|
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 ... |
944-1009 |
1.15e-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: 152.24 E-value: 1.15e-43
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281306779 944 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 1009
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 ... |
827-897 |
3.23e-42 |
|
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: 148.48 E-value: 3.23e-42
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281306779 827 FAQWDGPTVVSWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEMVSLT 897
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 ... |
1029-1100 |
5.49e-41 |
|
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: 144.77 E-value: 5.49e-41
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281306779 1029 DVLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALVLQIPTQNTQARQVMEREFNNLL 1100
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 ... |
948-1007 |
1.40e-30 |
|
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: 114.94 E-value: 1.40e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 948 WIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1007
Cdd:cd09495 1 WWVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLVHLKVTSQLHHLSLKCGIHVLH 60
|
|
| SAM_liprin-kazrin_repeat3 |
cd09496 |
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of ... |
1037-1098 |
6.25e-27 |
|
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: 104.54 E-value: 6.25e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281306779 1037 QVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALVLQIPTQNTQARQVMEREFNN 1098
Cdd:cd09496 1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETEFNN 62
|
|
| SAM_liprin-kazrin_repeat1 |
cd09494 |
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
834-892 |
5.03e-25 |
|
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: 98.84 E-value: 5.03e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 281306779 834 TVVSWLELWVGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQE 892
Cdd:cd09494 1 RVCAWLEDFGLMP-MYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
|
|
| SAM_kazrin_repeat3 |
cd09570 |
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin ... |
1029-1100 |
1.80e-19 |
|
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: 83.65 E-value: 1.80e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281306779 1029 DVLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALVLQIPTQNTQARQVMEREFNNLL 1100
Cdd:cd09570 1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
|
|
| SAM_kazrin_repeat2 |
cd09567 |
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ... |
943-1007 |
4.39e-16 |
|
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: 73.60 E-value: 4.39e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281306779 943 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1007
Cdd:cd09567 1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
|
|
| SAM_liprin-beta1,2_repeat2 |
cd09566 |
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ... |
943-1007 |
5.25e-16 |
|
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: 73.50 E-value: 5.25e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281306779 943 DMNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLrVHLKMVDSFHRTSLQYGIMCLK 1007
Cdd:cd09566 1 KLDTHWV-LRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDL-LHLKVTSALHHASIRRGIQVLR 63
|
|
| SAM_liprin-beta1,2_repeat3 |
cd09569 |
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ... |
1029-1100 |
5.96e-16 |
|
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: 73.64 E-value: 5.96e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281306779 1029 DVLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALVLQIPTQNTQARQVMEREFNNLL 1100
Cdd:cd09569 1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
|
|
| SAM_kazrin_repeat1 |
cd09564 |
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ... |
828-892 |
1.19e-15 |
|
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: 72.48 E-value: 1.19e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281306779 828 AQWDGPTVVSWLELWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQE 892
Cdd:cd09564 2 SRWKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
227-472 |
4.96e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 80.37 E-value: 4.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 227 RVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRYL 306
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 307 AAQ----REATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAE 382
Cdd:COG1196 313 ELEerleELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 383 ERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSE----- 457
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAElleea 472
|
250 260
....*....|....*....|
gi 281306779 458 -----EIEKLRQEVDQLKGR 472
Cdd:COG1196 473 alleaALAELLEELAEAAAR 492
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
943-1007 |
6.18e-14 |
|
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: 67.68 E-value: 6.18e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281306779 943 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1007
Cdd:pfam00536 1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
159-492 |
4.30e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.20 E-value: 4.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 159 EHHKALDEKVRER-LRAALERVTTLEEQLAGAHQQVSALQqgAGIRDGVAEEEEtvdlgpkrlwkdDTGRVEELQGLLEK 237
Cdd:COG1196 213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELE--AELEELEAELAE------------LEAELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 238 QNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHD 317
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 318 LNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERhgnIEEHLRQLEG 397
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE---LEEALAELEE 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 398 QLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRlsEEIEKLRQEVDQLKGRGGPFV 477
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR--LLLLLEAEADYEGFLEGVKAA 513
|
330
....*....|....*
gi 281306779 478 DGIHSRSHVGSTTDV 492
Cdd:COG1196 514 LLLAGLRGLAGAVAV 528
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
85-469 |
1.51e-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: 72.40 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 85 RELSMCREQLLEREEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKrqaqspsgvssevevLKALKSLFEHHKAL 164
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQ---------------ISALRKDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 165 DEKVRERLRAALERVTTLEEQLAGAHQQVsalqqgAGIRDGVAEEEEtvdlgpkrlwkddtgRVEELQGLLEKQNYELSQ 244
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERL------EEAEEELAEAEA---------------EIEELEAQIEQLKEELKA 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 245 ARERLVTLSATVTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLEN 324
Cdd:TIGR02168 801 LREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 325 ELANkeslhrqceekarhLQELLEVAEQKLQQTMrkaETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQ 404
Cdd:TIGR02168 881 ERAS--------------LEEALALLRSELEELS---EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281306779 405 elaRVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKER-------MAALEEKGRLSEEIEKLRQEVDQL 469
Cdd:TIGR02168 944 ---RLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIkelgpvnLAAIEEYEELKERYDFLTAQKEDL 1012
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
218-472 |
4.02e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 70.87 E-value: 4.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 218 KRLWKDDTGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEE----LSGKHQRDLREALAQKED 293
Cdd:TIGR02169 155 RRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERyqalLKEKREYEGYELLKEKEA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 294 MEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHL--QELLEVAEQ--KLQQTMRKAE-TLPEVE 368
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeEEQLRVKEKigELEAEIASLErSIAEKE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 369 AELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQ-----REKMN------EDHNKRLSDTVDRL------L 431
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEeyaelKEELEdlraelEEVDKEFAETRDELkdyrekL 394
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 281306779 432 SESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGR 472
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
19-409 |
1.23e-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: 69.32 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 19 GADADANFEQLMVNML-----DEREKLLESL----------RESQETLVATQ---SRLQDALHERD-QLQR-HLNSALPQ 78
Cdd:TIGR02168 134 GKRSYSIIEQGKISEIieakpEERRAIFEEAagiskykerrKETERKLERTRenlDRLEDILNELErQLKSlERQAEKAE 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 79 EFATLTRELSmcREQLLEREEEISELKAERNNTRLLLEHLECLVSRHERSLRMTvvkrqaqspsgvSSEVEVLKALKSlf 158
Cdd:TIGR02168 214 RYKELKAELR--ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQEL------------EEKLEELRLEVS-- 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 159 EHHKALDEkVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGIRDGVAEEEETVDLGPKRLWKDDTGRVEELQGLLEKQ 238
Cdd:TIGR02168 278 ELEEEIEE-LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESL 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 239 NYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATS---- 314
Cdd:TIGR02168 357 EAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaelk 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 315 -IHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKaetlpevEAELSQRIAALTKAEERHGNIEEHLR 393
Cdd:TIGR02168 437 eLQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE-------LAQLQARLDSLERLQENLEGFSEGVK 509
|
410
....*....|....*.
gi 281306779 394 QLEGQLEEKNQELARV 409
Cdd:TIGR02168 510 ALLKNQSGLSGILGVL 525
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
241-469 |
1.45e-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: 69.32 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 241 ELSQARERLVTLSatVTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQRE----ATSIH 316
Cdd:TIGR02168 221 ELRELELALLVLR--LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyalANEIS 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 317 DL-------NDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIE 389
Cdd:TIGR02168 299 RLeqqkqilRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 390 EHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQ-LHLKERMAALEEKGRLSEEIEKLRQEVDQ 468
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKkLEEAELKELQAELEELEEELEELQEELER 458
|
.
gi 281306779 469 L 469
Cdd:TIGR02168 459 L 459
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
20-472 |
1.79e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 20 ADADANFEQLMVNMLDEREKLLESLRESQETLVATQSRLQDALHERDQLQRHLNSALpQEFATLTRELSMCREQLLEREE 99
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA-EELLEALRAAAELAAQLEELEE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 100 EISELKAERNNTRLLLEHLEclvSRHERSLRMTVVKRQAQSpsgvsSEVEVLKALKSLFEHHKALDEKVRERLRAALERV 179
Cdd:COG1196 408 AEEALLERLERLEEELEELE---EALAELEEEEEEEEEALE-----EAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 180 TTLEEQLAGAHQQVSALQQGAGIRDGVAEEEETVDLgpKRLWKDDTGRVEELQGLLEKqnYELSQARERLVTLSATVTEL 259
Cdd:COG1196 480 AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL--LAGLRGLAGAVAVLIGVEAA--YEAALEAALAAALQNIVVED 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 260 EEDLGTARRDLIKSEE-------LSGKHQRDLREALAQKEDMEERITTL--EKRYLAAQREATSIHDLNDKLENE-LANK 329
Cdd:COG1196 556 DEVAAAAIEYLKAAKAgratflpLDKIRARAALAAALARGAIGAAVDLVasDLREADARYYVLGDTLLGRTLVAArLEAA 635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 330 ESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHgniEEHLRQLEGQLEEKNQELARV 409
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE---ELELEEALLAEEEEERELAEA 712
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281306779 410 RQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGR 472
Cdd:COG1196 713 EEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
38-469 |
1.87e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.53 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 38 EKLLESLRESQETLVATQSRLQDA-LHERdqlqrhLNsALPQEFATLTRElsmcreqllereeeISELKAERNNTRLLLE 116
Cdd:PRK02224 179 ERVLSDQRGSLDQLKAQIEEKEEKdLHER------LN-GLESELAELDEE--------------IERYEEQREQARETRD 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 117 HLECLVSRHERSLrmtvvkrqaqspsgvsSEVEVLKALKSLFEHHKALDEKVRERLRaalERVTTLEEQLAGAHQQVSAL 196
Cdd:PRK02224 238 EADEVLEEHEERR----------------EELETLEAEIEDLRETIAETEREREELA---EEVRDLRERLEELEEERDDL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 197 QQGAGIRDGvaeEEETVDLGPKRLWKDDtgrvEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEEL 276
Cdd:PRK02224 299 LAEAGLDDA---DAEAVEARREELEDRD----EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 277 SGKHQRDLREALAQKEDMEERITTLEKRYLAAqreATSIHDLNDKLENELANKESLHRQCEEkarhlqelLEVAEQKLQQ 356
Cdd:PRK02224 372 LEEAREAVEDRREEIEELEEEIEELRERFGDA---PVDLGNAEDFLEELREERDELREREAE--------LEATLRTARE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 357 TMRKAETL------PEVEAEL--SQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQRekmnedhnKRLSDTVD 428
Cdd:PRK02224 441 RVEEAEALleagkcPECGQPVegSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL--------VEAEDRIE 512
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 281306779 429 RLLsESNERLQLHLKERMAALEEKgrlSEEIEKLRQEVDQL 469
Cdd:PRK02224 513 RLE-ERREDLEELIAERRETIEEK---RERAEELRERAAEL 549
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
34-470 |
3.53e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.78 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 34 LDEREKLLESLRESQETLVATQSRLQDALHERDQLQRHLnSALPQEFATLTRELSmcreQLLEREEEISELKAERNNTRL 113
Cdd:PRK03918 278 LEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRL-SRLEEEINGIEERIK----ELEEKEERLEELKKKLKELEK 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 114 LLEHLEclvSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKAlDEKVRERLRAALERVTTLEEQLAGAHQQV 193
Cdd:PRK03918 353 RLEELE---ERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKA-KEEIEEEISKITARIGELKKEIKELKKAI 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 194 SALQQGAGI----RDGVAEEEEtvdlgpKRLWKDDTGRVEELQGLLEKQNYELSQARERLVTLSaTVTELEEDLGTARR- 268
Cdd:PRK03918 429 EELKKAKGKcpvcGRELTEEHR------KELLEEYTAELKRIEKELKEIEEKERKLRKELRELE-KVLKKESELIKLKEl 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 269 -DLIKS--EELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDK---LENELANKES----LHRQCEE 338
Cdd:PRK03918 502 aEQLKEleEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKlaeLEKKLDELEEelaeLLKELEE 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 339 KARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQreKMNED 418
Cdd:PRK03918 582 LGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK--KYSEE 659
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 281306779 419 HNKRLSDTVDRL------LSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLK 470
Cdd:PRK03918 660 EYEELREEYLELsrelagLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLE 717
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
146-544 |
5.20e-11 |
|
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: 67.07 E-value: 5.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 146 SEVEVLKALKSLFEHHKALDEKVRERL--RAALERVTTLEEQLAGAHQQVSALQQGAGIRDGVAEEEETVDLGPKRLWKD 223
Cdd:pfam17380 266 TENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 224 DTGRVEELQglLEKQNYELSQARERLVTLSATVTELEEDLGTARRDliKSEELsgkhQRDLREALAQKEDMEERittlEK 303
Cdd:pfam17380 346 RERELERIR--QEERKRELERIRQEEIAMEISRMRELERLQMERQQ--KNERV----RQELEAARKVKILEEER----QR 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 304 RYLAAQREATSIhdlndKLENELANKESLHRQCEEKARHLQELLEvAEQKLQQTMrkaETLPEVEAELSQRIAALTKAEE 383
Cdd:pfam17380 414 KIQQQKVEMEQI-----RAEQEEARQREVRRLEEERAREMERVRL-EEQERQQQV---ERLRQQEEERKRKKLELEKEKR 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 384 RHGNIEEHLRQ-LEGQLEEKNQELARVRQREKM----NEDHNKRLSDTVDRLLSESNERLQLHLKER-------MAALEE 451
Cdd:pfam17380 485 DRKRAEEQRRKiLEKELEERKQAMIEEERKRKLlekeMEERQKAIYEEERRREAEEERRKQQEMEERrriqeqmRKATEE 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 452 KGRLsEEIEKLRQEVDQLkgrggpfVDGIHSRSHVGSTTDVR-----FSLSTAAHVPPGLHRRYTALREESAKDWKPAPL 526
Cdd:pfam17380 565 RSRL-EAMEREREMMRQI-------VESEKARAEYEATTPITtikpiYRPRISEYQPPDVESHMIRFTTQSPEWATPSPA 636
|
410
....*....|....*...
