKAKEEIEEEiSKITARIGELKKEIKELKkaiEELKKAkgkcpvcgr 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 290 ------RKDLIKS--EEMNtKLQREVREAMAQKEDMEERITTLEKrYLAAQREATSVHDLNDKLENeiankdsmhrqted 361
Cdd:PRK03918 444 elteehRKELLEEytAELK-RIEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQLKE-------------- 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 362 knrqLQERLE-LAEQKLQQTLRKAETLPEVEAELAQRVAALSKSgpLSSGssAAKEAKLLELTSKLRKAEERHGNIEERL 440
Cdd:PRK03918 508 ----LEEKLKkYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKE--LEKL--EELKKKLAELEKKLDELEEELAELLKEL 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 441 RQM----EAQLEEKNQELqrarqrEKMNEEHNkRLSDTVDKL--LSESNERLQLHLKERMAALEDKNSLLREVEN----- 509
Cdd:PRK03918 580 EELgfesVEELEERLKEL------EPFYNEYL-ELKDAEKELerEEKELKKLEEELDKAFEELAETEKRLEELRKeleel 652
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 564332108 510 -------------------------AKKQLEETQHDKDQLVLNIEALKAELEQMR 539
Cdd:PRK03918 653 ekkyseeeyeelreeylelsrelagLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
262-539 |
2.06e-07 |
|
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: 55.73 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 262 AREQSQMKERLASLSSHAAELEEDLDTARKDLikseemnTKLQREVREAMA-QKEDMEERITTLEKRYLAAQREATSVHD 340
Cdd:COG3096 842 RQRRSELERELAQHRAQEQQLRQQLDQLKEQL-------QLLNKLLPQANLlADETLADRLEELREELDAAQEAQAFIQQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 341 LNDKLEnEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLpeveAELAQRVAALS--KSGPLSSGSSAAKEAk 418
Cdd:COG3096 915 HGKALA-QLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFAL----SEVVQRRPHFSyeDAVGLLGENSDLNEK- 988
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 419 lleLTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQ----RARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERM 494
Cdd:COG3096 989 ---LRARLEQAEEARREAREQLRQAQAQYSQYNQVLAslksSRDAKQQTLQELEQELEELGVQADAEAEERARIRRDELH 1065
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 564332108 495 AALEDKNSLLREVEnakKQLEETQHDKDQLVLNIEALKAELEQMR 539
Cdd:COG3096 1066 EELSQNRSRRSQLE---KQLTRCEAEMDSLQKRLRKAERDYKQER 1107
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
249-545 |
2.10e-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: 55.41 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 249 AKVLELQEvidrqarEQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRY 328
Cdd:TIGR04523 218 SQISELKK-------QNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 329 ---------LAAQREAtsvhDLNDKLENEIANKDSMHRQTE---DKNRQLQERLELAEQKLQQTLRKAETL-PEVEAELA 395
Cdd:TIGR04523 291 nqlkseisdLNNQKEQ----DWNKELKSELKNQEKKLEEIQnqiSQNNKIISQLNEQISQLKKELTNSESEnSEKQRELE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 396 QRVAALSKSgpLSSGSSAAKEAKLLE-----LTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKR 470
Cdd:TIGR04523 367 EKQNEIEKL--KKENQSYKQEIKNLEsqindLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 471 LS--DTVDKLLSESNERLQLHLKERMAALE------------------DKNSLLREVENAKKQLEETQHD----KDQLVL 526
Cdd:TIGR04523 445 LTnqDSVKELIIKNLDNTRESLETQLKVLSrsinkikqnleqkqkelkSKEKELKKLNEEKKELEEKVKDltkkISSLKE 524
|
330
....*....|....*....
gi 564332108 527 NIEALKAELEQMRLRGSSL 545
Cdd:TIGR04523 525 KIEKLESEKKEKESKISDL 543
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
45-687 |
2.95e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNtALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLL 124
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELY-ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 125 LEHLECLVSRHERSLRMTVVKRQAQSpagvsSEVEVLKALKSLFEHHKALDEKVRERLRVALercSLLEEELGATHKELM 204
Cdd:TIGR02168 332 LDELAEELAELEEKLEELKEELESLE-----AELEELEAELEELESRLEELEEQLETLRSKV---AQLELQIASLNNEIE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 205 ILKEQNSQKKALTEGMLDGNHEQENAPSTNGKRSSDGSLSHEDLAKVlELQEVIDRQAREQSQMKERLASLSSHAAELEE 284
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELE-ELQEELERLEEALEELREELEEAEQALDAAER 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 285 DLDT--ARKDLIKS-EEMNTKLQREVREAMAQKEDME-------ERITTLEK------RYLAAQREATSVHDLNDKLE-- 346
Cdd:TIGR02168 483 ELAQlqARLDSLERlQENLEGFSEGVKALLKNQSGLSgilgvlsELISVDEGyeaaieAALGGRLQAVVVENLNAAKKai 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 347 ---------------------NEIANKDSMHRQTEDKNRQLQERLELAEQKLQ-------QTLRKAETLP---EVEAELA 395
Cdd:TIGR02168 563 aflkqnelgrvtflpldsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllGGVLVVDDLDnalELAKKLR 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 396 QRVAALSKSGPL------SSGSSAAKEAKLLELTSKLRkaeerhgNIEERLRQMEAQLEEKNQELQRAR-QREKMNEEHN 468
Cdd:TIGR02168 643 PGYRIVTLDGDLvrpggvITGGSAKTNSSILERRREIE-------ELEEKIEELEEKIAELEKALAELRkELEELEEELE 715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 469 K--RLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVL-------NIEALKAELEQMR 539
Cdd:TIGR02168 716 QlrKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEelaeaeaEIEELEAQIEQLK 795
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 540 LRGSSLHhgrphlgsvpdfrfSVADGHVDAYSTSAVLRRPQKGRLAALRDEPSKVQTLNEQDWERAQQAS-VLANVAQAF 618
Cdd:TIGR02168 796 EELKALR--------------EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSeDIESLAAEI 861
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564332108 619 EsdvdvsDGEDDRDTLLSSVDLLSPSgQADAQTLAMMLQEQLDAINKEIRliQEEKENTEQRAEEIESR 687
Cdd:TIGR02168 862 E------ELEELIEELESELEALLNE-RASLEEALALLRSELEELSEELR--ELESKRSELRRELEELR 921
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
334-547 |
2.98e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 334 EATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQ--ERLELAEQKLQQTLRKAETLPEVEAEL-----AQRVAALSKSGP 406
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALrlwfaQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 407 LSSGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQM----EAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSES 482
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564332108 483 NERLQLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQlvlNIEALKAELEQMRLRGSSLHH 547
Cdd:COG4913 379 AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR---ELRELEAEIASLERRKSNIPA 440
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
1004-1059 |
4.13e-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: 4.13e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 564332108 1004 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLR 1059
Cdd:smart00454 11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
909-975 |
4.30e-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: 4.30e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564332108 909 FAQWDGPTVVVWLELWvGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEI 975
Cdd:smart00454 1 VSQWSPESVADWLESI-GLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
169-534 |
4.41e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 169 EHHKALDEKVRERLRVAlERCSLLEEELGATHKElmilkEQNSQKKALTEGMLDGNHEQENAPSTNGKRSSDGSLSHEDL 248
Cdd:PTZ00121 1216 EARKAEDAKKAEAVKKA-EEAKKDAEEAKKAEEE-----RNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEK 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 249 AKVLELQEVIDR----QAREQSQMKERLASLSSHAAELEEDLDTARKdliKSEEMNTKLQREVREAMAQKEDMEERITTL 324
Cdd:PTZ00121 1290 KKADEAKKAEEKkkadEAKKKAEEAKKADEAKKKAEEAKKKADAAKK---KAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 325 EKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTL--------------------RKA 384
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAkkkaeekkkadeakkkaeeaKKA 1446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 385 ETLPEvEAELAQRVAALSKSGPLSSGSSAAK----EAKLLELTSK-----------LRKAEERHGNIEERLRQMEAQLEE 449
Cdd:PTZ00121 1447 DEAKK-KAEEAKKAEEAKKKAEEAKKADEAKkkaeEAKKADEAKKkaeeakkkadeAKKAAEAKKKADEAKKAEEAKKAD 1525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 450 KNQELQRARQREKMNEEHNKRLSDTVDKL--LSESNERLQLHLKERmaALEDKNSLLREVENAKKQLEETQHDKDQLVLN 527
Cdd:PTZ00121 1526 EAKKAEEAKKADEAKKAEEKKKADELKKAeeLKKAEEKKKAEEAKK--AEEDKNMALRKAEEAKKAEEARIEEVMKLYEE 1603
|
....*..
gi 564332108 528 IEALKAE 534
Cdd:PTZ00121 1604 EKKMKAE 1610
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
44-487 |
5.00e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 5.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 44 LEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTA-LPQEFAALTKELNVCREQLLEREEEIAELKAERNNTR 122
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLpLYQELEALEAELAELPERLEELEERLEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 123 LLLEHLEclvsRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKE 202
Cdd:COG4717 167 ELEAELA----ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 203 LMILKEQNSQKKALTEGMLDGNheqenAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAEL 282
Cdd:COG4717 243 ERLKEARLLLLIAAALLALLGL-----GGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 283 EEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDK 362
Cdd:COG4717 318 EEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEY 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 363 nRQLQERLELAEQKLQQTLRKAETLPEV--EAELAQRVAALsksgplssgssaakEAKLLELTSKLRKAEERHGNIEERL 440
Cdd:COG4717 398 -QELKEELEELEEQLEELLGELEELLEAldEEELEEELEEL--------------EEELEELEEELEELREELAELEAEL 462
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 564332108 441 RQMEAQ--LEEKNQELQRARQREKMNEEHNKRLsDTVDKLLSESNERLQ 487
Cdd:COG4717 463 EQLEEDgeLAELLQELEELKAELRELAEEWAAL-KLALELLEEAREEYR 510
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
258-461 |
5.05e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.68 E-value: 5.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 258 IDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREV----REAMAQKEDMEERITTLEKRYLAAQR 333
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIdklqAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 334 ------------EATSVHDLNDKLEneiaNKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAAL 401
Cdd:COG3883 98 sggsvsyldvllGSESFSDFLDRLS----ALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 402 SKsgplssgSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQRE 461
Cdd:COG3883 174 EA-------QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
253-508 |
6.91e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.98 E-value: 6.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 253 ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQ 332
Cdd:COG4372 49 QLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 333 REATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQtLRKAETLPEVEAELAQ-RVAALSKSGPLSSGS 411
Cdd:COG4372 129 QQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA-LSEAEAEQALDELLKEaNRNAEKEEELAEAEK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 412 SAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLK 491
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287
|
250
....*....|....*..
gi 564332108 492 ERMAALEDKNSLLREVE 508
Cdd:COG4372 288 LEEAALELKLLALLLNL 304
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
246-539 |
1.20e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 246 EDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERItTLE 325
Cdd:PRK03918 221 EELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYI-KLS 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 326 KRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQE---RLELAEQKLQQTLRKAETLPEVEAELAQRVAALS 402
Cdd:PRK03918 300 EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEElkkKLKELEKRLEELEERHELYEEAKAKKEELERLKK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 403 KSGPLSSGSSaakEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQ---ELQRARQR-----EKMNEEHNKRLSDT 474
Cdd:PRK03918 380 RLTGLTPEKL---EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKaieELKKAKGKcpvcgRELTEEHRKELLEE 456
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564332108 475 VDKLLSESNERLQ------LHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQL-VLNIEALKAELEQMR 539
Cdd:PRK03918 457 YTAELKRIEKELKeieekeRKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLkKYNLEELEKKAEEYE 528
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
44-539 |
1.32e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 44 LEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTaLPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRL 123
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEE-LEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRD 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 124 LLEHLECLVSRHErslrmtvvkrqaqspagvssevevlKALKSLFEHHKALDEKVRErlrvALERCSLLEEELGATHKEl 203
Cdd:PRK02224 329 RLEECRVAAQAHN-------------------------EEAESLREDADDLEERAEE----LREEAAELESELEEAREA- 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 204 miLKEQNSQKKALTEGMLDGNHEQENAPSTNGK-------RSSDGSLSHEDLAKV-LELQEVIDRQAREQSQMKE----- 270
Cdd:PRK02224 379 --VEDRREEIEELEEEIEELRERFGDAPVDLGNaedfleeLREERDELREREAELeATLRTARERVEEAEALLEAgkcpe 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 271 --RLASLSSHAAELEEDldtarkdliksEEMNTKLQREVREAMAQKEDMEERITTLEKrYLAAQREATSVHDLNDKLENE 348
Cdd:PRK02224 457 cgQPVEGSPHVETIEED-----------RERVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIERLEERREDLEEL 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 349 IANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALsksgplssgssaakEAKLLELTSKLrk 428
Cdd:PRK02224 525 IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAEL--------------NSKLAELKERI-- 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 429 aeERHGNIEERLrqmeAQLEEKNQELQRARQREK----MNEEHNKRLS---DTVDKLLSESNE-RLQlhlkermAALEDK 500
Cdd:PRK02224 589 --ESLERIRTLL----AAIADAEDEIERLREKREalaeLNDERRERLAekrERKRELEAEFDEaRIE-------EAREDK 655
|
490 500 510
....*....|....*....|....*....|....*....
