|
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 ... |
945-1010 |
9.55e-44 |
|
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: 152.63 E-value: 9.55e-44
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966922630 945 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 1010
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 ... |
828-898 |
4.05e-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: 148.10 E-value: 4.05e-42
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966922630 828 FAQWDGPTVVSWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEMVSLT 898
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 ... |
1030-1101 |
4.94e-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: 145.15 E-value: 4.94e-41
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966922630 1030 DVLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALILQIPTQNTQARQVMEREFNNLL 1101
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 ... |
949-1008 |
5.86e-31 |
|
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: 115.71 E-value: 5.86e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 949 WIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1008
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 ... |
1038-1099 |
8.80e-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: 104.16 E-value: 8.80e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966922630 1038 QVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALILQIPTQNTQARQVMEREFNN 1099
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 ... |
835-893 |
3.76e-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: 99.22 E-value: 3.76e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 966922630 835 TVVSWLELWVGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQE 893
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 ... |
1030-1101 |
2.43e-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: 83.26 E-value: 2.43e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966922630 1030 DVLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALILQIPTQNTQARQVMEREFNNLL 1101
Cdd:cd09570 1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
|
|
| SAM_liprin-beta1,2_repeat3 |
cd09569 |
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ... |
1030-1101 |
2.02e-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: 74.80 E-value: 2.02e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966922630 1030 DVLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALILQIPTQNTQARQVMEREFNNLL 1101
Cdd:cd09569 1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
|
|
| SAM_kazrin_repeat2 |
cd09567 |
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ... |
944-1008 |
2.80e-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: 74.37 E-value: 2.80e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966922630 944 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1008
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 ... |
944-1008 |
3.26e-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: 73.88 E-value: 3.26e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966922630 944 DMNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLrVHLKMVDSFHRTSLQYGIMCLK 1008
Cdd:cd09566 1 KLDTHWV-LRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDL-LHLKVTSALHHASIRRGIQVLR 63
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
221-472 |
5.63e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.45 E-value: 5.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 221 WKEDAGRVEELQELLEKQNFELSQARERLVTLTATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITT 300
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 301 LEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTK 380
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 381 AEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIE 460
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
250
....*....|..
gi 966922630 461 KLRQEVDQLKGR 472
Cdd:COG1196 481 ELLEELAEAAAR 492
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
227-471 |
7.03e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.06 E-value: 7.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 227 RVEELQELLEKQNFELSQARERLVTLTATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDME-------ERIT 299
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEqdiarleERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 300 TLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALT 379
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 380 KAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEI 459
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
250
....*....|..
gi 966922630 460 EKLRQEVDQLKG 471
Cdd:COG1196 473 ALLEAALAELLE 484
|
|
| SAM_kazrin_repeat1 |
cd09564 |
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ... |
829-893 |
1.21e-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: 1.21e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966922630 829 AQWDGPTVVSWLELWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQE 893
Cdd:cd09564 2 SRWKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
159-474 |
9.41e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.60 E-value: 9.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 159 EHHKALDEKVRER-LRAALERVTTLEEQLAGAHQQVSALQqgagvldgAAEEEGTVELgpkrlwKEDAGRVEELQELLEK 237
Cdd:COG1196 213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELE--------AELEELEAEL------AELEAELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 238 QNFELSQARERLVTLTATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHD 317
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 318 LNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEG 397
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966922630 398 QLEEKNQELARVRQREkmnedhnKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGRGG 474
Cdd:COG1196 439 EEEEALEEAAEEEAEL-------EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
944-1008 |
4.99e-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: 4.99e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966922630 944 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1008
Cdd:pfam00536 1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
36-439 |
1.15e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.86 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 36 EREKLLESLR----ESQETLAATQSRLQDALHERDQLQrhlnsalpQEFATLTRELSMCREQLLEREEEISELKAERNNT 111
Cdd:TIGR02168 674 ERRREIEELEekieELEEKIAELEKALAELRKELEELE--------EELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 112 RLLLEHLECLVSRHErslrmtvvkrqaqspsgvSSEVEVLKALKSLFEHHKALDEK---VRERLRAALERVTTLEEQLAG 188
Cdd:TIGR02168 746 EERIAQLSKELTELE------------------AEIEELEERLEEAEEELAEAEAEieeLEAQIEQLKEELKALREALDE 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 189 AHQQVSALQQGAGVLDGAAEEEGTvelgpkrlwkedagRVEELQELLEKQNFELSQARERLVTLTATVTELEEDLGTARR 268
Cdd:TIGR02168 808 LRAELTLLNEEAANLRERLESLER--------------RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES 873
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 269 DLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREAtsiHDLNDKLENELANKESLhrqcEEKARHLQE-LL 347
Cdd:TIGR02168 874 ELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL---EELREKLAQLELRLEGL----EVRIDNLQErLS 946
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 348 EVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNI----EEHLRQLEGQLEEKNQE---LARVRQR-----EKM 415
Cdd:TIGR02168 947 EEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVnlaaIEEYEELKERYDFLTAQkedLTEAKETleeaiEEI 1026
|
410 420
....*....|....*....|....
gi 966922630 416 NEDHNKRLSDTVDRLlsesNERLQ 439
Cdd:TIGR02168 1027 DREARERFKDTFDQV----NENFQ 1046
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
225-469 |
2.13e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.09 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 225 AGRVEELQELLEKQNFELSQARERLVTLTATVTELEEDLgtarrdliksEELSSKHQRdlrealaqkedMEERITTLEKR 304
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKL----------EELRLEVSE-----------LEEEIEELQKE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 305 YLAAQREatsIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEER 384
Cdd:TIGR02168 290 LYALANE---ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 385 HGNIEEHLRQLEGQLEEKNQELARVRQREKM-------NEDHNKRLSDTVDRLLSESNERLQ-LHLKERMAALEEKGRLS 456
Cdd:TIGR02168 367 LEELESRLEELEEQLETLRSKVAQLELQIASlnneierLEARLERLEDRRERLQQEIEELLKkLEEAELKELQAELEELE 446
|
250
....*....|...
gi 966922630 457 EEIEKLRQEVDQL 469
Cdd:TIGR02168 447 EELEELQEELERL 459
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
18-409 |
2.77e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 74.71 E-value: 2.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 18 LGADADANFEQLMVNML-----DEREKLLESL----------RESQETLAATQ---SRLQDALHERD-QLQR-HLNSALP 77
Cdd:TIGR02168 133 LGKRSYSIIEQGKISEIieakpEERRAIFEEAagiskykerrKETERKLERTRenlDRLEDILNELErQLKSlERQAEKA 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 78 QEFATLTRELSmcREQLLEREEEISELKAERNNTRLLLEHLECLVSRHERSLRMTvvkrqaqspsgvSSEVEVLKALKSl 157
Cdd:TIGR02168 213 ERYKELKAELR--ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQEL------------EEKLEELRLEVS- 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 158 fEHHKALDEkVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVLDGAAEEEGTVELGPKRLWKEDAGRVEELQELLEK 237
Cdd:TIGR02168 278 -ELEEEIEE-LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELES 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 238 QNFELSQARERLVTLTATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATS--- 314
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEael 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 315 --IHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKaetlpevEAELAQRIAALTKAEERHGNIEEHL 392
Cdd:TIGR02168 436 keLQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE-------LAQLQARLDSLERLQENLEGFSEGV 508
|
410
....*....|....*..
gi 966922630 393 RQLEGQLEEKNQELARV 409
Cdd:TIGR02168 509 KALLKNQSGLSGILGVL 525
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
38-469 |
1.12e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 72.77 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 38 EKLLESLRESQETLAATQSRLQDA-LHERdqlqrhLNsALPQEFATLTRElsmcreqllereeeISELKAERNNTRLLLE 116
Cdd:PRK02224 179 ERVLSDQRGSLDQLKAQIEEKEEKdLHER------LN-GLESELAELDEE--------------IERYEEQREQARETRD 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 117 HLECLVSRHERSLrmtvvkrqaqspsgvsSEVEVLKALKSLFEHHKALDEKVRERLRaalERVTTLEEQLAGAHQQVSAL 196
Cdd:PRK02224 238 EADEVLEEHEERR----------------EELETLEAEIEDLRETIAETEREREELA---EEVRDLRERLEELEEERDDL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 197 QQGAGVLDGAAEeegTVELGPKRLWKEDagrvEELQELLEKQNFELSQARERLVTLTATVTELEEDLGTARRDLIKSEEL 276
Cdd:PRK02224 299 LAEAGLDDADAE---AVEARREELEDRD----EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 277 SSKHQRDLREALAQKEDMEERITTLEKRYLAAqreATSIHDLNDKLENELANKESLHRQCEEkarhlqelLEVAEQKLQQ 356
Cdd:PRK02224 372 LEEAREAVEDRREEIEELEEEIEELRERFGDA---PVDLGNAEDFLEELREERDELREREAE--------LEATLRTARE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 357 TMRKAETL------PEVEAEL--AQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQRekmnedhnKRLSDTVD 428
Cdd:PRK02224 441 RVEEAEALleagkcPECGQPVegSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL--------VEAEDRIE 512
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 966922630 429 RLLsESNERLQLHLKERMAALEEKgrlSEEIEKLRQEVDQL 469
Cdd:PRK02224 513 RLE-ERREDLEELIAERRETIEEK---RERAEELRERAAEL 549
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
85-469 |
1.23e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.78 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 85 RELSMCREQLLEREEEISELKAERNNTRLLLEHLeclvsrherslrmtvvkrqaqspsgvssEVEVLKALKSLFEHHKAL 164
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEEL----------------------------EEELEQLRKELEELSRQI 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 165 DEkVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVLDGAAEEEGTVElgpkrlwKEDAGRVEELQELLEKQNFELSQ 244
Cdd:TIGR02168 729 SA-LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL-------AEAEAEIEELEAQIEQLKEELKA 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 245 ARERLVTLTATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLEN 324
Cdd:TIGR02168 801 LREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 325 ELANkeslhrqceekarhLQELLEVAEQKLQQTMrkaETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQ 404
Cdd:TIGR02168 881 ERAS--------------LEEALALLRSELEELS---EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966922630 405 elaRVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKER-------MAALEEKGRLSEEIEKLRQEVDQL 469
Cdd:TIGR02168 944 ---RLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIkelgpvnLAAIEEYEELKERYDFLTAQKEDL 1012
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
20-472 |
1.42e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.28 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 20 ADADANFEQLMVNMLDEREKLLESLRESQETLAATQSRLQDALHERDQLQRHLNSALpQEFATLTRELSMCREQLLEREE 99
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA-EELLEALRAAAELAAQLEELEE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 100 EISELKAERNNTRLLLEHLEclvSRHERSLRMTVVKRQAQSpsgvsSEVEVLKALKSLFEHHKALDEKVRERLRAALERV 179
Cdd:COG1196 408 AEEALLERLERLEEELEELE---EALAELEEEEEEEEEALE-----EAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 180 TTLEEQLAGAHQQVSALQQGAGVLDGAAEEEGTVELGPKRlwkedAGRVEELQELLEKQNFELSQARERL-VTLTATVTE 258
Cdd:COG1196 480 AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL-----RGLAGAVAVLIGVEAAYEAALEAALaAALQNIVVE 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 259 LEEDLGTARRDLIKSEE-------LSSKHQRDLREALAQKEDMEERITTL--EKRYLAAQREATSIHDLNDKLENE-LAN 328
Cdd:COG1196 555 DDEVAAAAIEYLKAAKAgratflpLDKIRARAALAAALARGAIGAAVDLVasDLREADARYYVLGDTLLGRTLVAArLEA 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 329 KESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHgniEEHLRQLEGQLEEKNQELAR 408
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE---ELELEEALLAEEEEERELAE 711
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966922630 409 VRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGR 472
Cdd:COG1196 712 AEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
228-472 |
5.56e-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: 70.48 E-value: 5.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 228 VEELQELLEKQNFELSQARERLVTLTATVTELEEDLGTARRDLIKSEE----LSSKHQRDLREALAQKEDMEERITTLEK 303
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERyqalLKEKREYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 304 RYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHL--QELLEVAEQ--KLQQTMRKAE-TLPEVEAELAQRIAAL 378
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeEEQLRVKEKigELEAEIASLErSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 379 TKAEERHGNIEEHLRQLEGQLEEKNQELARVRQ-----REKMN------EDHNKRLSDTVDRL------LSESNERLQLH 441
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEeyaelKEELEdlraelEEVDKEFAETRDELkdyrekLEKLKREINEL 404
|
250 260 270
....*....|....*....|....*....|.
gi 966922630 442 LKERMAALEEKGRLSEEIEKLRQEVDQLKGR 472
Cdd:TIGR02169 405 KRELDRLQEELQRLSEELADLNAAIAGIEAK 435
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
226-473 |
2.14e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.40 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 226 GRVEEL--QELLEKqnFELSQARERLVTLTATVTELEEDLGTARRDLIKSEELSSKHQRdLREALAQKEDMEERITTLek 303
Cdd:COG4913 207 GDLDDFvrEYMLEE--PDTFEAADALVEHFDDLERAHEALEDAREQIELLEPIRELAER-YAAARERLAELEYLRAAL-- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 304 RYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQtmRKAETLPEVEAELAQRIAALTKAEE 383
Cdd:COG4913 282 RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG--NGGDRLEQLEREIERLERELEERER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 384 RHGNIEEHLRQLEGQLEEKNQELARVRQRekmnedhnkrlsdtVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLR 463
Cdd:COG4913 360 RRARLEALLAALGLPLPASAEEFAALRAE--------------AAALLEALEEELEALEEALAEAEAALRDLRRELRELE 425
|
250
....*....|
gi 966922630 464 QEVDQLKGRG 473
Cdd:COG4913 426 AEIASLERRK 435
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
36-470 |
2.37e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.17 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 36 EREKLLESLRESQETLAATQSRLQDALHERDQLQ---RHLNSALP--QEFATLTRELSMCREQLLEREEEISELKAERNN 110
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEERIEELKKEIEELEekvKELKELKEkaEEYIKLSEFYEEYLDELREIEKRLSRLEEEING 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 111 TRLLLEHLECLVSR-HERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALD-----EKVRERLRAALERVTTLEE 184
Cdd:PRK03918 326 IEERIKELEEKEERlEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLtgltpEKLEKELEELEKAKEEIEE 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 185 QLAGAHQQVSALQQGAGVLDGAAEE----EGTVELGPKRLWKEDAGRV-EELQELLEKQNFELSQARERLVTLTATVTEL 259
Cdd:PRK03918 406 EISKITARIGELKKEIKELKKAIEElkkaKGKCPVCGRELTEEHRKELlEEYTAELKRIEKELKEIEEKERKLRKELREL 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 260 EEDLGTARR--------DLIKS--EELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDK---LENEL 326
Cdd:PRK03918 486 EKVLKKESEliklkelaEQLKEleEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKlaeLEKKL 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 327 ANKES----LHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEK 402
Cdd:PRK03918 566 DELEEelaeLLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEEL 645
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966922630 403 NQELARVRQreKMNEDHNKRLSDTVDRL------LSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLK 470
Cdd:PRK03918 646 RKELEELEK--KYSEEEYEELREEYLELsrelagLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLE 717
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
20-439 |
2.46e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 20 ADADANFEQLMVNMLDEREKLLESLRESQETLAATQSRLQDALHERDQLQRHLNSALPQEFATLTRELSmcreqlleREE 99
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL--------LEA 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 100 EISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHH------KALDEKVRERLR 173
Cdd:COG1196 478 ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAleaalaAALQNIVVEDDE 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 174 AALERVTTLEEQLAGAHQQVSALQQGAGVLDGAAEEEGTVELGPkrlwkedAGRVEELQELLEKQNFELSQARERLVTLT 253
Cdd:COG1196 558 VAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAV-------DLVASDLREADARYYVLGDTLLGRTLVAA 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 254 ATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLH 333
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA 710
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 334 RQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEK---N----QEL 406
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvNllaiEEY 790
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 966922630 407 ARVRQR-EKMNEDHN------KRLSDTVDRLLSESNERLQ 439
Cdd:COG1196 791 EELEERyDFLSEQREdleearETLEEAIEEIDRETRERFL 830
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
146-470 |
4.28e-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: 67.46 E-value: 4.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 146 SEVEVLKALKSLFEHHKALDEKVRERL--RAALERVTTLEEQLAGAHQQVSALQQGAGVLDGAAEEEGTVELGPKRLWKE 223
Cdd:pfam17380 266 TENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 224 DAGRVEELQelLEKQNFELSQAR-ERLVTLTATVTELEedlgtarRDLIKSEELSSKHQRDLREALAQKEDMEERittlE 302
Cdd:pfam17380 346 RERELERIR--QEERKRELERIRqEEIAMEISRMRELE-------RLQMERQQKNERVRQELEAARKVKILEEER----Q 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 303 KRYLAAQREATSIhdlndKLENELANKESLHRQCEEKARHLQELLEvAEQKLQQTMrkaETLPEVEAELAQRIAALTKAE 382
Cdd:pfam17380 413 RKIQQQKVEMEQI-----RAEQEEARQREVRRLEEERAREMERVRL-EEQERQQQV---ERLRQQEEERKRKKLELEKEK 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 383 ERHGNIEEHLRQ-LEGQLEEKNQELARVRQREKM----NEDHNKRLSDTVDRLLSESNERLQLHLKER-------MAALE 450
Cdd:pfam17380 484 RDRKRAEEQRRKiLEKELEERKQAMIEEERKRKLlekeMEERQKAIYEEERRREAEEERRKQQEMEERrriqeqmRKATE 563
|
330 340
....*....|....*....|
gi 966922630 451 EKGRLsEEIEKLRQEVDQLK 470
Cdd:pfam17380 564 ERSRL-EAMEREREMMRQIV 582
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
16-472 |
7.30e-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: 7.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 16 PPLGADADA---NFEQLM---VNMLDEREK--LLESLRESQETLAATQSRLQD------------ALHERDQLQRHLnSA 75
Cdd:COG4913 221 PDTFEAADAlveHFDDLErahEALEDAREQieLLEPIRELAERYAAARERLAEleylraalrlwfAQRRLELLEAEL-EE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 76 LPQEFATLTRELSMCREQLLEREEEISELKAERNNTRL-LLEHLECLVSRHERSLRMTVVKRQAQS----------PSGV 144
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDELEAQIRGNGGdRLEQLEREIERLERELEERERRRARLEallaalglplPASA 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 145 SSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVLD--------------GAAEEE 210
Cdd:COG4913 380 EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIParllalrdalaealGLDEAE 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 211 ------------------GTVE--LGPKRL---------------------------------WKEDAGRVEELQELLEK 237
Cdd:COG4913 460 lpfvgelievrpeeerwrGAIErvLGGFALtllvppehyaaalrwvnrlhlrgrlvyervrtgLPDPERPRLDPDSLAGK 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 238 QNFELSQARERLVTLTATVTEL-----EEDLGTARRD-----LIKSEelSSKHQRDLREALAQK----EDMEERITTLEK 303
Cdd:COG4913 540 LDFKPHPFRAWLEAELGRRFDYvcvdsPEELRRHPRAitragQVKGN--GTRHEKDDRRRIRSRyvlgFDNRAKLAALEA 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 304 RYLAAQREAtsihdlnDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQqTMRKAETLPEVEAELAQRIAA---LTK 380
Cdd:COG4913 618 ELAELEEEL-------AEAEERLEALEAELDALQERREALQRLAEYSWDEID-VASAEREIAELEAELERLDASsddLAA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 381 AEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIE 460
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE 769
|
570
....*....|..