gi 281306779 527 PGVLAATTTPAFDSDPEI 544
Cdd:pfam17380 637 TWNPEWNTVTAEEETPGI 654
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
247-473 |
7.80e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.86 E-value: 7.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 247 ERLVTLSATVTELEEDLGTARRDLIKSEELSGKHQRdLREALAQKEDMEERITTLekRYLAAQREATSIHDLNDKLENEL 326
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLEPIRELAER-YAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 327 ANKESLHRQCEEKARHLQELLEVAEQKLQQtmRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQEL 406
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQIRG--NGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEF 382
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281306779 407 ARVRQRekmnedhnkrlsdtVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGRG 473
Cdd:COG4913 383 AALRAE--------------AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK 435
|
|
| SAM_liprin-beta1,2_repeat1 |
cd09563 |
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
827-891 |
1.20e-10 |
|
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: 58.01 E-value: 1.20e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281306779 827 FAQWDGPTVVSWL-ELWVGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQ 891
Cdd:cd09563 1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
26-472 |
1.20e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.09 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 26 FEQLMVNMLDER-EKLLESLRESQETLVATQSRLQDALHERDQLQRHLNSALPQEFATLTRElsmcreqllereeeISEL 104
Cdd:COG4913 285 FAQRRLELLEAElEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLERE--------------IERL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 105 KAERNNTRLLLEHLECLVsrheRSLRMTVvkrqaqsPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEE 184
Cdd:COG4913 351 ERELEERERRRARLEALL----AALGLPL-------PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 185 QLAGAHQQVSALQQGAG--------IRD------GVAEEE-----ETVDLGPK-RLWKD--------------------- 223
Cdd:COG4913 420 ELRELEAEIASLERRKSniparllaLRDalaealGLDEAElpfvgELIEVRPEeERWRGaiervlggfaltllvppehya 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 224 ---------------DTGRVEEL-----------QGLLEKQNYELSQARERLVTLSATVTEL-----EEDLGTARRD--- 269
Cdd:COG4913 500 aalrwvnrlhlrgrlVYERVRTGlpdperprldpDSLAGKLDFKPHPFRAWLEAELGRRFDYvcvdsPEELRRHPRAitr 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 270 --LIKSEelSGKHQRDLREALAQK----EDMEERITTLEKRYLAAQREAtsihdlnDKLENELANKESLHRQCEEKARHL 343
Cdd:COG4913 580 agQVKGN--GTRHEKDDRRRIRSRyvlgFDNRAKLAALEAELAELEEEL-------AEAEERLEALEAELDALQERREAL 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 344 QELLEV--AEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNK 421
Cdd:COG4913 651 QRLAEYswDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 281306779 422 RLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGR 472
Cdd:COG4913 731 ELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRAR 781
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
159-468 |
1.25e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.32 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 159 EHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGIRDgvAEEEETVDlgpkrlwkdDTGRVEELQGLLEKQ 238
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKK--AEEKKKAE---------EAKKAEEDKNMALRK 1582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 239 NYELSQARERLVTLSATVTELE-----EDLGTARRDLIKSEELSgKHQRDLREALAQKEDMEERITTLEKRYLAAQREAT 313
Cdd:PTZ00121 1583 AEEAKKAEEARIEEVMKLYEEEkkmkaEEAKKAEEAKIKAEELK-KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKI 1661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 314 SIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKlqqtmRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLR 393
Cdd:PTZ00121 1662 KAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA-----KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAK 1736
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281306779 394 QlEGQLEEKNQELARVRQREKmnedhnkrlsDTVDRLLSESNERLQLHLKERMAALEEKgrLSEEIEKLRQEVDQ 468
Cdd:PTZ00121 1737 K-EAEEDKKKAEEAKKDEEEK----------KKIAHLKKEEEKKAEEIRKEKEAVIEEE--LDEEDEKRRMEVDK 1798
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
21-640 |
1.27e-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: 65.91 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 21 DADANFEQLMVNMLDErEKLLESLREsqeTLVATQSRLQDALHERDQLQ----RHLNSALPQEFATLTRELSMCREQLLE 96
Cdd:pfam15921 167 DSNTQIEQLRKMMLSH-EGVLQEIRS---ILVDFEEASGKKIYEHDSMStmhfRSLGSAISKILRELDTEISYLKGRIFP 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 97 REEEISELKAE-RNNTRLLLEH----LECLVSRHERSL-----RMTVVKRQAQSpsgVSSEVEV------------LKAL 154
Cdd:pfam15921 243 VEDQLEALKSEsQNKIELLLQQhqdrIEQLISEHEVEItglteKASSARSQANS---IQSQLEIiqeqarnqnsmyMRQL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 155 KSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHqqvSALQQGAGIRDGVAEEEETVD-------------------- 214
Cdd:pfam15921 320 SDLESTVSQLRSELREAKRMYEDKIEELEKQLVLAN---SELTEARTERDQFSQESGNLDdqlqklladlhkrekelsle 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 215 -LGPKRLWKDDTG--------------------RVE--------ELQGLLEKQNYELSQARERLVTLSATVTELEEDLGT 265
Cdd:pfam15921 397 kEQNKRLWDRDTGnsitidhlrrelddrnmevqRLEallkamksECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEM 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 266 ARRDLiksEELSGKHQ---------RDLREALAQKEDMEE----RITTLEKRYLAAQREATSIHDLNDKLENELANKESL 332
Cdd:pfam15921 477 LRKVV---EELTAKKMtlessertvSDLTASLQEKERAIEatnaEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEAL 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 333 HRQCEEKARHLQELLEVAEQKLQ---QTMRKAETLPEVEAELSQRIaaltkaEERHGNIEEhLRQLEGQLEEKNQEL-AR 408
Cdd:pfam15921 554 KLQMAEKDKVIEILRQQIENMTQlvgQHGRTAGAMQVEKAQLEKEI------NDRRLELQE-FKILKDKKDAKIRELeAR 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 409 VRQRE----KMNEDHNKRLSDTVDRllseSNERLQLhLKERMAALEEKGRLSEEIEKLRQEVDQlkgrggpfvdgiHSRS 484
Cdd:pfam15921 627 VSDLElekvKLVNAGSERLRAVKDI----KQERDQL-LNEVKTSRNELNSLSEDYEVLKRNFRN------------KSEE 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 485 HVGSTTDVRFSLSTAAhvpPGLHRRYTALREESAKDWKPAPLPgvlaatttpafdsdpeisdvdedepgglVGTQVDVIS 564
Cdd:pfam15921 690 METTTNKLKMQLKSAQ---SELEQTRNTLKSMEGSDGHAMKVA----------------------------MGMQKQITA 738
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281306779 565 PGGHSDA-QTLAMMLQEQLDAINQEIRMIQEEKE--STELRAEEIETRVTSGSMEALNLTQLRKRGSIPTSLTALSLAS 640
Cdd:pfam15921 739 KRGQIDAlQSKIQFLEEAMTNANKEKHFLKEEKNklSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKAS 817
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
227-470 |
1.75e-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: 65.47 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 227 RVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEkRYL 306
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE-EDL 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 307 AAQREAtsIHDLNDKL-ENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALtkaEERH 385
Cdd:TIGR02169 775 HKLEEA--LNDLEARLsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL---KEQI 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 386 GNIEEHLRQLEGQLEEKNQELARVRQREKmneDHNKRLSDtvdrlLSESNERLQLHLKErmaALEEKGRLSEEIEKLRQE 465
Cdd:TIGR02169 850 KSIEKEIENLNGKKEELEEELEELEAALR---DLESRLGD-----LKKERDELEAQLRE---LERKIEELEAQIEKKRKR 918
|
....*
gi 281306779 466 VDQLK 470
Cdd:TIGR02169 919 LSELK 923
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
227-474 |
2.14e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.09 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 227 RVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSGK---HQRDLREALAQKEDMEERITTLEK 303
Cdd:PRK03918 187 RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEieeLEKELESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 304 RylaaqreatsIHDLNDKLEnELANKESLHRQCEEKA---RHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTK 380
Cdd:PRK03918 267 R----------IEELKKEIE-ELEEKVKELKELKEKAeeyIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 381 AEERHGNIEEHLRQLE---GQLEEKNQELARVRQREKMNEDHNKRLSDtvdrllsESNERLQLHLKErmaALEEKGRLSE 457
Cdd:PRK03918 336 KEERLEELKKKLKELEkrlEELEERHELYEEAKAKKEELERLKKRLTG-------LTPEKLEKELEE---LEKAKEEIEE 405
|
250
....*....|....*..
gi 281306779 458 EIEKLRQEVDQLKGRGG 474
Cdd:PRK03918 406 EISKITARIGELKKEIK 422
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
36-418 |
3.74e-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: 64.70 E-value: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 36 EREKLLESLRESQETLVATQSRLQDALHERDQLQRHLNSALpqEFATLTRELsmcreqlleREEEISELKAERNNTRLLL 115
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE--RYQALLKEK---------REYEGYELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 116 EHLECLVSRHERSLRMTVVKRQAQspsgvssEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSA 195
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISEL-------EKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 196 LQQGAgiRDGVAEEEET-VDLGPKRLWKDD-TGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLiks 273
Cdd:TIGR02169 313 KEREL--EDAEERLAKLeAEIDKLLAEIEElEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL--- 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 274 eelsgkhqRDLREALAQ-KEDMEERITTLEKRYLAAQREATSIHDLNdkleNELANKESLHRQCEEKARHLQELLEVAEQ 352
Cdd:TIGR02169 388 --------KDYREKLEKlKREINELKRELDRLQEELQRLSEELADLN----AAIAGIEAKINELEEEKEDKALEIKKQEW 455
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281306779 353 KLQQTmrkaetlpeveaelsqrIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNED 418
Cdd:TIGR02169 456 KLEQL-----------------AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
36-439 |
5.92e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 5.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 36 EREKLLESLRESQETLVATQSRLQDALHERDQLQRHLNSALPQEFATLTRELSMCREQLLEREEEISELKAERNNTRLLL 115
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 116 EHL-ECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDE--KVRERLRAALERVTTLEEQLAGAHQQ 192
Cdd:COG1196 477 AALaELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVliGVEAAYEAALEAALAAALQNIVVEDD 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 193 VSALQQGAGI---RDGVAEEEETVDLGPKRLWKDDTGRVEELQGLL----EKQNYELSQARERLVTLSATVTELEEDLGT 265
Cdd:COG1196 557 EVAAAAIEYLkaaKAGRATFLPLDKIRARAALAAALARGAIGAAVDlvasDLREADARYYVLGDTLLGRTLVAARLEAAL 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 266 AR------RDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEK 339
Cdd:COG1196 637 RRavtlagRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER 716
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 340 ARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEK---N----QELARVRQR 412
Cdd:COG1196 717 LEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvNllaiEEYEELEER 796
|
410 420 430
....*....|....*....|....*....|....
gi 281306779 413 -EKMNEDHN------KRLSDTVDRLLSESNERLQ 439
Cdd:COG1196 797 yDFLSEQREdleearETLEEAIEEIDRETRERFL 830
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
146-484 |
6.24e-10 |
|
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: 63.92 E-value: 6.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 146 SEVEVLKALKSLFEHHKALDEkVRERLRAALERVTTLEEQLAGAHQQVSALqqgagiRDGVAEEEETVDlgpkrlwkDDT 225
Cdd:TIGR02168 223 RELELALLVLRLEELREELEE-LQEELKEAEEELEELTAELQELEEKLEEL------RLEVSELEEEIE--------ELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 226 GRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRY 305
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 306 LAAqreatsiHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEerh 385
Cdd:TIGR02168 368 EEL-------ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE--- 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 386 gnieehlrqLEGQLEEKNQELARVRQREkmnEDHNKRLSDTVDRLLSESNERLQL-----HLKERMAALEekgRLSEEIE 460
Cdd:TIGR02168 438 ---------LQAELEELEEELEELQEEL---ERLEEALEELREELEEAEQALDAAerelaQLQARLDSLE---RLQENLE 502
|
330 340 350
....*....|....*....|....*....|.
gi 281306779 461 KLRQEV-------DQLKGRGGPFVDGIHSRS 484
Cdd:TIGR02168 503 GFSEGVkallknqSGLSGILGVLSELISVDE 533
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
229-407 |
7.42e-10 |
|
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: 60.71 E-value: 7.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 229 EELQGLLEKQNY--ELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRyl 306
Cdd:COG1579 4 EDLRALLDLQELdsELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 307 aaQREATSIHDLNDkLENELANKESLHRQCEEKARHLQELLEVAEQKLQqtmrkaetlpEVEAELSQRIAALTKAEERHG 386
Cdd:COG1579 82 --LGNVRNNKEYEA-LQKEIESLKRRISDLEDEILELMERIEELEEELA----------ELEAELAELEAELEEKKAELD 148
|
170 180
....*....|....*....|.
gi 281306779 387 NIEEHLRQLEGQLEEKNQELA 407
Cdd:COG1579 149 EELAELEAELEELEAEREELA 169
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
142-472 |
1.12e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.77 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 142 SGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALqqgagiRDGVAEEEETvdlgpkrlw 221
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL------EEKVKELKEL--------- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 222 KDDTGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLgtarrdliksEELSGKHQRdLREALAQKEDMEERITTL 301
Cdd:PRK03918 289 KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI----------KELEEKEER-LEELKKKLKELEKRLEEL 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 302 EKRYLAAQrEATSIHDLNDKLENELANKESlhrqceEKarhLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKA 381
Cdd:PRK03918 358 EERHELYE-EAKAKKEELERLKKRLTGLTP------EK---LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKA 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 382 EER-----------HGNIEEHLRqlEGQLEEKNQELARVRQREKMNEDHNKRLSD---TVDRLLSESNERLQLH-LKERM 446
Cdd:PRK03918 428 IEElkkakgkcpvcGRELTEEHR--KELLEEYTAELKRIEKELKEIEEKERKLRKelrELEKVLKKESELIKLKeLAEQL 505
|
330 340 350
....*....|....*....|....*....|....*
gi 281306779 447 AALEEK---------GRLSEEIEKLRQEVDQLKGR 472
Cdd:PRK03918 506 KELEEKlkkynleelEKKAEEYEKLKEKLIKLKGE 540
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
35-474 |
1.81e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.98 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 35 DEREKLLESLRESQETLVA---TQSRLQDALHERDQLQRHLnSALPQEFATLTRELSMCREQLLEREEEISELKAERNNT 111
Cdd:PRK02224 227 EQREQARETRDEADEVLEEheeRREELETLEAEIEDLRETI-AETEREREELAEEVRDLRERLEELEEERDDLLAEAGLD 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 112 RL----LLEHLECLVSRHERSLRMTVVKRQAQSpsgvssevEVLKALKSLFEHHKALDEKVRErlraALERVTTLEEQLA 187
Cdd:PRK02224 306 DAdaeaVEARREELEDRDEELRDRLEECRVAAQ--------AHNEEAESLREDADDLEERAEE----LREEAAELESELE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 188 GAHQQVSALQ-QGAGIRDGVAEEEETVDLGPKRLwkddtgrvEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTA 266
Cdd:PRK02224 374 EAREAVEDRReEIEELEEEIEELRERFGDAPVDL--------GNAEDFLEELREERDELREREAELEATLRTARERVEEA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 267 RR---------------------DLIKSEELSGKHQRDLREALAQKEDMEERITTLEKrYLAAQREATSIHDLNDKLENE 325
Cdd:PRK02224 446 EAlleagkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIERLEERREDLEEL 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 326 LANKESL----HRQCEEKARHLQELLEVAEQK---LQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLrqleGQ 398
Cdd:PRK02224 525 IAERRETieekRERAEELRERAAELEAEAEEKreaAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLL----AA 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 399 LEEKNQELARVRQREK----MNEDHNKRLSDTVDR---LLSESNE-RLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLK 470
Cdd:PRK02224 601 IADAEDEIERLREKREalaeLNDERRERLAEKRERkreLEAEFDEaRIEEAREDKERAEEYLEQVEEKLDELREERDDLQ 680
|
....
gi 281306779 471 GRGG 474
Cdd:PRK02224 681 AEIG 684
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
40-469 |
8.48e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.78 E-value: 8.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 40 LLESLRESQETLVATQSRL-QDALHERDQLQRHLNSA--LPQEFATLTRELSMCREQLLEREEEISELKAERNNTRLLLE 116
Cdd:COG4717 47 LLERLEKEADELFKPQGRKpELNLKELKELEEELKEAeeKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 117 HLECL--VSRHERSL-----RMTVVKRQAQSPSGVSSEVEVLKAlkSLFEHHKALDEKVRERLRAALERVTTLEEQLAGA 189
Cdd:COG4717 127 LLPLYqeLEALEAELaelpeRLEELEERLEELRELEEELEELEA--ELAELQEELEELLEQLSLATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 190 HQQVSALQQG-AGIRDGVAEEEETVD-LGPKRLWKDDTGRVEELQGL---------LEKQNYELSQARERLVTLSATVTE 258
Cdd:COG4717 205 QQRLAELEEElEEAQEELEELEEELEqLENELEAAALEERLKEARLLlliaaallaLLGLGGSLLSLILTIAGVLFLVLG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 259 LeedLGTARRDLIKSEELSGKHQRDLREALAQKE-DMEERITTLEKRYLAAQREATSIHDLNDKLENelanKESLHRQCE 337
Cdd:COG4717 285 L---LALLFLLLAREKASLGKEAEELQALPALEElEEEELEELLAALGLPPDLSPEELLELLDRIEE----LQELLREAE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 338 EKARHLQelLEVAEQKLQQTMRKAETlpEVEAELSQRIAALTKAEErhgnIEEHLRQLEGQLEEKNQELARVRQREKmNE 417
Cdd:COG4717 358 ELEEELQ--LEELEQEIAALLAEAGV--EDEEELRAALEQAEEYQE----LKEELEELEEQLEELLGELEELLEALD-EE 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 418 DHNKRLSDTVDRLLSESNERLQLH-----LKERMAALEEKGRLSE---EIEKLRQEVDQL 469
Cdd:COG4717 429 ELEEELEELEEELEELEEELEELReelaeLEAELEQLEEDGELAEllqELEELKAELREL 488
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
261-475 |
8.58e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.08 E-value: 8.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 261 EDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKA 340
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 341 RHLQEL----------LEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAE---ERHGNIEEHLRQLEGQLEEKNQELA 407
Cdd:PRK03918 238 EEIEELekeleslegsKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKekaEEYIKLSEFYEEYLDELREIEKRLS 317
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281306779 408 RVRQREKMNEDHNKRLSDTVDRLlsESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGRGGP 475
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERL--EELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTG 383
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
163-414 |
1.00e-08 |
|
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: 59.97 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 163 ALDEKVRERLRAALERVTTLEEQLAgahQQVSALQQGAGIRDGVAEEEETVD--LGPKRLWKDDT--GRVEELqgllEKQ 238
Cdd:COG3096 829 AFAPDPEAELAALRQRRSELERELA---QHRAQEQQLRQQLDQLKEQLQLLNklLPQANLLADETlaDRLEEL----REE 901
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 239 NYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELsgkhQRDLREALAQKEDMEERITTLEkrYLAAQREATSIHD- 317
Cdd:COG3096 902 LDAAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQL----QADYLQAKEQQRRLKQQIFALS--EVVQRRPHFSYEDa 975
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 318 ---------LNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQ--QTMR--KAETLPEVEAELSQ-RIAALTKAEE 383
Cdd:COG3096 976 vgllgensdLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLAslKSSRdaKQQTLQELEQELEElGVQADAEAEE 1055
|
250 260 270
....*....|....*....|....*....|.