gi 564332108 501 NSLLREVENAKKQLEETQHDKDQLVLNIEALKAELEQMR 539
Cdd:PRK02224 656 ERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELE 694
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
32-524 |
1.51e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 32 ADSHFEQLMVSMLEER-DRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTA-------LPQEFAALTKELNVCREQ 103
Cdd:COG4913 281 LRLWFAQRRLELLEAElEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrleqLEREIERLERELEERERR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 104 LLEREEEIA-----------ELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSP--AGVSSEVEVLKALKSLFEH 170
Cdd:COG4913 361 RARLEALLAalglplpasaeEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRelRELEAEIASLERRKSNIPA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 171 HkalDEKVRERLRvalERCSLLEEEL---------GATHKE-------------LMILKEQNSQKKAL-------TEGML 221
Cdd:COG4913 441 R---LLALRDALA---EALGLDEAELpfvgelievRPEEERwrgaiervlggfaLTLLVPPEHYAAALrwvnrlhLRGRL 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 222 DGNHEQENAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQareqsqmkerLASLSSHA-AELEEDLDTARKD-----LIK 295
Cdd:COG4913 515 VYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAE----------LGRRFDYVcVDSPEELRRHPRAitragQVK 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 296 SE----EMNTklQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIankdsmhrqtedknRQLQERLE 371
Cdd:COG4913 585 GNgtrhEKDD--RRRIRSRYVLGFDNRAKLAALEAELAELEEELAEAEERLEALEAEL--------------DALQERRE 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 372 lAEQKLQQTLRKAETLPEVEAELAQRVAALSKsgpLSSGSSaakeaKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKN 451
Cdd:COG4913 649 -ALQRLAEYSWDEIDVASAEREIAELEAELER---LDASSD-----DLAALEEQLEELEAELEELEEELDELKGEIGRLE 719
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564332108 452 QELQRARQREkmneehnKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQL 524
Cdd:COG4913 720 KELEQAEEEL-------DELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRA 785
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
45-455 |
1.53e-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: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALpqEFAALTKELnvcreqlleREEEIAELKAERNNTRLL 124
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE--RYQALLKEK---------REYEGYELLKEKEALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 125 LEHLECLVSRHERSLRmtvvKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKvrERLRValercsllEEELGATHKELM 204
Cdd:TIGR02169 239 KEAIERQLASLEEELE----KLTEEISELEKRLEEIEQLLEELNKKIKDLGEE--EQLRV--------KEKIGELEAEIA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 205 ILKEQNSQKKaltegmldgnHEQENApstNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLAslsshaaELEE 284
Cdd:TIGR02169 305 SLERSIAEKE----------RELEDA---EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYA-------ELKE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 285 DLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNR 364
Cdd:TIGR02169 365 ELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKE 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 365 QLQERLELAEQKLQQTlrkAETLPEVEAELAQRVAALSKSgplssgssaakEAKLLELTSKLRKAEERHGNIEERLRQME 444
Cdd:TIGR02169 445 DKALEIKKQEWKLEQL---AADLSKYEQELYDLKEEYDRV-----------EKELSKLQRELAEAEAQARASEERVRGGR 510
|
410
....*....|.
gi 564332108 445 AQLEEKNQELQ 455
Cdd:TIGR02169 511 AVEEVLKASIQ 521
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
364-536 |
1.55e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.47 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 364 RQLQERLELAEQKLQQTLRKAETlpevEAELAQRVAALsksgplssgssAAKEaKLLELTSKL-RKAEERHGNI---EER 439
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKK----EAEAIKKEALL-----------EAKE-EIHKLRNEFeKELRERRNELqklEKR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 440 LRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLK--ERMAAL---EDKNSLLREVEnakkql 514
Cdd:PRK12704 91 LLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQelERISGLtaeEAKEILLEKVE------ 164
|
170 180
....*....|....*....|..
gi 564332108 515 EETQHDKDQLVLNIEAlKAELE 536
Cdd:PRK12704 165 EEARHEAAVLIKEIEE-EAKEE 185
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
160-538 |
1.56e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 160 VLKALKSLFEhhKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNSQKKALTEGMLDGNHEQENApstnGKRSS 239
Cdd:COG4717 39 LLAFIRAMLL--ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEEL----EAELE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 240 DGSLSHEDLAKVLELQEVIDRQAREQSQM----------KERLASLsshaAELEEDLDTARKDLIKSEEMNTKLQREVRE 309
Cdd:COG4717 113 ELREELEKLEKLLQLLPLYQELEALEAELaelperleelEERLEEL----RELEEELEELEAELAELQEELEELLEQLSL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 310 AMAQK-EDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELA--------------- 373
Cdd:COG4717 189 ATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLiaaallallglggsl 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 374 ----------------------------EQKLQQTLRKAETLPEVEAELAQRVAALSKSGPLSSGSSAAKEAKLLELTSK 425
Cdd:COG4717 269 lsliltiagvlflvlgllallflllareKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 426 LRKAEERHGNIEERLRQMEAQlEEKNQELQRA--------RQREKMNEEHNKRLsdtvdKLLSESNERLQLHLKERMAAL 497
Cdd:COG4717 349 LQELLREAEELEEELQLEELE-QEIAALLAEAgvedeeelRAALEQAEEYQELK-----EELEELEEQLEELLGELEELL 422
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 564332108 498 E--DKNSLLREVENAKKQLEETQHDKDQLVLNIEALKAELEQM 538
Cdd:COG4717 423 EalDEEELEEELEELEEELEELEEELEELREELAELEAELEQL 465
|
|
| SAM_superfamily |
cd09487 |
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
1004-1055 |
1.58e-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: 1.58e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 564332108 1004 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRNSFQCGI 1055
Cdd:cd09487 4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
269-545 |
1.85e-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: 52.33 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 269 KERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEK-------RYLAAQREATSVHDL 341
Cdd:TIGR04523 95 KDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKeleklnnKYNDLKKQKEELENE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 342 NDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQqtlrKAETLPEVEAELAQRVAALSKSGPLssgssaaKEAKLLE 421
Cdd:TIGR04523 175 LNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQ----KNKSLESQISELKKQNNQLKDNIEK-------KQQEINE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 422 LTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRArqrEKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKN 501
Cdd:TIGR04523 244 KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN---NKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQE 320
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 564332108 502 SLLREVENakkQLEETQHDKDQLVLNIEALKAELEQMRLRGSSL 545
Cdd:TIGR04523 321 KKLEEIQN---QISQNNKIISQLNEQISQLKKELTNSESENSEK 361
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
246-688 |
2.01e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 246 EDLAKVLELQEVID-RQAREQSQMKERLASLSSHAAELEEDLDTARK-DLIKSEEMNTKLQREVREAMAQKEDMEERITT 323
Cdd:PTZ00121 1185 EEVRKAEELRKAEDaRKAEAARKAEEERKAEEARKAEDAKKAEAVKKaEEAKKDAEEAKKAEEERNNEEIRKFEEARMAH 1264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 324 LEKRYLAAQ----REATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQE--RLELAEQKLQQTLRKAETLPEvEAELAQR 397
Cdd:PTZ00121 1265 FARRQAAIKaeeaRKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEakKADEAKKKAEEAKKKADAAKK-KAEEAKK 1343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 398 VAALSKSGPLSSGSSA-----AKEAKLLELTSKLRKAEERHGNIEERLRQMEA-----QLEEKNQELQRARQREKMNEEH 467
Cdd:PTZ00121 1344 AAEAAKAEAEAAADEAeaaeeKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAkkkaeEDKKKADELKKAAAAKKKADEA 1423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 468 NKRLSDT--VDKLLSESNErlqlhlKERMAALEDKNSLLREVENAKKQLEETQH-----DKDQLVLNIEALKAELEQMRL 540
Cdd:PTZ00121 1424 KKKAEEKkkADEAKKKAEE------AKKADEAKKKAEEAKKAEEAKKKAEEAKKadeakKKAEEAKKADEAKKKAEEAKK 1497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 541 RGSSLHHGRPHLGSVPDFRFSVADGHVDAYSTSAVLRRPQKGRLAalrDEPSKVQTLNEQdwERAQQASVLANVAQAFES 620
Cdd:PTZ00121 1498 KADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKA---EEKKKADELKKA--EELKKAEEKKKAEEAKKA 1572
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 621 dvdvsdgEDDRDTLLSSVDLLSPSGQADAQTLAMMLQEQLDAINKEIRLIQEEKENTEQ--RAEEIESRV 688
Cdd:PTZ00121 1573 -------EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkKAEEEKKKV 1635
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
1082-1152 |
2.06e-06 |
|
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: 46.52 E-value: 2.06e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564332108 1082 VLVWSNDRVIRWILSIGLKEFANNLIESGVHGALLALDETFDfsalaLLLQIPTQNTQARAVLEREFNNLL 1152
Cdd:smart00454 1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEE-----DLKELGITKLGHRKKILKAIQKLK 66
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
31-539 |
2.06e-06 |
|
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: 52.43 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 31 DADSHFEQLMVSMLEERDrlldTLRETQETLALTQGKLHEVGHERDSLQ----RQLNTALPQEFAALTKELNVCREQLLE 106
Cdd:pfam15921 167 DSNTQIEQLRKMMLSHEG----VLQEIRSILVDFEEASGKKIYEHDSMStmhfRSLGSAISKILRELDTEISYLKGRIFP 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 107 REEEIAELKAE-RNNTRLLLEH----LECLVSRHERSLR-MTVVKRQAQSPA-GVSSEVEV------------LKALKSL 167
Cdd:pfam15921 243 VEDQLEALKSEsQNKIELLLQQhqdrIEQLISEHEVEITgLTEKASSARSQAnSIQSQLEIiqeqarnqnsmyMRQLSDL 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 168 FEHHKALDEKVRERLRVALERCSLLEEELGATHKELM---ILKEQNSQKKA----LTEGMLDGNHEQENAPSTNGK---- 236
Cdd:pfam15921 323 ESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTearTERDQFSQESGnlddQLQKLLADLHKREKELSLEKEqnkr 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 237 ---RSSDGSLSHEDLAKVL-------------------ELQEVIDRQAREQSQMKERLASLSSHAAELE----------E 284
Cdd:pfam15921 403 lwdRDTGNSITIDHLRRELddrnmevqrleallkamksECQGQMERQMAAIQGKNESLEKVSSLTAQLEstkemlrkvvE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 285 DLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNR 364
Cdd:pfam15921 483 ELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDK 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 365 QLQERLELAEQKLQQTLRKAETLPEVEAELAQrvaaLSKSgpLSSGSSAAKEAKLLE--LTSKLRKAEERHGNIE-ERLR 441
Cdd:pfam15921 563 VIEILRQQIENMTQLVGQHGRTAGAMQVEKAQ----LEKE--INDRRLELQEFKILKdkKDAKIRELEARVSDLElEKVK 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 442 QMEAQLEeknqelqRARQREKMNEEHnkrlsdtvDKLLSE-SNERLQLHlkermAALEDKNSLLREVENAKKQLEETqhd 520
Cdd:pfam15921 637 LVNAGSE-------RLRAVKDIKQER--------DQLLNEvKTSRNELN-----SLSEDYEVLKRNFRNKSEEMETT--- 693
|
570
....*....|....*....