gi 966922630 461 KLRQEVDQLKGR 472
Cdd:COG4913 770 NLEERIDALRAR 781
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
142-472 |
8.36e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.63 E-value: 8.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 142 SGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVLDgaaeeegtvELgpkrlw 221
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK---------EL------ 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 222 KEDAGRVEELQELLEKQNFELSQARERLVTLTATVTELEEDLgtarrdliksEELSSKHQRdLREALAQKEDMEERITTL 301
Cdd:PRK03918 289 KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI----------KELEEKEER-LEELKKKLKELEKRLEEL 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 302 EKRYLAAQrEATSIHDLNDKLENELANKESlhrqceEKarhLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKA 381
Cdd:PRK03918 358 EERHELYE-EAKAKKEELERLKKRLTGLTP------EK---LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKA 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 382 EER-----------HGNIEEHLRqlEGQLEEKNQELARVRQREKMNEDHNKRLSD---TVDRLLSESNERLQLH-LKERM 446
Cdd:PRK03918 428 IEElkkakgkcpvcGRELTEEHR--KELLEEYTAELKRIEKELKEIEEKERKLRKelrELEKVLKKESELIKLKeLAEQL 505
|
330 340 350
....*....|....*....|....*....|....*
gi 966922630 447 AALEEK---------GRLSEEIEKLRQEVDQLKGR 472
Cdd:PRK03918 506 KELEEKlkkynleelEKKAEEYEKLKEKLIKLKGE 540
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
159-468 |
1.02e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.70 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 159 EHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVldGAAEEEGTVElgPKRLWKEDAG----RVEELQEL 234
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEEL--KKAEEKKKAE--EAKKAEEDKNmalrKAEEAKKA 1589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 235 LEKQNFELSQARERLVTLTATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATs 314
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK- 1668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 315 ihdlndKLENELANKESLHRQCEEKARHLQELLEVAEQKlqqtmRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQ 394
Cdd:PTZ00121 1669 ------KAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA-----KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966922630 395 lEGQLEEKNQELARVRQREKmnedhnkrlsDTVDRLLSESNERLQLHLKERMAALEEKgrLSEEIEKLRQEVDQ 468
Cdd:PTZ00121 1738 -EAEEDKKKAEEAKKDEEEK----------KKIAHLKKEEEKKAEEIRKEKEAVIEEE--LDEEDEKRRMEVDK 1798
|
|
| SAM_liprin-beta1,2_repeat1 |
cd09563 |
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
828-892 |
1.22e-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: 1.22e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966922630 828 FAQWDGPTVVSWL-ELWVGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQ 892
Cdd:cd09563 1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
229-407 |
1.23e-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: 63.02 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 229 EELQELLEKQNF--ELSQARERLVTLTATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRyl 306
Cdd:COG1579 4 EDLRALLDLQELdsELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 307 aaQREATSIHDLNDkLENELANKESLHRQCEEKARHLQELLEVAEQKLQqtmrkaetlpEVEAELAQRIAALTKAEERHG 386
Cdd:COG1579 82 --LGNVRNNKEYEA-LQKEIESLKRRISDLEDEILELMERIEELEEELA----------ELEAELAELEAELEEKKAELD 148
|
170 180
....*....|....*....|.
gi 966922630 387 NIEEHLRQLEGQLEEKNQELA 407
Cdd:COG1579 149 EELAELEAELEELEAEREELA 169
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
227-474 |
1.65e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.47 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 227 RVEELQELLEKQNFELSQARERLVTLTATVTELEEDLGTARRDLIKSEELSSK---HQRDLREALAQKEDMEERITTLEK 303
Cdd:PRK03918 187 RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEieeLEKELESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 304 RylaaqreatsIHDLNDKLEnELANKESLHRQCEEKA---RHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTK 380
Cdd:PRK03918 267 R----------IEELKKEIE-ELEEKVKELKELKEKAeeyIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 381 AEERHGNIEEHLRQLE---GQLEEKNQELARVRQREKMNEDHNKRLSDtvdrllsESNERLQLHLKErmaALEEKGRLSE 457
Cdd:PRK03918 336 KEERLEELKKKLKELEkrlEELEERHELYEEAKAKKEELERLKKRLTG-------LTPEKLEKELEE---LEKAKEEIEE 405
|
250
....*....|....*..
gi 966922630 458 EIEKLRQEVDQLKGRGG 474
Cdd:PRK03918 406 EISKITARIGELKKEIK 422
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
227-470 |
2.63e-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: 65.09 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 227 RVEELQELLEKQNFELSQARERLVTLTATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEkRYL 306
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE-EDL 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 307 AAQREAtsIHDLNDKL-ENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALtkaEERH 385
Cdd:TIGR02169 775 HKLEEA--LNDLEARLsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL---KEQI 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 386 GNIEEHLRQLEGQLEEKNQELARVRQREKmneDHNKRLSDtvdrlLSESNERLQLHLKErmaALEEKGRLSEEIEKLRQE 465
Cdd:TIGR02169 850 KSIEKEIENLNGKKEELEEELEELEAALR---DLESRLGD-----LKKERDELEAQLRE---LERKIEELEAQIEKKRKR 918
|
....*
gi 966922630 466 VDQLK 470
Cdd:TIGR02169 919 LSELK 923
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
21-639 |
4.00e-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: 64.37 E-value: 4.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 21 DADANFEQLMVNMLDErEKLLESLREsqeTLAATQSRLQDALHERDQLQ----RHLNSALPQEFATLTRELSMCREQLLE 96
Cdd:pfam15921 167 DSNTQIEQLRKMMLSH-EGVLQEIRS---ILVDFEEASGKKIYEHDSMStmhfRSLGSAISKILRELDTEISYLKGRIFP 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 97 REEEISELKAE-RNNTRLLLEH----LECLVSRHERSL-----RMTVVKRQAQSpsgVSSEVEV------------LKAL 154
Cdd:pfam15921 243 VEDQLEALKSEsQNKIELLLQQhqdrIEQLISEHEVEItglteKASSARSQANS---IQSQLEIiqeqarnqnsmyMRQL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 155 KSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVS-------ALQQGAGVLDG----------AAEEEGTVELGP 217
Cdd:pfam15921 320 SDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTearterdQFSQESGNLDDqlqklladlhKREKELSLEKEQ 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 218 -KRLWKEDAGR---VEELQELLEKQNFELSQARERLVTLTATVT-ELEEDLGTARRDLIKSEELSSkhqrdLREAL-AQK 291
Cdd:pfam15921 400 nKRLWDRDTGNsitIDHLRRELDDRNMEVQRLEALLKAMKSECQgQMERQMAAIQGKNESLEKVSS-----LTAQLeSTK 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 292 EDMEERITTLEKRYLAAQREATSIHDLNDKLEnelaNKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAE- 370
Cdd:pfam15921 475 EMLRKVVEELTAKKMTLESSERTVSDLTASLQ----EKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTEc 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 371 --LAQRIAALTKAEERHGNIEEHLRQLEGQlEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAA 448
Cdd:pfam15921 551 eaLKLQMAEKDKVIEILRQQIENMTQLVGQ-HGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSD 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 449 LE-EKGRL----SEE---IEKLRQEVDQLkgrggpfvdgvhsrshMGSAADVRFSLGTTTHAPPGVHRRYsalREESAKD 520
Cdd:pfam15921 630 LElEKVKLvnagSERlraVKDIKQERDQL----------------LNEVKTSRNELNSLSEDYEVLKRNF---RNKSEEM 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 521 WETSPLPGMLAPAAAPAFDSDPEISDADEDEPGGLVGSA-----DVVSPSGHSDA-QTLAMMLQEQLDAINEEIRMIQEE 594
Cdd:pfam15921 691 ETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAmgmqkQITAKRGQIDAlQSKIQFLEEAMTNANKEKHFLKEE 770
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 966922630 595 KE--STELRAEEIETRVTSGSMEALNLKQLRKRGSIPTSLTALSLAS 639
Cdd:pfam15921 771 KNklSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKAS 817
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
35-474 |
4.35e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.29 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 35 DEREKLLESLRESQETLAA---TQSRLQDALHERDQLQRHLnSALPQEFATLTRELSMCREQLLEREEEISELKAERNNT 111
Cdd:PRK02224 227 EQREQARETRDEADEVLEEheeRREELETLEAEIEDLRETI-AETEREREELAEEVRDLRERLEELEEERDDLLAEAGLD 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 112 RL----LLEHLECLVSRHERSLRMTVVKRQAQSpsgvssevEVLKALKSLFEHHKALDEKVRErlraALERVTTLEEQLA 187
Cdd:PRK02224 306 DAdaeaVEARREELEDRDEELRDRLEECRVAAQ--------AHNEEAESLREDADDLEERAEE----LREEAAELESELE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 188 GAHQQVSALQQGAGVLDGAAEE-EGTVELGPkrlwkEDAGRVEELQELLEKqnfELSQARERLVTLTATVTELEEDLGTA 266
Cdd:PRK02224 374 EAREAVEDRREEIEELEEEIEElRERFGDAP-----VDLGNAEDFLEELRE---ERDELREREAELEATLRTARERVEEA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 267 RR---------------------DLIKSEELSSKHQRDLREALAQKEDMEERITTLEKrYLAAQREATSIHDLNDKLENE 325
Cdd:PRK02224 446 EAlleagkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIERLEERREDLEEL 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 326 LANKESL----HRQCEEKARHLQELLEVAEQK---LQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLrqleGQ 398
Cdd:PRK02224 525 IAERRETieekRERAEELRERAAELEAEAEEKreaAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLL----AA 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 399 LEEKNQELARVRQREK----MNEDHNKRLSDTVDR---LLSESNE-RLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLK 470
Cdd:PRK02224 601 IADAEDEIERLREKREalaeLNDERRERLAEKRERkreLEAEFDEaRIEEAREDKERAEEYLEQVEEKLDELREERDDLQ 680
|
....
gi 966922630 471 GRGG 474
Cdd:PRK02224 681 AEIG 684
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
166-476 |
4.42e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 64.21 E-value: 4.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 166 EKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAG-------VLDGAAEEEGTVELGPKRLwkedAGRVEELQELLEKQ 238
Cdd:PRK04863 379 EENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIqyqqavqALERAKQLCGLPDLTADNA----EDWLEEFQAKEQEA 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 239 NFELSQARERLVTLTATVTELEEDLGTARRdlIKSEELSSKHQRDLREALAQKEdmeerittlEKRYLAAQREAtsihdl 318
Cdd:PRK04863 455 TEELLSLEQKLSVAQAAHSQFEQAYQLVRK--IAGEVSRSEAWDVARELLRRLR---------EQRHLAEQLQQ------ 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 319 ndkLENELANKESLHRQceekARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQ 398
Cdd:PRK04863 518 ---LRMRLSELEQRLRQ----QQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQ 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 399 LEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESN---ERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGRGGP 475
Cdd:PRK04863 591 LQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQdvtEYMQQLLERERELTVERDELAARKQALDEEIERLSQPGGS 670
|
.
gi 966922630 476 F 476
Cdd:PRK04863 671 E 671
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
42-469 |
5.66e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.91 E-value: 5.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 42 ESLRESQETLAATQSRLQDALHE-RDQLQRHLNSA----------------LPQEFATLTRELSMCREQLLEREEEISEL 104
Cdd:PRK02224 310 EAVEARREELEDRDEELRDRLEEcRVAAQAHNEEAeslredaddleeraeeLREEAAELESELEEAREAVEDRREEIEEL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 105 KAERNNTRL-----------LLEHLECLVSRHERslrmtVVKRQAQSPSGVSSEVEVLKALKSLFEHHKA-------LDE 166
Cdd:PRK02224 390 EEEIEELRErfgdapvdlgnAEDFLEELREERDE-----LREREAELEATLRTARERVEEAEALLEAGKCpecgqpvEGS 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 167 KVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVLDGAAEEEGTVElgpkRLwkedAGRVEELQELLEKQNFELSQAR 246
Cdd:PRK02224 465 PHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIE----RL----EERREDLEELIAERRETIEEKR 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 247 ERLVTLTATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEkrylaaqreatsihdlndKLENEL 326
Cdd:PRK02224 537 ERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE------------------RIRTLL 598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 327 ANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQriAALTKAEERHGNIEEHLRQLEGQLEEKNQEL 406
Cdd:PRK02224 599 AAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDE--ARIEEAREDKERAEEYLEQVEEKLDELREER 676
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966922630 407 ARVRQREKMNEDHNKRLSDtvdrllsesnerlqlhLKERMAALEEKgrlSEEIEKLRQEVDQL 469
Cdd:PRK02224 677 DDLQAEIGAVENELEELEE----------------LRERREALENR---VEALEALYDEAEEL 720
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
267-472 |
1.15e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 267 RRDLIksEELS--SKHQRDLREALAQKEDMEERIT-------TLEKRY--LAAQRE-ATSIHDLNDKLEnELANKESLHR 334
Cdd:COG1196 157 RRAII--EEAAgiSKYKERKEEAERKLEATEENLErledilgELERQLepLERQAEkAERYRELKEELK-ELEAELLLLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 335 qceekARHLQELLEVAEQKLQQTMRKAETLpevEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREK 414
Cdd:COG1196 234 -----LRELEAELEELEAELEELEAELEEL---EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966922630 415 MNEDHNKRLSDTVDRL---LSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGR 472
Cdd:COG1196 306 RLEERRRELEERLEELeeeLAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
34-465 |
1.41e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 34 LDEREKLLESLRESQETLAATQSRLQDALHERDQLQRHLNSA---------------LPQEFATLTRELSMCREQLLERE 98
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELreeleklekllqllpLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 99 EEISELKAERNNTRLLLEHLEclvsRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALER 178
Cdd:COG4717 153 ERLEELRELEEELEELEAELA----ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 179 VTTLEEQLAGAH--QQVSALQQGAG------VLDGAAEEEGTVELGPKRLWKEDAGRVEELQELLEKQNFELSQARERLV 250
Cdd:COG4717 229 LEQLENELEAAAleERLKEARLLLLiaaallALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 251 TLTATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLND---KLENELA 327
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEagvEDEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 328 NKESLHRQCEEkarhLQELLEVAEQKLqqtmrkAETLPEVEAELAQriAALTKAEERHGNIEEHLRQLEGQLEEKNQELA 407
Cdd:COG4717 389 AALEQAEEYQE----LKEELEELEEQL------EELLGELEELLEA--LDEEELEEELEELEEELEELEEELEELREELA 456
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966922630 408 RVRQREKMNEDhnkrlSDTVDRLLSEsnerlQLHLKERMAALEEKGR--------LSEEIEKLRQE 465
Cdd:COG4717 457 ELEAELEQLEE-----DGELAELLQE-----LEELKAELRELAEEWAalklalelLEEAREEYREE 512
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-470 |
2.40e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 101 ISELKAERNNTRLLLEH-------LECLVSRHERSLRMtvVKRQAQSpsgvsseVEVLKALKS-LFEHHKALDEKVRERL 172
Cdd:TIGR02168 167 ISKYKERRKETERKLERtrenldrLEDILNELERQLKS--LERQAEK-------AERYKELKAeLRELELALLVLRLEEL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 173 RAALERvttLEEQLAGAHQQVSALQQGAGVLDGAAEEegtvelgpKRLwkedagRVEELQELLEKQNFELSQARERLVTL 252
Cdd:TIGR02168 238 REELEE---LQEELKEAEEELEELTAELQELEEKLEE--------LRL------EVSELEEEIEELQKELYALANEISRL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 253 TATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAaqreatsihdlndkLENELANKESL 332
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELES--------------LEAELEELEAE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 333 HRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEER-HGNIEEHLRQLE--------GQLEEKN 403
Cdd:TIGR02168 367 LEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERlQQEIEELLKKLEeaelkelqAELEELE 446
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966922630 404 QELARVRQREkmnEDHNKRLSDTVDRLLSESNERLQL-----HLKERMAALEekgRLSEEIEKLRQEVDQLK 470
Cdd:TIGR02168 447 EELEELQEEL---ERLEEALEELREELEEAEQALDAAerelaQLQARLDSLE---RLQENLEGFSEGVKALL 512
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
163-414 |
3.73e-09 |
|
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: 61.51 E-value: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 163 ALDEKVRERLRAALERVTTLEEQLAgahQQVSALQQGAGVLDGAAEEEGTVE--LGPKRLWKED--AGRVEELQELLEkq 238
Cdd:COG3096 829 AFAPDPEAELAALRQRRSELERELA---QHRAQEQQLRQQLDQLKEQLQLLNklLPQANLLADEtlADRLEELREELD-- 903
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 239 nfELSQARERLVTLTATVTELEEDLGTARRDLIKSEELsskhQRDLREALAQKEDMEERITTLEkrYLAAQREATSIHD- 317
Cdd:COG3096 904 --AAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQL----QADYLQAKEQQRRLKQQIFALS--EVVQRRPHFSYEDa 975
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 318 ---------LNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAAL-----TKAEE 383
Cdd:COG3096 976 vgllgensdLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELgvqadAEAEE 1055
|
250 260 270
....*....|....*....|....*....|.