gi 281306779 384 RhgnIEEHLRQLEGQLeekNQELARVRQREK 414
Cdd:COG3096 1056 R---ARIRRDELHEEL---SQNRSRRSQLEK 1080
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
31-465 |
1.77e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 31 VNMLDEREKLLESLRESQETL------VATQSRLQDALHERDQLQRHLNSaLPQEFATLTRELsmcreqllereeeisel 104
Cdd:COG4717 94 QEELEELEEELEELEAELEELreelekLEKLLQLLPLYQELEALEAELAE-LPERLEELEERL----------------- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 105 kAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEE 184
Cdd:COG4717 156 -EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 185 QLAGAH--QQVSALQQGAGIRDGVAEEEETVDLGPKRLWKDD------TGRVEELQGLLEKQNYELSQARERLVTLSATV 256
Cdd:COG4717 235 ELEAAAleERLKEARLLLLIAAALLALLGLGGSLLSLILTIAgvlflvLGLLALLFLLLAREKASLGKEAEELQALPALE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 257 TELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLND---KLENELANKESLH 333
Cdd:COG4717 315 ELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEagvEDEEELRAALEQA 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 334 RQCEEkarhLQELLEVAEQKLqqtmrkAETLPEVEAELSQriAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQRE 413
Cdd:COG4717 395 EEYQE----LKEELEELEEQL------EELLGELEELLEA--LDEEELEEELEELEEELEELEEELEELREELAELEAEL 462
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 414 KMNEDhnkrlSDTVDRLLSEsnerlQLHLKERMAALEEKGR--------LSEEIEKLRQE 465
Cdd:COG4717 463 EQLEE-----DGELAELLQE-----LEELKAELRELAEEWAalklalelLEEAREEYREE 512
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
61-409 |
2.16e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 61 ALHERDQLQRHLNSALpQEFATLTRELSMCREQLLEREEEISELKAERNNTRLLLEHLeclvsrheRSLRMTVVKRQAQS 140
Cdd:COG1196 230 LLLKLRELEAELEELE-AELEELEAELEELEAELAELEAELEELRLELEELELELEEA--------QAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 141 PSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGIRDGVAEEEETVDLGPKRL 220
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 221 WKDDTGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITT 300
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 301 LEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEE-KARHLQELLEVAEQKLQQTMRKAE----TLPEVEAELSQRI 375
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEaEADYEGFLEGVKAALLLAGLRGLAgavaVLIGVEAAYEAAL 540
|
330 340 350
....*....|....*....|....*....|....
gi 281306779 376 AALTKAEERHGNIEEHLRQLEGQLEEKNQELARV 409
Cdd:COG1196 541 EAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRA 574
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
177-469 |
3.37e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.13 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 177 ERVTTLEEQLAGAHQQVSALQQG-AGIRDGVAEEEETVDLGPKRlwkddtgrvEELQGLLEKQNYELSQARERLVTLSAT 255
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVEERlERAEDLVEAEDRIERLEERR---------EDLEELIAERRETIEEKRERAEELRER 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 256 VTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKrylaaqreatsIHDLNDKLENELANKESLhrq 335
Cdd:PRK02224 546 AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER-----------IRTLLAAIADAEDEIERL--- 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 336 cEEKARHLQELLEVAEQKLQQtmrKAETLPEVEAELSQriAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKM 415
Cdd:PRK02224 612 -REKREALAELNDERRERLAE---KRERKRELEAEFDE--ARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGA 685
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 281306779 416 NEDHNKRLSDtvdrllsesnerlqlhLKERMAALEEKgrlSEEIEKLRQEVDQL 469
Cdd:PRK02224 686 VENELEELEE----------------LRERREALENR---VEALEALYDEAEEL 720
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
241-465 |
3.84e-08 |
|
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: 57.08 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 241 ELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREatsIHDLND 320
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE---LEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 321 KLENELANKESLHRQCEEKarhlqelLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERhgnieehLRQLEGQLE 400
Cdd:COG4942 105 ELAELLRALYRLGRQPPLA-------LLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE-------LAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281306779 401 EKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQE 465
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
827-893 |
4.87e-08 |
|
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: 50.76 E-value: 4.87e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281306779 827 FAQWDGPTVVSWLELWvGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEM 893
Cdd:smart00454 1 VSQWSPESVADWLESI-GLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
246-472 |
5.73e-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: 5.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 246 RERLVTLSATVTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENE 325
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 326 LANKESLHR-------QCEEKARHLQELLE-----VAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLR 393
Cdd:TIGR02169 753 IENVKSELKelearieELEEDLHKLEEALNdlearLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 394 QLEGQLEEKNQEL-ARVRQREKMNEDHNKRLSDTVDRLlsesnERLQLHLKErmaALEEKGRLSEEIEKLRQEVDQLKGR 472
Cdd:TIGR02169 833 KEIQELQEQRIDLkEQIKSIEKEIENLNGKKEELEEEL-----EELEAALRD---LESRLGDLKKERDELEAQLRELERK 904
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
229-430 |
6.12e-08 |
|
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: 56.31 E-value: 6.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 229 EELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRYlAA 308
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL-AE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 309 QREATSIHDLNDKLENELANKESLhrQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERhgnI 388
Cdd:COG4942 109 LLRALYRLGRQPPLALLLSPEDFL--DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE---L 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 281306779 389 EEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRL 430
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
222-465 |
8.68e-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: 56.61 E-value: 8.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 222 KDDTGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERIttl 301
Cdd:TIGR02169 712 SDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL--- 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 302 ekrylaAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAAL-TK 380
Cdd:TIGR02169 789 ------SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLnGK 862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 381 AEERHGNIEEHLRQLEgQLEEKNQELARVRqrekmnEDHNKRLSDTVDRL--LSESNERLQLHLKERMAALEEKGRLSEE 458
Cdd:TIGR02169 863 KEELEEELEELEAALR-DLESRLGDLKKER------DELEAQLRELERKIeeLEAQIEKKRKRLSELKAKLEALEEELSE 935
|
....*..
gi 281306779 459 IEKLRQE 465
Cdd:TIGR02169 936 IEDPKGE 942
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
952-1007 |
9.56e-08 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 49.99 E-value: 9.56e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 281306779 952 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1007
Cdd:smart00454 11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
33-380 |
1.04e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 33 MLDEREKLLESLRESQETLVATQSRLQDALHERDQLQRHLNsALPQEFATLTRELSMCREQLLEREEEISELKAErnntr 112
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE-QLEQEEEKLKERLEELEEDLSSLEQEIENVKSE----- 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 113 llLEHLECLVSRHERSLrmtvVKRQAQ--------SPSGVSsevEVLKALKSLFEHHKALDEKVRErLRAALERVTTLEE 184
Cdd:TIGR02169 760 --LKELEARIEELEEDL----HKLEEAlndlearlSHSRIP---EIQAELSKLEEEVSRIEARLRE-IEQKLNRLTLEKE 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 185 QLAGAHQQvsALQQGAGIRDGVAEEEETVDlgpkrlwkDDTGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLG 264
Cdd:TIGR02169 830 YLEKEIQE--LQEQRIDLKEQIKSIEKEIE--------NLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 265 TArrdlikseelsgkhQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANK---ESLHRQCEEKAR 341
Cdd:TIGR02169 900 EL--------------ERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEElslEDVQAELQRVEE 965
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 281306779 342 HLQELLEV---AEQKLQQTMR-------KAETLPEVEAELSQRIAALTK 380
Cdd:TIGR02169 966 EIRALEPVnmlAIQEYEEVLKrldelkeKRAKLEEERKAILERIEEYEK 1014
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
183-470 |
1.11e-07 |
|
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: 56.28 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 183 EEQLAGAHQQVSALQQGAGIRDGVAEEEETV-----DLGPKRLWKDDTGRVEELQGLLEKQNYELSQARERLVTLSATVT 257
Cdd:pfam15921 162 EDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIlvdfeEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIF 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 258 ELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEerITTLEKRYLAAQREATSIHDLNDKLENELANKESLHrqce 337
Cdd:pfam15921 242 PVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVE--ITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMY---- 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 338 ekARHLQELLEVAEQkLQQTMRKA-----ETLPEVEAELSQRIAALTKAE-------ERHGNIEEHLRQLEGQLEEKNQE 405
Cdd:pfam15921 316 --MRQLSDLESTVSQ-LRSELREAkrmyeDKIEELEKQLVLANSELTEARterdqfsQESGNLDDQLQKLLADLHKREKE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 406 LARVRQREKMNEDHNKRLSDTVDRLLSESNER-----------------LQLHLKERMAALEEKGRLSEEIEKLRQEVDQ 468
Cdd:pfam15921 393 LSLEKEQNKRLWDRDTGNSITIDHLRRELDDRnmevqrleallkamkseCQGQMERQMAAIQGKNESLEKVSSLTAQLES 472
|
..
gi 281306779 469 LK 470
Cdd:pfam15921 473 TK 474
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
259-470 |
1.58e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 259 LEEDLGTARRDLIKSE----ELSGKHQRDLREALAQKEDMEERITTLEKRYlaaqreatsihdlnDKLENELANKESLHR 334
Cdd:COG4717 47 LLERLEKEADELFKPQgrkpELNLKELKELEEELKEAEEKEEEYAELQEEL--------------EELEEELEELEAELE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 335 QCEEKARHLQELLEVAE--QKLQQTMRKAETLPEVEAELSQRIAALTKAEERhgnieehLRQLEGQLEEKNQELARVRQR 412
Cdd:COG4717 113 ELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRELEEE-------LEELEAELAELQEELEELLEQ 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 281306779 413 ekmnedhnkrLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLK 470
Cdd:COG4717 186 ----------LSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
38-468 |
1.63e-07 |
|
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: 55.75 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 38 EKLLESLRESQETLVATQ---SRLQDALHERDQLQRHLNSALPQEfATLTRELSmcreqllereeEISELKAERNNTRll 114
Cdd:TIGR00618 225 EKELKHLREALQQTQQSHaylTQKREAQEEQLKKQQLLKQLRARI-EELRAQEA-----------VLEETQERINRAR-- 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 115 leHLECLVsrhERSLRMTVVKRQAQspsgvssevevlkalkslfEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVS 194
Cdd:TIGR00618 291 --KAAPLA---AHIKAVTQIEQQAQ-------------------RIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 195 ALQ-QGAGIRDGVAEEEETvdlgpkrLWKDDTGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKS 273
Cdd:TIGR00618 347 LQTlHSQEIHIRDAHEVAT-------SIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAF 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 274 EELSGKHQRDLREALAQKEDMEERITTLEKRY---LAAQREATSIHDLNDKLENELANKESLHRQCEE-KARHLQELLEV 349
Cdd:TIGR00618 420 RDLQGQLAHAKKQQELQQRYAELCAAAITCTAqceKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRkKAVVLARLLEL 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 350 AEQklQQTMRKAETLPEVEAELSQRIAALT----KAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSD 425
Cdd:TIGR00618 500 QEE--PCPLCGSCIHPNPARQDIDNPGPLTrrmqRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQ 577
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 281306779 426 TVDRLLSESNERLQL-----HLKERMAALEEKGRLSEEIEKLRQEVDQ 468
Cdd:TIGR00618 578 CDNRSKEDIPNLQNItvrlqDLTEKLSEAEDMLACEQHALLRKLQPEQ 625
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
284-464 |
2.33e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.00 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 284 LREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEvaeqklqqtmrKAET 363
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG-----------NVRN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 364 LPEVEAeLSQRIAALtkaEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLK 443
Cdd:COG1579 88 NKEYEA-LQKEIESL---KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
170 180
....*....|....*....|..
gi 281306779 444 ERMAALEE-KGRLSEEIEKLRQ 464
Cdd:COG1579 164 EREELAAKiPPELLALYERIRK 185
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
37-470 |
2.36e-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: 55.23 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 37 REKLLESLRESQETLVATQSRLQDALHERDQLQRHLNsalpQEFATLTRELSmcrEQLLEREEEISELKAERNNTRlllE 116
Cdd:pfam12128 253 LESAELRLSHLHFGYKSDETLIASRQEERQETSAELN----QLLRTLDDQWK---EKRDELNGELSAADAAVAKDR---S 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 117 HLECLVSRHERSLRMTVVKR---QAQSPSgVSSEVEVLKalkslfEHHKALDEKVRERLRAALERVTTLEEQLAgahqqv 193
Cdd:pfam12128 323 ELEALEDQHGAFLDADIETAaadQEQLPS-WQSELENLE------ERLKALTGKHQDVTAKYNRRRSKIKEQNN------ 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 194 salQQGAGIRDGVAEEEETVDLGPKRLWKDDTGRVEELQGLLEKQNYELSQARERLVtLSATVTELEEDLGTARRDLIKS 273
Cdd:pfam12128 390 ---RDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLK-SRLGELKLRLNQATATPELLLQ 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 274 EELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANK-ESLHRQCEEKARHLQELLEVAEQ 352
Cdd:pfam12128 466 LENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSAlDELELQLFPQAGTLLHFLRKEAP 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 353 KLQQTMRK---AETL------PEV-----------------------------EAELSQRIAALTKA----EERHGNIEE 390
Cdd:pfam12128 546 DWEQSIGKvisPELLhrtdldPEVwdgsvggelnlygvkldlkridvpewaasEEELRERLDKAEEAlqsaREKQAAAEE 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 391 HLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDtvdrllsesnERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLK 470
Cdd:pfam12128 626 QLVQANGELEKASREETFARTALKNARLDLRRLFD----------EKQSEKDKKNKALAERKDSANERLNSLEAQLKQLD 695
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
234-470 |
2.42e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.03 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 234 LLEKQNyELSQARERLVTLSATVTELEEDLGTARRDliKSEELSGKHQRDLREALAQKEDMEERITTLEKrylaaqreat 313
Cdd:TIGR04523 269 LSEKQK-ELEQNNKKIKELEKQLNQLKSEISDLNNQ--KEQDWNKELKSELKNQEKKLEEIQNQISQNNK---------- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 314 SIHDLND---KLENELANKES----LHRQCEEKARHLQELLEVAEQKLQQTmrkaETLPEVEAELSQRIaalTKAEERHG 386
Cdd:TIGR04523 336 IISQLNEqisQLKKELTNSESenseKQRELEEKQNEIEKLKKENQSYKQEI----KNLESQINDLESKI---QNQEKLNQ 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 387 NIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLS--DTVDRLLSESNERLQLHLKERMAALEekgrlsEEIEKLRQ 464
Cdd:TIGR04523 409 QKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTnqDSVKELIIKNLDNTRESLETQLKVLS------RSINKIKQ 482
|
....*.
gi 281306779 465 EVDQLK 470
Cdd:TIGR04523 483 NLEQKQ 488
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
112-351 |
2.60e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 112 RLLLEHLECLVSRHERslrMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVR-----ERLRAALERVTTLEEQL 186
Cdd:COG4913 228 DALVEHFDDLERAHEA---LEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRlwfaqRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 187 AGAHQQVSALQQGagiRDGVAEEEETVDlgpKRLWKDDTGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTA 266
Cdd:COG4913 305 ARLEAELERLEAR---LDALREELDELE---AQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 267 RRDLiksEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLE--------NELANKESLHRQCEE 338
Cdd:COG4913 379 AEEF---AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLErrksnipaRLLALRDALAEALGL 455
|
250
....*....|....*.
gi 281306779 339 KARHLQ---ELLEVAE 351
Cdd:COG4913 456 DEAELPfvgELIEVRP 471
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
35-470 |
4.13e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 4.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 35 DEREKLLESLRESQETLVATQSRLQDALHERDQLqrhlNSALPQefatLTRELSMcreqLLEREEEISELKAERNNTRLL 114
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEVLREINEI----SSELPE----LREELEK----LEKEVKELEELKEEIEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 115 LEHLECLVSRHERSLRMTV-----VKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGA 189
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEerieeLKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 190 HQQVSALQQG-----------AGIRDGVAEEEETVdlgpkRLWKDDTGRVEELQGLLEK-QNYELSQARERLVTLSATVT 257
Cdd:PRK03918 327 EERIKELEEKeerleelkkklKELEKRLEELEERH-----ELYEEAKAKKEELERLKKRlTGLTPEKLEKELEELEKAKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 258 ELEEDLG--TARRDLIKSE-----------------------ELSGKHQRDL-REALAQKEDMEERITTLEKRYLAAQRE 311
Cdd:PRK03918 402 EIEEEISkiTARIGELKKEikelkkaieelkkakgkcpvcgrELTEEHRKELlEEYTAELKRIEKELKEIEEKERKLRKE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 312 ATsihdlndKLENELANKESLHRQCE--EKARHLQELLE-VAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNI 388
Cdd:PRK03918 482 LR-------ELEKVLKKESELIKLKElaEQLKELEEKLKkYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEEL 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 389 EEHLRQLEGQLEEKNQELARVRQR----------------EKMNEDHNK--RLSDTVDRLLSESnERLQLHLKERMAALE 450
Cdd:PRK03918 555 KKKLAELEKKLDELEEELAELLKEleelgfesveeleerlKELEPFYNEylELKDAEKELEREE-KELKKLEEELDKAFE 633
|
490 500
....*....|....*....|
gi 281306779 451 EKGRLSEEIEKLRQEVDQLK 470
Cdd:PRK03918 634 ELAETEKRLEELRKELEELE 653
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
253-469 |
4.44e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 4.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 253 SATVTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREatsIHDLNDKLENELANKESL 332
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE---LAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 333 HRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQR 412
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 281306779 413 EKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQL 469
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
34-380 |
6.92e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 6.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 34 LDEREKLLESLRESQETLVATQSRLQDALherDQLQRHLNSALPQEFATLTRELSMCREQLLEREEEISELKAERNNTRL 113
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEEL---EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 114 LLEHLECLVSRHER--------------SLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERV 179
Cdd:COG4717 228 ELEQLENELEAAALeerlkearlllliaAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEEL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 180 TTLEEQLAGAHQQVSALQQGAGIRDGVAEEEETVDLGPKRLWKDDTGRVEELQGLLEKQNYELSQAR------------- 246
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAllaeagvedeeel 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 247 ERLVTLSATVTELEEDLGTARRDL--IKSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLEN 324
Cdd:COG4717 388 RAALEQAEEYQELKEELEELEEQLeeLLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE 467
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281306779 325 --ELANKESLHRQCEEKARHLQE---LLEVAEQKLQQTMRKA--ETLPEVEAELSQRIAALTK 380
Cdd:COG4717 468 dgELAELLQELEELKAELRELAEewaALKLALELLEEAREEYreERLPPVLERASEYFSRLTD 530
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
281-470 |
8.71e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 8.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 281 QRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRK 360
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 361 AETLpevEAELSQRIAALTK------------------AEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKR 422
Cdd:COG4942 99 LEAQ---KEELAELLRALYRlgrqpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 281306779 423 LSDTVDRlLSESNERLQLHLKERMAALEekgRLSEEIEKLRQEVDQLK 470
Cdd:COG4942 176 LEALLAE-LEEERAALEALKAERQKLLA---RLEKELAELAAELAELQ 219
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
135-470 |
1.50e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 135 KRQAQSPSGVSSEVEVLKALKSLFEHHKALDE--KVRERLRAALERVTTLEEQlagahQQVSALQQGAgirdgvaEEEET 212
Cdd:PTZ00121 1417 KKKADEAKKKAEEKKKADEAKKKAEEAKKADEakKKAEEAKKAEEAKKKAEEA-----KKADEAKKKA-------EEAKK 1484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 213 VDLGPKRLwKDDTGRVEELQGLLE--KQNYELSQARERLVTLSATVTELEEDLGTARR--------DLIKSEELsgKHQR 282
Cdd:PTZ00121 1485 ADEAKKKA-EEAKKKADEAKKAAEakKKADEAKKAEEAKKADEAKKAEEAKKADEAKKaeekkkadELKKAEEL--KKAE 1561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 283 DLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKlqqtmRKAE 362
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK-----KKVE 1636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 363 TLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDtvdrllsESNERLQLHL 442
Cdd:PTZ00121 1637 QLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE-------EAKKAEELKK 1709
|
330 340 350
....*....|....*....|....*....|..