gi 564332108 521 KDQLVLNIEALKAELEQMR 539
Cdd:pfam15921 694 TNKLKMQLKSAQSELEQTR 712
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
156-488 |
2.43e-06 |
|
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: 52.05 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 156 SEVEVLKALKSLFEHHKALDEKVR---------ERLRVA-------LERCSLLEEELGATHKELmilkEQNSQKKALTEG 219
Cdd:pfam17380 266 TENEFLNQLLHIVQHQKAVSERQQqekfekmeqERLRQEkeekareVERRRKLEEAEKARQAEM----DRQAAIYAEQER 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 220 M-LDGNHEQENAPSTNGKRSSDgSLSHEDLAKVLELQEVIDRQAREQSQMKERLaslsshaaelEEDLDTARKDLIKSEE 298
Cdd:pfam17380 342 MaMERERELERIRQEERKRELE-RIRQEEIAMEISRMRELERLQMERQQKNERV----------RQELEAARKVKILEEE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 299 MNTKLQREVREaMAQKEDMEERITTLEKRYLAAQREatsvHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQ 378
Cdd:pfam17380 411 RQRKIQQQKVE-MEQIRAEQEEARQREVRRLEEERA----REMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRD 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 379 QTLRKAETLPEVEAELAQRVAALSKSgplsSGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRAR 458
Cdd:pfam17380 486 RKRAEEQRRKILEKELEERKQAMIEE----ERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKA 561
|
330 340 350
....*....|....*....|....*....|
gi 564332108 459 QREKMNEEHNKRLSDTVDKLLSESNERLQL 488
Cdd:pfam17380 562 TEERSRLEAMEREREMMRQIVESEKARAEY 591
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
421-685 |
2.65e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 421 ELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQR-ARQREKMNEehnkrlsdtVDKLLSESNE-RLQLHLKERMAALE 498
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERlRREREKAER---------YQALLKEKREyEGYELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 499 DKNSLLREVENAKKQLEETQHDKDQLVLNIEALKAELEQMRLRGSSLHHGRphlgsVPDFRFSVADGHVD---AYSTSAV 575
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEE-----QLRVKEKIGELEAEiasLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 576 LRRPQK---GRLAALRDEPSKVQ-TLNEQDWERAQQASVLANVAQAFESDvdvsdgEDDRDTLLSSVDLLSPSGQA---- 647
Cdd:TIGR02169 313 KERELEdaeERLAKLEAEIDKLLaEIEELEREIEEERKRRDKLTEEYAEL------KEELEDLRAELEEVDKEFAEtrde 386
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 564332108 648 --DAQTLAMMLQEQLDAINKEIRLIQEEKENTEQRAEEIE 685
Cdd:TIGR02169 387 lkDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN 426
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
132-539 |
3.60e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 132 VSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKslfEHHKALDEKVRERLRVALERCSLLEEELGATHkelmiLKEQNS 211
Cdd:PTZ00121 1254 IRKFEEARMAHFARRQAAIKAEEARKADELKKAE---EKKKADEAKKAEEKKKADEAKKKAEEAKKADE-----AKKKAE 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 212 QKKALTEGMLDGNHEQENAPSTNGKRSsdgslshEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARK 291
Cdd:PTZ00121 1326 EAKKKADAAKKKAEEAKKAAEAAKAEA-------EAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKK 1398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 292 dliKSEEMNTKLQrEVREAMAQKEDMEERITTLEKRYLAAQ-----REATSVHDLNDKLEnEIANKDSMHRQTEDKnRQL 366
Cdd:PTZ00121 1399 ---KAEEDKKKAD-ELKKAAAAKKKADEAKKKAEEKKKADEakkkaEEAKKADEAKKKAE-EAKKAEEAKKKAEEA-KKA 1472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 367 QERLELAEQKlqqtlRKAETLPEVEAELAQRVAALSKSGPLSSGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQ 446
Cdd:PTZ00121 1473 DEAKKKAEEA-----KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK 1547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 447 LEE--KNQELQRARQR----EKMNEEHNKRLSDTVDKLLSESNE-RLQLHLKERMAALEDKNSLLREVENAKKQLEETQH 519
Cdd:PTZ00121 1548 ADElkKAEELKKAEEKkkaeEAKKAEEDKNMALRKAEEAKKAEEaRIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK 1627
|
410 420
....*....|....*....|
gi 564332108 520 DKDQLVLNIEALKAELEQMR 539
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKK 1647
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
303-516 |
3.82e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 303 LQREVREAMAQKEDMEERITTLEKRYLAAQREatsvhdLND-KLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTL 381
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAA------LEEfRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 382 RKAETLPEVEAELAQRVAALSKSGPLSSGSS--AAKEAKLLELTSKLRkaeERHGNIEERLRQMEAQLEEKNQELQRARQ 459
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQSPVIQQLRAqlAELEAELAELSARYT---PNHPDVIALRAQIAALRAQLQQEAQRILA 316
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 564332108 460 REKMNEEHNKRLSDTVDKLLSESNERLQlhlkeRMAALEDK-NSLLREVENAKKQLEE 516
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLA-----ELPELEAElRRLEREVEVARELYES 369
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
46-537 |
4.31e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 4.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 46 ERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNtalpqefaALTKELNVCREQLLEREEEIAELKAERNNTRLLL 125
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQ--------ELEEKLEELRLEVSELEEEIEELQKELYALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 126 EHLECLVSRH---ERSLRMTVVKRQAQSPAGVSSEVEVLKALK-------SLFEHHKALDEKV---RERLRVALERCSLL 192
Cdd:TIGR02168 298 SRLEQQKQILrerLANLERQLEELEAQLEELESKLDELAEELAeleekleELKEELESLEAELeelEAELEELESRLEEL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 193 EEELGATHKELMILKEQ----NSQKKALTEGMLDGNHEQENAPSTNGKRSSDGSLS--HEDLAKVLELQEVIDRQAREQS 266
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQiaslNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAelKELQAELEELEEELEELQEELE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 267 QMKERLASLSSHAAELEEDLDTARKDLIKS----------EEMNTKLQREVREAMAQKEDME-------ERITTLEK--- 326
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLqarldslerlQENLEGFSEGVKALLKNQSGLSgilgvlsELISVDEGyea 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 327 ---RYLAAQREATSVHDLNDKLE-----------------------NEIANKDSMHRQTEDKNRQLQERLELAEQKLQ-- 378
Cdd:TIGR02168 538 aieAALGGRLQAVVVENLNAAKKaiaflkqnelgrvtflpldsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRka 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 379 -----QTLRKAETLP---EVEAELAQRVAALSKSGPL------SSGSSAAKEAKLLELTSKLRkaeerhgNIEERLRQME 444
Cdd:TIGR02168 618 lsyllGGVLVVDDLDnalELAKKLRPGYRIVTLDGDLvrpggvITGGSAKTNSSILERRREIE-------ELEEKIEELE 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 445 AQLEEKNQELQRAR-QREKMNEEHNK--RLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQHDK 521
Cdd:TIGR02168 691 EKIAELEKALAELRkELEELEEELEQlrKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
|
570
....*....|....*.
gi 564332108 522 DQLVLNIEALKAELEQ 537
Cdd:TIGR02168 771 EEAEEELAEAEAEIEE 786
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
232-466 |
7.38e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 7.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 232 STNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAM 311
Cdd:COG4372 14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 312 AQKEDMEERITTLEKRYLAAQREAtsvhdlnDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVE 391
Cdd:COG4372 94 AELAQAQEELESLQEEAEELQEEL-------EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564332108 392 AELAQRVAALSKSGPLSSGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEE 466
Cdd:COG4372 167 AALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA 241
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
47-537 |
8.36e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 8.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 47 RDRLLDTLRETQETLALTQGKLHEVG-HERDSLQRQLNTA--LPQEFAALTKELNvcreqllEREEEIAELKAERNNTRL 123
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNlKELKELEEELKEAeeKEEEYAELQEELE-------ELEEELEELEAELEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 124 LLEHLECLVSRHERSLRMTVVKRQaqspagvssevevlkaLKSLFEHHKALDEKVRERLRvALERCSLLEEELGATHKEL 203
Cdd:COG4717 117 ELEKLEKLLQLLPLYQELEALEAE----------------LAELPERLEELEERLEELRE-LEEELEELEAELAELQEEL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 204 MILKEQNSQKKALTEGMLDGNHEQ-ENAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAEL 282
Cdd:COG4717 180 EELLEQLSLATEEELQDLAEELEElQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 283 EedLDTARKDLIKSEEMNTKLQREVREAMA--------QKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDS 354
Cdd:COG4717 260 A--LLGLGGSLLSLILTIAGVLFLVLGLLAllflllarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 355 MHRQTEDKNRQLQERLELAEqKLQQTLRKAETLPEVEAELAQrvaalsksgplssgssaAKEAKLLELTSKLRKAEERHg 434
Cdd:COG4717 338 ELLELLDRIEELQELLREAE-ELEEELQLEELEQEIAALLAE-----------------AGVEDEEELRAALEQAEEYQ- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 435 NIEERLRQMEAQLEEKNQELQRARQREKmNEEHNKRLSDTVDKLLSESNERLQLH-----LKERMAALEDKNSL---LRE 506
Cdd:COG4717 399 ELKEELEELEEQLEELLGELEELLEALD-EEELEEELEELEEELEELEEELEELReelaeLEAELEQLEEDGELaelLQE 477
|
490 500 510
....*....|....*....|....*....|.
gi 564332108 507 VENAKKQLEETQHDKDQLVLNIEALKAELEQ 537
Cdd:COG4717 478 LEELKAELRELAEEWAALKLALELLEEAREE 508
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
416-539 |
9.56e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 9.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 416 EAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQR-EKMNEEHNKRLSD---------TVDKLL-SESNE 484
Cdd:COG3883 36 QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEiEERREELGERARAlyrsggsvsYLDVLLgSESFS 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 564332108 485 RL--QLHLKERMAalEDKNSLLREVENAKKQLEETQHDKDQLVLNIEALKAELEQMR 539
Cdd:COG3883 116 DFldRLSALSKIA--DADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
246-537 |
9.73e-06 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 49.69 E-value: 9.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 246 EDLAK-VLELQEVID---RQAREQSQMKERLASL---SSHAAELEEDLDTARKDLiksEEMNtKLQREVR-------EAM 311
Cdd:pfam05622 90 EELEKeVLELQHRNEeltSLAEEAQALKDEMDILresSDKVKKLEATVETYKKKL---EDLG-DLRRQVKlleernaEYM 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 312 AQKEDMEERIttleKRY--LAAQREATS--VHDLNDKLENEIANKDsmhrQTEDKNRQLQERLELAEQKLQQTLRKAETL 387
Cdd:pfam05622 166 QRTLQLEEEL----KKAnaLRGQLETYKrqVQELHGKLSEESKKAD----KLEFEYKKLEEKLEALQKEKERLIIERDTL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 388 PE----------VEAELAQRVAALSKSGPlsSGSSAAKEAKLLELTSKLRK--------AEERHGNIEERLRQMEAQLEE 449
Cdd:pfam05622 238 REtneelrcaqlQQAELSQADALLSPSSD--PGDNLAAEIMPAEIREKLIRlqhenkmlRLGQEGSYRERLTELQQLLED 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 450 KNQELQRARQREKMNeehNKRLSdtvdkLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVLNIE 529
Cdd:pfam05622 316 ANRRKNELETQNRLA---NQRIL-----ELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIE 387
|
....*...
gi 564332108 530 ALKAELEQ 537
Cdd:pfam05622 388 ELEPKQDS 395
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
169-506 |
1.21e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 169 EHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNSQKKALTEGMLDGNHEQENAPSTNGKRSsdgslshEDL 248
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKA-------EEA 1586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 249 AKVLELQ-EVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKR 327
Cdd:PTZ00121 1587 KKAEEARiEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 328 YLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKlqqtlRKAETLPEVEAELAQRVAALSKSgpl 407
Cdd:PTZ00121 1667 AKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEK-----KKAEELKKAEEENKIKAEEAKKE--- 1738
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 408 ssgssaAKEAKlleltsklRKAEErhgnieerLRQMEaqlEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQ 487
Cdd:PTZ00121 1739 ------AEEDK--------KKAEE--------AKKDE---EEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRR 1793
|
330
....*....|....*....