gi 966922630 384 RhgnIEEHLRQLEGQLeekNQELARVRQREK 414
Cdd:COG3096 1056 R---ARIRRDELHEEL---SQNRSRRSQLEK 1080
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
217-405 |
4.25e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 4.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 217 PKRLWKEDAGRVEELQELLEKQNFELSQARERLVTLTATVTELEEDLGTARRDLIKSEelsskHQRDLREALAQKEDMEE 296
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE-----KLLQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 297 RITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKarhLQELLEVAEQKLQQTMRKAEtlpEVEAELAQRIA 376
Cdd:COG4717 140 ELAELPERLEELEERLEELRELEEELEELEAELAELQEELEEL---LEQLSLATEEELQDLAEELE---ELQQRLAELEE 213
|
170 180
....*....|....*....|....*....
gi 966922630 377 ALTKAEERHGNIEEHLRQLEGQLEEKNQE 405
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
31-467 |
4.64e-09 |
|
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: 60.89 E-value: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 31 VNMLDEREKLL-ESLRESQETLAATQSRLQD-------------ALHERDQLQRHLNSALPQEFATLTRELSmcrEQLLE 96
Cdd:pfam05483 270 ANQLEEKTKLQdENLKELIEKKDHLTKELEDikmslqrsmstqkALEEDLQIATKTICQLTEEKEAQMEELN---KAKAA 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 97 REEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgvsSEVEVLKALKS-----LFEHHKALDEKvrER 171
Cdd:pfam05483 347 HSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS-----SELEEMTKFKNnkeveLEELKKILAED--EK 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 172 LRAALERVTTLEEQLAGAHQQVSALQQGAGVLDGAAEEEGTVELGPKRLWKEDagrVEELQELLEKQ---NFELSQARER 248
Cdd:pfam05483 420 LLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKE---VEDLKTELEKEklkNIELTAHCDK 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 249 LVTLTATVTELEEDLgtarrdlikSEELSsKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHD----LNDKLEN 324
Cdd:pfam05483 497 LLLENKELTQEASDM---------TLELK-KHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREefiqKGDEVKC 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 325 ELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTK---AEERHGNIEE-HLRQLEGQLE 400
Cdd:pfam05483 567 KLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKkgsAENKQLNAYEiKVNKLELELA 646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 401 EKNQ---ELARVRQRE----KMNEDH-------NKRLSDTVDRLLSESNERLQLHLKErMAALEEKGRlsEEIEKLRQEV 466
Cdd:pfam05483 647 SAKQkfeEIIDNYQKEiedkKISEEKlleevekAKAIADEAVKLQKEIDKRCQHKIAE-MVALMEKHK--HQYDKIIEER 723
|
.
gi 966922630 467 D 467
Cdd:pfam05483 724 D 724
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
22-484 |
4.76e-09 |
|
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: 61.01 E-value: 4.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 22 ADANFEQLMVNMLDEREKLLESLRESQETLAATQSRLQDALHERDQLQRHLNSALPQEFATLTRELSMCREQLLEREEEI 101
Cdd:pfam12128 454 NQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQA 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 102 SELKA-ERNNTRLLLEHLECLVSR---HERSLRMTVVKRQAQSPS---GVSSEVEVLKALKSLFeHHKALDE---KVRER 171
Cdd:pfam12128 534 GTLLHfLRKEAPDWEQSIGKVISPellHRTDLDPEVWDGSVGGELnlyGVKLDLKRIDVPEWAA-SEEELRErldKAEEA 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 172 LRAALERVTTLEEQLAGAHQQVSALQQGagvLDGAAEEEGTVELGPKRLWKEDAGRVEELQELLEKqnfELSQARERLVT 251
Cdd:pfam12128 613 LQSAREKQAAAEEQLVQANGELEKASRE---ETFARTALKNARLDLRRLFDEKQSEKDKKNKALAE---RKDSANERLNS 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 252 LTATVTELEEDLGTA----RRDLIkseELSSKHQRDLREALAQKEDMEERI-TTLEKRYLAAQREATSIHDLNDkleNEL 326
Cdd:pfam12128 687 LEAQLKQLDKKHQAWleeqKEQKR---EARTEKQAYWQVVEGALDAQLALLkAAIAARRSGAKAELKALETWYK---RDL 760
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 327 ANK--------------ESLHRQCEEKARHLQELLE----VAEQKLQQTMRKAETLPEVEA---ELAQRIAALTK-AEER 384
Cdd:pfam12128 761 ASLgvdpdviaklkreiRTLERKIERIAVRRQEVLRyfdwYQETWLQRRPRLATQLSNIERaisELQQQLARLIAdTKLR 840
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 385 HGNIEEHLRQLEGQLEEKNQELARVRQR-EKMNEDHnkrlsdtvdrlLSESNERLQLHLKERMAALEE-KGRLSEEIEKL 462
Cdd:pfam12128 841 RAKLEMERKASEKQQVRLSENLRGLRCEmSKLATLK-----------EDANSEQAQGSIGERLAQLEDlKLKRDYLSESV 909
|
490 500
....*....|....*....|..
gi 966922630 463 RQEVDQLKGrggpfVDGVHSRS 484
Cdd:pfam12128 910 KKYVEHFKN-----VIADHSGS 926
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
261-475 |
7.25e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.08 E-value: 7.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 261 EDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKA 340
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 341 RHLQEL----------LEVAEQKLQQTMRKAETLPEVEAEL---AQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELA 407
Cdd:PRK03918 238 EEIEELekeleslegsKRKLEEKIRELEERIEELKKEIEELeekVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLS 317
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966922630 408 RVRQREKMNEDHNKRLSDTVDRLlsESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGRGGP 475
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERL--EELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTG 383
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
40-469 |
1.55e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 40 LLESLRESQETLAATQSRL-QDALHERDQLQRHLNSA--LPQEFATLTRELSMCREQLLEREEEISELKAERNNTRLLLE 116
Cdd:COG4717 47 LLERLEKEADELFKPQGRKpELNLKELKELEEELKEAeeKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 117 HLECL--VSRHERSL-----RMTVVKRQAQSPSGVSSEVEVLKAlkSLFEHHKALDEKVRERLRAALERVTTLEEQLAGA 189
Cdd:COG4717 127 LLPLYqeLEALEAELaelpeRLEELEERLEELRELEEELEELEA--ELAELQEELEELLEQLSLATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 190 HQQVSALQQGAGVLDGAAE--EEGTVELGPKRLWKEDAGRVEELQEL---------LEKQNFELSQARERLVTLTATVTE 258
Cdd:COG4717 205 QQRLAELEEELEEAQEELEelEEELEQLENELEAAALEERLKEARLLlliaaallaLLGLGGSLLSLILTIAGVLFLVLG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 259 LeedLGTARRDLIKSEELSSKHQRDLREALAQKE-DMEERITTLEKRYLAAQREATSIHDLNDKLEnelaNKESLHRQCE 337
Cdd:COG4717 285 L---LALLFLLLAREKASLGKEAEELQALPALEElEEEELEELLAALGLPPDLSPEELLELLDRIE----ELQELLREAE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 338 EKARHLQelLEVAEQKLQQTMRKAETlpEVEAELAQRIAALTKAEErhgnIEEHLRQLEGQLEEKNQELARVRQREKmNE 417
Cdd:COG4717 358 ELEEELQ--LEELEQEIAALLAEAGV--EDEEELRAALEQAEEYQE----LKEELEELEEQLEELLGELEELLEALD-EE 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 418 DHNKRLSDTVDRLLSESNERLQLH-----LKERMAALEEKGRLSE---EIEKLRQEVDQL 469
Cdd:COG4717 429 ELEEELEELEEELEELEEELEELReelaeLEAELEQLEEDGELAEllqELEELKAELREL 488
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
222-456 |
1.57e-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: 58.24 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 222 KEDAGRVEELQELLEKQNFELSQARERLVTLTATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTL 301
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 302 EKRY----LAAQREAT--------SIHDLNDkLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEA 369
Cdd:COG4942 103 KEELaellRALYRLGRqpplalllSPEDFLD-AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 370 ELAQRIAALTKAEERHgniEEHLRQLEGQLEEKNQELARVRQREkmnedhnKRLSDTVDRLLSESNERLQLHLKERMAAL 449
Cdd:COG4942 182 ELEEERAALEALKAER---QKLLARLEKELAELAAELAELQQEA-------EELEALIARLEAEAAAAAERTPAAGFAAL 251
|
....*..
gi 966922630 450 eeKGRLS 456
Cdd:COG4942 252 --KGKLP 256
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
232-465 |
1.78e-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: 57.85 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 232 QELLEKQNFELSQARERLVTLTATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQRE 311
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 312 atsIHDLNDKLENELANKESLHRQCEEKarhlqelLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERhgnieeh 391
Cdd:COG4942 99 ---LEAQKEELAELLRALYRLGRQPPLA-------LLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE------- 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966922630 392 LRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQE 465
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
35-470 |
2.17e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 35 DEREKLLESLRESQETLAATQSRLQDALHERDQLqrhlNSALPQefatLTRELSMcreqLLEREEEISELKAERNNTRLL 114
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEVLREINEI----SSELPE----LREELEK----LEKEVKELEELKEEIEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 115 LEHLECLVSRHERSLRMTV-----VKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGA 189
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEerieeLKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 190 HQQVS------------------------ALQQGAGVLDGAAEEEGTVELGPKRLWKEDAGRVEELQELLEKQNFELSQA 245
Cdd:PRK03918 327 EERIKeleekeerleelkkklkelekrleELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 246 RERLVTLTATVTELEEDLGTARRDLIKS----------------EELSSKHQRDLREALAQKEDMEERITTLEKR----- 304
Cdd:PRK03918 407 ISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgrelteehrKELLEEYTAELKRIEKELKEIEEKERKLRKElrele 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 305 -YLAAQREATSIHDLNDKLEN-----ELANKESLHRQCEEkARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAAL 378
Cdd:PRK03918 487 kVLKKESELIKLKELAEQLKEleeklKKYNLEELEKKAEE-YEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 379 TKAEERHGNIEEHLRQL----EGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLlsesnERLQLHLKErmaALEEKGR 454
Cdd:PRK03918 566 DELEEELAELLKELEELgfesVEELEERLKELEPFYNEYLELKDAEKELEREEKEL-----KKLEEELDK---AFEELAE 637
|
490
....*....|....*.
gi 966922630 455 LSEEIEKLRQEVDQLK 470
Cdd:PRK03918 638 TEKRLEELRKELEELE 653
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
229-470 |
2.52e-08 |
|
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: 58.49 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 229 EELQELLEKQNfELSQARERLVTLTATVTELEEDLGTARRDliKSEELSSKHQRDLREALAQKEDMEERITTLEKrylaa 308
Cdd:TIGR04523 264 KIKKQLSEKQK-ELEQNNKKIKELEKQLNQLKSEISDLNNQ--KEQDWNKELKSELKNQEKKLEEIQNQISQNNK----- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 309 qreatSIHDLND---KLENELANKES----LHRQCEEKARHLQELLEVAEQKLQQTmrkaETLPEVEAELAQRIaalTKA 381
Cdd:TIGR04523 336 -----IISQLNEqisQLKKELTNSESenseKQRELEEKQNEIEKLKKENQSYKQEI----KNLESQINDLESKI---QNQ 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 382 EERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLS--DTVDRLLSESNERLQLHLKERMAALEekgrlsEEI 459
Cdd:TIGR04523 404 EKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTnqDSVKELIIKNLDNTRESLETQLKVLS------RSI 477
|
250
....*....|.
gi 966922630 460 EKLRQEVDQLK 470
Cdd:TIGR04523 478 NKIKQNLEQKQ 488
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
828-894 |
4.21e-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: 51.14 E-value: 4.21e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966922630 828 FAQWDGPTVVSWLELWvGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEM 894
Cdd:smart00454 1 VSQWSPESVADWLESI-GLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
272-470 |
4.74e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 4.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 272 KSEELSSKHQRDLREALAQKEDMEERIttlekrylaaqREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAE 351
Cdd:COG4717 54 EADELFKPQGRKPELNLKELKELEEEL-----------KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 352 QKLQQTMRKAEtLPEVEAELAQRIAALTKAEERHgnieEHLRQLEGQLEEKNQELARVRQREkmnEDHNKRLSDTVDRLL 431
Cdd:COG4717 123 KLLQLLPLYQE-LEALEAELAELPERLEELEERL----EELRELEEELEELEAELAELQEEL---EELLEQLSLATEEEL 194
|
170 180 190
....*....|....*....|....*....|....*....
gi 966922630 432 SESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLK 470
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
34-470 |
4.89e-08 |
|
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: 57.54 E-value: 4.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 34 LDEREKLLESLRESQETLAATQSRLQDALHERDQLQRHLNSALPQEFATLTRELSmcrEQLLEREEEISELKAERNNTRl 113
Cdd:pfam12128 246 LQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWK---EKRDELNGELSAADAAVAKDR- 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 114 llEHLECLVSRHERSLRMTVVKR---QAQSPSgVSSEVEVL-KALKSLFEHHK-------ALDEKVRERLRAALERVT-- 180
Cdd:pfam12128 322 --SELEALEDQHGAFLDADIETAaadQEQLPS-WQSELENLeERLKALTGKHQdvtakynRRRSKIKEQNNRDIAGIKdk 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 181 ------TLEEQLAGAHQQVSAL------QQGAGVLDGAAEEEGTVE-LGPKRLWKEDAGRVEELQELLEKQNFELSQARE 247
Cdd:pfam12128 399 lakireARDRQLAVAEDDLQALeselreQLEAGKLEFNEEEYRLKSrLGELKLRLNQATATPELLLQLENFDERIERARE 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 248 RLVTLTATVTELEEDLGTARRdliKSEELSSKHQRDLREALAQKEDMEERITTLEKRylaaqrEATSIHDLNDKLEN--- 324
Cdd:pfam12128 479 EQEAANAEVERLQSELRQARK---RRDQASEALRQASRRLEERQSALDELELQLFPQ------AGTLLHFLRKEAPDweq 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 325 ---ELANKESLHR---QCEEKARHLQELLEVAEQKLQ----QTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQ 394
Cdd:pfam12128 550 sigKVISPELLHRtdlDPEVWDGSVGGELNLYGVKLDlkriDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQ 629
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966922630 395 LEGQLEEKNQELARVRQREKMNEDHNKRLSDtvdrllsesnERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLK 470
Cdd:pfam12128 630 ANGELEKASREETFARTALKNARLDLRRLFD----------EKQSEKDKKNKALAERKDSANERLNSLEAQLKQLD 695
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
32-468 |
7.29e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 56.90 E-value: 7.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 32 NMLDEREKLLESLRESQETLAATQsRLQDALHERDQLQRHLNSALPQEfATLTRELSmcreqllereeEISELKAERNNT 111
Cdd:TIGR00618 223 VLEKELKHLREALQQTQQSHAYLT-QKREAQEEQLKKQQLLKQLRARI-EELRAQEA-----------VLEETQERINRA 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 112 RllleHLECLVsrhERSLRMTVVKRQAQspsgvssevevlkalkslfEHHKALDEKVRERLRAALERVTTLEEQLAGAHQ 191
Cdd:TIGR00618 290 R----KAAPLA---AHIKAVTQIEQQAQ-------------------RIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 192 QVSaLQQGAgvldgAAEEEGTVELGPKRLWKEDAGRVEELQELLEKQNFELSQARERLVTLTATVTELEEDLGT------ 265
Cdd:TIGR00618 344 RRL-LQTLH-----SQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATidtrts 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 266 ARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHdlnDKLENELANKESLHRQCEEK-ARHLQ 344
Cdd:TIGR00618 418 AFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSL---KEREQQLQTKEQIHLQETRKkAVVLA 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 345 ELLEVAEQklQQTMRKAETLPEVEAELAQRIAALT----KAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHN 420
Cdd:TIGR00618 495 RLLELQEE--PCPLCGSCIHPNPARQDIDNPGPLTrrmqRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSF 572
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 966922630 421 KRLSDTVDRLLSESNERLQL-----HLKERMAALEEKGRLSEEIEKLRQEVDQ 468
Cdd:TIGR00618 573 SILTQCDNRSKEDIPNLQNItvrlqDLTEKLSEAEDMLACEQHALLRKLQPEQ 625
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
953-1008 |
8.52e-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: 50.37 E-value: 8.52e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 966922630 953 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1008
Cdd:smart00454 11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
246-472 |
1.53e-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: 55.84 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 246 RERLVTLTATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENE 325
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 326 LANKESLHR-------QCEEKARHLQELLE-----VAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLR 393
Cdd:TIGR02169 753 IENVKSELKelearieELEEDLHKLEEALNdlearLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 394 QLEGQLEEKNQEL-ARVRQREKMNEDHNKRLSDTVDRLlsesnERLQLHLKErmaALEEKGRLSEEIEKLRQEVDQLKGR 472
Cdd:TIGR02169 833 KEIQELQEQRIDLkEQIKSIEKEIENLNGKKEELEEEL-----EELEAALRD---LESRLGDLKKERDELEAQLRELERK 904
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
135-470 |
1.63e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 135 KRQAQSPSGVSSEVEVLKALKSLFEHHKALDE--KVRERLRAALERVTTLEEQlagahqqvsalqQGAGVLDGAAEEEGT 212
Cdd:PTZ00121 1417 KKKADEAKKKAEEKKKADEAKKKAEEAKKADEakKKAEEAKKAEEAKKKAEEA------------KKADEAKKKAEEAKK 1484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 213 VELGPKRLwKEDAGRVEELQELLE--KQNFELSQARERLVTLTATVTELEEDLGTARR--------DLIKSEELssKHQR 282
Cdd:PTZ00121 1485 ADEAKKKA-EEAKKKADEAKKAAEakKKADEAKKAEEAKKADEAKKAEEAKKADEAKKaeekkkadELKKAEEL--KKAE 1561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 283 DLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKlqqtmRKAE 362
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK-----KKVE 1636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 363 TLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDtvdrllsESNERLQLHL 442
Cdd:PTZ00121 1637 QLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE-------EAKKAEELKK 1709
|
330 340 350
....*....|....*....|....*....|..