gi 281306779 443 KErmaalEEKGRLSEEIEKLRQE----VDQLK 470
Cdd:PTZ00121 1710 KE-----AEEKKKAEELKKAEEEnkikAEEAK 1736
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
281-468 |
1.63e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 281 QRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELankESLHRQCEEKARHLQELLEVAEQKLQQTMRK 360
Cdd:COG3883 22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI---DKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 361 AETLPEVEA--------ELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLS 432
Cdd:COG3883 99 GGSVSYLDVllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 281306779 433 ESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQ 468
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
31-452 |
2.45e-06 |
|
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: 52.03 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 31 VNMLDEREKLL-ESLRESQETLVATQSRLQD-------------ALHERDQLQRHLNSALPQEFATLTRELSmcrEQLLE 96
Cdd:pfam05483 270 ANQLEEKTKLQdENLKELIEKKDHLTKELEDikmslqrsmstqkALEEDLQIATKTICQLTEEKEAQMEELN---KAKAA 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 97 REEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgvsSEVEVLKALKS-----LFEHHKALDEKvrER 171
Cdd:pfam05483 347 HSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS-----SELEEMTKFKNnkeveLEELKKILAED--EK 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 172 LRAALERVTTLEEQLAGAHQQVSALQQgagirdgvAEEEETVDL-----GPKRLWKDDTGRVEELQGLLEKQ-------- 238
Cdd:pfam05483 420 LLDEKKQFEKIAEELKGKEQELIFLLQ--------AREKEIHDLeiqltAIKTSEEHYLKEVEDLKTELEKEklknielt 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 239 ---------NYELSQ---------------------ARERLV----TLSATVTELEEDLGTARRDLI-----------KS 273
Cdd:pfam05483 492 ahcdkllleNKELTQeasdmtlelkkhqediinckkQEERMLkqieNLEEKEMNLRDELESVREEFIqkgdevkckldKS 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 274 EELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLN---------------------DKLENELANKESL 332
Cdd:pfam05483 572 EENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENkalkkkgsaenkqlnayeikvNKLELELASAKQK 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 333 HRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRI--AALTKAEERHGNIEEHLRQLEGQLEEKNQELARVR 410
Cdd:pfam05483 652 FEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIdkRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYK 731
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 281306779 411 QREKMNEDHNK----RLSDTVDRLLS---------ESNERLQLHLKERMAALEEK 452
Cdd:pfam05483 732 NKEQEQSSAKAaleiELSNIKAELLSlkkqleiekEEKEKLKMEAKENTAILKDK 786
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
27-469 |
2.64e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.89 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 27 EQLMVNMLDEREKLLE-SLRESQETLVATQSRL-QDALHERDQLQ-RHLNSALPQEFATLTRELSMCREQLLEREEEISE 103
Cdd:TIGR00618 408 EQATIDTRTSAFRDLQgQLAHAKKQQELQQRYAeLCAAAITCTAQcEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETR 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 104 LKAERNNTRLLLEHLECLVsrhERSLRMTVVKRQAQSPSGVSSEvEVLKALKSLFEHHKALdEKVRERLRAALERVTTLE 183
Cdd:TIGR00618 488 KKAVVLARLLELQEEPCPL---CGSCIHPNPARQDIDNPGPLTR-RMQRGEQTYAQLETSE-EDVYHQLTSERKQRASLK 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 184 EQLAGAHQQVSALQQ-----GAGIRDGVAEEEETVDLGPKRLWKDDTGRVEELQGLLEKQ----NYELS----QARERLV 250
Cdd:TIGR00618 563 EQMQEIQQSFSILTQcdnrsKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQpeqdLQDVRlhlqQCSQELA 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 251 TLSATVTELEEDLG------TARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDlNDKLEN 324
Cdd:TIGR00618 643 LKLTALHALQLTLTqervreHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEE-YDREFN 721
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 325 ELANKESLHRQceekarHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEG----QLE 400
Cdd:TIGR00618 722 EIENASSSLGS------DLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQffnrLRE 795
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281306779 401 EKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQL 469
Cdd:TIGR00618 796 EDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQL 864
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
227-371 |
2.80e-06 |
|
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: 49.92 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 227 RVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSG--KHQRDLREALAQKEDMEERITTLEKR 304
Cdd:COG1579 32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvRNNKEYEALQKEIESLKRRISDLEDE 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281306779 305 YLAAQREATSIHDLNDKLENELANKEslhRQCEEKARHLQELLEVAEQKLQQTMRKAETL-PEVEAEL 371
Cdd:COG1579 112 ILELMERIEELEEELAELEAELAELE---AELEEKKAELDEELAELEAELEELEAEREELaAKIPPEL 176
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
22-484 |
2.81e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 51.76 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 22 ADANFEQLMVNMLDEREKLLESLRESQETLVATQSRLQDALHERDQLQRHLNSALPQEFATLTRELSMCREQLLEREEEI 101
Cdd:pfam12128 454 NQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQA 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 102 SELKA-ERNNTRLLLEHLECLVSR---HERSLRMTVVKRQAQSPS---GVSSEVEVLKALKSLFeHHKALDE---KVRER 171
Cdd:pfam12128 534 GTLLHfLRKEAPDWEQSIGKVISPellHRTDLDPEVWDGSVGGELnlyGVKLDLKRIDVPEWAA-SEEELRErldKAEEA 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 172 LRAALERVTTLEEQLAGAHQQVSALQQGAGIrdgVAEEEETVDLGPKRLwkddTGRVEELQGLLEKQ-NYELSQARERLV 250
Cdd:pfam12128 613 LQSAREKQAAAEEQLVQANGELEKASREETF---ARTALKNARLDLRRL----FDEKQSEKDKKNKAlAERKDSANERLN 685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 251 TLSATVTELEEDLGTA----RRDLIkseELSGKHQRDLREALAQKEDMEERI-TTLEKRYLAAQREATSIHDLNDkleNE 325
Cdd:pfam12128 686 SLEAQLKQLDKKHQAWleeqKEQKR---EARTEKQAYWQVVEGALDAQLALLkAAIAARRSGAKAELKALETWYK---RD 759
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 326 LANK--------------ESLHRQCEEKARHLQELLE----VAEQKLQQTMRKAETLPEVEAELsqriaaltkaeerhgn 387
Cdd:pfam12128 760 LASLgvdpdviaklkreiRTLERKIERIAVRRQEVLRyfdwYQETWLQRRPRLATQLSNIERAI---------------- 823
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 388 ieehlRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSE---------------SNERLQLHLKERMAALEE- 451
Cdd:pfam12128 824 -----SELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGlrcemsklatlkedaNSEQAQGSIGERLAQLEDl 898
|
490 500 510
....*....|....*....|....*....|...
gi 281306779 452 KGRLSEEIEKLRQEVDQLKGrggpfVDGIHSRS 484
Cdd:pfam12128 899 KLKRDYLSESVKKYVEHFKN-----VIADHSGS 926
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
272-478 |
3.35e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.67 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 272 KSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAE 351
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 352 QKLQQTMRKAETLpevEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRL- 430
Cdd:COG4372 101 EELESLQEEAEEL---QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALs 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 281306779 431 LSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGRGGPFVD 478
Cdd:COG4372 178 EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKD 225
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
65-476 |
5.46e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.11 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 65 RDQLQRHLNSALpqefaTLTRELSMCREQLLEREEEISELKAErnntrlllehLECLVSRhERSLRMTVvkrQAQSPSgV 144
Cdd:PRK04863 278 ANERRVHLEEAL-----ELRRELYTSRRQLAAEQYRLVEMARE----------LAELNEA-ESDLEQDY---QAASDH-L 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 145 SSEVEVLKALKSLFEHHKALDEKVrERLRAALERVTTLEEQLAGAHQQVSALQQGA-GIRDGVAEEEETVDLGPKRL--W 221
Cdd:PRK04863 338 NLVQTALRQQEKIERYQADLEELE-ERLEEQNEVVEEADEQQEENEARAEAAEEEVdELKSQLADYQQALDVQQTRAiqY 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 222 KDDTGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSGKHQRDLR---------EALAQKE 292
Cdd:PRK04863 417 QQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQlvrkiagevSRSEAWD 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 293 DMEERITTLEK-RYLAAQREAtsihdlndkLENELANKESLHRQceekARHLQELLEVAEQKLQQTMRKAETLPEVEAEL 371
Cdd:PRK04863 497 VARELLRRLREqRHLAEQLQQ---------LRMRLSELEQRLRQ----QQRAERLLAEFCKRLGKNLDDEDELEQLQEEL 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 372 SQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESN---ERLQLHLKERMAA 448
Cdd:PRK04863 564 EARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQdvtEYMQQLLEREREL 643
|
410 420
....*....|....*....|....*...
gi 281306779 449 LEEKGRLSEEIEKLRQEVDQLKGRGGPF 476
Cdd:PRK04863 644 TVERDELAARKQALDEEIERLSQPGGSE 671
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
135-472 |
7.68e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 7.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 135 KRQAQSPSGVSSEVEVL-KALKSLFEHHKALDEKvRERLRAALERVTTLEEQLAGAHQQVSALQQGAGIRDGVAEEEETv 213
Cdd:COG4717 60 KPQGRKPELNLKELKELeEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 214 dlgpKRLWKDDTGRVEELqgllEKQNYELSQARERLVTLSATVTELEEDLGTARRDLikseelSGKHQRDLREALAQKED 293
Cdd:COG4717 138 ----EAELAELPERLEEL----EERLEELRELEEELEELEAELAELQEELEELLEQL------SLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 294 MEERITTLEKRYLAAQREATSIHDLNDKLENE------------------------------------------------ 325
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENEleaaaleerlkearlllliaaallallglggsllsliltiagvlflvl 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 326 ---------LANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVE-AELSQRIAALTKAEERHGNIEEHLRQL 395
Cdd:COG4717 284 gllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSpEELLELLDRIEELQELLREAEELEEEL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 396 E-GQLEEKNQEL-------------ARVRQREKMNEDhNKRLSDTVDRLLSESNERLQLHLKERMAALEEK-GRLSEEIE 460
Cdd:COG4717 364 QlEELEQEIAALlaeagvedeeelrAALEQAEEYQEL-KEELEELEEQLEELLGELEELLEALDEEELEEElEELEEELE 442
|
410
....*....|..
gi 281306779 461 KLRQEVDQLKGR 472
Cdd:COG4717 443 ELEEELEELREE 454
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
235-472 |
8.66e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 8.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 235 LEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREAts 314
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 315 ihdlnDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGnIEEHLRQ 394
Cdd:COG4372 118 -----EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQA-LDELLKE 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281306779 395 LEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGR 472
Cdd:COG4372 192 ANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILV 269
|
|
| SAM_superfamily |
cd09487 |
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
952-1003 |
1.09e-05 |
|
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: 43.77 E-value: 1.09e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 281306779 952 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGI 1003
Cdd:cd09487 4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
1030-1100 |
1.23e-05 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 44.18 E-value: 1.23e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281306779 1030 VLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALdeNFDHNTLAlvlQIPTQNTQARQVMEREFNNLL 1100
Cdd:pfam07647 1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK---RLGITSVGHRRKILKKIQELK 66
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
165-470 |
1.37e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 49.66 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 165 DEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGIRDGVAEEEETVDlgpkrlwkDDTGRVEELQGLLEKQNYELSQ 244
Cdd:TIGR00606 790 DVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELD--------TVVSKIELNRKLIQDQQEQIQH 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 245 ARERLVTLSATVTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLEN 324
Cdd:TIGR00606 862 LKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQD 941
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 325 ELankESLHRQCEEKARHLQELLE-VAEQKLQQTMRKaetlpevEAELSQRIAALTKAEERHGNIEEHLRQLEgqleekn 403
Cdd:TIGR00606 942 KV---NDIKEKVKNIHGYMKDIENkIQDGKDDYLKQK-------ETELNTVNAQLEECEKHQEKINEDMRLMR------- 1004
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281306779 404 QELARVRQREKMNEDHNKRLsdTVDRLLSESNERLQLHLKE--RMAALEEKgrlsEEIEKLRQEVDQLK 470
Cdd:TIGR00606 1005 QDIDTQKIQERWLQDNLTLR--KRENELKEVEEELKQHLKEmgQMQVLQMK----QEHQKLEENIDLIK 1067
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
31-468 |
1.54e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.51 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 31 VNMLDEREKLLESLRESQETLVATQSRLQDALHERDQLQ-------------RHLNSALPQEFATLTRELSMCREQLLER 97
Cdd:PRK01156 321 INKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEgyemdynsylksiESLKKKIEEYSKNIERMSAFISEILKIQ 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 98 EEEISELKAERNNTRLLLEHLECLVSRHERSLRmtvvkrqaqspSGVSSEVEVLKALKSLFEHHKAL-------DEKVRE 170
Cdd:PRK01156 401 EIDPDAIKKELNEINVKLQDISSKVSSLNQRIR-----------ALRENLDELSRNMEMLNGQSVCPvcgttlgEEKSNH 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 171 RLRAALERVTTLEEQLAGAHQQVSALqqgagirdgvaeEEETVDLGPK--RLWKDDTGRVEELQGLLEKQNYELSQARER 248
Cdd:PRK01156 470 IINHYNEKKSRLEEKIREIEIEVKDI------------DEKIVDLKKRkeYLESEEINKSINEYNKIESARADLEDIKIK 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 249 LVTLSATVTELE-----------EDLGTARRDLIKSeeLSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHD 317
Cdd:PRK01156 538 INELKDKHDKYEeiknrykslklEDLDSKRTSWLNA--LAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKS 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 318 LND----KLENELANKESLHRQCEEKARHLQELLEvaeqklqqtmrKAETLPEVEAELSQRIAALTKAEERHGNIEEHLR 393
Cdd:PRK01156 616 YIDksirEIENEANNLNNKYNEIQENKILIEKLRG-----------KIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLK 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 394 QLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVdrllSESNERLQlHLKERMAALEEKGRLSEEIEK------LRQEVD 467
Cdd:PRK01156 685 KSRKALDDAKANRARLESTIEILRTRINELSDRI----NDINETLE-SMKKIKKAIGDLKRLREAFDKsgvpamIRKSAS 759
|
.