gi 564332108 488 LHLKERMAALEDKNSLLRE 506
Cdd:PTZ00121 1794 MEVDKKIKDIFDNFANIIE 1812
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
258-456 |
1.49e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 258 IDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATS 337
Cdd:COG4913 666 AEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 338 VH--DLNDKLENEIANK--DSMHRQTEDKNRQLQERLELAEQKLQQTLRK---------------AETLPEVEAELAQrv 398
Cdd:COG4913 746 ELraLLEERFAAALGDAveRELRENLEERIDALRARLNRAEEELERAMRAfnrewpaetadldadLESLPEYLALLDR-- 823
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564332108 399 aaLSKSGpLssgssAAKEAKLLELtskLRKAEER-----HGNIEERLRQMEAQLEEKNQELQR 456
Cdd:COG4913 824 --LEEDG-L-----PEYEERFKEL---LNENSIEfvadlLSKLRRAIREIKERIDPLNDSLKR 875
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
422-541 |
1.82e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 47.13 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 422 LTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLlsesNERLQLHLK---ERMA--A 496
Cdd:COG1842 14 INALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKW----EEKARLALEkgrEDLAreA 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 564332108 497 LEDKNSLLREVENAKKQLEETQHDKDQLVLNIEALKAELEQMRLR 541
Cdd:COG1842 90 LERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAK 134
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
37-477 |
2.06e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 37 EQLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELnvcreqllEREEEIAELKA 116
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA--------LLEAALAELLE 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 117 ERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKslfehhKALDEKVRERLRVALERCSLLEEEL 196
Cdd:COG1196 485 ELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVE------AAYEAALEAALAAALQNIVVEDDEV 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 197 GATHKELmiLKEQNSQKKALTEGMLDGNHEQENAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASLS 276
Cdd:COG1196 559 AAAAIEY--LKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAAL 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 277 SHAAELEEDLdtarkdLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMH 356
Cdd:COG1196 637 RRAVTLAGRL------REVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA 710
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 357 RQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSGPlssgssaaKEAKLLELTSKLRKAEERHGNI 436
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP--------DLEELERELERLEREIEALGPV 782
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 564332108 437 -----------EERLRQMEAQLEeknqELQRARQR-----EKMNEEHNKRLSDTVDK 477
Cdd:COG1196 783 nllaieeyeelEERYDFLSEQRE----DLEEARETleeaiEEIDRETRERFLETFDA 835
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
343-539 |
2.20e-05 |
|
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: 46.98 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 343 DKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAEtlPEVEAELAQRVAALSKSgplssgsSAAKEAKLLEL 422
Cdd:pfam04012 39 VKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGN--EELAREALAEKKSLEKQ-------AEALETQLAQQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 423 TSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEehnkrlsdTVDKLLSESNERLQLHLKERMAALEDKNS 502
Cdd:pfam04012 110 RSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAAKAQEAVQT--------SLGSLSTSSATDSFERIEEKIEEREARAD 181
|
170 180 190
....*....|....*....|....*....|....*..
gi 564332108 503 LLREVENAKKQLEETqhdkDQLVLNIEALKAELEQMR 539
Cdd:pfam04012 182 AAAELASAVDLDAKL----EQAGIQMEVSEDVLARLK 214
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
245-540 |
2.48e-05 |
|
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: 48.35 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 245 HEDL-AKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITT 323
Cdd:pfam07888 96 HEELeEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQ 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 324 LEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQK---LQQTLRKAETLPEVEAELAQRVAA 400
Cdd:pfam07888 176 LQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKeaeNEALLEELRSLQERLNASERKVEG 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 401 LskSGPLSSGSSAAKEAKlleltSKLRKAEERHGNIEERLRQMEAQLEEKN----QELQRARQREKMNEEHNKRLSDTVD 476
Cdd:pfam07888 256 L--GEELSSMAAQRDRTQ-----AELHQARLQAAQLTLQLADASLALREGRarwaQERETLQQSAEADKDRIEKLSAELQ 328
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564332108 477 KLlsesNERLQlhlKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVLNIEALKAELEQMRL 540
Cdd:pfam07888 329 RL----EERLQ---EERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQA 385
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
250-538 |
2.88e-05 |
|
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: 48.56 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 250 KVLELQevidRQAREQSQMKERLASLsshaaELEEDLDTaRKDLIKSEEMNTKLQREVREAMAqkedmeeRITTLEKRYL 329
Cdd:pfam05483 113 KIIEAQ----RKAIQELQFENEKVSL-----KLEEEIQE-NKDLIKENNATRHLCNLLKETCA-------RSAEKTKKYE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 330 AAQREATSVH-DLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQtlrkaetlpeVEAELAQRVAALSKSGPLS 408
Cdd:pfam05483 176 YEREETRQVYmDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQH----------LEEEYKKEINDKEKQVSLL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 409 SGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQE--------------LQRARQREKMNEEHNKRLSDT 474
Cdd:pfam05483 246 LIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKkdhltkeledikmsLQRSMSTQKALEEDLQIATKT 325
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564332108 475 VDKLLSESNERLQLHLKERMA------ALEDKNSLLREVENAKKQLEETQHDKDQLV-LNIEALKAELEQM 538
Cdd:pfam05483 326 ICQLTEEKEAQMEELNKAKAAhsfvvtEFEATTCSLEELLRTEQQRLEKNEDQLKIItMELQKKSSELEEM 396
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
417-537 |
2.97e-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: 46.84 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 417 AKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEhnkrlsdtvdKLLSESNER----LQL---H 489
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE----------QLGNVRNNKeyeaLQKeieS 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 564332108 490 LKERMAALEDK-NSLLREVENAKKQLEETQHDKDQLVLNIEALKAELEQ 537
Cdd:COG1579 101 LKRRISDLEDEiLELMERIEELEEELAELEAELAELEAELEEKKAELDE 149
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
360-559 |
3.08e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 360 EDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSGPLSSGS--SAAKEAKLLELTSKLRKAEERHG--- 434
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEidVASAEREIAELEAELERLDASSDdla 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 435 NIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQL 514
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELR 768
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 564332108 515 EETQHDKDQLVLNIEALKAELEQMRLR-----GSSLHHGRPHLGSVPDFR 559
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERAMRAfnrewPAETADLDADLESLPEYL 818
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
314-545 |
3.27e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 48.37 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 314 KEDMEERITTLEKRYLAAQREATSVHDLNDKLEnEIANKDsmhrQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEA- 392
Cdd:PRK11281 38 EADVQAQLDALNKQKLLEAEDKLVQQDLEQTLA-LLDKID----RQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDe 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 393 ELAQRVAALSksgplssgssaakeaklleltsklrkaeerhgnieerLRQMEAQLEEKNQELQRARqrekmneehnKRLS 472
Cdd:PRK11281 113 ETRETLSTLS-------------------------------------LRQLESRLAQTLDQLQNAQ----------NDLA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564332108 473 DTVDKLLSESN--ERLQLHLKERMAALEDKNSLLREVENAKKQLEETQhdKDQLVLNIEALKAELEQMR--LRGSSL 545
Cdd:PRK11281 146 EYNSQLVSLQTqpERAQAALYANSQRLQQIRNLLKGGKVGGKALRPSQ--RVLLQAEQALLNAQNDLQRksLEGNTQ 220
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
193-545 |
3.32e-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: 48.25 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 193 EEELGATHKELMILKEQNSQ-KKALTEgmLDGNHEQENAPST--NGKRSSDGSLSHED-------LAKVLELQEVIDRQA 262
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKaESELKE--LEKKHQQLCEEKNalQEQLQAETELCAEAeemrarlAARKQELEEILHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 263 REQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLN 342
Cdd:pfam01576 82 SRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 343 DKLENEIANKDSMHRQ-TEDKNRQ------LQERLElAEQKLQQTLRKAETLPEVEA-ELAQRVAALSKSGPLSSGSSAA 414
Cdd:pfam01576 162 SEFTSNLAEEEEKAKSlSKLKNKHeamisdLEERLK-KEEKGRQELEKAKRKLEGEStDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 415 KEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSEsnerLQLHLKERM 494
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTE----LEDTLDTTA 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 564332108 495 AALEDKNSLLREVENAKKQLEETQHDKDQLVLN--------IEALKAELEQMRLRGSSL 545
Cdd:pfam01576 317 AQQELRSKREQEVTELKKALEEETRSHEAQLQEmrqkhtqaLEELTEQLEQAKRNKANL 375
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
113-549 |
3.40e-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: 48.25 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 113 ELKAERNNTRLLLEH-LECLVSRHERSLRmTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKvrERLRVALERCSL 191
Cdd:pfam01576 320 ELRSKREQEVTELKKaLEEETRSHEAQLQ-EMRQKHTQALEELTEQLEQAKRNKANLEKAKQALES--ENAELQAELRTL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 192 LEEELGATHK---------ELMI-LKEQNSQKKALTEGMLDGNHEQENAPSTNGKRSSDGSLSHEDLAKV-LELQeviDR 260
Cdd:pfam01576 397 QQAKQDSEHKrkklegqlqELQArLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLeSQLQ---DT 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 261 QAREQSQMKERLaSLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQ----KEDMEERITTLEKRYLAAQREAT 336
Cdd:pfam01576 474 QELLQEETRQKL-NLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQlsdmKKKLEEDAGTLEALEEGKKRLQR 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 337 SVHDLNDKLENEIANKDSMHRQTE-------------DKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSK 403
Cdd:pfam01576 553 ELEALTQQLEEKAAAYDKLEKTKNrlqqelddllvdlDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAR 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 404 SgplssgssaaKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEE---------KN-QELQRA-RQREKMNEEHNKRLS 472
Cdd:pfam01576 633 E----------KETRALSLARALEEALEAKEELERTNKQLRAEMEDlvsskddvgKNvHELERSkRALEQQVEEMKTQLE 702
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 473 DTVDKLLSESNERLQLHLKerMAAL----------------EDKNSLLREVENAKKQLEETQHDKDQLVLNIEALKAELE 536
Cdd:pfam01576 703 ELEDELQATEDAKLRLEVN--MQALkaqferdlqardeqgeEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLK 780
|
490
....*....|...
gi 564332108 537 QMRLRGSSLHHGR 549
Cdd:pfam01576 781 ELEAQIDAANKGR 793
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
234-532 |
3.79e-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: 48.09 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 234 NGKRSSDGSLSHEDLAKVLELQEVIdrqaREQSQMKERLASLSSHAAELEEDLDtarkdliKSEEMNTKLQREVREAMAQ 313
Cdd:TIGR04523 352 TNSESENSEKQRELEEKQNEIEKLK----KENQSYKQEIKNLESQINDLESKIQ-------NQEKLNQQKDEQIKKLQQE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 314 KEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIAN----KDSMHRQTEDKNRQ---LQERLELAEQKLQQTLRKAET 386
Cdd:TIGR04523 421 KELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNldntRESLETQLKVLSRSinkIKQNLEQKQKELKSKEKELKK 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 387 LPEVEAELAQRVAALSKSGPLSSGSSAAKEAKLLELTSKLRKAEERHGNIEERLR--QMEAQLEEKNQELQRARQREKMN 464
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKkeNLEKEIDEKNKEIEELKQTQKSL 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 465 EEHNKRLSDTVDKLLSESNE-RLQLHLKERMAA-LED----------------------KNSLLREVENAKKQLEETQHD 520
Cdd:TIGR04523 581 KKKQEEKQELIDQKEKEKKDlIKEIEEKEKKISsLEKelekakkeneklssiiknikskKNKLKQEVKQIKETIKEIRNK 660
|
330
....*....|..
gi 564332108 521 KDQLVLNIEALK 532
Cdd:TIGR04523 661 WPEIIKKIKESK 672
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
253-383 |
5.65e-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: 45.28 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 253 ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREA-MAQKEDMEERITTLEKRYLAA 331
Cdd:pfam15619 57 ELPQLIARHNEEVRVLRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKnLAEREELQKKLEQLEAKLEDK 136
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 564332108 332 QREatsVHDLNDKLEN-------EIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRK 383
Cdd:pfam15619 137 DEK---IQDLERKLELenksfrrQLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKERE 192
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
129-536 |
7.69e-05 |
|
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: 46.81 E-value: 7.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 129 ECLVSRHErslrmtVVKRQAQSPAGVSSEVEVLKALKSLFEH-HKALDEKVrERLRVALERCSLLEEELGATHKELMILK 207
Cdd:pfam07888 38 ECLQERAE------LLQAQEAANRQREKEKERYKRDREQWERqRRELESRV-AELKEELRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 208 EQNSQKK-ALTEgmldgnHEQENAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERlaslsshaaeleedl 286
Cdd:pfam07888 111 EELSEEKdALLA------QRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEE--------------- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 287 DTARKDLikseemNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLeNEIANKDSMHRQTEDKNRQL 366
Cdd:pfam07888 170 EAERKQL------QAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKL-TTAHRKEAENEALLEELRSL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 367 QERLELAEQK---LQQTLRKAETLPE-VEAELAQ-RVAALSKSGPLSSGSSAAKEAK---LLELTSKLRKAEERHgnieE 438
Cdd:pfam07888 243 QERLNASERKvegLGEELSSMAAQRDrTQAELHQaRLQAAQLTLQLADASLALREGRarwAQERETLQQSAEADK----D 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 439 RLRQMEAQLEEKNQELQRAR-QREKMNEEHNkRLSDTVDKLLSESNERLQlhlkermaalEDKNSLlrevENAKKQLEET 517
Cdd:pfam07888 319 RIEKLSAELQRLEERLQEERmEREKLEVELG-REKDCNRVQLSESRRELQ----------ELKASL----RVAQKEKEQL 383
|
410
....*....|....*....