gi 966922630 443 KErmaalEEKGRLSEEIEKLRQE----VDQLK 470
Cdd:PTZ00121 1710 KE-----AEEKKKAEELKKAEEEnkikAEEAK 1736
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
34-380 |
2.11e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 34 LDEREKLLESLRESQETLAATQSRLQDALherDQLQRHLNSALPQEFATLTRELSMCREQLLEREEEISELKAERNNTRL 113
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEEL---EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 114 LLEHLECLVSRHER--------------SLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERV 179
Cdd:COG4717 228 ELEQLENELEAAALeerlkearlllliaAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEEL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 180 TTLEEQLAGAHQQVSALQQGAGVLDGAAEEEGTVELGPKRLWKEDAGRVEELQE-------------LLEKQNFELSQAR 246
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEelqleeleqeiaaLLAEAGVEDEEEL 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 247 ERLVTLTATVTELEEDLGTARRDL--IKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLEN 324
Cdd:COG4717 388 RAALEQAEEYQELKEELEELEEQLeeLLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE 467
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966922630 325 --ELANKESLHRQCEEKARHLQE---LLEVAEQKLQQTMRKA--ETLPEVEAELAQRIAALTK 380
Cdd:COG4717 468 dgELAELLQELEELKAELRELAEewaALKLALELLEEAREEYreERLPPVLERASEYFSRLTD 530
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
183-470 |
2.13e-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: 55.51 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 183 EEQLAGAHQQVSALQQGAGVLDGAAEEEGTV-----ELGPKRLWKEDAGRVEELQELLEKQNFELSQARERLVTLTATVT 257
Cdd:pfam15921 162 EDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIlvdfeEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIF 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 258 ELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEerITTLEKRYLAAQREATSIHDLNDKLENELANKESLHrqce 337
Cdd:pfam15921 242 PVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVE--ITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMY---- 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 338 ekARHLQELLEVAEQkLQQTMRKA-----ETLPEVEAELAQRIAALTKAE-------ERHGNIEEHLRQLEGQLEEKNQE 405
Cdd:pfam15921 316 --MRQLSDLESTVSQ-LRSELREAkrmyeDKIEELEKQLVLANSELTEARterdqfsQESGNLDDQLQKLLADLHKREKE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 406 LARVRQREKMNEDHNKRLSDTVDRLLSESNER-----------------LQLHLKERMAALEEKGRLSEEIEKLRQEVDQ 468
Cdd:pfam15921 393 LSLEKEQNKRLWDRDTGNSITIDHLRRELDDRnmevqrleallkamkseCQGQMERQMAAIQGKNESLEKVSSLTAQLES 472
|
..
gi 966922630 469 LK 470
Cdd:pfam15921 473 TK 474
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
45-463 |
4.29e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 4.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 45 RESQETLAATQ---SRLQDALHE----RDQLQRHLNSAlpQEFATLTRELSmcREQLLEREEEISELKAERNNTRLLLEH 117
Cdd:COG1196 175 EEAERKLEATEenlERLEDILGElerqLEPLERQAEKA--ERYRELKEELK--ELEAELLLLKLRELEAELEELEAELEE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 118 LECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEK------VRERLRAALERVTTLEEQLAGAHQ 191
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLeqdiarLEERRRELEERLEELEEELAELEE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 192 QVSALQQGAGVLDGAAEEEGTVELGPKRLWKEDAGRVEELQELLEKQNFELSQARERLVTLTATVTELEEDLGTARRDLI 271
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 272 KSEELsskhQRDLREALAQKEDMEERITTLEKRYLAAQREATS-IHDLNDKLENELANKESLHRQCEEKARHLQELLEVA 350
Cdd:COG1196 411 ALLER----LERLEEELEELEEALAELEEEEEEEEEALEEAAEeEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 351 EQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRL 430
Cdd:COG1196 487 AEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYL 566
|
410 420 430
....*....|....*....|....*....|...
gi 966922630 431 LSESNERLQLHLKERMAALEEKGRLSEEIEKLR 463
Cdd:COG1196 567 KAAKAGRATFLPLDKIRARAALAAALARGAIGA 599
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
284-464 |
5.35e-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: 52.23 E-value: 5.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 284 LREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELL-EVAEQKLQQTMRKae 362
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgNVRNNKEYEALQK-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 363 tlpEVEAelaqriaaltkAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHL 442
Cdd:COG1579 97 ---EIES-----------LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
170 180
....*....|....*....|...
gi 966922630 443 KERMAALEE-KGRLSEEIEKLRQ 464
Cdd:COG1579 163 AEREELAAKiPPELLALYERIRK 185
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
47-469 |
5.72e-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: 54.20 E-value: 5.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 47 SQETLAATQSRLQDALHERDQLQRHLnsalpQEFATLTRELSMCREQLLEREEEISELKAERNNTRLLLEHLECLVsrhE 126
Cdd:TIGR00618 436 QQRYAELCAAAITCTAQCEKLEKIHL-----QESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPL---C 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 127 RSLRMTVVKRQAQSPSGVSSEvEVLKALKSLFEHHKALdEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVLDGA 206
Cdd:TIGR00618 508 GSCIHPNPARQDIDNPGPLTR-RMQRGEQTYAQLETSE-EDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKED 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 207 AE-----EEGTVELGPKRLWKEDAGRvEELQELLEK--------------QNFELSQARErLVTLTATVTEL--EEDLGT 265
Cdd:TIGR00618 586 IPnlqniTVRLQDLTEKLSEAEDMLA-CEQHALLRKlqpeqdlqdvrlhlQQCSQELALK-LTALHALQLTLtqERVREH 663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 266 ARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDlNDKLENELANKESLHRQceekarHLQE 345
Cdd:TIGR00618 664 ALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEE-YDREFNEIENASSSLGS------DLAA 736
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 346 LLEVAEQKLQQTMRKAET-LPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQ---LEEKNQELARVRQREKMNEDHNK 421
Cdd:TIGR00618 737 REDALNQSLKELMHQARTvLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFnrlREEDTHLLKTLEAEIGQEIPSDE 816
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 966922630 422 RLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQL 469
Cdd:TIGR00618 817 DILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQL 864
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
34-465 |
5.83e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 5.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 34 LDEREKLLESLRESQETLAATQSRL-QDALHERDQLQRHLNSA--LPQEFATLTRELSMCREQLLEREEEISELKAERNN 110
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLeQDIARLEERRRELEERLeeLEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 111 TRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERvTTLEEQLAGAH 190
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL-EELEEALAELE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 191 QQVSALQQGAGVLDGAAEEEGTVELGPKRLWKEDAGRVEELQELLEKQNFELSQARERLVTLTATVTELEEDLGTARRDL 270
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 271 IKS------------------------EELSSKHQRDLREALAQ--------KEDMEERITTLEKRyLAAQREATSIHDL 318
Cdd:COG1196 515 LLAglrglagavavligveaayeaaleAALAAALQNIVVEDDEVaaaaieylKAAKAGRATFLPLD-KIRARAALAAALA 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 319 NDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQ 398
Cdd:COG1196 594 RGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAA 673
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966922630 399 LEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQE 465
Cdd:COG1196 674 LLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
227-377 |
9.47e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.46 E-value: 9.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 227 RVEELQELLEKQNFELSQARERLVTLTATVTELEEDLGTARRDLIKSEEL--SSKHQRDLREALAQKEDMEERITTLEKR 304
Cdd:COG1579 32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgNVRNNKEYEALQKEIESLKRRISDLEDE 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966922630 305 YLaaqreatsihDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAA 377
Cdd:COG1579 112 IL----------ELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
227-417 |
1.01e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.60 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 227 RVEELQELLEKQNFELSQARERLVTLTATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYL 306
Cdd:COG4372 46 ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 307 AAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMrkaetlpevEAELAQRIAALTKAEERHG 386
Cdd:COG4372 126 DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS---------EAEAEQALDELLKEANRNA 196
|
170 180 190
....*....|....*....|....*....|.
gi 966922630 387 NIEEHLRQLEGQLEEKNQELARVRQREKMNE 417
Cdd:COG4372 197 EKEEELAEAEKLIESLPRELAEELLEAKDSL 227
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
281-568 |
1.57e-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: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 281 QRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELankESLHRQCEEKARHLQELLEVAEQKLQQTMRK 360
Cdd:COG3883 22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI---DKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 361 AETLPEVEA--------ELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLS 432
Cdd:COG3883 99 GGSVSYLDVllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 433 ESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGRGGPFVDGVHSRSHMGSAADVRFSLGTTTHAPPGVHRRYSA 512
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAA 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 966922630 513 LREESakdWETSPLPGMLAPAAAPAFDSDPEISDADEDEPGGLVGSADVVSPSGHS 568
Cdd:COG3883 259 AGSAG---AAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAG 311
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
33-380 |
1.83e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 33 MLDEREKLLESLRESQETLAATQSRLQDALHERDQLQRHLNsALPQEFATLTRELSMCREQLLEREEEISELKAErnntr 112
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE-QLEQEEEKLKERLEELEEDLSSLEQEIENVKSE----- 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 113 llLEHLECLVSRHERSLrmtvVKRQAQ--------SPSGVSsevEVLKALKSLFEHHKALDEKVRErLRAALERVTTLEE 184
Cdd:TIGR02169 760 --LKELEARIEELEEDL----HKLEEAlndlearlSHSRIP---EIQAELSKLEEEVSRIEARLRE-IEQKLNRLTLEKE 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 185 QLAGAHQQvsALQQGAGVLDGAAEEEGTVElgpkrlwkEDAGRVEELQELLEKQNFELSQARERLVTLTATVTELEEDLG 264
Cdd:TIGR02169 830 YLEKEIQE--LQEQRIDLKEQIKSIEKEIE--------NLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 265 TARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQ 344
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQ 979
|
330 340 350
....*....|....*....|....*....|....*.
gi 966922630 345 ELLEVAEqKLQQTMRKAETLPEVEAELAQRIAALTK 380
Cdd:TIGR02169 980 EYEEVLK-RLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
20-471 |
2.12e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.43 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 20 ADADANFEQLMVNMLDEREKLLESLRESQETLAATQSRLQDALHERDQLQR---HLNSALPQEFATL---TRELSMCREQ 93
Cdd:pfam15921 320 SDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQesgNLDDQLQKLLADLhkrEKELSLEKEQ 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 94 LLE-------REEEISELKAERNNTRLLLEHLECLVsrheRSLRMTVVKRQAQSPSGVSSEVEVLKALKSLfehhKALDE 166
Cdd:pfam15921 400 NKRlwdrdtgNSITIDHLRRELDDRNMEVQRLEALL----KAMKSECQGQMERQMAAIQGKNESLEKVSSL----TAQLE 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 167 KVRERLRAALERVTTLEEQLAGAHQQVSALQQGAgvldgaAEEEGTVELGPKRLWKEDAGRVEELQEL--LEKQNFELSQ 244
Cdd:pfam15921 472 STKEMLRKVVEELTAKKMTLESSERTVSDLTASL------QEKERAIEATNAEITKLRSRVDLKLQELqhLKNEGDHLRN 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 245 ARERLVTLTATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERIT----TLEKRYLAAQREATSIHDLND 320
Cdd:pfam15921 546 VQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINdrrlELQEFKILKDKKDAKIRELEA 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 321 KLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEV--EAELAQRiAALTKAEErhgnIEEHLRQLEGQ 398
Cdd:pfam15921 626 RVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLseDYEVLKR-NFRNKSEE----METTTNKLKMQ 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 399 LEEKNQELARVRQREKMNEDHN-----------KRLS---DTVDRLLSESN---ERLQLHLKERMAALEEKGRLSEEIEK 461
Cdd:pfam15921 701 LKSAQSELEQTRNTLKSMEGSDghamkvamgmqKQITakrGQIDALQSKIQfleEAMTNANKEKHFLKEEKNKLSQELST 780
|
490
....*....|
gi 966922630 462 LRQEVDQLKG 471
Cdd:pfam15921 781 VATEKNKMAG 790
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
135-472 |
2.63e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 135 KRQAQSPSGVSSEVEVL-KALKSLFEHHKALDEKV--RERLRAALERVTTLEEQLAGAHQQVSALQQGAGVLDGAAEEEG 211
Cdd:COG4717 60 KPQGRKPELNLKELKELeEELKEAEEKEEEYAELQeeLEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 212 TVELGPKRL--WKEDAGRVEELQELLEKQNFELSQARERLVTLTATVT-ELEEDLGTARRDLIKSEELSSKHQRDLREAL 288
Cdd:COG4717 140 ELAELPERLeeLEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 289 AQKEDMEERITTLEKRYLAAQRE-------------------ATSIHDLNDKLEN-----------------ELANKESL 332
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEerlkearlllliaaallalLGLGGSLLSLILTiagvlflvlgllallflLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 333 HRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQR-IAALTKAEERHGNIEEHLRQLE-GQLEEKNQEL---- 406
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLElLDRIEELQELLREAEELEEELQlEELEQEIAALlaea 379
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966922630 407 ---------ARVRQREKMNEDhNKRLSDTVDRLLSESNERLQLHLKERMAALEEK-GRLSEEIEKLRQEVDQLKGR 472
Cdd:COG4717 380 gvedeeelrAALEQAEEYQEL-KEELEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREE 454
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
227-470 |
2.85e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 51.38 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 227 RVEELQELLEKQN--FELSQARERLVTLTATVTELEEDLGTARR---DLIKSEElssKHQRDLREALAQKEDMEERIttL 301
Cdd:PRK04778 83 DIEEQLFEAEELNdkFRFRKAKHEINEIESLLDLIEEDIEQILEelqELLESEE---KNREEVEQLKDLYRELRKSL--L 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 302 EKRYlaaqreatSIHDLNDKLENELANKESLHRQCEE--------KARhlqELLEVAEQKLQQTMRKAETLPEVEAELAQ 373
Cdd:PRK04778 158 ANRF--------SFGPALDELEKQLENLEEEFSQFVEltesgdyvEAR---EILDQLEEELAALEQIMEEIPELLKELQT 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 374 RI-AALTKAEE------------RHGNIEEHLRQLEGQLEEKNQELARVRQREKmnEDHNKRLSDTVDRLLsesnERLQL 440
Cdd:PRK04778 227 ELpDQLQELKAgyrelveegyhlDHLDIEKEIQDLKEQIDENLALLEELDLDEA--EEKNEEIQERIDQLY----DILER 300
|
250 260 270
....*....|....*....|....*....|
gi 966922630 441 HLKERMAALEEKGRLSEEIEKLRQEVDQLK 470
Cdd:PRK04778 301 EVKARKYVEKNSDTLPDFLEHAKEQNKELK 330
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
33-385 |
5.10e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.84 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 33 MLDEREKLLESLRESQETLAATQSrLQDALHERDQLQRHLN-SALPQEFATLTRELSMCREQLLEREEEISELKAERNNT 111
Cdd:TIGR02169 192 IIDEKRQQLERLRREREKAERYQA-LLKEKREYEGYELLKEkEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 112 RLLLEHLECLVSRhERSLRMTVVKRQAQSpsgVSSEVEVLK-ALKSLFEHHKALDEKVR---ERLRAALERVTTLEEQLA 187
Cdd:TIGR02169 271 EQLLEELNKKIKD-LGEEEQLRVKEKIGE---LEAEIASLErSIAEKERELEDAEERLAkleAEIDKLLAEIEELEREIE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 188 GAHQQVSALQqgagvlDGAAEEEGTVELGPKRLWKEDAgrveELQELLEkqnfELSQARERLVTLTatvTELEEDLGTAR 267
Cdd:TIGR02169 347 EERKRRDKLT------EEYAELKEELEDLRAELEEVDK----EFAETRD----ELKDYREKLEKLK---REINELKRELD 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 268 RDLIKSEELSSKhQRDLREALAQKED----MEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHL 343
Cdd:TIGR02169 410 RLQEELQRLSEE-LADLNAAIAGIEAkineLEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKL 488
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 966922630 344 QELLEVAEQKLQQTMRKAETLPEVEAELAQRI-------AALTKAEERH 385
Cdd:TIGR02169 489 QRELAEAEAQARASEERVRGGRAVEEVLKASIqgvhgtvAQLGSVGERY 537
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
1031-1102 |
7.01e-06 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 44.98 E-value: 7.01e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966922630 1031 VLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHntlalILQIPTQNTQARQVMEREFNNLLA 1102
Cdd:smart00454 1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEED-----LKELGITKLGHRKKILKAIQKLKE 67
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
169-412 |
7.14e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 7.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 169 RERLRAAL----ERVTTLEEQLAGAHQQVSALQQGAGVLDGAAEEEGTVElgpkrlwkedagRVEELQEllekqnfELSQ 244
Cdd:COG3206 170 REEARKALefleEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQ------------QLSELES-------QLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 245 ARERLVTLTATVTELEEDLGTARRDLikSEELSSKHQRDLREALAQkedMEERITTLEKRYLAAQREATSihdlndkLEN 324
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDAL--PELLQSPVIQQLRAQLAE---LEAELAELSARYTPNHPDVIA-------LRA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 325 ELANKEslhrqceekarhlQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQ 404
Cdd:COG3206 299 QIAALR-------------AQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARE 365
|
....*...