gi 281306779 468 Q 468
Cdd:PRK01156 760 Q 760
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
30-459 |
1.70e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 30 MVNMLDEREKLLESLRESQETLVATQSRLQDALHERDQLQRHLNSALPQEFATLTRELSMCREQLLEREEEISELKAERN 109
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIG 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 110 NTRLLLEHLECLVSRHERSLRMT-VVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRErLRAALERVttleEQLAG 188
Cdd:PRK03918 416 ELKKEIKELKKAIEELKKAKGKCpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERK-LRKELREL----EKVLK 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 189 AHQQVSALQQGAGIRDGVAEEEETVDLGP-KRLWKDDTGRVEELQGLlEKQNYELSQARERLVTLSATVTELEEDLGTAR 267
Cdd:PRK03918 491 KESELIKLKELAEQLKELEEKLKKYNLEElEKKAEEYEKLKEKLIKL-KGEIKSLKKELEKLEELKKKLAELEKKLDELE 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 268 rdliksEELSGKHQRDLREALAQKEDMEERITTLEKRY------LAAQREATSIHDLNDKLENELANKESLHRQCEEKAR 341
Cdd:PRK03918 570 ------EELAELLKELEELGFESVEELEERLKELEPFYneylelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE 643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 342 HLQELLEVAEQKLQQT--MRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDH 419
Cdd:PRK03918 644 ELRKELEELEKKYSEEeyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERV 723
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 281306779 420 NKrlsdtvdrlLSESNERLQLHLKERmaALEEKGRLSEEI 459
Cdd:PRK03918 724 EE---------LREKVKKYKALLKER--ALSKVGEIASEI 752
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
24-472 |
1.74e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.30 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 24 ANFEQLMVNMLDEREKLLESLRESQETLVATQSRLQDALHERDQLQRHLnSALPQEFATLTRELSMCREQLLEREEEISE 103
Cdd:TIGR02169 360 AELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREL-DRLQEELQRLSEELADLNAAIAGIEAKINE 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 104 LKAERNNTRLLLEHLE-------CLVSRHERSLRMTVVKRQAQSP--SGVSSEVEVLKALKSLFEHHKALDEKVRERLRA 174
Cdd:TIGR02169 439 LEEEKEDKALEIKKQEwkleqlaADLSKYEQELYDLKEEYDRVEKelSKLQRELAEAEAQARASEERVRGGRAVEEVLKA 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 175 ALERVTTLEEQLAGAHQQ-VSALQQGAGIR--------DGVAEEE----ETVDLGPKRLWKDDTGRVEELQGLLEKQN-- 239
Cdd:TIGR02169 519 SIQGVHGTVAQLGSVGERyATAIEVAAGNRlnnvvvedDAVAKEAiellKRRKAGRATFLPLNKMRDERRDLSILSEDgv 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 240 -------YELSQARERLVTLSATVTELEEDLGTARRDLI-------------KSEELSGKHQR------DLREALAQKED 293
Cdd:TIGR02169 599 igfavdlVEFDPKYEPAFKYVFGDTLVVEDIEAARRLMGkyrmvtlegelfeKSGAMTGGSRAprggilFSRSEPAELQR 678
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 294 MEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHR-------QCEEKARHLQELLEVAEQKLQQTMRKAET--- 363
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGeiekeieQLEQEEEKLKERLEELEEDLSSLEQEIENvks 758
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 364 -LPEVEAELSQRIAALTKAEERHGNIEEHL-----RQLEGQLEEKNQELARVRQR-----EKMNEDHNKR--LSDTVDRL 430
Cdd:TIGR02169 759 eLKELEARIEELEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEARlreieQKLNRLTLEKeyLEKEIQEL 838
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 281306779 431 LSESNErLQLHLKERMAALEE----KGRLSEEIEKLRQEVDQLKGR 472
Cdd:TIGR02169 839 QEQRID-LKEQIKSIEKEIENlngkKEELEEELEELEAALRDLESR 883
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
1030-1101 |
2.02e-05 |
|
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: 43.44 E-value: 2.02e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281306779 1030 VLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHntlalVLQIPTQNTQARQVMEREFNNLLA 1101
Cdd:smart00454 1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEED-----LKELGITKLGHRKKILKAIQKLKE 67
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
227-465 |
2.19e-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: 47.88 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 227 RVEELQGLLEKQNYELSQA-RERLvTLSATVTELEEDLgtarRDLIKSEELSgkhQRDLREALAQKEdmeERITTLEKRY 305
Cdd:pfam15905 95 RLQALEEELEKVEAKLNAAvREKT-SLSASVASLEKQL----LELTRVNELL---KAKFSEDGTQKK---MSSLSMELMK 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 306 LAAQREAtsihdlndKLENELANKESLHRQCEEKARHLQEL-LEVA--EQKLQQTMR-KAETLPEVEaELSQRIAALTKA 381
Cdd:pfam15905 164 LRNKLEA--------KMKEVMAKQEGMEGKLQVTQKNLEHSkGKVAqlEEKLVSTEKeKIEEKSETE-KLLEYITELSCV 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 382 EERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHN-----------KRLSDTVDRLLSESNERLQLHLKErMAALE 450
Cdd:pfam15905 235 SEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELskqikdlnekcKLLESEKEELLREYEEKEQTLNAE-LEELK 313
|
250
....*....|....*.
gi 281306779 451 EKGRL-SEEIEKLRQE 465
Cdd:pfam15905 314 EKLTLeEQEHQKLQQK 329
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
235-470 |
2.75e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.43 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 235 LEKQNYELSQARERLVTLSATVTELEEDLgtarrdliKSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATS 314
Cdd:pfam02463 171 KKEALKKLIEETENLAELIIDLEELKLQE--------LKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 315 IHDLNDK------------LENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIaaLTKAE 382
Cdd:pfam02463 243 QELLRDEqeeiesskqeieKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEK--LKESE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 383 ERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKL 462
Cdd:pfam02463 321 KEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELK 400
|
....*...
gi 281306779 463 RQEVDQLK 470
Cdd:pfam02463 401 SEEEKEAQ 408
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
245-412 |
3.19e-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: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 245 ARERLVTLSATVTELEEDLGTARRDLIKSEELSgKHQRDLREALAQKEDM----------EERITTLEKRY--------- 305
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAEL-DALQERREALQRLAEYswdeidvasaEREIAELEAELerldassdd 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 306 -LAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEER 384
Cdd:COG4913 687 lAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERE 766
|
170 180
....*....|....*....|....*....
gi 281306779 385 HG-NIEEHLRQLEGQLEEKNQELARVRQR 412
Cdd:COG4913 767 LReNLEERIDALRARLNRAEEELERAMRA 795
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
227-469 |
4.08e-05 |
|
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: 47.64 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 227 RVEELQGLLEKQNYELSQARERLVtlsatvtELEEDLGTAR-----RDLIKSEELSGKHQRDLREA----LAQKEDMEER 297
Cdd:COG5185 276 SSKRLNENANNLIKQFENTKEKIA-------EYTKSIDIKKateslEEQLAAAEAEQELEESKRETetgiQNLTAEIEQG 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 298 ITTLEKRYLAAQREATSIHDLND------KLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAEtlpeveael 371
Cdd:COG5185 349 QESLTENLEAIKEEIENIVGEVElsksseELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAAD--------- 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 372 sqriaalTKAEERHGNIEEHLRQLEgQLEEKNQELAR--VRQREKMNEDHNKRLSDTVDRLLSE-------SNERLQlHL 442
Cdd:COG5185 420 -------RQIEELQRQIEQATSSNE-EVSKLLNELISelNKVMREADEESQSRLEEAYDEINRSvrskkedLNEELT-QI 490
|
250 260 270
....*....|....*....|....*....|..
gi 281306779 443 KERMAAL-----EEKGRLSEEIEKLRQEVDQL 469
Cdd:COG5185 491 ESRVSTLkatleKLRAKLERQLEGVRSKLDQV 522
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
281-472 |
4.51e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 281 QRDLREALAQKEDMEERIttlekrylaaqrEATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRK 360
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEK------------EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEER 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 361 AETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQL 440
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDR 329
|
170 180 190
....*....|....*....|....*....|..
gi 281306779 441 HLKERMAAleekGRLSEEIEKLRQEVDQLKGR 472
Cdd:PRK02224 330 LEECRVAA----QAHNEEAESLREDADDLEER 357
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
320-470 |
5.43e-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: 45.83 E-value: 5.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 320 DKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAEtlPEVEAELSQRIAALTKAEERHG-----------NI 388
Cdd:pfam04012 39 VKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGN--EELAREALAEKKSLEKQAEALEtqlaqqrsaveQL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 389 EEHLRQLEGQLEEKNQELARVRQREKMNEdHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEK---LRQE 465
Cdd:pfam04012 117 RKQLAALETKIQQLKAKKNLLKARLKAAK-AQEAVQTSLGSLSTSSATDSFERIEEKIEEREARADAAAELASavdLDAK 195
|
....*
gi 281306779 466 VDQLK 470
Cdd:pfam04012 196 LEQAG 200
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
30-415 |
6.02e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 46.98 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 30 MVNMLDEREKLLESLRESQETLVATQSRLQDALHERDQLQRHLNS------ALPQEFATLTRELSmcreqllereeeisE 103
Cdd:pfam19220 15 MADRLEDLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQeraaygKLRRELAGLTRRLS--------------A 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 104 LKAERNNTRLLLEHLECLVSRHER---SLRMTVVKRQAQSPS---GVSSEVEVLKALKslfEHHKALdekvRERLRAALE 177
Cdd:pfam19220 81 AEGELEELVARLAKLEAALREAEAakeELRIELRDKTAQAEAlerQLAAETEQNRALE---EENKAL----REEAQAAEK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 178 RVTTLEEQLAGAHQqvsalqqgagiRDGVAEEEetvdlgpkrlwkddtgrVEELQGLLEKQNYELSQarerlvtLSATVT 257
Cdd:pfam19220 154 ALQRAEGELATARE-----------RLALLEQE-----------------NRRLQALSEEQAAELAE-------LTRRLA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 258 ELEEDLGTARRDLIKSE----ELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLH 333
Cdd:pfam19220 199 ELETQLDATRARLRALEgqlaAEQAERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAI 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 334 RQCEEKARH--------------LQELLEVAEQKLQQTMRKAETLPEVEAELSQRIA----ALTKAEERHGNIEEHLRQL 395
Cdd:pfam19220 279 RAAERRLKEasierdtlerrlagLEADLERRTQQFQEMQRARAELEERAEMLTKALAakdaALERAEERIASLSDRIAEL 358
|
410 420
....*....|....*....|....*..
gi 281306779 396 EGQ-------LEEKNQELARVRQREKM 415
Cdd:pfam19220 359 TKRfeveraaLEQANRRLKEELQRERA 385
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
166-411 |
7.73e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 7.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 166 EKVRERLRAALERVTTLEEQLAGAHQQVSALQQgagirdgvaeeeetvdlgpkrlwkddtgRVEELQGLLEKQNYELSQA 245
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNE----------------------------EYNELQAELEALQAEIDKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 246 RERLVTLSATVTELEEDLGTARRDLIKSEELSGkhqrdLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNdKLENE 325
Cdd:COG3883 71 QAEIAEAEAEIEERREELGERARALYRSGGSVS-----YLDVLLGSESFSDFLDRLSALSKIADADADLLEELK-ADKAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 326 LANKESlhrQCEEKARHLQELLEVAEQKLQqtmrkaetlpEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQE 405
Cdd:COG3883 145 LEAKKA---ELEAKLAELEALKAELEAAKA----------ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
....*.
gi 281306779 406 LARVRQ 411
Cdd:COG3883 212 AAAAAA 217
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
81-324 |
8.90e-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: 8.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 81 ATLTRELSMCREQLLEREEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgVSSEVE-------VLKA 153
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAE---LEAELErldassdDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 154 LKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGIRDGVAEEEETVDLGPKRLWKDDTGRV----E 229
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVErelrE 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 230 ELQGLLEKQNYELSQARERLVTL--------SATVTELEEDLGT-----ARRDLIKSEELSgKHQRDLREALaqKEDMEE 296
Cdd:COG4913 770 NLEERIDALRARLNRAEEELERAmrafnrewPAETADLDADLESlpeylALLDRLEEDGLP-EYEERFKELL--NENSIE 846
|
250 260
....*....|....*....|....*....
gi 281306779 297 RITTLEKRYLAAQREATS-IHDLNDKLEN 324
Cdd:COG4913 847 FVADLLSKLRRAIREIKErIDPLNDSLKR 875
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
166-476 |
1.04e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.87 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 166 EKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAG-IRDGVA--EEEETVDLGPKRLWKDDTGRVEELQGLLEKQNYEL 242
Cdd:COG3096 378 AEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIqYQQAVQalEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEV 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 243 SQARERLVTLSATVTELEEDLGTARRdlIKSE-ELSGKHQRdLREALAQKEdmeerittlEKRYLAAQREAtsihdlndk 321
Cdd:COG3096 458 LELEQKLSVADAARRQFEKAYELVCK--IAGEvERSQAWQT-ARELLRRYR---------SQQALAQRLQQ--------- 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 322 LENELANKEslhrQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEE 401
Cdd:COG3096 517 LRAQLAELE----QRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRA 592
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281306779 402 KNQELARVRQREKMNEDHNKRLSDTVDRLLSESNE----RLQLHLKERMAALEEKgRLSEEIEKLRQEVDQLKGRGGPF 476
Cdd:COG3096 593 RIKELAARAPAWLAAQDALERLREQSGEALADSQEvtaaMQQLLEREREATVERD-ELAARKQALESQIERLSQPGGAE 670
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
154-417 |
1.32e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 154 LKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQgagirdgvaeeeetvdlgpkrlwkddtgRVEELQG 233
Cdd:COG4372 15 LFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQARE----------------------------ELEQLEE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 234 LLEKQNYELSQARERLvtlsatvTELEEDLGTARRDLIKSEElsgkhqrDLREALAQKEDMEERITTLEKRYLAAQREAT 313
Cdd:COG4372 67 ELEQARSELEQLEEEL-------EELNEQLQAAQAELAQAQE-------ELESLQEEAEELQEELEELQKERQDLEQQRK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 314 SIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMrkaetlpevEAELSQRIAALTKAEERHGNIEEHLR 393
Cdd:COG4372 133 QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS---------EAEAEQALDELLKEANRNAEKEEELA 203
|
250 260
....*....|....*....|....
gi 281306779 394 QLEGQLEEKNQELARVRQREKMNE 417
Cdd:COG4372 204 EAEKLIESLPRELAEELLEAKDSL 227
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
301-472 |
1.47e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 301 LEKRYLAAQREATSIHDLNDKLE-NELANKESLHRQCEEKARHLQELlevaEQKLQQTMRKAETLPEVEAELSQRIAALT 379
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNlKELKELEEELKEAEEKEEEYAEL----QEELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 380 KAEERHGNIEEhLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEI 459
Cdd:COG4717 123 KLLQLLPLYQE-LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
170
....*....|...
gi 281306779 460 EKLRQEVDQLKGR 472
Cdd:COG4717 202 EELQQRLAELEEE 214
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
178-454 |
1.82e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.66 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 178 RVTTLEEQLAGAHQQVSALQQGAGIRDGVAEEEETVDLGPKRLWKddtGRVEELQGLLEKQNYELSQARERLVTLS---- 253
Cdd:pfam07888 28 RAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWE---RQRRELESRVAELKEELRQSREKHEELEekyk 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 254 ------------------------ATVTELEEDLGT-ARRDLIKSEELSGKHQRdLREALAQKEDMEERITTLEKRYLAA 308
Cdd:pfam07888 105 elsasseelseekdallaqraaheARIRELEEDIKTlTQRVLERETELERMKER-AKKAGAQRKEEEAERKQLQAKLQQT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 309 QREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQK---LQQTMRKAETLPEVeAELSQRIAALTKAEER- 384
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKeaeNEALLEELRSLQER-LNASERKVEGLGEELSs 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 385 ------HGNIEEH-----LRQLEGQLEEKN-----------QELARVRQREKMNEDHNKRLSDTVDRLlsesNERLQLHL 442
Cdd:pfam07888 263 maaqrdRTQAELHqarlqAAQLTLQLADASlalregrarwaQERETLQQSAEADKDRIEKLSAELQRL----EERLQEER 338
|
330
....*....|..
gi 281306779 443 KERMAALEEKGR 454
Cdd:pfam07888 339 MEREKLEVELGR 350
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
172-360 |
1.86e-04 |
|
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: 43.74 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 172 LRAALERVTTLEEQLAGAHQQVSALQqgagirdgvaeeEETVDLgpKRLWKDDT-------GRVEELQGLLEKQNYELSQ 244
Cdd:pfam15619 6 LSARLHKIKELQNELAELQSKLEELR------------KENRLL--KRLQKRQEkalgkyeGTESELPQLIARHNEEVRV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 245 ARERLVTLSATVTELEEDLGTARRDLIKSEElSGKHQRDLREA--LAQKEDMEERITTLEKRYLAAQREatsIHDLNDKL 322
Cdd:pfam15619 72 LRERLRRLQEKERDLERKLKEKEAELLRLRD-QLKRLEKLSEDknLAEREELQKKLEQLEAKLEDKDEK---IQDLERKL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 281306779 323 EN-------ELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRK 360
Cdd:pfam15619 148 ELenksfrrQLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKERE 192
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
158-465 |
2.42e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.34 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 158 FEHHKALDEKvRERLRAALERVTTLEEQLAGAHQQVSALQQG--AGIRDGVAEEEETVD------------LGPKRLWKD 223
Cdd:TIGR00618 186 FAKKKSLHGK-AELLTLRSQLLTLCTPCMPDTYHERKQVLEKelKHLREALQQTQQSHAyltqkreaqeeqLKKQQLLKQ 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 224 DTGRVEELQGL---LEKQNYELSQAR--ERLVTLSATVTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERI 298
Cdd:TIGR00618 265 LRARIEELRAQeavLEETQERINRARkaAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQR 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 299 TTLEKrylaAQREATSIHDLNDKLENELANKESLHRQcEEKARHLQELLEVAEQKLQQTMRKAETLPE----VEAELSQR 374
Cdd:TIGR00618 345 RLLQT----LHSQEIHIRDAHEVATSIREISCQQHTL-TQHIHTLQQQKTTLTQKLQSLCKELDILQReqatIDTRTSAF 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 375 IAALTKAEERHGNIEEHLRqlegQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKErmaalEEKGR 454
Cdd:TIGR00618 420 RDLQGQLAHAKKQQELQQR----YAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQE-----TRKKA 490
|
330
....*....|.