gi 564332108 518 QHDKDQLVLNIEALKAELE 536
Cdd:pfam07888 384 QAEKQELLEYIRQLEQRLE 402
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
226-518 |
7.88e-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: 7.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 226 EQENAPSTNGKRSSD-GSLSHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEE---DLDTARKDLIKSEEMNT 301
Cdd:TIGR04523 427 EIERLKETIIKNNSEiKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQkqkELKSKEKELKKLNEEKK 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 302 KLQREVREAMAQKEDMEERITTLEKRYLAAQREatsVHDLNDKLENEIANKDSmhRQTEDKNRQLQERLELAEQKLQQTL 381
Cdd:TIGR04523 507 ELEEKVKDLTKKISSLKEKIEKLESEKKEKESK---ISDLEDELNKDDFELKK--ENLEKEIDEKNKEIEELKQTQKSLK 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 382 RKAETLPEVEAELAQRVAALSKSgplssgsSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQ-- 459
Cdd:TIGR04523 582 KKQEEKQELIDQKEKEKKDLIKE-------IEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKEti 654
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564332108 460 ---REKMNE--EHNKRLSDTVD---KLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQ 518
Cdd:TIGR04523 655 keiRNKWPEiiKKIKESKTKIDdiiELMKDWLKELSLHYKKYITRMIRIKDLPKLEEKYKEIEKELK 721
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
246-523 |
8.31e-05 |
|
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: 46.34 E-value: 8.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 246 EDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERI--TT 323
Cdd:pfam15905 70 KESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRVNELLKAKFseDG 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 324 LEKRYLAAQREATsvhdlndKLENEIANKDsmhRQTEDKNRQLQERLELAEQKLQQTlrkaetlpevEAELAQRVAALSK 403
Cdd:pfam15905 150 TQKKMSSLSMELM-------KLRNKLEAKM---KEVMAKQEGMEGKLQVTQKNLEHS----------KGKVAQLEEKLVS 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 404 SGPLSSGSSAAKEaKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVD---KLLS 480
Cdd:pfam15905 210 TEKEKIEEKSETE-KLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNekcKLLE 288
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 564332108 481 ESNERLQLHLKERmaaledKNSLLREVENAKKQL--EETQHDKDQ 523
Cdd:pfam15905 289 SEKEELLREYEEK------EQTLNAELEELKEKLtlEEQEHQKLQ 327
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
357-590 |
9.35e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 9.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 357 RQTEDKNRQLQE---RLELAEQKLQQTLRKAETLPEVEaELAQRVAALSKSgplssgssaAKEAKLLELTSKLRKAEERH 433
Cdd:COG4913 221 PDTFEAADALVEhfdDLERAHEALEDAREQIELLEPIR-ELAERYAAARER---------LAELEYLRAALRLWFAQRRL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 434 GNIEERLRQMEAQLEEKNQELQRARQREkmnEEHNKRLSDTVDKLLSESNERLQlHLKERMAALEDKnslLREVENAKKQ 513
Cdd:COG4913 291 ELLEAELEELRAELARLEAELERLEARL---DALREELDELEAQIRGNGGDRLE-QLEREIERLERE---LEERERRRAR 363
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564332108 514 LEETQhdkDQLVLNIEALKAELEQMRLRGSSLhhgrphLGSVPDFRFSVAdghvDAYSTSAVLRRPQKGRLAALRDE 590
Cdd:COG4913 364 LEALL---AALGLPLPASAEEFAALRAEAAAL------LEALEEELEALE----EALAEAEAALRDLRRELRELEAE 427
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
343-499 |
1.29e-04 |
|
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: 44.92 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 343 DKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAEtlpEVEAELAQRVAALSKSGPLSSGSSAAKEAKllEL 422
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIK---RLELEIEEVEARIKKYEEQLGNVRNNKEYE--AL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564332108 423 TSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALED 499
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
320-541 |
1.46e-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: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 320 RITTLEKRYLAAQREATSVHDLNDKLENeIANKDSmhrqTEDKNRQLQERLELAEQKLQQtLRKaetlpEVEAELAQRVA 399
Cdd:pfam12795 1 KLDELEKAKLDEAAKKKLLQDLQQALSL-LDKIDA----SKQRAAAYQKALDDAPAELRE-LRQ-----ELAALQAKAEA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 400 ALSKSgpLSSGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTvDKLL 479
Cdd:pfam12795 70 APKEI--LASLSLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPP-GEPL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 480 SESnerLQLHLKERMAALEDKNSLLR-EVENA-------KKQLEETQHDKDQLVLNIEALKAELEQMRLR 541
Cdd:pfam12795 147 SEA---QRWALQAELAALKAQIDMLEqELLSNnnrqdllKARRDLLTLRIQRLEQQLQALQELLNEKRLQ 213
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
365-539 |
1.77e-04 |
|
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: 44.53 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 365 QLQERLELAE--QKLQQTLRKAETLPEVEAELAQRVAALSKSgplssgsSAAKEAKLLELTSKLRKAEERHGNIEERLRQ 442
Cdd:COG1579 5 DLRALLDLQEldSELDRLEHRLKELPAELAELEDELAALEAR-------LEAAKTELEDLEKEIKRLELEIEEVEARIKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 443 MEAQLEE-KNQELQRARQREKmnEEHNKRLSDTVDKLLsESNERLQlHLKERMAALEDknsllrEVENAKKQLEETQHDK 521
Cdd:COG1579 78 YEEQLGNvRNNKEYEALQKEI--ESLKRRISDLEDEIL-ELMERIE-ELEEELAELEA------ELAELEAELEEKKAEL 147
|
170
....*....|....*...
gi 564332108 522 DQLVLNIEALKAELEQMR 539
Cdd:COG1579 148 DEELAELEAELEELEAER 165
|
|
| SAM_STIM-1,2-like |
cd09504 |
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ... |
912-970 |
1.90e-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: 1.90e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564332108 912 WDGPTVVVWLELWVGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNPLHRLKLRL 970
Cdd:cd09504 5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
1004-1059 |
2.11e-04 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 40.72 E-value: 2.11e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 564332108 1004 EWLPSLGLPQYRSYFMECLVD-ARMLDHLTKKDLrGQLKMVDSFHRNSFQCGIMCLR 1059
Cdd:pfam07647 11 DWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDL-KRLGITSVGHRRKILKKIQELK 66
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
182-544 |
2.23e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 45.33 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 182 LRVALERCSLLEEELGATHKELMILKEQ--NSQKKALT-----EGMLDGNHEQENAPSTNGKRSSDGSLSHEDLAkvlel 254
Cdd:COG5185 175 NLKKLEIFGLTLGLLKGISELKKAEPSGtvNSIKESETgnlgsESTLLEKAKEIINIEEALKGFQDPESELEDLA----- 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 255 qEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEmntKLQREVREAMaqKEDMEERITTLEKRYLAAQRE 334
Cdd:COG5185 250 -QTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFE---NTKEKIAEYT--KSIDIKKATESLEEQLAAAEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 335 ATSVHDL-------NDKLENEIAN--KDSMHRQTEDKNRQLQ----ERLELAEQKLQQTLRKAETLPEveaELAQRVAAL 401
Cdd:COG5185 324 EQELEESkretetgIQNLTAEIEQgqESLTENLEAIKEEIENivgeVELSKSSEELDSFKDTIESTKE---SLDEIPQNQ 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 402 SKSGPLssgssaAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQ-ELQRARQREKMNEEHNKRLSDTVDKLLS 480
Cdd:COG5185 401 RGYAQE------ILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNElISELNKVMREADEESQSRLEEAYDEINR 474
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564332108 481 E-------SNERLQlHLKERMAALEDKNSLLREveNAKKQLEETQHDKDQLVLNIEALKAELEQMRLRGSS 544
Cdd:COG5185 475 SvrskkedLNEELT-QIESRVSTLKATLEKLRA--KLERQLEGVRSKLDQVAESLKDFMRARGYAHILALE 542
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
162-352 |
2.75e-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: 44.75 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 162 KALKSLFEHHKALDEKV---RERLRVALERCSLLEEELGATHKELMILKEQNSQKKALTEGMLDGNHEQENAPSTNGKRS 238
Cdd:COG4942 48 KEEKALLKQLAALERRIaalARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLS 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 239 SDGSLsheDLAKVLE-LQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDM 317
Cdd:COG4942 128 PEDFL---DAVRRLQyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARL 204
|
170 180 190
....*....|....*....|....*....|....*
gi 564332108 318 EERITTLEKRYLAAQREATSVHDLNDKLENEIANK 352
Cdd:COG4942 205 EKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
86-539 |
3.17e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 86 LPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALK 165
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEK 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 166 SLFEHHKAlDEKVRERLRVALERCSLLEEELGATHKELMILKEQNSQ----KKALTEgmldgnHEQENAPSTngkrssdg 241
Cdd:PRK03918 392 ELEELEKA-KEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcGRELTE------EHRKELLEE-------- 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 242 slSHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTArkDLIKS--EEMNTKLQREVREAMAQKEDMEE 319
Cdd:PRK03918 457 --YTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELA--EQLKEleEKLKKYNLEELEKKAEEYEKLKE 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 320 RITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVA 399
Cdd:PRK03918 533 KLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEK 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 400 ALSksgplssgssaAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEehNKRLSDTVDKLL 479
Cdd:PRK03918 613 ELE-----------REEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREE--YLELSRELAGLR 679
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 480 SESnERLQLHLKERMAALEDKNSLLREVENAKKQLEetqhdkdqlvlNIEALKAELEQMR 539
Cdd:PRK03918 680 AEL-EELEKRREEIKKTLEKLKEELEEREKAKKELE-----------KLEKALERVEELR 727
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
44-449 |
3.38e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 44 LEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRL 123
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 124 LLEHLECLVSRHERSLRmtvVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKEL 203
Cdd:COG4717 228 ELEQLENELEAAALEER---LKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 204 MILKEQNSQKKALTEGMLDGNHEQENAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELE 283
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 284 EDLdtarkdlikseemntklqREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDK--LENEIANKDSMHRQTED 361
Cdd:COG4717 385 EEL------------------RAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEeeLEEELEELEEELEELEE 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 362 KNRQLQERLELAEQKLQQtLRKAETLPEVEAELAQRVAALsksgplssgSSAAKEAKLLELTSK-LRKAEERHgnIEERL 440
Cdd:COG4717 447 ELEELREELAELEAELEQ-LEEDGELAELLQELEELKAEL---------RELAEEWAALKLALElLEEAREEY--REERL 514
|
....*....
gi 564332108 441 RQMEAQLEE 449
Cdd:COG4717 515 PPVLERASE 523
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
206-683 |
3.59e-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: 44.71 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 206 LKEQNSQKKALTEGMLDGNHEQENAPSTNGKRSSDGSLSHEDLAKVLELQEV-IDRQAREQSQMKERLASLSSHAAELEE 284
Cdd:pfam05483 284 LKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAqMEELNKAKAAHSFVVTEFEATTCSLEE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 285 DLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLE------KRYLAAQREATSVHDLNDKLENEIANKDS---- 354
Cdd:pfam05483 364 LLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEveleelKKILAEDEKLLDEKKQFEKIAEELKGKEQelif 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 355 MHRQTEDKNRQLQERLELAEQKLQQTLRKAETLP-EVEAELAQRVAALSKSGPLS-SGSSAAKEAKllELTSKLRKAEER 432
Cdd:pfam05483 444 LLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKtELEKEKLKNIELTAHCDKLLlENKELTQEAS--DMTLELKKHQED 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 433 HGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKK 512
Cdd:pfam05483 522 IINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKK 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 513 QLEETQHDKDQLVLNIEALK----AELEQMRLRGSSLHHGRPHLGSVPDFRFSVADGH-----VDAYSTSAVLRRPQKGR 583
Cdd:pfam05483 602 QIENKNKNIEELHQENKALKkkgsAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYqkeieDKKISEEKLLEEVEKAK 681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 584 LAAlrDEPSKVQtlNEQDWERAQQASVLANVAQAFESDVD-VSDGEDDRDTLLSSVDLLSPSGQADAQTLAMMLQEQLDA 662
Cdd:pfam05483 682 AIA--DEAVKLQ--KEIDKRCQHKIAEMVALMEKHKHQYDkIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLS 757
|
490 500
....*....|....*....|.