gi 966922630 405 ELARVRQR 412
Cdd:COG3206 366 LYESLLQR 373
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
227-465 |
7.18e-06 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 49.42 E-value: 7.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 227 RVEELQELLEKQNFELSQA-RERLvTLTATVTELEEDLgtarRDLIKSEE-LSSKHQRDLREALAQKEDMEerITTLEKR 304
Cdd:pfam15905 95 RLQALEEELEKVEAKLNAAvREKT-SLSASVASLEKQL----LELTRVNElLKAKFSEDGTQKKMSSLSME--LMKLRNK 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 305 YLAAQREATsihDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTmrKAETLpeveaELAQRIAALTKAEER 384
Cdd:pfam15905 168 LEAKMKEVM---AKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEE--KSETE-----KLLEYITELSCVSEQ 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 385 HGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHN-----------KRLSDTVDRLLSESNERLQLHLKErMAALEEKG 453
Cdd:pfam15905 238 VEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELskqikdlnekcKLLESEKEELLREYEEKEQTLNAE-LEELKEKL 316
|
250
....*....|...
gi 966922630 454 RL-SEEIEKLRQE 465
Cdd:pfam15905 317 TLeEQEHQKLQQK 329
|
|
| SAM_superfamily |
cd09487 |
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
953-1004 |
8.37e-06 |
|
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.
Pssm-ID: 188886 [Multi-domain] Cd Length: 56 Bit Score: 44.15 E-value: 8.37e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 966922630 953 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGI 1004
Cdd:cd09487 4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
223-470 |
9.10e-06 |
|
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: 50.36 E-value: 9.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 223 EDAGRVEELQELLEKQNfELSQARERLVTLTATVTELEEDLgtarrdliKSEELSSKHQRDLREALAQKEDMEERITTLE 302
Cdd:pfam02463 160 EEAAGSRLKRKKKEALK-KLIEETENLAELIIDLEELKLQE--------LKLKEQAKKALEYYQLKEKLELEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 303 KRYLAAQREATSIHDLNDK------------LENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAE 370
Cdd:pfam02463 231 YLKLNEERIDLLQELLRDEqeeiesskqeieKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 371 LAQRIaaLTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALE 450
Cdd:pfam02463 311 DDEEK--LKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSS 388
|
250 260
....*....|....*....|
gi 966922630 451 EKGRLSEEIEKLRQEVDQLK 470
Cdd:pfam02463 389 AAKLKEEELELKSEEEKEAQ 408
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
1031-1101 |
9.93e-06 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 44.18 E-value: 9.93e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966922630 1031 VLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALdeNFDHNTLAlilQIPTQNTQARQVMEREFNNLL 1101
Cdd:pfam07647 1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK---RLGITSVGHRRKILKKIQELK 66
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
245-412 |
1.30e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 245 ARERLVTLTATVTELEEDLGTARRDLIKSEELSsKHQRDLREALAQKEDM----------EERITTLEKRY--------- 305
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAEL-DALQERREALQRLAEYswdeidvasaEREIAELEAELerldassdd 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 306 -LAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEER 384
Cdd:COG4913 687 lAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERE 766
|
170 180
....*....|....*....|....*....
gi 966922630 385 HG-NIEEHLRQLEGQLEEKNQELARVRQR 412
Cdd:COG4913 767 LReNLEERIDALRARLNRAEEELERAMRA 795
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
230-470 |
1.48e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.25 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 230 ELQELLEKQNFELSQARERLVTLTATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERIttlekrylaaQ 309
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKEN----------Q 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 310 REATSIHDLNDK---LENELANKESLHRQCEEKARHLQ---ELLEVAEQKLQQTMRKAETlpEVEaELAQRIAALTKAEE 383
Cdd:TIGR04523 381 SYKQEIKNLESQindLESKIQNQEKLNQQKDEQIKKLQqekELLEKEIERLKETIIKNNS--EIK-DLTNQDSVKELIIK 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 384 RHGNIEEHLRQ----LEGQ-------LEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNErlqlhLKERMAALE-- 450
Cdd:TIGR04523 458 NLDNTRESLETqlkvLSRSinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS-----LKEKIEKLEse 532
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 966922630 451 -----------------------------EKGRLSEEIEKLRQEVDQLK 470
Cdd:TIGR04523 533 kkekeskisdledelnkddfelkkenlekEIDEKNKEIEELKQTQKSLK 581
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
223-469 |
1.63e-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: 49.19 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 223 EDAGRVEELQELLEKQNFELSQARERLVTLTATVTELEEDLgtARRDLIKSEELSSKHQRDLREA----LAQKEDMEERI 298
Cdd:COG5185 272 ENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATE--SLEEQLAAAEAEQELEESKRETetgiQNLTAEIEQGQ 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 299 TTLEKRYLAAQREATSIHDLND------KLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAEtlpeveaela 372
Cdd:COG5185 350 ESLTENLEAIKEEIENIVGEVElsksseELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAAD---------- 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 373 qriaalTKAEERHGNIEEHLRQLEgQLEEKNQELAR--VRQREKMNEDHNKRLSDTVDRLLSE-------SNERLQlHLK 443
Cdd:COG5185 420 ------RQIEELQRQIEQATSSNE-EVSKLLNELISelNKVMREADEESQSRLEEAYDEINRSvrskkedLNEELT-QIE 491
|
250 260 270
....*....|....*....|....*....|.
gi 966922630 444 ERMAAL-----EEKGRLSEEIEKLRQEVDQL 469
Cdd:COG5185 492 SRVSTLkatleKLRAKLERQLEGVRSKLDQV 522
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
166-476 |
1.63e-05 |
|
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: 49.57 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 166 EKVRERLRAALERVTTLEEQLAGAHQ-----QVSALQ--QGAGVLDGAAEEEGTVELGPKRLwkedAGRVEELQELLEKQ 238
Cdd:COG3096 378 AEAEARLEAAEEEVDSLKSQLADYQQaldvqQTRAIQyqQAVQALEKARALCGLPDLTPENA----EDYLAAFRAKEQQA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 239 NFELSQARERLVTLTATVTELEEDLGTARRdlIKSE-ELSSKHQRdLREALAQKEdmeerittlEKRYLAAQREAtsihd 317
Cdd:COG3096 454 TEEVLELEQKLSVADAARRQFEKAYELVCK--IAGEvERSQAWQT-ARELLRRYR---------SQQALAQRLQQ----- 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 318 lndkLENELANKEslhrQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEG 397
Cdd:COG3096 517 ----LRAQLAELE----QRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLE 588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 398 QLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNE----RLQLHLKERMAALEEKgRLSEEIEKLRQEVDQLKGRG 473
Cdd:COG3096 589 QLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEvtaaMQQLLEREREATVERD-ELAARKQALESQIERLSQPG 667
|
...
gi 966922630 474 GPF 476
Cdd:COG3096 668 GAE 670
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
30-415 |
2.02e-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: 48.53 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 30 MVNMLDEREKLLESLRESQETLAATQSRLQDALHERDQLQRHLNS------ALPQEFATLTRELSmcreqllereeeisE 103
Cdd:pfam19220 15 MADRLEDLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQeraaygKLRRELAGLTRRLS--------------A 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 104 LKAERNNTRLLLEHLECLVSRHER---SLRMTVVKRQAQSPS---GVSSEVEVLKALKslfEHHKALdekvRERLRAALE 177
Cdd:pfam19220 81 AEGELEELVARLAKLEAALREAEAakeELRIELRDKTAQAEAlerQLAAETEQNRALE---EENKAL----REEAQAAEK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 178 RVTTLEEQLAGAHQQVsalqqgagvldGAAEEEGTVelgpkrlwkedagrveeLQELLEKQNFELSQarerlvtLTATVT 257
Cdd:pfam19220 154 ALQRAEGELATARERL-----------ALLEQENRR-----------------LQALSEEQAAELAE-------LTRRLA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 258 ELEEDLGTARRDLIKSE----ELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLH 333
Cdd:pfam19220 199 ELETQLDATRARLRALEgqlaAEQAERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAI 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 334 RQCEEKARH--------------LQELLEVAEQKLQQTMRKAETLPEVEAELAQRIA----ALTKAEERHGNIEEHLRQL 395
Cdd:pfam19220 279 RAAERRLKEasierdtlerrlagLEADLERRTQQFQEMQRARAELEERAEMLTKALAakdaALERAEERIASLSDRIAEL 358
|
410 420
....*....|....*....|....*..
gi 966922630 396 EGQ-------LEEKNQELARVRQREKM 415
Cdd:pfam19220 359 TKRfeveraaLEQANRRLKEELQRERA 385
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
320-470 |
2.72e-05 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 46.60 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 320 DKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAEtlPEVEAELAQRIAALTKAEERHG-----------NI 388
Cdd:pfam04012 39 VKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGN--EELAREALAEKKSLEKQAEALEtqlaqqrsaveQL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 389 EEHLRQLEGQLEEKNQELARVRQREKMNEdHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEK---LRQE 465
Cdd:pfam04012 117 RKQLAALETKIQQLKAKKNLLKARLKAAK-AQEAVQTSLGSLSTSSATDSFERIEEKIEEREARADAAAELASavdLDAK 195
|
....*
gi 966922630 466 VDQLK 470
Cdd:pfam04012 196 LEQAG 200
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
105-464 |
2.95e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 105 KAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALkslfEHHKALDEKVRERLRAALERVTTLEE 184
Cdd:PTZ00121 1244 KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD----EAKKAEEKKKADEAKKKAEEAKKADE 1319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 185 qlagAHQQVSALQQGAGVLDGAAEEEGTVELGPKRLWKEDAGRVEELQELLEKQNFELSQARERLVTLTATVTEL---EE 261
Cdd:PTZ00121 1320 ----AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKkkaDE 1395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 262 DLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREAtsiHDLNDKLEnELANKESLHRQCEEKaR 341
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA---DEAKKKAE-EAKKAEEAKKKAEEA-K 1470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 342 HLQELLEVAEQKlqqtmRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNK 421
Cdd:PTZ00121 1471 KADEAKKKAEEA-----KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK 1545
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 966922630 422 RLSDTVDRL--LSESNERLQLHLKERmaALEEKGRLSEEIEKLRQ 464
Cdd:PTZ00121 1546 KKADELKKAeeLKKAEEKKKAEEAKK--AEEDKNMALRKAEEAKK 1588
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
81-324 |
3.25e-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: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 81 ATLTRELSMCREQLLEREEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgVSSEVE-------VLKA 153
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAE---LEAELErldassdDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 154 LKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVLDGAAEEEGTVELGpKRLWKEDAGRVEE--- 230
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE-ERFAAALGDAVERelr 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 231 --LQELLEKQNFELSQARERLVTL--------TATVTELEEDLGT-----ARRDLIKSEELsSKHQRDLREALaqKEDME 295
Cdd:COG4913 769 enLEERIDALRARLNRAEEELERAmrafnrewPAETADLDADLESlpeylALLDRLEEDGL-PEYEERFKELL--NENSI 845
|
250 260 270
....*....|....*....|....*....|
gi 966922630 296 ERITTLEKRYLAAQREATS-IHDLNDKLEN 324
Cdd:COG4913 846 EFVADLLSKLRRAIREIKErIDPLNDSLKR 875
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
169-465 |
4.70e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 47.55 E-value: 4.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 169 RERLRAALERVTTLEEQLAGAHQQVSALQQGAGVLDGAAEEEGTVELGPKRLWKEDAGRVEE-----LQELLEKQ-NFEL 242
Cdd:pfam02029 12 RRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREErrqkrLQEALERQkEFDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 243 SQARERL-VTLTATVTELEEDLGTARRDLIKSEELSSK-----------HQRDLREALAQ---KEDMEERITTLEKRYLA 307
Cdd:pfam02029 92 TIADEKEsVAERKENNEEEENSSWEKEEKRDSRLGRYKeeeteirekeyQENKWSTEVRQaeeEGEEEEDKSEEAEEVPT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 308 AQREATSIHDLNDKLENELA--NKESLHRQ---CEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAE 382
Cdd:pfam02029 172 ENFAKEEVKDEKIKKEKKVKyeSKVFLDQKrghPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 383 ErhgnieehLRQLEGQLEEKNQELARVRQREKMNE-DHNKRLSDTVDRLLSESNERLQLHLKERMAALEE-KGRLSEEIE 460
Cdd:pfam02029 252 E--------LRRRRQEKESEEFEKLRQKQQEAELElEELKKKREERRKLLEEEEQRRKQEEAERKLREEEeKRRMKEEIE 323
|
....*
gi 966922630 461 KLRQE 465
Cdd:pfam02029 324 RRRAE 328
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
281-472 |
4.88e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 281 QRDLREALAQKEDMEERIttlekrylaaqrEATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRK 360
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEK------------EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEER 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 361 AETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQL 440
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDR 329
|
170 180 190
....*....|....*....|....*....|..
gi 966922630 441 HLKERMAAleekGRLSEEIEKLRQEVDQLKGR 472
Cdd:PRK02224 330 LEECRVAA----QAHNEEAESLREDADDLEER 357
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
168-326 |
4.91e-05 |
|
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: 46.18 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 168 VRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVLD--GAAEEEGTVELGP-----KRLWKEDAGRVEELQELLEKQNF 240
Cdd:pfam00261 48 LEEELERTEERLAEALEKLEEAEKAADESERGRKVLEnrALKDEEKMEILEAqlkeaKEIAEEADRKYEEVARKLVVVEG 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 241 ELSQARERLVTLTATVTELEEDLGTAR---RDLIKSEELSSKHQRDLREALaqkEDMEERITTLEKRYLAAQREATSIHD 317
Cdd:pfam00261 128 DLERAEERAELAESKIVELEEELKVVGnnlKSLEASEEKASEREDKYEEQI---RFLTEKLKEAETRAEFAERSVQKLEK 204
|
....*....