gi 281306779 455 LSEEIEKLRQE 465
Cdd:TIGR00618 491 VVLARLLELQE 501
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
313-423 |
2.63e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.20 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 313 TSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRI-----AALTKAEERHGN 387
Cdd:PRK00409 509 KLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAekeaqQAIKEAKKEADE 588
|
90 100 110
....*....|....*....|....*....|....*....
gi 281306779 388 IEEHLRQLE--GQLEEKNQELARVRQR-EKMNEDHNKRL 423
Cdd:PRK00409 589 IIKELRQLQkgGYASVKAHELIEARKRlNKANEKKEKKK 627
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
230-470 |
2.78e-04 |
|
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: 45.01 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 230 ELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERIttlekrylaaQ 309
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKEN----------Q 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 310 REATSIHDLNDK---LENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHG 386
Cdd:TIGR04523 381 SYKQEIKNLESQindLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLD 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 387 NIEEHLRQ----LEGQ-------LEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNErlqlhLKERMAALE----- 450
Cdd:TIGR04523 461 NTRESLETqlkvLSRSinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS-----LKEKIEKLEsekke 535
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 281306779 451 --------------------------EKGRLSEEIEKLRQEVDQLK 470
Cdd:TIGR04523 536 keskisdledelnkddfelkkenlekEIDEKNKEIEELKQTQKSLK 581
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
258-470 |
2.85e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 44.11 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 258 ELEEDLGTARRDLI-KSEELSGKHQRDLREALAQkeDMEERITTLE-------KRYLAAQREATSIHDLNDK-------- 321
Cdd:cd16269 94 KLMEQLEEKKEEFCkQNEEASSKRCQALLQELSA--PLEEKISQGSysvpggyQLYLEDREKLVEKYRQVPRkgvkaeev 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 322 LENELANKESlhrqcEEKArHLQ--ELLEVAEQKLQQTMRKAETLpEVEAELSQRIAALT--KAEERHGNIEEHLRQLEG 397
Cdd:cd16269 172 LQEFLQSKEA-----EAEA-ILQadQALTEKEKEIEAERAKAEAA-EQERKLLEEQQRELeqKLEDQERSYEEHLRQLKE 244
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281306779 398 QLEEKNQelarvrqrekmnedhnkrlsdtvdRLLSESNERLQLHLKErMAALEEKGrLSEEIEKLRQEVDQLK 470
Cdd:cd16269 245 KMEEERE------------------------NLLKEQERALESKLKE-QEALLEEG-FKEQAELLQEEIRSLK 291
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
169-465 |
3.05e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.86 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 169 RERLRAALERVTTLEEQLAGAHQQVSALQQGAGIRDGVAEEEETVDLGPKRLWKDDTGRVEE-----LQGLLEKQNYELS 243
Cdd:pfam02029 12 RRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREErrqkrLQEALERQKEFDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 244 QARE--RLVTLSATVTELEEDLGTARRDLIKSEELSGK-----------HQRDLREALAQ---KEDMEERITTLEKRYLA 307
Cdd:pfam02029 92 TIADekESVAERKENNEEEENSSWEKEEKRDSRLGRYKeeeteirekeyQENKWSTEVRQaeeEGEEEEDKSEEAEEVPT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 308 AQREATSIHDLNDKLENELA--NKESLHRQ---CEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAE 382
Cdd:pfam02029 172 ENFAKEEVKDEKIKKEKKVKyeSKVFLDQKrghPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 383 ErhgnieehLRQLEGQLEEKNQELARVRQREKMNE-DHNKRLSDTVDRLLSESNERLQLHLKERMAALEE-KGRLSEEIE 460
Cdd:pfam02029 252 E--------LRRRRQEKESEEFEKLRQKQQEAELElEELKKKREERRKLLEEEEQRRKQEEAERKLREEEeKRRMKEEIE 323
|
....*
gi 281306779 461 KLRQE 465
Cdd:pfam02029 324 RRRAE 328
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
37-469 |
3.23e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 37 REKL--LESLRESQETLVATQSRLQDaLHERDQLQRHLNSAL----------PQEFATLTRELSMCREQLLEREEEISEL 104
Cdd:PRK04863 499 RELLrrLREQRHLAEQLQQLRMRLSE-LEQRLRQQQRAERLLaefckrlgknLDDEDELEQLQEELEARLESLSESVSEA 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 105 KAERNNTRLLLEHLECLVSRHE------RSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALdEKVRERLRAALER 178
Cdd:PRK04863 578 RERRMALRQQLEQLQARIQRLAarapawLAAQDALARLREQSGEEFEDSQDVTEYMQQLLEREREL-TVERDELAARKQA 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 179 vttLEEqlagahqQVSALQQGAGIRDG-------------VAEEEETVDLgpkrlwkDDTGRVEELQGLLEKQNY--ELS 243
Cdd:PRK04863 657 ---LDE-------EIERLSQPGGSEDPrlnalaerfggvlLSEIYDDVSL-------EDAPYFSALYGPARHAIVvpDLS 719
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 244 QARERLVTL--------------------SATVTELEEDL--GTARRDL----IKSEELSGKHQRDLR-EAL-AQKEDME 295
Cdd:PRK04863 720 DAAEQLAGLedcpedlyliegdpdsfddsVFSVEELEKAVvvKIADRQWrysrFPEVPLFGRAAREKRiEQLrAEREELA 799
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 296 ERITTLEKRYLAAQR--EATS------------------IHDLNDK---LENELANKESLHRQCEEKARHLQELLEVAEQ 352
Cdd:PRK04863 800 ERYATLSFDVQKLQRlhQAFSrfigshlavafeadpeaeLRQLNRRrveLERALADHESQEQQQRSQLEQAKEGLSALNR 879
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 353 KLQQTMRKA-ETLPEVEAELSQRIAALTKAE---ERHGNieeHLRQLEGQ---LEEKNQELARVRQR----EKMNEDHNK 421
Cdd:PRK04863 880 LLPRLNLLAdETLADRVEEIREQLDEAEEAKrfvQQHGN---ALAQLEPIvsvLQSDPEQFEQLKQDyqqaQQTQRDAKQ 956
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281306779 422 R---LSDTVDR-----------LLSESNErLQLHLKERMAALEEKGRlsEEIEKLRQEVDQL 469
Cdd:PRK04863 957 QafaLTEVVQRrahfsyedaaeMLAKNSD-LNEKLRQRLEQAEQERT--RAREQLRQAQAQL 1015
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
281-470 |
3.78e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 44.68 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 281 QRDLREALAQKEDMEERITTLekRYLAAQREATSIHDLND-KLENE---LANKESLHRQCEEKARHLQELLEVAEQKLQQ 356
Cdd:COG0497 171 KKELEELRADEAERARELDLL--RFQLEELEAAALQPGEEeELEEErrrLSNAEKLREALQEALEALSGGEGGALDLLGQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 357 TMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQRekMNEDHN--KRLSDTVDRLLSes 434
Cdd:COG0497 249 ALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEER--LALLRRlaRKYGVTVEELLA-- 324
|
170 180 190
....*....|....*....|....*....|....*.
gi 281306779 435 nerLQLHLKERMAALEEkgrLSEEIEKLRQEVDQLK 470
Cdd:COG0497 325 ---YAEELRAELAELEN---SDERLEELEAELAEAE 354
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
135-470 |
3.86e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 44.75 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 135 KRQAQSPSGVSSEV-EVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGIRdgvaEEEETV 213
Cdd:pfam09731 88 QVKIPRQSGVSSEVaEEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAIQ----AVKAHT 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 214 DLGPKRLWKDDTGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSeelsGKHQRDLREALAQKED 293
Cdd:pfam09731 164 DSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPK----LPEHLDNVEEKVEKAQ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 294 MEERITTLEKRYLAA-----QREATSIHD---LNDKLENELANKE------SLHRQCEEKARHLQELLEVAEQKLQQTMR 359
Cdd:pfam09731 240 SLAKLVDQYKELVASerivfQQELVSIFPdiiPVLKEDNLLSNDDlnsliaHAHREIDQLSKKLAELKKREEKHIERALE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 360 KA-ETLPEVEAELSQRIaaltkaeerhgniEEHLRQLEGQLEEKNQElARVRQREKM-----------NEDHNKRLSDTV 427
Cdd:pfam09731 320 KQkEELDKLAEELSARL-------------EEVRAADEAQLRLEFER-EREEIRESYeeklrtelerqAEAHEEHLKDVL 385
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 281306779 428 DRLLSESNERLQLHLKERMAalEEKGRLSEEIEKLRQEVDQLK 470
Cdd:pfam09731 386 VEQEIELQREFLQDIKEKVE--EERAGRLLKLNELLANLKGLE 426
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
273-410 |
3.91e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.19 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 273 SEELSGKHQR---------DLREALA----QKEDMEERITTLEKRYLAAQREatsihdlNDKLENELANKESLHRQCEEK 339
Cdd:PRK09039 45 SREISGKDSAldrlnsqiaELADLLSlerqGNQDLQDSVANLRASLSAAEAE-------RSRLQALLAELAGAGAAAEGR 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281306779 340 ARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAAL--------TKAEERHGNIEEHLRQLEGQLEEKNQELARVR 410
Cdd:PRK09039 118 AGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALeaaldaseKRDRESQAKIADLGRRLNVALAQRVQELNRYR 196
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
283-470 |
3.99e-04 |
|
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: 44.29 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 283 DLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMR--- 359
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRlet 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 360 -------KAETLPEVEAELSQRIAALTKAEE------------RHGNieEHLRQLEGQLE---EKNQELARVRQREKMNE 417
Cdd:pfam05622 81 arddyriKCEELEKEVLELQHRNEELTSLAEeaqalkdemdilRESS--DKVKKLEATVEtykKKLEDLGDLRRQVKLLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 418 DHN----------------------------KRLSDTVDRLLSESN--ERLQL---HLKERMAALE-EKGRLSEEIEKLR 463
Cdd:pfam05622 159 ERNaeymqrtlqleeelkkanalrgqletykRQVQELHGKLSEESKkaDKLEFeykKLEEKLEALQkEKERLIIERDTLR 238
|
....*..
gi 281306779 464 QEVDQLK 470
Cdd:pfam05622 239 ETNEELR 245
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
169-412 |
4.25e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 169 RERLRAAL----ERVTTLEEQLAGAHQQVSALQQGAGIRDGVAEEEETVDlgpkrlwkddtgRVEELQGllekqnyELSQ 244
Cdd:COG3206 170 REEARKALefleEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQ------------QLSELES-------QLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 245 ARERLVTLSATVTELEEDLGTARRDLikSEELSGKHQRDLREALAQkedMEERITTLEKRYLAAQREATSihdlndkLEN 324
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDAL--PELLQSPVIQQLRAQLAE---LEAELAELSARYTPNHPDVIA-------LRA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 325 ELANKEslhrqceekarhlQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQ 404
Cdd:COG3206 299 QIAALR-------------AQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARE 365
|
....*...
gi 281306779 405 ELARVRQR 412
Cdd:COG3206 366 LYESLLQR 373
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
257-472 |
5.18e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.58 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 257 TELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERIT--TLEKRYLAAQREATSIHDLNDKLENELANKESLHR 334
Cdd:pfam02463 156 LEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQelKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLN 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 335 QCEEKARHLQELLEVAEQKLQQTmrkaetLPEVEAELSQRIAALTKAEER-HGNIEEHLRQLEGQLEEKNQELARVRQRE 413
Cdd:pfam02463 236 EERIDLLQELLRDEQEEIESSKQ------EIEKEEEKLAQVLKENKEEEKeKKLQEEELKLLAKEEEELKSELLKLERRK 309
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 281306779 414 KMNEDhNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGR 472
Cdd:pfam02463 310 VDDEE-KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEK 367
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
247-406 |
5.72e-04 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 42.25 E-value: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 247 ERLVTLSATVTELEEDLGTARRDLI-----KSEELSGKHQRDLREALAQKED-MEERITTLEKRYLAAQREATS-IHDLN 319
Cdd:pfam01442 4 DSLDELSTYAEELQEQLGPVAQELVdrlekETEALRERLQKDLEEVRAKLEPyLEELQAKLGQNVEELRQRLEPyTEELR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 320 DKLENELankESLHRQCEEKARHLQELLEVAEQKLQQTMrkAETLPEVEAELSQRIAAL-----TKAEERHGNIEEHLRQ 394
Cdd:pfam01442 84 KRLNADA---EELQEKLAPYGEELRERLEQNVDALRARL--APYAEELRQKLAERLEELkeslaPYAEEVQAQLSQRLQE 158
|
170
....*....|..
gi 281306779 395 LEGQLEEKNQEL 406
Cdd:pfam01442 159 LREKLEPQAEDL 170
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
228-470 |
5.87e-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: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 228 VEELQGLLEKqnYELSQARERLVTLSATVTELEEDLGTARRDLiksEELSGKHQRDlREALaqkEDMEERITTLEKRYLA 307
Cdd:pfam06160 69 LFEAEELNDK--YRFKKAKKALDEIEELLDDIEEDIKQILEEL---DELLESEEKN-REEV---EELKDKYRELRKTLLA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 308 aQREA--TSIhdlnDKLENELANKESLHRQCEE--------KARHLQELLEVAEQKLQQTMRK--------AETLPEVEA 369
Cdd:pfam06160 140 -NRFSygPAI----DELEKQLAEIEEEFSQFEEltesgdylEAREVLEKLEEETDALEELMEDipplyeelKTELPDQLE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 370 ELSQRIAALTKAEER--HGNIEEHLRQLEGQLEE-----KNQELARVrqrEKMNEDHNKRLSDTVDRLLSESNERLQLHl 442
Cdd:pfam06160 215 ELKEGYREMEEEGYAleHLNVDKEIQQLEEQLEEnlallENLELDEA---EEALEEIEERIDQLYDLLEKEVDAKKYVE- 290
|
250 260
....*....|....*....|....*...
gi 281306779 443 kermaalEEKGRLSEEIEKLRQEVDQLK 470
Cdd:pfam06160 291 -------KNLPEIEDYLEHAEEQNKELK 311
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
38-340 |
6.03e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.12 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 38 EKLLESLRESQE-TLVATQSRLQ------DALHERDQLQRHLNsalpqefaTLTRELSmcreqllEREEEISELKAERNN 110
Cdd:PLN02939 131 EDLVGMIQNAEKnILLLNQARLQaledleKILTEKEALQGKIN--------ILEMRLS-------ETDARIKLAAQEKIH 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 111 TRLLLEHLEclvsrherSLRMTVVKRQAQSPSGVSSEVEVLKALKslfEHHKALDEKVrERLRAALERVTTLEEQLAGAH 190
Cdd:PLN02939 196 VEILEEQLE--------KLRNELLIRGATEGLCVHSLSKELDVLK---EENMLLKDDI-QFLKAELIEVAETEERVFKLE 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 191 QQVSALQqgAGIRD----GVAEEEETVDLGPKR---LWKddtgRVEELQGLLEKQNYELSQArerlvtlsATVTELEEDL 263
Cdd:PLN02939 264 KERSLLD--ASLREleskFIVAQEDVSKLSPLQydcWWE----KVENLQDLLDRATNQVEKA--------ALVLDQNQDL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 264 gtarRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQRE--------ATSIHDLNDKLENelANKESLHRQ 335
Cdd:PLN02939 330 ----RDKVDKLEASLKEANVSKFSSYKVELLQQKLKLLEERLQASDHEihsyiqlyQESIKEFQDTLSK--LKEESKKRS 403
|
....*
gi 281306779 336 CEEKA 340
Cdd:PLN02939 404 LEHPA 408
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
164-472 |
6.76e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 6.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 164 LDEKVRERLRAALERVTT------LEEQLAGAHQQVSALQQG--------AGIRDGVAEEEETVDLGPK----------- 218
Cdd:pfam01576 112 LDEEEAARQKLQLEKVTTeakikkLEEDILLLEDQNSKLSKErklleeriSEFTSNLAEEEEKAKSLSKlknkheamisd 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 219 ---RLWKDDTGRvEELQGLLEKQNYELSQARERLVTLSATVTELeedlgtaRRDLIKSEElsgkhqrDLREALAQKEDME 295
Cdd:pfam01576 192 leeRLKKEEKGR-QELEKAKRKLEGESTDLQEQIAELQAQIAEL-------RAQLAKKEE-------ELQAALARLEEET 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 296 ERITTLEKRYlaaqREATS-IHDLNDKLENELANKESLHRQCeekaRHLQELLEVAEQKLQQTMRKAETLPEVEAELSQR 374
Cdd:pfam01576 257 AQKNNALKKI----RELEAqISELQEDLESERAARNKAEKQR----RDLGEELEALKTELEDTLDTTAAQQELRSKREQE 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 375 IAALTKAEERHGNIEE----HLRQLEGQ-LEEKNQELARVRqREKMNEDHNKRlsdtvdRLLSESNErLQLHLKERMAAl 449
Cdd:pfam01576 329 VTELKKALEEETRSHEaqlqEMRQKHTQaLEELTEQLEQAK-RNKANLEKAKQ------ALESENAE-LQAELRTLQQA- 399
|
330 340
....*....|....*....|...