gi 564332108 663 INKEIRLIQEEKENTEQRAEE 683
Cdd:pfam05483 758 LKKQLEIEKEEKEKLKMEAKE 778
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
1082-1152 |
4.15e-04 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 39.95 E-value: 4.15e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564332108 1082 VLVWSNDRVIRWILSIGLKEFANNLIESGVHGALLALDETFDFsalalLLQIPTQNTQARAVLEREFNNLL 1152
Cdd:pfam07647 1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLRLTLED-----LKRLGITSVGHRRKILKKIQELK 66
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
298-541 |
4.48e-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: 44.71 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 298 EMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATsvhdlndKLENEIANKDSMHRQTEDKNRQLQERLELAEQKL 377
Cdd:pfam05483 212 EMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQIT-------EKENKMKDLTFLLEESRDKANQLEEKTKLQDENL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 378 QQTLRK----AETLPEVEAELAQRVA---ALSKSGPLSSGS----SAAKEAKLLELTsklrKAEERHGNIEERLRQMEAQ 446
Cdd:pfam05483 285 KELIEKkdhlTKELEDIKMSLQRSMStqkALEEDLQIATKTicqlTEEKEAQMEELN----KAKAAHSFVVTEFEATTCS 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 447 LEEKnqeLQRARQREKMNEEHNKRLSDTVDKLLSESNERLQL------HLKERMAALEDKNSLLREVENAKKQLEETQHD 520
Cdd:pfam05483 361 LEEL---LRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFknnkevELEELKKILAEDEKLLDEKKQFEKIAEELKGK 437
|
250 260
....*....|....*....|.
gi 564332108 521 KDQLVLNIEALKAELEQMRLR 541
Cdd:pfam05483 438 EQELIFLLQAREKEIHDLEIQ 458
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
177-545 |
4.70e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 44.46 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 177 KVRERLRV-ALERCSL------LEEELGATHKELMILKEQnsQKKALTEGMldgnheqenapSTNGKRSSDGSLSHEDLA 249
Cdd:PLN03229 334 KAAEKLRItAQELCRLqiadgiIPEPLGGAHADPSWTSQQ--IKIAINENM-----------DELGKMDTEELLKHRMLK 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 250 --KVLELQEVIDRQAREQSQMKERLASlSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQK--EDMEERITT-- 323
Cdd:PLN03229 401 frKIGGFQEGVPVDPERKVNMKKREAV-KTPVRELEGEVEKLKEQILKAKESSSKPSELALNEMIEKlkKEIDLEYTEav 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 324 ----LEKRyLAAQREATSVHDLNDKLENEIAnKDSMHRQTEDKNRQLQE---------RLE----------LAEQKLQQT 380
Cdd:PLN03229 480 iamgLQER-LENLREEFSKANSQDQLMHPVL-MEKIEKLKDEFNKRLSRapnylslkyKLDmlnefsrakaLSEKKSKAE 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 381 LRKAET---LPEV--EAELAQRVAALSKSGPLSSGSSAAK-EAKLLELTSKLRKAEE-------RHGNIE---ERLRQME 444
Cdd:PLN03229 558 KLKAEInkkFKEVmdRPEIKEKMEALKAEVASSGASSGDElDDDLKEKVEKMKKEIElelagvlKSMGLEvigVTKKNKD 637
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 445 AQLEEKNQELQRarQREKMNEEHNKRLSDTVDklLSESNERLQLhLKERMAaledKNSLLREVENAKK--QLEETQHDKD 522
Cdd:PLN03229 638 TAEQTPPPNLQE--KIESLNEEINKKIERVIR--SSDLKSKIEL-LKLEVA----KASKTPDVTEKEKieALEQQIKQKI 708
|
410 420
....*....|....*....|...
gi 564332108 523 QLVLNIEALKAELEQMRLRGSSL 545
Cdd:PLN03229 709 AEALNSSELKEKFEELEAELAAA 731
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
251-508 |
4.98e-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: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 251 VLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNT---------------------KLQREVRE 309
Cdd:pfam01576 140 ILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISdleerlkkeekgrqelekakrKLEGESTD 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 310 AMAQKEDMEERITTL-------EKRYLAAQ-----------------REATS-VHDLNDKLENEIAnkdsMHRQTEDKNR 364
Cdd:pfam01576 220 LQEQIAELQAQIAELraqlakkEEELQAALarleeetaqknnalkkiRELEAqISELQEDLESERA----ARNKAEKQRR 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 365 QLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSGPLSSGSSAAK--------EAKLLELTSKLRKAEERHGNI 436
Cdd:pfam01576 296 DLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQlqemrqkhTQALEELTEQLEQAKRNKANL 375
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564332108 437 EERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESN--ERLQLHLKERMAA----LEDKNSLLREVE 508
Cdd:pfam01576 376 EKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSesERQRAELAEKLSKlqseLESVSSLLNEAE 453
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
313-539 |
5.03e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 313 QKEDMEERITTLEKRYLAAQREATSvhdlNDKLENEIANKDSMHRQTEdkNRQLQERLELAEQKLQQTLRKAETLPEVE- 391
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTE----TGKAEEARKAEEAKKKAED--ARKAEEARKAEDARKAEEARKAEDAKRVEi 1156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 392 ---AELAQRvAALSKSGPLSSGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEE--------KNQELQRARQR 460
Cdd:PTZ00121 1157 arkAEDARK-AEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEarkaedakKAEAVKKAEEA 1235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 461 EKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSllREVENAKKQLEETQHD---KDQLVLNIEALKAELEQ 537
Cdd:PTZ00121 1236 KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA--RKADELKKAEEKKKADeakKAEEKKKADEAKKKAEE 1313
|
..
gi 564332108 538 MR 539
Cdd:PTZ00121 1314 AK 1315
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
281-537 |
5.15e-04 |
|
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: 44.07 E-value: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 281 ELEEDLDTARKDLIKSEEMNTKLqrEVREAMAQKEDMEERITTL----EKRYLAAQreatSVHDLNDKLENEIANKDSMH 356
Cdd:pfam06160 234 NVDKEIQQLEEQLEENLALLENL--ELDEAEEALEEIEERIDQLydllEKEVDAKK----YVEKNLPEIEDYLEHAEEQN 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 357 RQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALsksgplssgssAAKEAKLLELTSKLRKaeerhgnI 436
Cdd:pfam06160 308 KELKEELERVQQSYTLNENELERVRGLEKQLEELEKRYDEIVERL-----------EEKEVAYSELQEELEE-------I 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 437 EERLRQMEAQLEEKNQELQRARQREKmneEHNKRLsDTVDKLLSESNERLQlhlKERMAAL-EDKNSLLREVENakkQLE 515
Cdd:pfam06160 370 LEQLEEIEEEQEEFKESLQSLRKDEL---EAREKL-DEFKLELREIKRLVE---KSNLPGLpESYLDYFFDVSD---EIE 439
|
250 260
....*....|....*....|..
gi 564332108 516 ETQHDKDQLVLNIEALKAELEQ 537
Cdd:pfam06160 440 DLADELNEVPLNMDEVNRLLDE 461
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
176-454 |
5.46e-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: 44.43 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 176 EKVRERLRVALER-CSLLEEELGATHKELMILKEQ-NSQKKALTEGMLDGNHEQENAPSTNG----KRSSDGSL-----S 244
Cdd:pfam10174 449 ERIIERLKEQREReDRERLEELESLKKENKDLKEKvSALQPELTEKESSLIDLKEHASSLASsglkKDSKLKSLeiaveQ 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 245 HEDLAKVLELQEVIDRQAREQSQMKERLASLSSHaaeLEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTL 324
Cdd:pfam10174 529 KKEECSKLENQLKKAHNAEEAVRTNPEINDRIRL---LEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAEL 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 325 EKRYLAAQREATSvhdlndklenEIANKDSMhrQTEDKNRQLQErlelaeqkLQQTLRKAETLPEVEAE--LAQRVAALS 402
Cdd:pfam10174 606 ESLTLRQMKEQNK----------KVANIKHG--QQEMKKKGAQL--------LEEARRREDNLADNSQQlqLEELMGALE 665
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 564332108 403 KSgplssgsSAAKEAKLLELTSKLRKAEERHGNIE----ERLRQMEAQLEEKNQEL 454
Cdd:pfam10174 666 KT-------RQELDATKARLSSTQQSLAEKDGHLTnlraERRKQLEEILEMKQEAL 714
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
206-682 |
6.61e-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: 44.19 E-value: 6.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 206 LKEQNSQKKALTEGMLDGN-HEQENAPSTNGKRSSDGSLSHEDL-AKVLEL---QEVIDRQAREQSQMKErLASLSSHAA 280
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDqYTQLALMEFAKKKSLHGKAELLTLrSQLLTLctpCMPDTYHERKQVLEKE-LKHLREALQ 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 281 ELEEDLDTARKDLIKSEEmNTKLQREVREAMAQkedmEERITTLEKRyLAAQREATSVHDLNDKLENEIANKDSMHRQTE 360
Cdd:TIGR00618 237 QTQQSHAYLTQKREAQEE-QLKKQQLLKQLRAR----IEELRAQEAV-LEETQERINRARKAAPLAAHIKAVTQIEQQAQ 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 361 DKNRQLQERLELAEQKLQQTlrkaetlpevEAELAQRVAALSKSGPLSSGSSAAKEAKLLELTSKLRKAE-ERHGNIEER 439
Cdd:TIGR00618 311 RIHTELQSKMRSRAKLLMKR----------AAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREIsCQQHTLTQH 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 440 LRQMEAQLEEKNQELQRARQR-EKMNEEHNKRLSDTVD---------------KLLSESNERLQLHLKERMAALEDKNSL 503
Cdd:TIGR00618 381 IHTLQQQKTTLTQKLQSLCKElDILQREQATIDTRTSAfrdlqgqlahakkqqELQQRYAELCAAAITCTAQCEKLEKIH 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 504 LREVENAKKQLEETQHDKDQLVLNIEALKAELEQMRLRGSSLHhgRPHLGSVPDFrfsvADGHVDAYSTSAVLRRPQKG- 582
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEP--CPLCGSCIHP----NPARQDIDNPGPLTRRMQRGe 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 583 -RLAALRDEPSKV----QTLNEQDWERAQQASVLANVAQAFESDVDVSdgEDDRDTLLSSVDLLSPSGQADAQTLAMMLQ 657
Cdd:TIGR00618 535 qTYAQLETSEEDVyhqlTSERKQRASLKEQMQEIQQSFSILTQCDNRS--KEDIPNLQNITVRLQDLTEKLSEAEDMLAC 612
|
490 500 510
....*....|....*....|....*....|...
gi 564332108 658 E--------QLDAINKEIRLIQEEKENTEQRAE 682
Cdd:TIGR00618 613 EqhallrklQPEQDLQDVRLHLQQCSQELALKL 645
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
253-460 |
7.59e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 7.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 253 ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRY---- 328
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELaell 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 329 ---------------------LAAQREATSVHDLNDKLENEIankdsmhRQTEDKNRQLQERLELAEQKLQQtlrkaetL 387
Cdd:COG4942 111 ralyrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQA-------EELRADLAELAALRAELEAERAE-------L 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564332108 388 PEVEAELAQRVAALSKsgplssgSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQR 460
Cdd:COG4942 177 EALLAELEEERAALEA-------LKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
177-557 |
7.60e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.06 E-value: 7.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 177 KVRERLRVALERCSLLEEELGATHKEL------MILKEQNSQKKALTEGMLDGNHEQE----NAPSTNGKRSSDGSL-SH 245
Cdd:pfam12128 608 KAEEALQSAREKQAAAEEQLVQANGELekasreETFARTALKNARLDLRRLFDEKQSEkdkkNKALAERKDSANERLnSL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 246 EDLAKVLELQ-----EVIDRQAREQSQmkERLASLSshaaELEEDLDtARKDLIKSEemntKLQREVREAMAQKEDMEER 320
Cdd:pfam12128 688 EAQLKQLDKKhqawlEEQKEQKREART--EKQAYWQ----VVEGALD-AQLALLKAA----IAARRSGAKAELKALETWY 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 321 ITTLEKRYLAAQREAtsvhdlndKLENEIANkdsMHRQTEDKNRQLQERLE----LAEQKLQQTLRKAETLPEVEaelaq 396
Cdd:pfam12128 757 KRDLASLGVDPDVIA--------KLKREIRT---LERKIERIAVRRQEVLRyfdwYQETWLQRRPRLATQLSNIE----- 820
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 397 rvaalsksgplssgsSAAKEAKLlELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQR-EKMNEEHnkrlsdtv 475
Cdd:pfam12128 821 ---------------RAISELQQ-QLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEmSKLATLK-------- 876
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 476 dklLSESNERLQLHLKERMAALED-KNSLLREVENAKKQLEE-----TQHDKDQLVLNIEALKAELEQMRLRGSSLHHGR 549
Cdd:pfam12128 877 ---EDANSEQAQGSIGERLAQLEDlKLKRDYLSESVKKYVEHfknviADHSGSGLAETWESLREEDHYQNDKGIRLLDYR 953
|
....*...