gi 966922630 318 LNDKLENEL 326
Cdd:pfam00261 205 EVDRLEDEL 213
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
115-470 |
4.96e-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: 47.73 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 115 LEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEV-------------LKALKSLFEHHKALDEKVRERLRAA---LER 178
Cdd:TIGR00606 711 LKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIpelrnklqkvnrdIQRLKNDIEEQETLLGTIMPEEESAkvcLTD 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 179 VTTLEEQLAGAHQQVSALQQGAGVLDGAAEEEGTVELGPKRLWKED-----AGRVEELQELLEKQNFELSQARERLVTLT 253
Cdd:TIGR00606 791 VTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHeldtvVSKIELNRKLIQDQQEQIQHLKSKTNELK 870
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 254 ATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELankESLH 333
Cdd:TIGR00606 871 SEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKV---NDIK 947
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 334 RQCEEKARHLQELLE-VAEQKLQQTMRKaetlpevEAELAQRIAALTKAEERHGNIEEHLRQLEgqleeknQELARVRQR 412
Cdd:TIGR00606 948 EKVKNIHGYMKDIENkIQDGKDDYLKQK-------ETELNTVNAQLEECEKHQEKINEDMRLMR-------QDIDTQKIQ 1013
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 413 EKMNEDHNKRLsdTVDRLLSESNERLQLHLKE--RMAALEEKgrlsEEIEKLRQEVDQLK 470
Cdd:TIGR00606 1014 ERWLQDNLTLR--KRENELKEVEEELKQHLKEmgQMQVLQMK----QEHQKLEENIDLIK 1067
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
228-470 |
6.14e-05 |
|
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: 47.16 E-value: 6.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 228 VEELQELLEKQNFelSQARERLVTLTATVTELEEDLGTARR---DLIKSEELSSKHQRDLREalaqkedmeeRITTLEKR 304
Cdd:pfam06160 69 LFEAEELNDKYRF--KKAKKALDEIEELLDDIEEDIKQILEeldELLESEEKNREEVEELKD----------KYRELRKT 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 305 YLAaQREA--TSIhdlnDKLENELANKESLHRQCEE--------KARHLQELLEVAEQKLQQTMRK--------AETLPE 366
Cdd:pfam06160 137 LLA-NRFSygPAI----DELEKQLAEIEEEFSQFEEltesgdylEAREVLEKLEEETDALEELMEDipplyeelKTELPD 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 367 VEAELAQRIAALTKAEER--HGNIEEHLRQLEGQLEE-----KNQELARVrqrEKMNEDHNKRLSDTVDRLLSESNERLQ 439
Cdd:pfam06160 212 QLEELKEGYREMEEEGYAleHLNVDKEIQQLEEQLEEnlallENLELDEA---EEALEEIEERIDQLYDLLEKEVDAKKY 288
|
250 260 270
....*....|....*....|....*....|.
gi 966922630 440 LHlkermaalEEKGRLSEEIEKLRQEVDQLK 470
Cdd:pfam06160 289 VE--------KNLPEIEDYLEHAEEQNKELK 311
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
31-468 |
6.21e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.20 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 31 VNMLDEREKLLESLRESQETLAATQSRLQDALHERDQLQ-------------RHLNSALPQEFATLTRELSMCREQLLER 97
Cdd:PRK01156 321 INKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEgyemdynsylksiESLKKKIEEYSKNIERMSAFISEILKIQ 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 98 EEEISELKAERNNTRLLLEHLECLVSRHERSLRmtvvkrqaqspSGVSSEVEVLKALKSLFEHHKAL-------DEKVRE 170
Cdd:PRK01156 401 EIDPDAIKKELNEINVKLQDISSKVSSLNQRIR-----------ALRENLDELSRNMEMLNGQSVCPvcgttlgEEKSNH 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 171 RLRAALERVTTLEEQLAGAHQQVSALQqgagvldgaaEEEGTVELGPKRLWKEDAGRVEELQELLEKQNFELSQARERLV 250
Cdd:PRK01156 470 IINHYNEKKSRLEEKIREIEIEVKDID----------EKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKIN 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 251 TLTATVTELE-----------EDLGTARRDLIKSeeLSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLN 319
Cdd:PRK01156 540 ELKDKHDKYEeiknrykslklEDLDSKRTSWLNA--LAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYI 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 320 D----KLENELANKESLHRQCEEKARHLQELLEvaeqklqqtmrKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQL 395
Cdd:PRK01156 618 DksirEIENEANNLNNKYNEIQENKILIEKLRG-----------KIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKS 686
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966922630 396 EGQLEEKNQELARVRQREKMNEDHNKRLSDTVdrllSESNERLQlHLKERMAALEEKGRLSEEIEK------LRQEVDQ 468
Cdd:PRK01156 687 RKALDDAKANRARLESTIEILRTRINELSDRI----NDINETLE-SMKKIKKAIGDLKRLREAFDKsgvpamIRKSASQ 760
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
160-412 |
6.23e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.99 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 160 HHKALD-----EKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVLDGAAEEEGTVELGPkrlwkedagrvEELQEL 234
Cdd:COG0497 143 QRELLDafaglEELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAAALQP-----------GEEEEL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 235 LEKQNfELSQARERLVTLTATVTELEED-------LGTARRDLIK----SEELSSKHQRdLREALAQKEDMeerittlek 303
Cdd:COG0497 212 EEERR-RLSNAEKLREALQEALEALSGGeggaldlLGQALRALERlaeyDPSLAELAER-LESALIELEEA--------- 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 304 rylaaqreATSIHDLNDKLENElankeslhrqceekarhlQELLEVAEQKLQ---QTMRK----AETLPEVEAELAQRIA 376
Cdd:COG0497 281 --------ASELRRYLDSLEFD------------------PERLEEVEERLAllrRLARKygvtVEELLAYAEELRAELA 334
|
250 260 270
....*....|....*....|....*....|....*.
gi 966922630 377 ALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQR 412
Cdd:COG0497 335 ELENSDERLEELEAELAEAEAELLEAAEKLSAARKK 370
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
226-472 |
9.40e-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: 46.89 E-value: 9.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 226 GRVEELQELLEKQNFELS-------QARERLVTLTATV--TELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEE 296
Cdd:pfam02463 116 VTKKEVAELLESQGISPEaynflvqGGKIEIIAMMKPErrLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEEL 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 297 RIT--TLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTmrkaetLPEVEAELAQR 374
Cdd:pfam02463 196 KLQelKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQ------EIEKEEEKLAQ 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 375 IAALTKAEER-HGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDhNKRLSDTVDRLLSESNERLQLHLKERMAALEEKG 453
Cdd:pfam02463 270 VLKENKEEEKeKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE-KLKESEKEKKKAEKELKKEKEEIEELEKELKELE 348
|
250
....*....|....*....
gi 966922630 454 RLSEEIEKLRQEVDQLKGR 472
Cdd:pfam02463 349 IKREAEEEEEEELEKLQEK 367
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
172-360 |
1.09e-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: 44.51 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 172 LRAALERVTTLEEQLAGAHQQVSALQQGAGVLdgaaeeegtvelgpKRLWKEDA---GRVE----ELQELLEKQNFELSQ 244
Cdd:pfam15619 6 LSARLHKIKELQNELAELQSKLEELRKENRLL--------------KRLQKRQEkalGKYEgtesELPQLIARHNEEVRV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 245 ARERLVTLTATVTELEEDLGTARRDLIKSEElSSKHQRDLREA--LAQKEDMEERITTLEKRYLAAQREatsIHDLNDKL 322
Cdd:pfam15619 72 LRERLRRLQEKERDLERKLKEKEAELLRLRD-QLKRLEKLSEDknLAEREELQKKLEQLEAKLEDKDEK---IQDLERKL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 966922630 323 EN-------ELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRK 360
Cdd:pfam15619 148 ELenksfrrQLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKERE 192
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
166-469 |
1.16e-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: 46.71 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 166 EKVRERLRAALERVTT-LEEQL--AGAHQQV-SALQQGAGVLDGAAEEEGTV-ELGPKRLWKEDAGRVEELQELLEkqnf 240
Cdd:pfam01576 291 EKQRRDLGEELEALKTeLEDTLdtTAAQQELrSKREQEVTELKKALEEETRShEAQLQEMRQKHTQALEELTEQLE---- 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 241 elsQARERLVTLTATVTELEEDlgtaRRDLikSEELSSKHQRDLrEALAQKEDMEERITTLEKRYLAAQREATSIHDLND 320
Cdd:pfam01576 367 ---QAKRNKANLEKAKQALESE----NAEL--QAELRTLQQAKQ-DSEHKRKKLEGQLQELQARLSESERQRAELAEKLS 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 321 KLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMrkaETLPEveaELAQRIAALTKAEErhgnIEEHLRQLEGQLE 400
Cdd:pfam01576 437 KLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQ---ELLQE---ETRQKLNLSTRLRQ----LEDERNSLQEQLE 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 401 EknqELARVRQREKMNEDHNKRLSDTVDRL---------LSESNERLQLHLKERMAALEEKGRLSEEIEK----LRQEVD 467
Cdd:pfam01576 507 E---EEEAKRNVERQLSTLQAQLSDMKKKLeedagtleaLEEGKKRLQRELEALTQQLEEKAAAYDKLEKtknrLQQELD 583
|
..
gi 966922630 468 QL 469
Cdd:pfam01576 584 DL 585
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
313-423 |
1.19e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.36 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 313 TSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAEL---AQRIA--ALTKAEERHGN 387
Cdd:PRK00409 509 KLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLleeAEKEAqqAIKEAKKEADE 588
|
90 100 110
....*....|....*....|....*....|....*....
gi 966922630 388 IEEHLRQLE--GQLEEKNQELARVRQR-EKMNEDHNKRL 423
Cdd:PRK00409 589 IIKELRQLQkgGYASVKAHELIEARKRlNKANEKKEKKK 627
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
301-472 |
1.40e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 301 LEKRYLAAQREATSIHDLNDKLE-NELANKESLHRQCEEKARHLQELlevaEQKLQQTMRKAETLPEVEAELAQRIAALT 379
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNlKELKELEEELKEAEEKEEEYAEL----QEELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 380 KAEERHGNIEEhLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEI 459
Cdd:COG4717 123 KLLQLLPLYQE-LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
170
....*....|...
gi 966922630 460 EKLRQEVDQLKGR 472
Cdd:COG4717 202 EELQQRLAELEEE 214
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
151-465 |
1.56e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.12 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 151 LKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVLDGAAEEEGTVElgpkRLWKEDAGRVEE 230
Cdd:TIGR00618 196 AELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQ----QLLKQLRARIEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 231 LQEL---LEKQNFELSQAR--ERLVTLTATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKry 305
Cdd:TIGR00618 272 LRAQeavLEETQERINRARkaAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQT-- 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 306 laAQREATSIHDLNDKLENELANKESLHRQcEEKARHLQELLEVAEQKLQQTMRKAETLPE----VEAELAQRIAALTKA 381
Cdd:TIGR00618 350 --LHSQEIHIRDAHEVATSIREISCQQHTL-TQHIHTLQQQKTTLTQKLQSLCKELDILQReqatIDTRTSAFRDLQGQL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 382 EERHGNIEEHLRqlegQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKErmaalEEKGRLSEEIEK 461
Cdd:TIGR00618 427 AHAKKQQELQQR----YAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQE-----TRKKAVVLARLL 497
|
....
gi 966922630 462 LRQE 465
Cdd:TIGR00618 498 ELQE 501
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
227-472 |
1.91e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.58 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 227 RVEELQELLEKQNFELSQARERLVTL--------TATVTeLEEDLGTARRDLiksEELSSKHQRDLREALAQKEDMEERI 298
Cdd:pfam10174 402 KIENLQEQLRDKDKQLAGLKERVKSLqtdssntdTALTT-LEEALSEKERII---ERLKEQREREDRERLEELESLKKEN 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 299 TTLEKRYLAAQREAT----SIHDLNDK---LENELANKESLHRQCE---EKARHLQELLEVAEQKLQQTMRKAETLPEV- 367
Cdd:pfam10174 478 KDLKEKVSALQPELTekesSLIDLKEHassLASSGLKKDSKLKSLEiavEQKKEECSKLENQLKKAHNAEEAVRTNPEIn 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 368 ------EAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELA-----RVRQ-REKMNEDHNKRLSDTVDRllSESN 435
Cdd:pfam10174 558 drirllEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAeleslTLRQmKEQNKKVANIKHGQQEMK--KKGA 635
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 966922630 436 ERLQLHLKERMAA--------LEEkgrLSEEIEKLRQEVDQLKGR 472
Cdd:pfam10174 636 QLLEEARRREDNLadnsqqlqLEE---LMGALEKTRQELDATKAR 677
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
149-470 |
2.36e-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: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 149 EVLKALKSLFEHHKALDEKVRERLR------AALERVTTLEEQLAGAHQQVSALQQGAGVLDGAAEEEGTVELGPKR--- 219
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKkqqllkQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAqri 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 220 ---LWKEDAGRVEELQEL--LEKQNFELSQARERLVTLTATVTELEE--DLGTARRDlIKSEELSSKHQrdLREALAQKE 292
Cdd:TIGR00618 313 hteLQSKMRSRAKLLMKRaaHVKQQSSIEEQRRLLQTLHSQEIHIRDahEVATSIRE-ISCQQHTLTQH--IHTLQQQKT 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 293 DMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQ-QTMRKAE------TLP 365
Cdd:TIGR00618 390 TLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQcEKLEKIHlqesaqSLK 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 366 EVEAELAQRiAALTKAEERHGNIEEHL--------RQLEGQLEEKNQEL----------ARVRQREKMNEDHNKRLSDTV 427
Cdd:TIGR00618 470 EREQQLQTK-EQIHLQETRKKAVVLARllelqeepCPLCGSCIHPNPARqdidnpgpltRRMQRGEQTYAQLETSEEDVY 548
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 966922630 428 DRLLSESNERLQLHLKERMAALEEKG------RLSEEIEKLRQEVDQLK 470
Cdd:TIGR00618 549 HQLTSERKQRASLKEQMQEIQQSFSIltqcdnRSKEDIPNLQNITVRLQ 597
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
281-470 |
3.22e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 44.68 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 281 QRDLREALAQKEDMEERITTLekRYLAAQREATSIHDLND-KLENE---LANKESLHRQCEEKARHLQELLEVAEQKLQQ 356
Cdd:COG0497 171 KKELEELRADEAERARELDLL--RFQLEELEAAALQPGEEeELEEErrrLSNAEKLREALQEALEALSGGEGGALDLLGQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 357 TMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQRekMNEDHN--KRLSDTVDRLLSes 434
Cdd:COG0497 249 ALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEER--LALLRRlaRKYGVTVEELLA-- 324
|
170 180 190
....*....|....*....|....*....|....*.
gi 966922630 435 nerLQLHLKERMAALEEkgrLSEEIEKLRQEVDQLK 470
Cdd:COG0497 325 ---YAEELRAELAELEN---SDERLEELEAELAEAE 354
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
258-470 |
3.32e-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: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 258 ELEEDLGTARRDLI-KSEELSSKHQRDLREALAQkeDMEERITTLE-------KRYLAAQREATSIHDLNDK-------- 321
Cdd:cd16269 94 KLMEQLEEKKEEFCkQNEEASSKRCQALLQELSA--PLEEKISQGSysvpggyQLYLEDREKLVEKYRQVPRkgvkaeev 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 322 LENELANKESLHR-------QCEEKARHLqellEVAEQKLQQTMRKAETLPEVEAELAQRIaaltKAEERhgNIEEHLRQ 394
Cdd:cd16269 172 LQEFLQSKEAEAEailqadqALTEKEKEI----EAERAKAEAAEQERKLLEEQQRELEQKL----EDQER--SYEEHLRQ 241
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966922630 395 LEGQLEEKNQelarvrqrekmnedhnkrlsdtvdRLLSESNERLQLHLKErMAALEEKGrLSEEIEKLRQEVDQLK 470
Cdd:cd16269 242 LKEKMEEERE------------------------NLLKEQERALESKLKE-QEALLEEG-FKEQAELLQEEIRSLK 291
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
283-470 |
3.89e-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: 44.68 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 283 DLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMR--- 359
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRlet 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 360 -------KAETLPEVEAELAQRIAALTKAEE------------RHGNieEHLRQLEGQLE---EKNQELARVRQREKMNE 417
Cdd:pfam05622 81 arddyriKCEELEKEVLELQHRNEELTSLAEeaqalkdemdilRESS--DKVKKLEATVEtykKKLEDLGDLRRQVKLLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 418 DHN----------------------------KRLSDTVDRLLSESN--ERLQL---HLKERMAALE-EKGRLSEEIEKLR 463
Cdd:pfam05622 159 ERNaeymqrtlqleeelkkanalrgqletykRQVQELHGKLSEESKkaDKLEFeykKLEEKLEALQkEKERLIIERDTLR 238
|
....*..
gi 966922630 464 QEVDQLK 470
Cdd:pfam05622 239 ETNEELR 245
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
34-430 |
4.31e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 34 LDEREKLLESLRESQETLAATQSRLQDALHERDQLQ------RHLNSALPQEFATLTRELSMCREQLLEREEEISELKAE 107
Cdd:TIGR00618 506 LCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLEtseedvYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKED 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 108 RNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgVSSEVEVLKALKSLFEHHKAldekvrERLRAALERVTTLEEQLA 187
Cdd:TIGR00618 586 IPNLQNITVRLQDLTEKLSEAEDMLACEQHALL---RKLQPEQDLQDVRLHLQQCS------QELALKLTALHALQLTLT 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 188 GAHQQVSALqqgagvldgaaeeegTVELGPKRLWKEDAGRVEELQELLEkqnfELSQARERLVTLTATVTELEEDLGTAR 267
Cdd:TIGR00618 657 QERVREHAL---------------SIRVLPKELLASRQLALQKMQSEKE----QLTYWKEMLAQCQTLLRELETHIEEYD 717
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 268 RDLIKSEELSSKHQRDLR---EALAQ--KEDMEERITTLEKRYLAAQR---EATSIHDLNDKLENELANKESLHRQCEEK 339
Cdd:TIGR00618 718 REFNEIENASSSLGSDLAareDALNQslKELMHQARTVLKARTEAHFNnneEVTAALQTGAELSHLAAEIQFFNRLREED 797
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 340 ARHLQELLEVAEQKLQQTmrKAETLPEVEAELAQRIAALTKAEERHGNIEEhLRQLEGQLEEKNQELARVRQREKmnedh 419
Cdd:TIGR00618 798 THLLKTLEAEIGQEIPSD--EDILNLQCETLVQEEEQFLSRLEEKSATLGE-ITHQLLKYEECSKQLAQLTQEQA----- 869
|
410
....*....|.