gi 281306779 450 eeKGRLSEEIEKLRQEVDQLKGR 472
Cdd:pfam01576 400 --KQDSEHKRKKLEGQLQELQAR 420
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
168-326 |
6.83e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 42.71 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 168 VRERLRAALERVTTLEEQLAGAHQQVSALQQG-AGIRDGVAEEEETVDL------GPKRLWKDDTGRVEELQGLLEKQNY 240
Cdd:pfam00261 48 LEEELERTEERLAEALEKLEEAEKAADESERGrKVLENRALKDEEKMEIleaqlkEAKEIAEEADRKYEEVARKLVVVEG 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 241 ELSQARERLVTLSATVTELEEDLGTARRDLiKSEELSGKhqrdlrEALAQKEDMEERITTL-------EKRYLAAQREAT 313
Cdd:pfam00261 128 DLERAEERAELAESKIVELEEELKVVGNNL-KSLEASEE------KASEREDKYEEQIRFLteklkeaETRAEFAERSVQ 200
|
170
....*....|...
gi 281306779 314 SIHDLNDKLENEL 326
Cdd:pfam00261 201 KLEKEVDRLEDEL 213
|
|
| SAM_STIM-1,2-like |
cd09504 |
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ... |
830-888 |
7.70e-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: 39.24 E-value: 7.70e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281306779 830 WDGPTVVSWLELWVGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNALHRLKLRL 888
Cdd:cd09504 5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
286-411 |
8.16e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 8.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 286 EALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLEnELANKEslhrQCEEKARHLQELLEVAEQKLQQTMRKAETLP 365
Cdd:PRK11281 33 GDLPTEADVQAQLDALNKQKLLEAEDKLVQQDLEQTLA-LLDKID----RQKEETEQLKQQLAQAPAKLRQAQAELEALK 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 281306779 366 EVEA-ELSQRIAALTkaeerhgnieehLRQLEGQLEEKNQELARVRQ 411
Cdd:PRK11281 108 DDNDeETRETLSTLS------------LRQLESRLAQTLDQLQNAQN 142
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
106-411 |
8.36e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.67 E-value: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 106 AERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPsgvssevEVLKALKSLFehhKALDEKVRERLRAALERVTTLEEQ 185
Cdd:pfam12128 247 QQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQ-------ETSAELNQLL---RTLDDQWKEKRDELNGELSAADAA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 186 LAGAHQQVSALQQGAGIRDGVAEEEETVDLGPKRLWKDDTGRVEE-LQGLLEKQNyELSQARERLVtlSATVTELEEDLG 264
Cdd:pfam12128 317 VAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEErLKALTGKHQ-DVTAKYNRRR--SKIKEQNNRDIA 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 265 TARRDLIKSEELSGKHQRDLREALAQ-----KEDMEERITTLEKrylAAQREATSIHDLNDKLENELANKESLHRQceek 339
Cdd:pfam12128 394 GIKDKLAKIREARDRQLAVAEDDLQAleselREQLEAGKLEFNE---EEYRLKSRLGELKLRLNQATATPELLLQL---- 466
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281306779 340 aRHLQELLEVAEQKLQQTMRKAETLpeveaelsQRiaALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQ 411
Cdd:pfam12128 467 -ENFDERIERAREEQEAANAEVERL--------QS--ELRQARKRRDQASEALRQASRRLEERQSALDELEL 527
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
160-412 |
8.45e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.53 E-value: 8.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 160 HHKALD-----EKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAG-IRDGVAEEEEtVDLGPkrlwkddtGRVEELQG 233
Cdd:COG0497 143 QRELLDafaglEELLEEYREAYRAWRALKKELEELRADEAERARELDlLRFQLEELEA-AALQP--------GEEEELEE 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 234 LLEKqnyeLSQARERLVTLSATVTELEED-------LGTARRDLIK----SEELSGKHQRdLREALAQKEDMeerittle 302
Cdd:COG0497 214 ERRR----LSNAEKLREALQEALEALSGGeggaldlLGQALRALERlaeyDPSLAELAER-LESALIELEEA-------- 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 303 krylaaqreATSIHDLNDKLENElankeslhrqceekarhlQELLEVAEQKLQ---QTMRK----AETLPEVEAELSQRI 375
Cdd:COG0497 281 ---------ASELRRYLDSLEFD------------------PERLEEVEERLAllrRLARKygvtVEELLAYAEELRAEL 333
|
250 260 270
....*....|....*....|....*....|....*..
gi 281306779 376 AALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQR 412
Cdd:COG0497 334 AELENSDERLEELEAELAEAEAELLEAAEKLSAARKK 370
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
367-470 |
8.82e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 8.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 367 VEAELSQRIAALTKAEERHGNIEEHlrQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLlSESNERLQLHLKERM 446
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKE--HEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEK-DERIERLERELSEAR 454
|
90 100
....*....|....*....|....
gi 281306779 447 AALEEKGRLSEEIEKLRQEVDQLK 470
Cdd:COG2433 455 SEERREIRKDREISRLDREIERLE 478
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
53-430 |
9.94e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.42 E-value: 9.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 53 ATQSRLQDALHERDQLQ------RHLNSALPQEFATLTRELSMCREQLLEREEEISELKAERNNTRLLLEHLECLVSRHE 126
Cdd:TIGR00618 525 PLTRRMQRGEQTYAQLEtseedvYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLS 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 127 RSLRMTVVKRQAQSpsgVSSEVEVLKALKSLFEHHKAldekvrERLRAALERVTTLEEQLAGAHQQVSALQqgagIRDGV 206
Cdd:TIGR00618 605 EAEDMLACEQHALL---RKLQPEQDLQDVRLHLQQCS------QELALKLTALHALQLTLTQERVREHALS----IRVLP 671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 207 AEEEETVDLGPKRLwkddTGRVEELQGLLEKQNYELSQARE---RLVTLSATVTELEEDLGTARRDLikseelsgkHQRD 283
Cdd:TIGR00618 672 KELLASRQLALQKM----QSEKEQLTYWKEMLAQCQTLLREletHIEEYDREFNEIENASSSLGSDL---------AARE 738
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 284 LREALAQKEDMEERITTLEKRYLAAQR---EATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTmrK 360
Cdd:TIGR00618 739 DALNQSLKELMHQARTVLKARTEAHFNnneEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSD--E 816
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 361 AETLPEVEAELSQRIAALTKAEERHGNIEEhLRQLEGQLEEKNQELARVRQREKmnedhnkRLSDTVDRL 430
Cdd:TIGR00618 817 DILNLQCETLVQEEEQFLSRLEEKSATLGE-ITHQLLKYEECSKQLAQLTQEQA-------KIIQLSDKL 878
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
33-468 |
1.12e-03 |
|
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: 43.27 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 33 MLDEREKLLESLRESQETLVATQSRLQDALherDQLQRHLNsALPQEFATLTRELSMCREQLLEREEEISELKAERNNTR 112
Cdd:pfam10174 360 FLNKKTKQLQDLTEEKSTLAGEIRDLKDML---DVKERKIN-VLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTD 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 113 LLLEHLECLVSRHERslrmtvvkrqaqspsgvsseveVLKALKslfeHHKALDEKVRerlraaLERVTTLEEQLAGAHQQ 192
Cdd:pfam10174 436 TALTTLEEALSEKER----------------------IIERLK----EQREREDRER------LEELESLKKENKDLKEK 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 193 VSALQQGAGIRDGVAEE--EETVDLGPKRLWKDDtgRVEELQGLLEKQNYELSQARERL-----VTLSATVT-ELEEDLG 264
Cdd:pfam10174 484 VSALQPELTEKESSLIDlkEHASSLASSGLKKDS--KLKSLEIAVEQKKEECSKLENQLkkahnAEEAVRTNpEINDRIR 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 265 TARRDLIKSEELSGKHQRD-------LREALAQKEDMEERITTLEKRYLAAQREATSihdlndklenELANKEslHRQCE 337
Cdd:pfam10174 562 LLEQEVARYKEESGKAQAEverllgiLREVENEKNDKDKKIAELESLTLRQMKEQNK----------KVANIK--HGQQE 629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 338 EKARHLQELLEVAEQKlqqtmrKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQ--REKM 415
Cdd:pfam10174 630 MKKKGAQLLEEARRRE------DNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAerRKQL 703
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 281306779 416 NEdhnkRLSDTVDRLLSESNER------LQLHLKERMAALEEKGRLSEEIEKLRQEVDQ 468
Cdd:pfam10174 704 EE----ILEMKQEALLAAISEKdanialLELSSSKKKKTQEEVMALKREKDRLVHQLKQ 758
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
149-470 |
1.46e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.03 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 149 EVLKALKSLFEHHKALDEKVRERLR------AALERVTTLEEQLAGAHQQVSALQQG------AGIRDGVAEEEETVDLG 216
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKkqqllkQLRARIEELRAQEAVLEETQERINRArkaaplAAHIKAVTQIEQQAQRI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 217 PKRLWKDDTGRVEELQ--GLLEKQNYELSQARERLVTLSATVTELEE--DLGTARRDlIKSEELSGKHQrdLREALAQKE 292
Cdd:TIGR00618 313 HTELQSKMRSRAKLLMkrAAHVKQQSSIEEQRRLLQTLHSQEIHIRDahEVATSIRE-ISCQQHTLTQH--IHTLQQQKT 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 293 DMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQ-QTMRKAE------TLP 365
Cdd:TIGR00618 390 TLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQcEKLEKIHlqesaqSLK 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 366 EVEAELSQRiAALTKAEERHGNIEEHL--------RQLEGQLEEKNQEL----------ARVRQREKMNEDHNKRLSDTV 427
Cdd:TIGR00618 470 EREQQLQTK-EQIHLQETRKKAVVLARllelqeepCPLCGSCIHPNPARqdidnpgpltRRMQRGEQTYAQLETSEEDVY 548
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 281306779 428 DRLLSESNERLQLHLKERMAALEEKG------RLSEEIEKLRQEVDQLK 470
Cdd:TIGR00618 549 HQLTSERKQRASLKEQMQEIQQSFSIltqcdnRSKEDIPNLQNITVRLQ 597
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
28-473 |
1.50e-03 |
|
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: 42.79 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 28 QLMVNMLDEREKLLESLRESQETLVATQSRLQDALHERDQLQRHLNSALPQEFATLTRELSMCREQLLEREEEISELKAE 107
Cdd:pfam05483 183 QVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 108 RNNTRLLLEHLECLVSRHERSLRMTVVKRQAqspsgVSSEVEVLK-ALKSLFEHHKALDEKvrerLRAALERVTTLEEQl 186
Cdd:pfam05483 263 LEESRDKANQLEEKTKLQDENLKELIEKKDH-----LTKELEDIKmSLQRSMSTQKALEED----LQIATKTICQLTEE- 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 187 agAHQQVSALQQGAGIRDGVAEEEETVDLGPKRLWKDDTGRVEE-------LQGLLEKQNYELSQARERLVTLSATVTEL 259
Cdd:pfam05483 333 --KEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKnedqlkiITMELQKKSSELEEMTKFKNNKEVELEEL 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 260 EEDLGTARRDLIK-------SEELSGKHQrDLREALAQKE----DMEERITTLEKrylAAQREATSIHDLNDKLENELAN 328
Cdd:pfam05483 411 KKILAEDEKLLDEkkqfekiAEELKGKEQ-ELIFLLQAREkeihDLEIQLTAIKT---SEEHYLKEVEDLKTELEKEKLK 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 329 KESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETlpeveaelsqrIAALTKAEERH----GNIEEHLRQLEGQLEEKNQ 404
Cdd:pfam05483 487 NIELTAHCDKLLLENKELTQEASDMTLELKKHQED-----------IINCKKQEERMlkqiENLEEKEMNLRDELESVRE 555
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281306779 405 ELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGRG 473
Cdd:pfam05483 556 EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKG 624
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
253-469 |
1.76e-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: 42.85 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 253 SATVTELEEDLGTARR---DLIKS----EELSGKHQRDLREALAQKEDMEER-------ITTLEKRYLAAQREATSIHDL 318
Cdd:pfam01576 355 TQALEELTEQLEQAKRnkaNLEKAkqalESENAELQAELRTLQQAKQDSEHKrkklegqLQELQARLSESERQRAELAEK 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 319 NDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAAL----TKAEERHGNIEEHLRQ 394
Cdd:pfam01576 435 LSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLederNSLQEQLEEEEEAKRN 514
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281306779 395 LEGQLEEKNQELARVRQreKMNEDhnkrlSDTVDrLLSESNERLQLHLKERMAALEEKGRLSEEIEK----LRQEVDQL 469
Cdd:pfam01576 515 VERQLSTLQAQLSDMKK--KLEED-----AGTLE-ALEEGKKRLQRELEALTQQLEEKAAAYDKLEKtknrLQQELDDL 585
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
829-893 |
1.82e-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: 1.82e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281306779 829 QWDGPTVVSWLElWVGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNALHRLKLRLAIQEM 893
Cdd:pfam00536 2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
31-374 |
1.84e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 31 VNMLDEREKLLESLRESQETLVATQSRLQDALHERDQLQrhlnsalpqefatltrelsmcreqllEREEEISELKAERNN 110
Cdd:PRK02224 467 VETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLV--------------------------EAEDRIERLEERRED 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 111 -TRLLLEHLECLvsrHERSLRMTVVKRQAQspsgvssevevlkALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGA 189
Cdd:PRK02224 521 lEELIAERRETI---EEKRERAEELRERAA-------------ELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAEL 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 190 HQQVSALQQgagIRDGVAEEEETVDlgpkrlwkddtgRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARrd 269
Cdd:PRK02224 585 KERIESLER---IRTLLAAIADAED------------EIERLREKREALAELNDERRERLAEKRERKRELEAEFDEAR-- 647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 270 likSEELSGKHQRdlreALAQKEDMEERITTLEKRYLAAQREATSIhdlndklENELANKESL---HRQCEEKARHLQEL 346
Cdd:PRK02224 648 ---IEEAREDKER----AEEYLEQVEEKLDELREERDDLQAEIGAV-------ENELEELEELrerREALENRVEALEAL 713
|
330 340
....*....|....*....|....*...
gi 281306779 347 LEVAEQkLQQTMRkaetlpEVEAELSQR 374
Cdd:PRK02224 714 YDEAEE-LESMYG------DLRAELRQR 734
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
269-486 |
2.10e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 269 DLIKSE-ELSGKHQRDLREALAQkedmeeRITTLEKRYLAAQREATSIHDLNDKLENELANkesLHRQCEEKARHLQEL- 346
Cdd:PHA02562 191 DHIQQQiKTYNKNIEEQRKKNGE------NIARKQNKYDELVEEAKTIKAEIEELTDELLN---LVMDIEDPSAALNKLn 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 347 -------LEVAE-QKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNED 418
Cdd:PHA02562 262 taaakikSKIEQfQKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLE 341
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281306779 419 HNKRLSdTVDRLLS---ESNERLQLHLKErmaALEEKGRLSEEIEKLRQEVDQLKGRGGPFVDGIHSRSHV 486
Cdd:PHA02562 342 LKNKIS-TNKQSLItlvDKAKKVKAAIEE---LQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRGIV 408
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
227-472 |
2.17e-03 |
|
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: 42.12 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 227 RVEELQGLLEKQNYELSQARERLVTLSA-------TVTELEEDLGTARRDLiksEELSGKHQRDLREALAQKEDMEERIT 299
Cdd:pfam10174 402 KIENLQEQLRDKDKQLAGLKERVKSLQTdssntdtALTTLEEALSEKERII---ERLKEQREREDRERLEELESLKKENK 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 300 TLEKRYLAAQREAT----SIHDLNDK---LENELANKESLHRQCE---EKARHLQELLEVAEQKLQQTMRKAETLPEV-- 367
Cdd:pfam10174 479 DLKEKVSALQPELTekesSLIDLKEHassLASSGLKKDSKLKSLEiavEQKKEECSKLENQLKKAHNAEEAVRTNPEInd 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 368 -----EAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELA-----RVRQ-REKMNEDHNKRLSDTVDRllSESNE 436
Cdd:pfam10174 559 rirllEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAeleslTLRQmKEQNKKVANIKHGQQEMK--KKGAQ 636
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 281306779 437 RLQLHLKERMAA--------LEEkgrLSEEIEKLRQEVDQLKGR 472
Cdd:pfam10174 637 LLEEARRREDNLadnsqqlqLEE---LMGALEKTRQELDATKAR 677
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
952-1007 |
2.18e-03 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 37.63 E-value: 2.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 281306779 952 EWLPSLGLPQYRSYFMECLVD-ARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1007
Cdd:pfam07647 11 DWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLK-RLGITSVGHRRKILKKIQELK 66
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
149-472 |
2.77e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.96 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 149 EVLKALKSLFEHHKALD--EKVRERLRAALERVttLEEQLAGAHQQVSALQQGAGiRDGVAEEEETVDLGPK-------- 218
Cdd:TIGR00606 259 HNLSKIMKLDNEIKALKsrKKQMEKDNSELELK--MEKVFQGTDEQLNDLYHNHQ-RTVREKERELVDCQREleklnker 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 219 RLWKDDTGRVEELQGLLEKQ---NYELSQARERLVTLSATVTELEedlgTARRDLIKSEELSGKHQRDLREALAQKEDME 295
Cdd:TIGR00606 336 RLLNQEKTELLVEQGRLQLQadrHQEHIRARDSLIQSLATRLELD----GFERGPFSERQIKNFHTLVIERQEDEAKTAA 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 296 ERITTLEKRYLAAQREATSIHDLNDKLENELANKEslhrqceEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRI 375
Cdd:TIGR00606 412 QLCADLQSKERLKQEQADEIRDEKKGLGRTIELKK-------EILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAE 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 376 AALTKAEE----------------RHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNkrlsdTVDRLLSESNERLQ 439
Cdd:TIGR00606 485 RELSKAEKnsltetlkkevkslqnEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKM-----DKDEQIRKIKSRHS 559
|
330 340 350
....*....|....*....|....*....|...