gi 564332108 550 PHLGSVPD 557
Cdd:pfam12128 954 KLVPYLEQ 961
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
296-536 |
8.99e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 8.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 296 SEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQ 375
Cdd:COG4372 1 GDRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 376 KLQQTLRKAETLPEVEAELAQRVAALSKsgplssgSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQ 455
Cdd:COG4372 81 ELEELNEQLQAAQAELAQAQEELESLQE-------EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 456 RARQREKMNEEHNKRLSDTVDKL-LSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVLNIEALKAE 534
Cdd:COG4372 154 ELEEQLESLQEELAALEQELQALsEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233
|
..
gi 564332108 535 LE 536
Cdd:COG4372 234 AL 235
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
154-538 |
1.21e-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: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 154 VSSEVEVLKALKSLFEHHKALDEKVRErLRVALERcslLEEELGATHKELMILKEQNSQKKALTEGMLDGNHEQenapst 233
Cdd:pfam01576 670 VSSKDDVGKNVHELERSKRALEQQVEE-MKTQLEE---LEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQ------ 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 234 ngkrssdGSLSHEDLAK-VLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTAR-------KDLIKSEEMNTKLQR 305
Cdd:pfam01576 740 -------GEEKRRQLVKqVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANkgreeavKQLKKLQAQMKDLQR 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 306 EVREAMAQKEDM-------EERITTLEKRYL-------AAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLE 371
Cdd:pfam01576 813 ELEEARASRDEIlaqskesEKKLKNLEAELLqlqedlaASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIA 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 372 LAEQKLQQTLRKAETLPEVEAELAQRV----AALSKSGPLSSGSSAAKE----------AKLLELTSKLR-KAEERHGNI 436
Cdd:pfam01576 893 QLEEELEEEQSNTELLNDRLRKSTLQVeqltTELAAERSTSQKSESARQqlerqnkelkAKLQEMEGTVKsKFKSSIAAL 972
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 437 EERLRQMEAQLEEKNQELQRARQREKMNEehnKRLSDTVdkLLSESNERLQLHLKERMaalEDKNSLLREVenaKKQLEE 516
Cdd:pfam01576 973 EAKIAQLEEQLEQESRERQAANKLVRRTE---KKLKEVL--LQVEDERRHADQYKDQA---EKGNSRMKQL---KRQLEE 1041
|
410 420
....*....|....*....|..
gi 564332108 517 TQHDKDQLVLNIEALKAELEQM 538
Cdd:pfam01576 1042 AEEEASRANAARRKLQRELDDA 1063
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
45-452 |
1.53e-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: 43.02 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 45 EERDRLLD-------TLRETQETLALTQGKLHEVGHERDSLQRQlNTALPQEFAALTKELNVCREQLLER------EEEI 111
Cdd:COG3096 278 NERRELSEralelrrELFGARRQLAEEQYRLVEMARELEELSAR-ESDLEQDYQAASDHLNLVQTALRQQekieryQEDL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 112 AELkAERnntrlLLEHLECLVSRHERSLRmtvvkRQAQSPAgvsSEVEVlKALKS-LFEHHKALDE---------KVRER 181
Cdd:COG3096 357 EEL-TER-----LEEQEEVVEEAAEQLAE-----AEARLEA---AEEEV-DSLKSqLADYQQALDVqqtraiqyqQAVQA 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 182 LRVALERCSLLEEELGATHKELMILKEQnsqKKALTEGMLDGNHeqenapstngkRSSDGSLSHEDLAKVLELQEVID-- 259
Cdd:COG3096 422 LEKARALCGLPDLTPENAEDYLAAFRAK---EQQATEEVLELEQ-----------KLSVADAARRQFEKAYELVCKIAge 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 260 --------------RQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAmaqkEDMEERITTLE 325
Cdd:COG3096 488 versqawqtarellRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAA----EELEELLAELE 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 326 krylaAQREatsvhDLNDKLENEIANKDSMHRQTEdknrQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAalsksg 405
Cdd:COG3096 564 -----AQLE-----ELEEQAAEAVEQRSELRQQLE----QLRARIKELAARAPAWLAAQDALERLREQSGEALA------ 623
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 564332108 406 plssgSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQ 452
Cdd:COG3096 624 -----DSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQ 665
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
246-484 |
1.67e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.61 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 246 EDLAKVLE-LQE-----VIDRQAREQSqmkERLASLSSHAAELEEDLDTARKDLiKSEEMNTKLQREVReamaqKEDMEE 319
Cdd:PRK05771 16 SYKDEVLEaLHElgvvhIEDLKEELSN---ERLRKLRSLLTKLSEALDKLRSYL-PKLNPLREEKKKVS-----VKSLEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 320 RITTLEKRYLAAQREAtsvhdlnDKLENEIANKDSMHRQTEDKNRQLQ--ERLELAEQKLQQT--------LRKAETLPE 389
Cdd:PRK05771 87 LIKDVEEELEKIEKEI-------KELEEEISELENEIKELEQEIERLEpwGNFDLDLSLLLGFkyvsvfvgTVPEDKLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 390 VEAELAQRVAALSKSGPLSSGSSAAKEAKLLELTSK-LRKAEER------HGNIEERLRQMEAQLEEKNQELQRARQR-E 461
Cdd:PRK05771 160 LKLESDVENVEYISTDKGYVYVVVVVLKELSDEVEEeLKKLGFErleleeEGTPSELIREIKEELEEIEKERESLLEElK 239
|
250 260
....*....|....*....|...
gi 564332108 462 KMNEEHNKRLSDTVDKLLSESNE 484
Cdd:PRK05771 240 ELAKKYLEELLALYEYLEIELER 262
|
|
| SAM_SARM1-like_repeat1 |
cd09501 |
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
1004-1051 |
1.82e-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: 1.82e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 564332108 1004 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSF 1051
Cdd:cd09501 11 TWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLRKRF 58
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
911-973 |
1.88e-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: 1.88e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564332108 911 QWDGPTVVVWLElWVGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQ 973
Cdd:pfam00536 2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQ 61
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
238-510 |
2.35e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 238 SSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEED-LDTARKDLIKSEEMntklQREVREAMAQKED 316
Cdd:PRK01156 475 NEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNkIESARADLEDIKIK----INELKDKHDKYEE 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 317 MEERITTLEKRYLAAQRE----ATSVHDLNDkLENEIANKDSMHRQTEDKNRQLQE---RLELAEQKLQQTLRKAET--- 386
Cdd:PRK01156 551 IKNRYKSLKLEDLDSKRTswlnALAVISLID-IETNRSRSNEIKKQLNDLESRLQEieiGFPDDKSYIDKSIREIENean 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 387 -----LPEVEAELAQRVAALSKSGPLSSGSSAAK--EAKLLELTSKLRKaeerhgnIEERLRQMEAQLEEKNQELQRARQ 459
Cdd:PRK01156 630 nlnnkYNEIQENKILIEKLRGKIDNYKKQIAEIDsiIPDLKEITSRIND-------IEDNLKKSRKALDDAKANRARLES 702
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 564332108 460 REKMNEEHNKRLSDTVdkllSESNERLqlhlkERMAALEDKNSLLREVENA 510
Cdd:PRK01156 703 TIEILRTRINELSDRI----NDINETL-----ESMKKIKKAIGDLKRLREA 744
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
44-688 |
2.60e-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: 42.36 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 44 LEERDRLLDTLRETQETLALTQGKLHE-----VGHERDSLQRQLN------TALPQEFAALTKELN--------VCREQL 104
Cdd:TIGR02169 210 AERYQALLKEKREYEGYELLKEKEALErqkeaIERQLASLEEELEklteeiSELEKRLEEIEQLLEelnkkikdLGEEEQ 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 105 LEREEEIAELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSP--AGVSSEVEVLKALKSLFEHHKALDEKVRERL 182
Cdd:TIGR02169 290 LRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAeiEELEREIEEERKRRDKLTEEYAELKEELEDL 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 183 RVALERcslLEEELGATHKELMILKEQnsqKKALTEGMLDGNHEQENAPSTNGKRSSDGSLSHEDLA----KVLELQEVI 258
Cdd:TIGR02169 370 RAELEE---VDKEFAETRDELKDYREK---LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAgieaKINELEEEK 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 259 DRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERIT---------------- 322
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRggraveevlkasiqgv 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 323 --------TLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDK---------NRQLQERLELAEQKLQQTLRKAE 385
Cdd:TIGR02169 524 hgtvaqlgSVGERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKagratflplNKMRDERRDLSILSEDGVIGFAV 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 386 TLPEVEAELAQRVAALSKSGPLSSGSSAAK-----------EAKLLE----LTSKLRKAEERHGN---IEERLRQMEAQL 447
Cdd:TIGR02169 604 DLVEFDPKYEPAFKYVFGDTLVVEDIEAARrlmgkyrmvtlEGELFEksgaMTGGSRAPRGGILFsrsEPAELQRLRERL 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 448 EEKNQELQRARQREkmneEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQHDkdqlvln 527
Cdd:TIGR02169 684 EGLKRELSSLQSEL----RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE------- 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 528 IEALKAELEQMRLRgsslhhgrphlgsvpdfrfsvadghVDAYSTSAVLRRPQKGRLAAlRDEPSKVQTLNEQdwERAQQ 607
Cdd:TIGR02169 753 IENVKSELKELEAR-------------------------IEELEEDLHKLEEALNDLEA-RLSHSRIPEIQAE--LSKLE 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 608 ASVLANVAQAFESDVDVSDGEDDRDTLLSSVdllspsgqADAQTLAMMLQEQLDAINKEIRLIQEEKENTEQRAEEIESR 687
Cdd:TIGR02169 805 EEVSRIEARLREIEQKLNRLTLEKEYLEKEI--------QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA 876
|
.
gi 564332108 688 V 688
Cdd:TIGR02169 877 L 877
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
416-530 |
2.69e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 40.64 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 416 EAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLqlhlkERMA 495
Cdd:pfam12072 70 ERELKERRNELQRQERRLLQKEETLDRKDESLEKKEESLEKKEKELEAQQQQLEEKEEELEELIEEQRQEL-----ERIS 144
|
90 100 110
....*....|....*....|....*....|....*...
gi 564332108 496 AL---EDKNSLLREVEnakkqlEETQHDKDQLVLNIEA 530
Cdd:pfam12072 145 GLtseEAKEILLDEVE------EELRHEAAVMIKEIEE 176
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
295-534 |
3.71e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 41.71 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 295 KSEEMNTKLQ------REVREAMAQKEDMEERITTLEKRYLAAqreatsvHDLNDKLENEIAN-KDSMHRQTEDKN--RQ 365
Cdd:PRK10246 312 QIEEVNTRLQstmalrARIRHHAAKQSAELQAQQQSLNTWLAE-------HDRFRQWNNELAGwRAQFSQQTSDREqlRQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 366 LQERLELAEQKLQQTlrKAETLPEVEAELAQRVAALSKSGPLSS------GSSAAKEAKLLELTSKLRKAEERHGNIEER 439
Cdd:PRK10246 385 WQQQLTHAEQKLNAL--PAITLTLTADEVAAALAQHAEQRPLRQrlvalhGQIVPQQKRLAQLQVAIQNVTQEQTQRNAA 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 440 LRQMEAQLEEKNQELQRAR------QREKMNEEHNKRLS----------------DTVDKLLSESNERLQLHLKERMAAL 497
Cdd:PRK10246 463 LNEMRQRYKEKTQQLADVKticeqeARIKDLEAQRAQLQagqpcplcgstshpavEAYQALEPGVNQSRLDALEKEVKKL 542
|
250 260 270
....*....|....*....|....*....|....*...
gi 564332108 498 EDKNSLLR-EVENAKKQLEETQHDKDQLVLNIEALKAE 534
Cdd:PRK10246 543 GEEGAALRgQLDALTKQLQRDESEAQSLRQEEQALTQQ 580
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
250-396 |
3.71e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 250 KVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQR--EVREAMAQKEDMEERITTLEKR 327
Cdd:COG3206 206 GLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSAR 285
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 328 YLAAQREATSVHDLNDKLENEIAN-KDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQ 396
Cdd:COG3206 286 YTPNHPDVIALRAQIAALRAQLQQeAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
|
|
| Stathmin |
pfam00836 |
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ... |
404-523 |
4.13e-03 |
|
Stathmin family; The Stathmin family of proteins play an important role in the regulation of the microtubule cytoskeleton. They regulate microtubule dynamics by promoting depolymerization of microtubules and/or preventing polymerization of tubulin heterodimers.