gi 966922630 420 nkRLSDTVDRL 430
Cdd:TIGR00618 870 --KIIQLSDKL 878
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
31-374 |
4.32e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 31 VNMLDEREKLLESLRESQETLAATQSRLQDALHERDQLQrhlnsalpqefatltrelsmcreqllEREEEISELKAERNN 110
Cdd:PRK02224 467 VETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLV--------------------------EAEDRIERLEERRED 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 111 -TRLLLEHLECLvsrHERSLRMTVVKRQAQspsgvssevevlkALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGA 189
Cdd:PRK02224 521 lEELIAERRETI---EEKRERAEELRERAA-------------ELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAEL 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 190 HQQVSALQQGAGVLDGAAEEEgtvelgpkrlwkedaGRVEELQELLEKQNFELSQARERLVTLTATVTELEEDLGTARrd 269
Cdd:PRK02224 585 KERIESLERIRTLLAAIADAE---------------DEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEAR-- 647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 270 likSEELSSKHQRdlreALAQKEDMEERITTLEKRYLAAQREATSIhdlndklENELANKESL---HRQCEEKARHLQEL 346
Cdd:PRK02224 648 ---IEEAREDKER----AEEYLEQVEEKLDELREERDDLQAEIGAV-------ENELEELEELrerREALENRVEALEAL 713
|
330 340
....*....|....*....|....*...
gi 966922630 347 LEVAEQkLQQTMRkaetlpEVEAELAQR 374
Cdd:PRK02224 714 YDEAEE-LESMYG------DLRAELRQR 734
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
286-411 |
4.88e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.52 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 286 EALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLEnELANKEslhrQCEEKARHLQELLEVAEQKLQQTMRKAETLP 365
Cdd:PRK11281 33 GDLPTEADVQAQLDALNKQKLLEAEDKLVQQDLEQTLA-LLDKID----RQKEETEQLKQQLAQAPAKLRQAQAELEALK 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 966922630 366 EVEA-ELAQRIAALTkaeerhgnieehLRQLEGQLEEKNQELARVRQ 411
Cdd:PRK11281 108 DDNDeETRETLSTLS------------LRQLESRLAQTLDQLQNAQN 142
|
|
| DUF4472 |
pfam14739 |
Domain of unknown function (DUF4472); This family is specific to the Chordates. Some members ... |
231-326 |
5.29e-04 |
|
Domain of unknown function (DUF4472); This family is specific to the Chordates. Some members also carry Kinesin-motor domains at their N-terminus, Kinesin, pfam00225.
Pssm-ID: 464291 [Multi-domain] Cd Length: 107 Bit Score: 40.75 E-value: 5.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 231 LQELLEKQNFELSQareRLVTLTATVTELEEDLGTARRdlikseELSSKHQRdLREALAQKEDMEERITTLEKRYLAAQR 310
Cdd:pfam14739 22 LREQYEAEKFELKN---KLLNLENRVLELELRLEKAAE------EIQDLRER-LRELEDDRRELAEEFVALKKNYQALSK 91
|
90
....*....|....*.
gi 966922630 311 EATSIHDLNDKLENEL 326
Cdd:pfam14739 92 ELEAEVAKNQELSLEL 107
|
|
| SAM_STIM-1,2-like |
cd09504 |
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ... |
831-889 |
6.28e-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: 39.62 E-value: 6.28e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966922630 831 WDGPTVVSWLELWVGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNALHRLKLRL 889
Cdd:cd09504 5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
247-406 |
8.74e-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: 41.48 E-value: 8.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 247 ERLVTLTATVTELEEDLGTARRDLIkseELSSKHQRDLREALAQK-EDMEERITTlekrYLAAQRE--ATSIHDLNDKLE 323
Cdd:pfam01442 4 DSLDELSTYAEELQEQLGPVAQELV---DRLEKETEALRERLQKDlEEVRAKLEP----YLEELQAklGQNVEELRQRLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 324 NELankESLHRQCEEKARHLQELLEVAEQKLQQTMRK---------AETLPEVEAELAQRIAAL-----TKAEERHGNIE 389
Cdd:pfam01442 77 PYT---EELRKRLNADAEELQEKLAPYGEELRERLEQnvdalrarlAPYAEELRQKLAERLEELkeslaPYAEEVQAQLS 153
|
170
....*....|....*..
gi 966922630 390 EHLRQLEGQLEEKNQEL 406
Cdd:pfam01442 154 QRLQELREKLEPQAEDL 170
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
228-470 |
9.24e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.59 E-value: 9.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 228 VEELQELLEKQNFELSQARERLVTLTATVTELEEdlgtARRDLI-KSEELSSKhqrdLREALAQKEDMEERITTLEKRYL 306
Cdd:COG1340 10 LEELEEKIEELREEIEELKEKRDELNEELKELAE----KRDELNaQVKELREE----AQELREKRDELNEKVKELKEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 307 AAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELlevaeQKLQQTMrkaETLPEVEAELAQRIAALTK-AEERh 385
Cdd:COG1340 82 ELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERL-----EWRQQTE---VLSPEEEKELVEKIKELEKeLEKA- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 386 gnieEHLRQLEGQLEEKNQELARVRQREkmnEDHNKRLSDTVDRLLSESNERLQLhLKERMAALEEKGRLSEEIEKLRQE 465
Cdd:COG1340 153 ----KKALEKNEKLKELRAELKELRKEA---EEIHKKIKELAEEAQELHEEMIEL-YKEADELRKEADELHKEIVEAQEK 224
|
....*
gi 966922630 466 VDQLK 470
Cdd:COG1340 225 ADELH 229
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
164-472 |
1.02e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.63 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 164 LDEKVRERLRAALERVTT------LEEQLAGAHQQVSALQQGAGVL--------DGAAEEEGTVELGPK----------- 218
Cdd:pfam01576 112 LDEEEAARQKLQLEKVTTeakikkLEEDILLLEDQNSKLSKERKLLeeriseftSNLAEEEEKAKSLSKlknkheamisd 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 219 ---RLWKEDAGRvEELQELLEKQNFELSQARERLVTLTATVTELeedlgtaRRDLIKSEElsskhqrDLREALAQKEDME 295
Cdd:pfam01576 192 leeRLKKEEKGR-QELEKAKRKLEGESTDLQEQIAELQAQIAEL-------RAQLAKKEE-------ELQAALARLEEET 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 296 ERITTLEKRYlaaqREATS-IHDLNDKLENELANKESLHRQCeekaRHLQELLEVAEQKLQQTMRKAETLPEVEAELAQR 374
Cdd:pfam01576 257 AQKNNALKKI----RELEAqISELQEDLESERAARNKAEKQR----RDLGEELEALKTELEDTLDTTAAQQELRSKREQE 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 375 IAALTKAEERHGNIEE----HLRQLEGQ-LEEKNQELARVRqREKMNEDHNKRlsdtvdRLLSESNErLQLHLKERMAAl 449
Cdd:pfam01576 329 VTELKKALEEETRSHEaqlqEMRQKHTQaLEELTEQLEQAK-RNKANLEKAKQ------ALESENAE-LQAELRTLQQA- 399
|
330 340
....*....|....*....|...
gi 966922630 450 eeKGRLSEEIEKLRQEVDQLKGR 472
Cdd:pfam01576 400 --KQDSEHKRKKLEGQLQELQAR 420
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
367-470 |
1.02e-03 |
|
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: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 367 VEAELAQRIAALTKAEERHGNIEEHlrQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLlSESNERLQLHLKERM 446
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKE--HEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEK-DERIERLERELSEAR 454
|
90 100
....*....|....*....|....
gi 966922630 447 AALEEKGRLSEEIEKLRQEVDQLK 470
Cdd:COG2433 455 SEERREIRKDREISRLDREIERLE 478
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
166-423 |
1.08e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 166 EKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVLDGAAEEEGTveLGPKRLwkedAGRVEELQELLEkqnfELSQA 245
Cdd:PRK04863 840 RQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNL--LADETL----ADRVEEIREQLD----EAEEA 909
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 246 RERLVTLTATVTELEEDLGTARRDLIKSEELsskhQRDLREALAQKEDMEERITTL----EKR----YLAAQREATSIHD 317
Cdd:PRK04863 910 KRFVQQHGNALAQLEPIVSVLQSDPEQFEQL----KQDYQQAQQTQRDAKQQAFALtevvQRRahfsYEDAAEMLAKNSD 985
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 318 LNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALT---------KAEERHGNI 388
Cdd:PRK04863 986 LNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGvpadsgaeeRARARRDEL 1065
|
250 260 270
....*....|....*....|....*....|....*.
gi 966922630 389 EEHLRQLEGQleeKNQ-ELARVRQREKMNEdHNKRL 423
Cdd:PRK04863 1066 HARLSANRSR---RNQlEKQLTFCEAEMDN-LTKKL 1097
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
159-472 |
1.17e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 159 EHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQgagvldgaAEEEGTVELGPKrlwKEDAGRVEELQELLE-- 236
Cdd:PTZ00121 1168 EARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARK--------AEEERKAEEARK---AEDAKKAEAVKKAEEak 1236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 237 KQNFELSQA-RERLVTLTATVTELEEDLGTARRDLIKSEElsSKHQRDLREALAQKEDMEERITTLEKRYLAAQR---EA 312
Cdd:PTZ00121 1237 KDAEEAKKAeEERNNEEIRKFEEARMAHFARRQAAIKAEE--ARKADELKKAEEKKKADEAKKAEEKKKADEAKKkaeEA 1314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 313 TSIHDLNDKLENELANKESLHRQCEE-----------------KARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRI 375
Cdd:PTZ00121 1315 KKADEAKKKAEEAKKKADAAKKKAEEakkaaeaakaeaeaaadEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAD 1394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 376 AALTKAEERHGNIEEHLRQLEgqlEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRL 455
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKKAAA---AKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
330 340
....*....|....*....|
gi 966922630 456 SEEIEKLRQE---VDQLKGR 472
Cdd:PTZ00121 1472 ADEAKKKAEEakkADEAKKK 1491
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
22-340 |
1.23e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.97 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 22 ADANFEQLMvNMLDEREKllESLRESQETLAATQsRLQDALHERDQLQRHLNsalpqefaTLTRELSmcreqllEREEEI 101
Cdd:PLN02939 126 SDFQLEDLV-GMIQNAEK--NILLLNQARLQALE-DLEKILTEKEALQGKIN--------ILEMRLS-------ETDARI 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 102 SELKAERNNTRLLLEHLEclvsrherSLRMTVVKRQAQSPSGVSSEVEVLKALKslfEHHKALDEKVrERLRAALERVTT 181
Cdd:PLN02939 187 KLAAQEKIHVEILEEQLE--------KLRNELLIRGATEGLCVHSLSKELDVLK---EENMLLKDDI-QFLKAELIEVAE 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 182 LEEQLAGAHQQVSALQQGAGVLDG--AAEEEGTVELGPKR---LWKedagRVEELQELLEKQNFELSQArerlvtltATV 256
Cdd:PLN02939 255 TEERVFKLEKERSLLDASLRELESkfIVAQEDVSKLSPLQydcWWE----KVENLQDLLDRATNQVEKA--------ALV 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 257 TELEEDLgtarRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQRE--------ATSIHDLNDKLENelAN 328
Cdd:PLN02939 323 LDQNQDL----RDKVDKLEASLKEANVSKFSSYKVELLQQKLKLLEERLQASDHEihsyiqlyQESIKEFQDTLSK--LK 396
|
330
....*....|..
gi 966922630 329 KESLHRQCEEKA 340
Cdd:PLN02939 397 EESKKRSLEHPA 408
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
178-472 |
1.25e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.96 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 178 RVTTLEEQLAGAHQQVSALQQGAGVLDGAAEEEGTVELGPKRLWKedaGRVEELQELLEKQNFELSQARERLVTLTATVT 257
Cdd:pfam07888 28 RAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWE---RQRRELESRVAELKEELRQSREKHEELEEKYK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 258 ELEEDLGTARRDLIKSEELSSKHQRDLREalaqkedMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQce 337
Cdd:pfam07888 105 ELSASSEELSEEKDALLAQRAAHEARIRE-------LEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQ-- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 338 ekarhLQELLEVAEQKLQqtmRKAETLPEVEAELAQRIAaltkaeerhgnieeHLRQLEGQLEEKNQELARVRQREKMNE 417
Cdd:pfam07888 176 -----LQAKLQQTEEELR---SLSKEFQELRNSLAQRDT--------------QVLQLQDTITTLTQKLTTAHRKEAENE 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 966922630 418 DHNKRLSDTVDRLlsESNERLQLHLKERMAAL-EEKGRLSEEIEKLRQEVDQLKGR 472
Cdd:pfam07888 234 ALLEELRSLQERL--NASERKVEGLGEELSSMaAQRDRTQAELHQARLQAAQLTLQ 287
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
320-470 |
1.54e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 320 DKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAetlpeveAELAQRIAALtkaEERHGNIEEHLRQLEGQL 399
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI-------RALEQELAAL---EAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 400 EEKNQELA-RVRQREKMNED-------HNKRLSDTVDRL--LSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQL 469
Cdd:COG4942 100 EAQKEELAeLLRALYRLGRQpplalllSPEDFLDAVRRLqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
.
gi 966922630 470 K 470
Cdd:COG4942 180 L 180
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
218-465 |
1.55e-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: 42.70 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 218 KRLWKEDAGRVEELQ---ELLEKQNFELSQARERLvtlTATVTELEEDlgtarrdlIKSEELSSKHQRDLREALaqkedm 294
Cdd:TIGR04523 404 EKLNQQKDEQIKKLQqekELLEKEIERLKETIIKN---NSEIKDLTNQ--------DSVKELIIKNLDNTRESL------ 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 295 EERITTLEKRYLAAQREAtsihdlnDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLpevEAELAQR 374
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNL-------EQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKL---ESEKKEK 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 375 IAALTKAEERHGNIEEHLR--QLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNErlqlhLKERMAALEEK 452
Cdd:TIGR04523 537 ESKISDLEDELNKDDFELKkeNLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKD-----LIKEIEEKEKK 611
|
250
....*....|....
gi 966922630 453 -GRLSEEIEKLRQE 465
Cdd:TIGR04523 612 iSSLEKELEKAKKE 625
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
830-894 |
1.56e-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: 1.56e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966922630 830 QWDGPTVVSWLElWVGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNALHRLKLRLAIQEM 894
Cdd:pfam00536 2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
119-467 |
1.66e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.57 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 119 ECLVSRHErslrmtVVKRQAQSPSGVSSEVEVLKALKSLFEH-HKALDEKV---RERLRAALERVTTLEEQLAGAHQQVS 194
Cdd:pfam07888 38 ECLQERAE------LLQAQEAANRQREKEKERYKRDREQWERqRRELESRVaelKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 195 ALQQGAGVLDGAAEEEgtvelgpKRLWKEDAGRVEELQELLEKQNFELSQARERLVTLTATVTELEEDLGTARRDLIKSE 274
Cdd:pfam07888 112 ELSEEKDALLAQRAAH-------EARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 275 ELS---SKHQRDLREALAQKED----MEERITTLEKRYLAAQREATSIHDLNDKLEN--ELAN---------KESLHRQC 336
Cdd:pfam07888 185 EELrslSKEFQELRNSLAQRDTqvlqLQDTITTLTQKLTTAHRKEAENEALLEELRSlqERLNaserkveglGEELSSMA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 337 EEKARHLQELLEVAEQKLQQTMRKAET---LPEVEAELAQ-RIAALTKAEERHGNIEE---HLRQLEGQLEEKNQELARV 409
Cdd:pfam07888 265 AQRDRTQAELHQARLQAAQLTLQLADAslaLREGRARWAQeRETLQQSAEADKDRIEKlsaELQRLEERLQEERMEREKL 344
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 966922630 410 RQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVD 467
Cdd:pfam07888 345 EVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLE 402
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
272-383 |
1.73e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 272 KSEELSSKHQRDLREALAQKEDMEERittLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAE 351
Cdd:PRK12704 65 EIHKLRNEFEKELRERRNELQKLEKR---LLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQL 141
|
90 100 110
....*....|....*....|....*....|....*...