gi 281306779 440 LHLKERMAALEEKGRLSEEIEKLRQEVDQLKGR 472
Cdd:TIGR00606 560 DELTSLLGYFPNKKQLEDWLHSKSKEINQTRDR 592
|
|
| SAM_Neurabin-like |
cd09512 |
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ... |
1030-1069 |
2.88e-03 |
|
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like (Neural actin-binding) subfamily is a putative protein-protein interaction domain. This group currently includes the SAM domains of neurobin-I, SAMD14 and neurobin-I/SAMD14-like proteins. Most are multidomain proteins and in addition to SAM domain they contain other protein-binding domains such as PDZ and actin-binding domains. Members of this subfamily participate in signal transduction. Neurabin-I is involved in the regulation of Ca signaling intensity in alpha-adrenergic receptors; it forms a functional pair of opposing regulators with neurabin-II. Neurabins are expressed almost exclusively in neuronal cells. They are known to interact with protein phosphatase 1 and inhibit its activity; they also can bind actin filaments; however, the exact role of the SAM domain is unclear, since SAM doesn't participate in these interactions.
Pssm-ID: 188911 [Multi-domain] Cd Length: 70 Bit Score: 37.63 E-value: 2.88e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 281306779 1030 VLVWTNDQVVHWVQSIGLRDYAGNLHESGVHG-ALLALDEN 1069
Cdd:cd09512 4 VSEWSVQQVCQWLMGLGLEQYIPEFTANNIDGqQLLQLDSS 44
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
309-470 |
3.77e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 309 QREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNI 388
Cdd:COG4372 20 PKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 389 EEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERlqlhlKERMAALEEKG-RLSEEIEKLRQEVD 467
Cdd:COG4372 100 QEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER-----EEELKELEEQLeSLQEELAALEQELQ 174
|
...
gi 281306779 468 QLK 470
Cdd:COG4372 175 ALS 177
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
40-471 |
4.21e-03 |
|
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: 41.35 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 40 LLESLRESQETLVATQSRLQdALHERDQLQRHLNSALPQEFATLTRELSMCREQLLEREEEISELKAERNNT-------R 112
Cdd:pfam10174 58 LKEQYRVTQEENQHLQLTIQ-ALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQakelfllR 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 113 LLLEHLE--------CLVSRHErSLRMTVVKRQAQS-PSGVSSEVEVLKALKSLFEHHKA-----LDEKVRE--RLRAAL 176
Cdd:pfam10174 137 KTLEEMElrietqkqTLGARDE-SIKKLLEMLQSKGlPKKSGEEDWERTRRIAEAEMQLGhlevlLDQKEKEniHLREEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 177 ERvttlEEQLAGAHQQVSALQQgagirdgVAEEEETVDLGPKRLWKDDTGRVEELQ--GLL--EKQNYELSQA---RERL 249
Cdd:pfam10174 216 HR----RNQLQPDPAKTKALQT-------VIEMKDTKISSLERNIRDLEDEVQMLKtnGLLhtEDREEEIKQMevyKSHS 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 250 VTLSATVTELEEDLGTarrdliKSEELSGKHQRdLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANK 329
Cdd:pfam10174 285 KFMKNKIDQLKQELSK------KESELLALQTK-LETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEK 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 330 ES--------LHRQCEEKA------RHLQELLEVAEQKLQQTMRKAETLPEV-------EAELSQRIAALtkaEERHGNI 388
Cdd:pfam10174 358 ESflnkktkqLQDLTEEKStlageiRDLKDMLDVKERKINVLQKKIENLQEQlrdkdkqLAGLKERVKSL---QTDSSNT 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 389 EEHLRQLEGQLEEKNQELARVRQ------REKMNE-----DHNKRLSDTVDRLLSESNERLQ--LHLKERMAALEEKG-- 453
Cdd:pfam10174 435 DTALTTLEEALSEKERIIERLKEqreredRERLEEleslkKENKDLKEKVSALQPELTEKESslIDLKEHASSLASSGlk 514
|
490 500
....*....|....*....|....
gi 281306779 454 ------RLSEEIEKLRQEVDQLKG 471
Cdd:pfam10174 515 kdsklkSLEIAVEQKKEECSKLEN 538
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
272-474 |
4.22e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 41.38 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 272 KSEELSGKHQRDLREALAQKEdMEERITTLEKRylAAQREATSIHDLNDKLenelanKESLHRQCEEKARHLQELLEVAE 351
Cdd:PLN03229 555 KAEKLKAEINKKFKEVMDRPE-IKEKMEALKAE--VASSGASSGDELDDDL------KEKVEKMKKEIELELAGVLKSMG 625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 352 QKLQQTMRKAETLPEVEA--ELSQRIAALTkaEERHGNIEEHLR--QLEGQLEEKNQELARVrqrekmnedhnkrlSDTV 427
Cdd:PLN03229 626 LEVIGVTKKNKDTAEQTPppNLQEKIESLN--EEINKKIERVIRssDLKSKIELLKLEVAKA--------------SKTP 689
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 281306779 428 DRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGRGG 474
Cdd:PLN03229 690 DVTEKEKIEALEQQIKQKIAEALNSSELKEKFEELEAELAAARETAA 736
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
229-353 |
4.36e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 41.20 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 229 EELQGL-LEKQNYE--LSQARERLVTLSATVTELEEDLGTARRDLIKSEELSGKhqrdlreALAQKEDMEERITTLEKRY 305
Cdd:pfam05911 688 EEFEQLkSEKENLEveLASCTENLESTKSQLQESEQLIAELRSELASLKESNSL-------AETQLKCMAESYEDLETRL 760
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 281306779 306 LAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQK 353
Cdd:pfam05911 761 TELEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQEQLERNEKK 808
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
261-470 |
4.44e-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: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 261 EDLGTARRDLIKS-EELsgkhQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDL---NDKLENELANKES----L 332
Cdd:TIGR04523 155 EKLNNKYNDLKKQkEEL----ENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKiqkNKSLESQISELKKqnnqL 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 333 HRQCEEKARHLQEL---LEVAEQKLQQTMrkaETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLE----EKNQE 405
Cdd:TIGR04523 231 KDNIEKKQQEINEKtteISNTQTQLNQLK---DEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdlnnQKEQD 307
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 406 LAR-----VRQREKMNEDHNKRLSDTvDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLK 470
Cdd:TIGR04523 308 WNKelkseLKNQEKKLEEIQNQISQN-NKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLK 376
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
235-465 |
4.60e-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: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 235 LEKQNYELSQARERLvtlSATVTELEEDLgtarRDLIKSE---ELSGKHQRDLREALaqkedmEERITTLEKRYLAAQRE 311
Cdd:TIGR04523 417 LQQEKELLEKEIERL---KETIIKNNSEI----KDLTNQDsvkELIIKNLDNTRESL------ETQLKVLSRSINKIKQN 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 312 AtsihdlnDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLpevEAELSQRIAALTKAEERHGNIEEH 391
Cdd:TIGR04523 484 L-------EQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKL---ESEKKEKESKISDLEDELNKDDFE 553
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281306779 392 LR--QLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNErlqlhLKERMAALEEK-GRLSEEIEKLRQE 465
Cdd:TIGR04523 554 LKkeNLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKD-----LIKEIEEKEKKiSSLEKELEKAKKE 625
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
32-522 |
4.89e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.26 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 32 NMLDER-EKLLESLR-----ESQETLVATQSRlQDALHERDQLQRHLNSAlPQEFATLTRELSMCREQLLEREEEISELK 105
Cdd:pfam15921 425 NMEVQRlEALLKAMKsecqgQMERQMAAIQGK-NESLEKVSSLTAQLEST-KEMLRKVVEELTAKKMTLESSERTVSDLT 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 106 AERNNTRLLLE----HLECLVSRHERSLR-MTVVKRQAQSPSGVSSEVEVLKAlkslfehHKALDEKVRERLRAALERVT 180
Cdd:pfam15921 503 ASLQEKERAIEatnaEITKLRSRVDLKLQeLQHLKNEGDHLRNVQTECEALKL-------QMAEKDKVIEILRQQIENMT 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 181 TLEEQ---LAGAhQQVSALQQGAGIRDGVAEEEETVDLGPKRlwkddTGRVEELQGL---LEKQNYELSQA-RERLVTLS 253
Cdd:pfam15921 576 QLVGQhgrTAGA-MQVEKAQLEKEINDRRLELQEFKILKDKK-----DAKIRELEARvsdLELEKVKLVNAgSERLRAVK 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 254 ATVTELEE---DLGTARRDLIKSEELSGKHQRDLREalaQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENE--LAN 328
Cdd:pfam15921 650 DIKQERDQllnEVKTSRNELNSLSEDYEVLKRNFRN---KSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSdgHAM 726
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 329 KESLHRQCEEKARH-----LQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEK- 402
Cdd:pfam15921 727 KVAMGMQKQITAKRgqidaLQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKv 806
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 403 -NQELARVRQREKMNEdhnkrLSDTVDRLLSESnERLQLHLKERMAALEEKGRLSEEIEKLRQevdqlkgrggpFVDGIH 481
Cdd:pfam15921 807 aNMEVALDKASLQFAE-----CQDIIQRQEQES-VRLKLQHTLDVKELQGPGYTSNSSMKPRL-----------LQPASF 869
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 281306779 482 SRSHvgstTDVRFSLSTAAHVPPGlHRRYTALREESAKDWK 522
Cdd:pfam15921 870 TRTH----SNVPSSQSTASFLSHH-SRKTNALKEDPTRDLK 905
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
343-470 |
5.11e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 343 LQELLEVAEQKLQQTMRKAETLPEVE-AELSQRIAALtkaEERHGNIEEHLRQLEGQLEEKNQELARVRQR---EKMNED 418
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERElTEEEEEIRRL---EEQVERLEAEVEELEAELEEKDERIERLERElseARSEER 458
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 281306779 419 HNKRLSDTVDRLLSEsNERLQLHLKErmaaleekgrLSEEIEKLRQEVDQLK 470
Cdd:COG2433 459 REIRKDREISRLDRE-IERLERELEE----------ERERIEELKRKLERLK 499
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
38-469 |
5.33e-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: 40.93 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 38 EKLLESLRESQETLVATQSRLQDALHERDQLQRHLNSALPQeFATLTRELsmcreqlleREEEISELKAERNNtRLLLEH 117
Cdd:pfam01576 232 AELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQ-ISELQEDL---------ESERAARNKAEKQR-RDLGEE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 118 LECLVSRHERSLRMTVVKRQAQSPSgvSSEVEVLK-ALKSLFEHHKALDEKVRERLRAALErvtTLEEQLAGAHQQVSAL 196
Cdd:pfam01576 301 LEALKTELEDTLDTTAAQQELRSKR--EQEVTELKkALEEETRSHEAQLQEMRQKHTQALE---ELTEQLEQAKRNKANL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 197 QQGAgirdgVAEEEETVDLgpkrlwkddtgrVEELQgLLEKQNYELSQARERLvtlSATVTELEEDLGTARRDLIKSEEL 276
Cdd:pfam01576 376 EKAK-----QALESENAEL------------QAELR-TLQQAKQDSEHKRKKL---EGQLQELQARLSESERQRAELAEK 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 277 SGKHQRDLREALAQKEDMEERITTLEKRYLAAQreaTSIHDLNDKLENELANKESLH---RQCEEKARHLQELLEVAEQK 353
Cdd:pfam01576 435 LSKLQSELESVSSLLNEAEGKNIKLSKDVSSLE---SQLQDTQELLQEETRQKLNLStrlRQLEDERNSLQEQLEEEEEA 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 354 LQQTMRKAET----LPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARvrqrekmnedhnkrlsdtvdr 429
Cdd:pfam01576 512 KRNVERQLSTlqaqLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDK--------------------- 570
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 281306779 430 lLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQL 469
Cdd:pfam01576 571 -LEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQM 609
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
347-470 |
5.70e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 347 LEVAEQKLQQTMRKAETlpeVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQR-EKMNEDHNKRL-- 423
Cdd:COG3883 18 IQAKQKELSELQAELEA---AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEiEERREELGERAra 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281306779 424 --------------------SDTVDRL-----LSESNERLQLHLKERMAALEE-KGRLSEEIEKLRQEVDQLK 470
Cdd:COG3883 95 lyrsggsvsyldvllgsesfSDFLDRLsalskIADADADLLEELKADKAELEAkKAELEAKLAELEALKAELE 167
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
228-470 |
7.24e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 228 VEELQGLLEKQNYELSQARERLVTLSATVTELEEdlgtARRDLI-KSEELSGKhqrdLREALAQKEDMEERITTLEKRYL 306
Cdd:COG1340 10 LEELEEKIEELREEIEELKEKRDELNEELKELAE----KRDELNaQVKELREE----AQELREKRDELNEKVKELKEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 307 AAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELlevaeQKLQQTMrkaETLPEVEAELSQRIAALTK-AEERh 385
Cdd:COG1340 82 ELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERL-----EWRQQTE---VLSPEEEKELVEKIKELEKeLEKA- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 386 gnieEHLRQLEGQLEEKNQELARVRQREkmnEDHNKRLSDTVDRLLSESNERLQLhLKERMAALEEKGRLSEEIEKLRQE 465
Cdd:COG1340 153 ----KKALEKNEKLKELRAELKELRKEA---EEIHKKIKELAEEAQELHEEMIEL-YKEADELRKEADELHKEIVEAQEK 224
|
....*
gi 281306779 466 VDQLK 470
Cdd:COG1340 225 ADELH 229
|
|
| SAM_SARM1-like_repeat1 |
cd09501 |
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
952-996 |
7.79e-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: 36.13 E-value: 7.79e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 281306779 952 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHR 996
Cdd:cd09501 11 TWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLR 55
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
172-423 |
7.94e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 7.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 172 LRAALERVTTLEEQLA---GAHQQVSalQQGAGIRDGVAEEEETVDLGPkrLWKDDT--GRVEELqgllEKQNYELSQAR 246
Cdd:PRK04863 839 LRQLNRRRVELERALAdheSQEQQQR--SQLEQAKEGLSALNRLLPRLN--LLADETlaDRVEEI----REQLDEAEEAK 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 247 ERLVTLSATVTELEEDLGTARRDLIKSEELsgkhQRDLREALAQKEDMEERITTL----EKR----YLAAQREATSIHDL 318
Cdd:PRK04863 911 RFVQQHGNALAQLEPIVSVLQSDPEQFEQL----KQDYQQAQQTQRDAKQQAFALtevvQRRahfsYEDAAEMLAKNSDL 986
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 319 NDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALT---------KAEERHGNIE 389
Cdd:PRK04863 987 NEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGvpadsgaeeRARARRDELH 1066
|
250 260 270
....*....|....*....|....*....|....*
gi 281306779 390 EHLRQLEGQleeKNQ-ELARVRQREKMNEdHNKRL 423
Cdd:PRK04863 1067 ARLSANRSR---RNQlEKQLTFCEAEMDN-LTKKL 1097
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
376-472 |
8.24e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.04 E-value: 8.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306779 376 AALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRL-------LSESNERLQLHLKERMAA 448
Cdd:COG1842 16 ALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWeekarlaLEKGREDLAREALERKAE 95
|
90 100 110
....*....|....*....|....*....|..
gi 281306779 449 LEEK--------GRLSEEIEKLRQEVDQLKGR 472
Cdd:COG1842 96 LEAQaealeaqlAQLEEQVEKLKEALRQLESK 127
|
|
| |