Pssm-ID: 459956 [Multi-domain] Cd Length: 136 Bit Score: 38.87 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 404 SGPLSSGSSAAKEAKLLELTSKLRKAEERHGNIEErlrQMEAQLEEKNQELQRARQreKMNEEHNKRLSDTVDKLlsesN 483
Cdd:pfam00836 29 APPKLSLSPKKKDSSLEEIQKKLEAAEERRKSLEA---QKLKQLAEKREKEEEALQ--KADEENNNFSKMAEEKL----K 99
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 564332108 484 ERLQLHLKERMAALEDKNSLLREVEnakKQLEETQHDKDQ 523
Cdd:pfam00836 100 QKMEAYKENREAQIAALKEKLKEKE---KHVEEVRKNKEQ 136
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
342-471 |
4.48e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 342 NDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRvaalsksgplssgssAAKEAKlle 421
Cdd:PRK00409 515 KEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEE---------------AEKEAQ--- 576
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 564332108 422 ltSKLRKAEERHGNIEERLRQMEAQL--EEKNQELQRARQR-EKMNEEHNKRL 471
Cdd:PRK00409 577 --QAIKEAKKEADEIIKELRQLQKGGyaSVKAHELIEARKRlNKANEKKEKKK 627
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
272-538 |
4.91e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.97 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 272 LASLSSHAAELEEDLDT-----ARKDLIKSEEMNTKLQ---REVREAMA----QKEDMEERITTLEKRY------LAAQR 333
Cdd:PRK04778 81 LPDIEEQLFEAEELNDKfrfrkAKHEINEIESLLDLIEediEQILEELQelleSEEKNREEVEQLKDLYrelrksLLANR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 334 EatSVHDLNDKLENEIANKDSMHRQ----TEDKN-RQLQERLELAEQKLQQTLRKAETLPEVEAELAQRV-AALSKsgpL 407
Cdd:PRK04778 161 F--SFGPALDELEKQLENLEEEFSQfvelTESGDyVEAREILDQLEEELAALEQIMEEIPELLKELQTELpDQLQE---L 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 408 SSGSSAAKEAKL----LELTSKLRKAEERHGNIEERLRQME-AQLEEKNQELQR--------------ARQREkmnEEHN 468
Cdd:PRK04778 236 KAGYRELVEEGYhldhLDIEKEIQDLKEQIDENLALLEELDlDEAEEKNEEIQEridqlydilerevkARKYV---EKNS 312
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564332108 469 KRLSDTVDKlLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVLNIEA-------LKAELEQM 538
Cdd:PRK04778 313 DTLPDFLEH-AKEQNKELKEEIDRVKQSYTLNESELESVRQLEKQLESLEKQYDEITERIAEqeiayseLQEELEEI 388
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
222-540 |
4.92e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.43 E-value: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 222 DGNHEQENAPSTNG---KRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEE 298
Cdd:PLN02939 70 DENGQLENTSLRTVmelPQKSTSSDDDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 299 MNTKLQREVREAMAQKEDMEERITTLEKRY--------LAAQrEATSVHDLNDKLENeiANKDSMHRQTEDKNRQLQERL 370
Cdd:PLN02939 150 ARLQALEDLEKILTEKEALQGKINILEMRLsetdarikLAAQ-EKIHVEILEEQLEK--LRNELLIRGATEGLCVHSLSK 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 371 ELAEQKLQQTLRKA------ETLPEVeAELAQRVAALSKsgplssgSSAAKEAKLLELTSKLRKAEERHGNIEErlRQME 444
Cdd:PLN02939 227 ELDVLKEENMLLKDdiqflkAELIEV-AETEERVFKLEK-------ERSLLDASLRELESKFIVAQEDVSKLSP--LQYD 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 445 AqLEEKNQELQRARQREKMNEEH-------NKRLSDTVDKL---LSESN------ERLQLhLKERMAALEDKnsLLREVE 508
Cdd:PLN02939 297 C-WWEKVENLQDLLDRATNQVEKaalvldqNQDLRDKVDKLeasLKEANvskfssYKVEL-LQQKLKLLEER--LQASDH 372
|
330 340 350
....*....|....*....|....*....|..
gi 564332108 509 NAKKQLEETQHDKDQLVLNIEALKAELEQMRL 540
Cdd:PLN02939 373 EIHSYIQLYQESIKEFQDTLSKLKEESKKRSL 404
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
344-535 |
5.05e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.81 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 344 KLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETlpeveaELAqRVAALSKsgplssgssAAKEAKLLELT 423
Cdd:COG1842 41 EARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKGRE------DLA-REALERK---------AELEAQAEALE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 424 SKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNeEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSL 503
Cdd:COG1842 105 AQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAA-KAQEKVNEALSGIDSDDATSALERMEEKIEEMEARAEA 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 564332108 504 LREVENAK---KQLEETQHDK---DQLvlniEALKAEL 535
Cdd:COG1842 184 AAELAAGDsldDELAELEADSeveDEL----AALKAKM 217
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
284-539 |
5.43e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 284 EDLDTARKDLIKSEEMN----TKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQT 359
Cdd:TIGR04523 78 KILEQQIKDLNDKLKKNkdkiNKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 360 EDKNRQLQERLELAEQKL----QQTLRKAETLPEVEAELAQRVAALSKsgplssgsSAAKEAKLLELTSKLRKAEERHGN 435
Cdd:TIGR04523 158 NNKYNDLKKQKEELENELnlleKEKLNIQKNIDKIKNKLLKLELLLSN--------LKKKIQKNKSLESQISELKKQNNQ 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 436 IEERLRQMEAQLEEKNQELQRARQREKM----NEEHNKRLSD------TVDKLLSESNERLQlHLKERMAALEDK----- 500
Cdd:TIGR04523 230 LKDNIEKKQQEINEKTTEISNTQTQLNQlkdeQNKIKKQLSEkqkeleQNNKKIKELEKQLN-QLKSEISDLNNQkeqdw 308
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 564332108 501 -NSLLREVENAKKQLEETQHDKDQLVLNIEALKAELEQMR 539
Cdd:TIGR04523 309 nKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLK 348
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
177-546 |
6.35e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.83 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 177 KVRERLRVALE-RCSLLEEELGAT---HKELMILKEQNSQKKALTEgMLDGNHEQENAPSTNGKRSSDGSLSHEDLAKVL 252
Cdd:COG5022 831 KLRETEEVEFSlKAEVLIQKFGRSlkaKKRFSLLKKETIYLQSAQR-VELAERQLQELKIDVKSISSLKLVNLELESEII 909
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 253 ELQEVIDRQAREQSQMKerlaslSSHAAELEEDLDTArkDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEkrylaaq 332
Cdd:COG5022 910 ELKKSLSSDLIENLEFK------TELIARLKKLLNNI--DLEEGPSIEYVKLPELNKLHEVESKLKETSEEYE------- 974
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 333 reatsvhDLNDKLENEIANKDSMHRQTEDKNRQLQERLElaEQKLQQtlRKAETLPEVEAELAQRVAALSKsgPLSSGSS 412
Cdd:COG5022 975 -------DLLKKSTILVREGNKANSELKNFKKELAELSK--QYGALQ--ESTKQLKELPVEVAELQSASKI--ISSESTE 1041
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 413 AAKEAKLLELTSKLRKAEERH-GNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNER------ 485
Cdd:COG5022 1042 LSILKPLQKLKGLLLLENNQLqARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLqfivaq 1121
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564332108 486 -LQLHLKERMAALedKNSLLREVENAKKQLEETQHDKDQL--VLNIEAL-----KAELEQMRLRGSSLH 546
Cdd:COG5022 1122 mIKLNLLQEISKF--LSQLVNTLEPVFQKLSVLQLELDGLfwEANLEALpspppFAALSEKRLYQSALY 1188
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
281-456 |
8.25e-03 |
|
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: 39.28 E-value: 8.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 281 ELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERIT-TLEKRYLAAQREATSVhdlNDKLENEIANKDSMHRQT 359
Cdd:pfam04012 33 DMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQaALTKGNEELAREALAE---KKSLEKQAEALETQLAQQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 360 EDKNRQLQERLELAEQKLQQTLRKAETLpEVEAELAQRVAALSKS-GPLSSGSSAAK----EAKLLELTSKLRKAEERHG 434
Cdd:pfam04012 110 RSAVEQLRKQLAALETKIQQLKAKKNLL-KARLKAAKAQEAVQTSlGSLSTSSATDSferiEEKIEEREARADAAAELAS 188
|
170 180
....*....|....*....|....
gi 564332108 435 --NIEERLRQMEAQLEEKNQELQR 456
Cdd:pfam04012 189 avDLDAKLEQAGIQMEVSEDVLAR 212
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
176-337 |
8.45e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 8.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 176 EKVRERLRVALERCSLLEEELGATHKELMILKEQNSQKKALTEGMLDGNHEQENAPST-----NGKRSSD--------GS 242
Cdd:COG3883 47 EELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYldvllGSESFSDfldrlsalSK 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 243 LSHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERIT 322
Cdd:COG3883 127 IADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
170
....*....|....*
gi 564332108 323 TLEKRYLAAQREATS 337
Cdd:COG3883 207 AAEAAAAAAAAAAAA 221
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
255-403 |
8.80e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.95 E-value: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 255 QEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRyLAAQRe 334
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQE-LDSEK- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 335 ATSVHDLndkleneiankdsmhRQTEDKNRQ----------LQERLELAEQKLQQTLRKAETL-PEVEAELAQRVAALSK 403
Cdd:PRK09039 130 QVSARAL---------------AQVELLNQQiaalrrqlaaLEAALDASEKRDRESQAKIADLgRRLNVALAQRVQELNR 194
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
255-471 |
8.84e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 40.02 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 255 QEVIDRQAREQSQMKERLASLSShaaELEEDLDTARKDLIKSEEmNTKLQREVREAMAQkEDMEErittleKRYLAAQRE 334
Cdd:pfam15558 54 LLLQQSQEQWQAEKEQRKARLGR---EERRRADRREKQVIEKES-RWREQAEDQENQRQ-EKLER------ARQEAEQRK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 335 ATSVHDLNDKLENEiankdsmHRQTEDKNRQLQERLELAEQKLQqtLRKAETLPEVEAE-LAQRVAALSKSGPLSSGSSA 413
Cdd:pfam15558 123 QCQEQRLKEKEEEL-------QALREQNSLQLQERLEEACHKRQ--LKEREEQKKVQENnLSELLNHQARKVLVDCQAKA 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 414 AKEAKLLELTSKLRKAEERH-GNIEERLRQMEAQLEEKNQELQRARQR-EKMNEEHNKRL 471
Cdd:pfam15558 194 EELLRRLSLEQSLQRSQENYeQLVEERHRELREKAQKEEEQFQRAKWRaEEKEEERQEHK 253
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
264-401 |
9.14e-03 |
|
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: 38.73 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332108 264 EQSQMKERLASLSSHAAELEEDLDTARKD---LIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAA-QREATSVH 339
Cdd:pfam13851 55 ENKRLTEPLQKAQEEVEELRKQLENYEKDkqsLKNLKARLKVLEKELKDLKWEHEVLEQRFEKVERERDELyDKFEAAIQ 134
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564332108 340 DLNDK-------LENEIANkdsMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAAL 401
Cdd:pfam13851 135 DVQQKtglknllLEKKLQA---LGETLEKKEAQLNEVLAAANLDPDALQAVTEKLEDVLESKNQLIKDL 200
|
|
| |