gi 966922630 352 QKLQQTMR------KAETLPEVEAELAQRIAALTKAEE 383
Cdd:PRK12704 142 QELERISGltaeeaKEILLEKVEEEARHEAAVLIKEIE 179
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
229-353 |
1.82e-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: 42.74 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 229 EELQEL-LEKQNFE--LSQARERLVTLTATVTELEEDLGTARRDLIKSEELSSKhqrdlreALAQKEDMEERITTLEKRY 305
Cdd:pfam05911 688 EEFEQLkSEKENLEveLASCTENLESTKSQLQESEQLIAELRSELASLKESNSL-------AETQLKCMAESYEDLETRL 760
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 966922630 306 LAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQK 353
Cdd:pfam05911 761 TELEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQEQLERNEKK 808
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
953-1008 |
1.87e-03 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 38.02 E-value: 1.87e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 966922630 953 EWLPSLGLPQYRSYFMECLVD-ARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1008
Cdd:pfam07647 11 DWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLK-RLGITSVGHRRKILKKIQELK 66
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
27-303 |
2.40e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.35 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 27 EQLMVNMLDEREKLLESLRESQETLAATQSRLQDALHERDQLQRHLnSALPQEFATLTRELSMCREQLLEREEEISELKA 106
Cdd:TIGR02168 788 EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI-AATERRLEDLEEQIEELSEDIESLAAEIEELEE 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 107 ERNNTRLLLEHLECLVSRHERSLRmtvvkrqaqspsgvssevEVLKALKSLFEHHKALDEKVRErLRAALERvttLEEQL 186
Cdd:TIGR02168 867 LIEELESELEALLNERASLEEALA------------------LLRSELEELSEELRELESKRSE-LRRELEE---LREKL 924
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 187 AGAHQQVSALQQGAGVLDGAAEEEGTVELgpkrlwkedagrvEELQELLEKQNFELSQARERLVTLTATVTELeedlgtA 266
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQERLSEEYSLTL-------------EEAEALENKIEDDEEEARRRLKRLENKIKEL------G 985
|
250 260 270
....*....|....*....|....*....|....*..
gi 966922630 267 RRDLIKSEELSSKHQRdLREALAQKEDMEERITTLEK 303
Cdd:TIGR02168 986 PVNLAAIEEYEELKER-YDFLTAQKEDLTEAKETLEE 1021
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
135-470 |
2.40e-03 |
|
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: 42.05 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 135 KRQAQSPSGVSSEV-EVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVldGAAEEEgtV 213
Cdd:pfam09731 88 QVKIPRQSGVSSEVaEEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAI--QAVKAH--T 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 214 ELGPKRLWKEDAGRVEELQELLEKQNFELSQARERLVTLTATVTELEEDLGTARRDLIKSeelsSKHQRDLREALAQKED 293
Cdd:pfam09731 164 DSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPK----LPEHLDNVEEKVEKAQ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 294 MEERITTLEKRYLAA-----QREATSIH-DLNDKL-ENELANKESLHRQCEekarHLQELLEVAEQKLQqTMRKAETLpE 366
Cdd:pfam09731 240 SLAKLVDQYKELVASerivfQQELVSIFpDIIPVLkEDNLLSNDDLNSLIA----HAHREIDQLSKKLA-ELKKREEK-H 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 367 VEAELAQRIAALTKAEER-HGNIEEHLRQLEGQLEEKNQElARVRQREKM-----------NEDHNKRLSDTVDRLLSES 434
Cdd:pfam09731 314 IERALEKQKEELDKLAEElSARLEEVRAADEAQLRLEFER-EREEIRESYeeklrtelerqAEAHEEHLKDVLVEQEIEL 392
|
330 340 350
....*....|....*....|....*....|....*.
gi 966922630 435 NERLQLHLKERMAalEEKGRLSEEIEKLRQEVDQLK 470
Cdd:pfam09731 393 QREFLQDIKEKVE--EERAGRLLKLNELLANLKGLE 426
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
272-474 |
2.41e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 42.15 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 272 KSEELSSKHQRDLREALAQKEdMEERITTLEKRylAAQREATSIHDLNDKLenelanKESLHRQCEEKARHLQELLEVAE 351
Cdd:PLN03229 555 KAEKLKAEINKKFKEVMDRPE-IKEKMEALKAE--VASSGASSGDELDDDL------KEKVEKMKKEIELELAGVLKSMG 625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 352 QKLQQTMRKAETLPEVEA--ELAQRIAALTkaEERHGNIEEHLR--QLEGQLEEKNQELARVrqrekmnedhnkrlSDTV 427
Cdd:PLN03229 626 LEVIGVTKKNKDTAEQTPppNLQEKIESLN--EEINKKIERVIRssDLKSKIELLKLEVAKA--------------SKTP 689
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 966922630 428 DRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGRGG 474
Cdd:PLN03229 690 DVTEKEKIEALEQQIKQKIAEALNSSELKEKFEELEAELAAARETAA 736
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
257-471 |
2.54e-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: 42.08 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 257 TELEEDLGTARRDLIKSEELSSKHQRDLRE-ALAQKEDMEERITTLEK----------------RYLAAQREATSI-HDL 318
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKElEKKHQQLCEEKNALQEQlqaetelcaeaeemraRLAARKQELEEIlHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 319 NDKLENELANKESLHRQCEEKARHLQEL------LEVAEQKLQQTMRKAET-LPEVEAELAQRIAALTKAEERHGNIEEH 391
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLeeqldeEEAARQKLQLEKVTTEAkIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 392 LRQLEGQLEEknqELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLH-LKERMAAleEKGRLSEEIEKLRQEVDQLK 470
Cdd:pfam01576 161 ISEFTSNLAE---EEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEkAKRKLEG--ESTDLQEQIAELQAQIAELR 235
|
.
gi 966922630 471 G 471
Cdd:pfam01576 236 A 236
|
|
| SAM_Neurabin-like |
cd09512 |
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ... |
1031-1070 |
2.64e-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: 2.64e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 966922630 1031 VLVWTNDQVVHWVQSIGLRDYAGNLHESGVHG-ALLALDEN 1070
Cdd:cd09512 4 VSEWSVQQVCQWLMGLGLEQYIPEFTANNIDGqQLLQLDSS 44
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
231-466 |
3.88e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.19 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 231 LQELLEKQNFELSQARERLVTLTATVTELEEDLGTARRDLIKSEE----LSSKHQRDL-REALAQKEDMEERITTLEKry 305
Cdd:COG1842 28 LDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEkarlALEKGREDLaREALERKAELEAQAEALEA-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 306 laaqreatsihdlndklenelankesLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLpeveaeLAQRIAAltKAEERh 385
Cdd:COG1842 106 --------------------------QLAQLEEQVEKLKEALRQLESKLEELKAKKDTL------KARAKAA--KAQEK- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 386 gnIEEHLRQLEGqlEEKNQELARVRQREKMNEDhnkrLSDTVDRLLSESNerlqlhLKERMAALEEKGRLSEEIEKLRQE 465
Cdd:COG1842 151 --VNEALSGIDS--DDATSALERMEEKIEEMEA----RAEAAAELAAGDS------LDDELAELEADSEVEDELAALKAK 216
|
.
gi 966922630 466 V 466
Cdd:COG1842 217 M 217
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
218-470 |
4.05e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.54 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 218 KRLWKEDAGRVEELQELLEKQNFELSQARERLVTLTATVTELEEDLgtarrDLIKSEELSSKHQR-DLREALAQKEDMEE 296
Cdd:TIGR04523 137 KKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEK-----LNIQKNIDKIKNKLlKLELLLSNLKKKIQ 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 297 RITTLEKRYLAAQREATSIHDLNDKLENELANKeslhrqceekarhlQELLEVAEQKLQQTMrkaETLPEVEAELAQRIA 376
Cdd:TIGR04523 212 KNKSLESQISELKKQNNQLKDNIEKKQQEINEK--------------TTEISNTQTQLNQLK---DEQNKIKKQLSEKQK 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 377 ALTKAEERHGNIEEHLRQLEGQLE----EKNQELAR-----VRQREKMNEDHNKRLSDTvDRLLSESNERLQLHLKERMA 447
Cdd:TIGR04523 275 ELEQNNKKIKELEKQLNQLKSEISdlnnQKEQDWNKelkseLKNQEKKLEEIQNQISQN-NKIISQLNEQISQLKKELTN 353
|
250 260
....*....|....*....|...
gi 966922630 448 ALEEKGRLSEEIEKLRQEVDQLK 470
Cdd:TIGR04523 354 SESENSEKQRELEEKQNEIEKLK 376
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
40-471 |
4.63e-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: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 40 LLESLRESQETLAATQSRLQdALHERDQLQRHLNSALPQEFATLTRELSMCREQLLEREEEISELKAERNNT-------R 112
Cdd:pfam10174 58 LKEQYRVTQEENQHLQLTIQ-ALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQakelfllR 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 113 LLLEHLECLVSRHERSL--RMTVVKR-----QAQS-PSGVSSEVEVLKALKSLFEHHKA-----LDEKVRE--RLRAALE 177
Cdd:pfam10174 137 KTLEEMELRIETQKQTLgaRDESIKKllemlQSKGlPKKSGEEDWERTRRIAEAEMQLGhlevlLDQKEKEniHLREELH 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 178 RvttlEEQLAGAHQQVSALQQgagVLDGAAEEEGTVELGPKRLwkedagrvEELQELLeKQNFELS--QARERLVTLTAT 255
Cdd:pfam10174 217 R----RNQLQPDPAKTKALQT---VIEMKDTKISSLERNIRDL--------EDEVQML-KTNGLLHteDREEEIKQMEVY 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 256 VTE---LEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKES- 331
Cdd:pfam10174 281 KSHskfMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESf 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 332 -------LHRQCEEKA------RHLQELLEVAEQKLQQTMRKAETLPEV-------EAELAQRIAALtkaEERHGNIEEH 391
Cdd:pfam10174 361 lnkktkqLQDLTEEKStlageiRDLKDMLDVKERKINVLQKKIENLQEQlrdkdkqLAGLKERVKSL---QTDSSNTDTA 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 392 LRQLEGQLEEKNQELARVRQ------REKMNE-----DHNKRLSDTVDRLLSESNERLQ--LHLKERMAALEEKG----- 453
Cdd:pfam10174 438 LTTLEEALSEKERIIERLKEqreredRERLEEleslkKENKDLKEKVSALQPELTEKESslIDLKEHASSLASSGlkkds 517
|
490 500
....*....|....*....|.
gi 966922630 454 ---RLSEEIEKLRQEVDQLKG 471
Cdd:pfam10174 518 klkSLEIAVEQKKEECSKLEN 538
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
273-410 |
4.70e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 273 SEELSSKHQR---------DLREALA----QKEDMEERITTLEKRYLAAQREatsihdlNDKLENELANKESLHRQCEEK 339
Cdd:PRK09039 45 SREISGKDSAldrlnsqiaELADLLSlerqGNQDLQDSVANLRASLSAAEAE-------RSRLQALLAELAGAGAAAEGR 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966922630 340 ARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAAL--------TKAEERHGNIEEHLRQLEGQLEEKNQELARVR 410
Cdd:PRK09039 118 AGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALeaaldaseKRDRESQAKIADLGRRLNVALAQRVQELNRYR 196
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
269-484 |
5.90e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 5.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 269 DLIKSE-ELSSKHQRDLREALAQkedmeeRITTLEKRYLAAQREATSIHDLNDKLENELANkesLHRQCEEKARHLQEL- 346
Cdd:PHA02562 191 DHIQQQiKTYNKNIEEQRKKNGE------NIARKQNKYDELVEEAKTIKAEIEELTDELLN---LVMDIEDPSAALNKLn 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 347 -------LEVAE-QKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNED 418
Cdd:PHA02562 262 taaakikSKIEQfQKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLE 341
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966922630 419 HNKRLSdTVDRLLS---ESNERLQLHLKErmaALEEKGRLSEEIEKLRQEVDQLKGRGGPFVDGVHSRS 484
Cdd:PHA02562 342 LKNKIS-TNKQSLItlvDKAKKVKAAIEE---LQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRG 406
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
343-470 |
6.44e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.61 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 343 LQELLEVAEQKLQQTMRKAETLPEVE-AELAQRIAALtkaEERHGNIEEHLRQLEGQLEEKNQELARVRQR---EKMNED 418
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERElTEEEEEIRRL---EEQVERLEAEVEELEAELEEKDERIERLERElseARSEER 458
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 966922630 419 HNKRLSDTVDRLLSEsNERLQLHLKErmaaleekgrLSEEIEKLRQEVDQLK 470
Cdd:COG2433 459 REIRKDREISRLDRE-IERLERELEE----------ERERIEELKRKLERLK 499
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
33-468 |
6.50e-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: 40.58 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 33 MLDEREKLLESLRESQETLAATQSRLQDALherDQLQRHLNsALPQEFATLTRELSMCREQLLEREEEISELKAERNNTR 112
Cdd:pfam10174 360 FLNKKTKQLQDLTEEKSTLAGEIRDLKDML---DVKERKIN-VLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTD 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 113 LLLEHLECLVSRHERslrmtvvkrqaqspsgvsseveVLKALKslfeHHKALDEKVRerlraaLERVTTLEEQLAGAHQQ 192
Cdd:pfam10174 436 TALTTLEEALSEKER----------------------IIERLK----EQREREDRER------LEELESLKKENKDLKEK 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 193 VSALQ-----QGAGVLDGAAEEEGTVELGPKRLWKEDA--GRVEELQELLEKQNFELSQARERLVTLTATvTELEEDLGT 265
Cdd:pfam10174 484 VSALQpelteKESSLIDLKEHASSLASSGLKKDSKLKSleIAVEQKKEECSKLENQLKKAHNAEEAVRTN-PEINDRIRL 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 266 ARRDLIKSEELSSKHQRD-------LREALAQKEDMEERITTLEKRYLAAQREATSihdlndklenELANKEslHRQCEE 338
Cdd:pfam10174 563 LEQEVARYKEESGKAQAEverllgiLREVENEKNDKDKKIAELESLTLRQMKEQNK----------KVANIK--HGQQEM 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 339 KARHLQELLEVAEQKlqqtmrKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQ--REKMN 416
Cdd:pfam10174 631 KKKGAQLLEEARRRE------DNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAerRKQLE 704
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 966922630 417 EdhnkRLSDTVDRLLSESNER------LQLHLKERMAALEEKGRLSEEIEKLRQEVDQ 468
Cdd:pfam10174 705 E----ILEMKQEALLAAISEKdanialLELSSSKKKKTQEEVMALKREKDRLVHQLKQ 758
|
|
| SAM_SARM1-like_repeat1 |
cd09501 |
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
953-997 |
7.07e-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: 36.51 E-value: 7.07e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 966922630 953 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHR 997
Cdd:cd09501 11 TWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLR 55
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
104-358 |
7.15e-03 |
|
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: 40.44 E-value: 7.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 104 LKAERNNTRLLLEHLECL-VSRHERSLRMTVVKRQAQSPSGVSSEV---EVLKALKSLFEHHKALDEK----VRERLRA- 174
Cdd:pfam05622 230 LIIERDTLRETNEELRCAqLQQAELSQADALLSPSSDPGDNLAAEImpaEIREKLIRLQHENKMLRLGqegsYRERLTEl 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 175 ------ALERVTTLEEQLAGAHQQVSALQQGAGVLDGAAEEEGTVELGPKRLWKEdagrVEELQELLEKQNFELSQARER 248
Cdd:pfam05622 310 qqlledANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQK----LEEHLEKLHEAQSELQKKKEQ 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 249 LVTLTATVTeleedlgtarrdlikseelSSKHQR--DLREALAQKED----MEERIttleKRYLAAQREAtsIHDLNDKL 322
Cdd:pfam05622 386 IEELEPKQD-------------------SNLAQKidELQEALRKKDEdmkaMEERY----KKYVEKAKSV--IKTLDPKQ 440
|
250 260 270
....*....|....*....|....*....|....*...
gi 966922630 323 ENELANK-ESLHRQCEEKARHLQEL-LEVAEQKLQQTM 358
Cdd:pfam05622 441 NPASPPEiQALKNQLLEKDKKIEHLeRDFEKSKLQREQ 478
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
219-378 |
7.21e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 39.12 E-value: 7.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 219 RLWKEDAGRVEELQELLEKQNFELSQARERLVT----LTATVTELEEDLGTARRD---LIKSEELSSKHQRDLREALAQK 291
Cdd:pfam13851 29 KSLKEEIAELKKKEERNEKLMSEIQQENKRLTEplqkAQEEVEELRKQLENYEKDkqsLKNLKARLKVLEKELKDLKWEH 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 292 EDMEERITTLEKRYLAA-QREATSIHDLNDKLENE---LANK-ESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPE 366
Cdd:pfam13851 109 EVLEQRFEKVERERDELyDKFEAAIQDVQQKTGLKnllLEKKlQALGETLEKKEAQLNEVLAAANLDPDALQAVTEKLED 188
|
170
....*....|..
gi 966922630 367 VEAELAQRIAAL 378
Cdd:pfam13851 189 VLESKNQLIKDL 200
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
176-469 |
7.76e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.20 E-value: 7.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 176 LERVTTLEEQLAGAHQQVSALQqgagvLDGAAEEEGTVElgpkrlwkedaGRVEELQELLEKqnfelsqarerlvtltat 255
Cdd:PRK04778 255 EKEIQDLKEQIDENLALLEELD-----LDEAEEKNEEIQ-----------ERIDQLYDILER------------------ 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 256 vtELEedlgtARRDLiksEELSSKHQRDLREALAQKEDMEERITTLEKRYLaaqreatsihdLNdklENELANKESLHRQ 335
Cdd:PRK04778 301 --EVK-----ARKYV---EKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYT-----------LN---ESELESVRQLEKQ 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966922630 336 ceekarhLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQR--- 412
Cdd:PRK04778 357 -------LESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKlhe 429
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966922630 413 -----EKMN-----EDHNKRLSDTVDRL--LSESNERLQLHLKERMAALEEkgrLSEEIEKLRQEVDQL 469
Cdd:PRK04778 430 ikrylEKSNlpglpEDYLEMFFEVSDEIeaLAEELEEKPINMEAVNRLLEE---ATEDVETLEEETEEL 495
|
|
| |
