|
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 ... |
890-955 |
1.15e-43 |
|
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.
Pssm-ID: 188964 Cd Length: 66 Bit Score: 152.24 E-value: 1.15e-43
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017363566 890 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 955
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 ... |
782-852 |
2.12e-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: 148.87 E-value: 2.12e-42
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017363566 782 FAQWDGPTVVSWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEMVSLT 852
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 ... |
975-1046 |
3.10e-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: 145.54 E-value: 3.10e-41
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363566 975 DVLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALILQIPTQNTQARQVMEREFNNLL 1046
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 ... |
894-953 |
6.92e-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: 6.92e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 894 WIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 953
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 ... |
983-1044 |
9.16e-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: 103.77 E-value: 9.16e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363566 983 QVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALILQIPTQNTQARQVMEREFNN 1044
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 ... |
789-847 |
2.76e-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: 99.61 E-value: 2.76e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2017363566 789 TVVSWLELWVGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQE 847
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 ... |
975-1046 |
2.32e-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: 2.32e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363566 975 DVLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALILQIPTQNTQARQVMEREFNNLL 1046
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 ... |
975-1046 |
1.93e-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: 1.93e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363566 975 DVLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALILQIPTQNTQARQVMEREFNNLL 1046
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 ... |
889-953 |
2.98e-16 |
|
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188966 Cd Length: 65 Bit Score: 73.98 E-value: 2.98e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363566 889 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 953
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 ... |
889-953 |
3.78e-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: 3.78e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363566 889 DMNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLrVHLKMVDSFHRTSLQYGIMCLK 953
Cdd:cd09566 1 KLDTHWV-LRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDL-LHLKVTSALHHASIRRGIQVLR 63
|
|
| SAM_kazrin_repeat1 |
cd09564 |
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ... |
783-847 |
9.79e-16 |
|
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrin contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved into interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188963 Cd Length: 70 Bit Score: 72.87 E-value: 9.79e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363566 783 AQWDGPTVVSWLELWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQE 847
Cdd:cd09564 2 SRWKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
889-953 |
5.00e-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: 5.00e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363566 889 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 953
Cdd:pfam00536 1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
147-426 |
2.24e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.63 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 147 EVEVLKALKSLFEHHKALDEkVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVElgpkrlwKEDTG 226
Cdd:TIGR02168 711 EEELEQLRKELEELSRQISA-LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL-------AEAEA 782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 227 RVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYL 306
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 307 AAQREATSIHDLNDKLENELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQELArvRQREKMNEDHNK--RLSDTVDR 384
Cdd:TIGR02168 863 ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE--ELREKLAQLELRleGLEVRIDN 940
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2017363566 385 LLSESNERLQLHLkerMAALEEKGRLSEEIEKLRQEVDQLKG 426
Cdd:TIGR02168 941 LQERLSEEYSLTL---EEAEALENKIEDDEEEARRRLKRLEN 979
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
159-425 |
1.03e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 159 EHHKALDEKVRER-LRAALERVTTLEEQLAGAHQQVSALQqgagvrdgAAEEEGTVELgpkrlwKEDTGRVEELQELLEK 237
Cdd:COG1196 213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELE--------AELEELEAEL------AELEAELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 238 QNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHD 317
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 318 LNDKLENELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHL 397
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
250 260
....*....|....*....|....*...
gi 2017363566 398 KERMAALEEKGRLSEEIEKLRQEVDQLK 425
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLA 466
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
147-435 |
2.60e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 147 EVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKRLWKEdtg 226
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE--- 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 227 RVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYL 306
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 307 AAQREATSIHDLNDKLENELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLL 386
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2017363566 387 SESNERLQLHLKERMAALEEKGRlsEEIEKLRQEVDQLKGRGGPFVDGV 435
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAAR--LLLLLEAEADYEGFLEGVKAALLL 516
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
9-424 |
3.40e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.49 E-value: 3.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 9 NEGDRLGPPHGADADANFEQL--MVNMLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNS--------ALPQ 78
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELkeLEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKlekllqllPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 79 EFATLTRELSMCREQLLEREEEISELKAERNNTRLLLEHLEclvsRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLF 158
Cdd:COG4717 133 ELEALEAELAELPERLEELEERLEELRELEEELEELEAELA----ELQEELEELLEQLSLATEEELQDLAEELEELQQRL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 159 EHHKALDEKVRERLRAALERVTTLEEQLAGAH--QQVSALQQGAGVRDGAAEEEGTVELGPKRLWKED------TGRVEE 230
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQLENELEAAAleERLKEARLLLLIAAALLALLGLGGSLLSLILTIAgvlflvLGLLAL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 231 LQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQR 310
Cdd:COG4717 289 LFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEEL 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 311 EATSIHDLNDKLENELANKESLHRQAEERHgNIEEHLRQLEGQLEEKNQELARVRQREKmNEDHNKRLSDTVDRLLSESN 390
Cdd:COG4717 369 EQEIAALLAEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQLEELLGELEELLEALD-EEELEEELEELEEELEELEE 446
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2017363566 391 ERLQLH-----LKERMAALEEKGRLSE---EIEKLRQEVDQL 424
Cdd:COG4717 447 ELEELReelaeLEAELEQLEEDGELAEllqELEELKAELREL 488
|
|
| SAM_liprin-beta1,2_repeat1 |
cd09563 |
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
782-846 |
9.49e-11 |
|
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta protein contain three copies (repeats) of SAM domain. They may form heterodimers with liprins-alpha through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta is potentially able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.
Pssm-ID: 188962 Cd Length: 64 Bit Score: 58.39 E-value: 9.49e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017363566 782 FAQWDGPTVVSWL-ELWVGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQ 846
Cdd:cd09563 1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
36-427 |
1.56e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 36 EREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSALPQEFATLTRELSMCREQLLEREEEISELKAERNNTRLLL 115
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 116 EHL-ECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEkvrerLRAALERVTTLEEQLAGAhqqvs 194
Cdd:COG1196 477 AALaELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV-----LIGVEAAYEAALEAALAA----- 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 195 aLQQGAGVRDGAAEEEGTVELGPKRLwkedtGRVEELQELLEKQNFELSQARERLVTLTTTV----TELEEDLGTARRDL 270
Cdd:COG1196 547 -ALQNIVVEDDEVAAAAIEYLKAAKA-----GRATFLPLDKIRARAALAAALARGAIGAAVDlvasDLREADARYYVLGD 620
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 271 IKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHdlNDKLENELANKESLHRQAEERHGNIEEHLRQL 350
Cdd:COG1196 621 TLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGS--RRELLAALLEAEAELEELAERLAEEELELEEA 698
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017363566 351 EGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGR 427
Cdd:COG1196 699 LLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
21-594 |
3.18e-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: 64.75 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 21 DADANFEQLMVNMLDErEKLLESLREsqeTLAATQSRLQDAIHERDQLQ----RHLNSALPQEFATLTRELSMCREQLLE 96
Cdd:pfam15921 167 DSNTQIEQLRKMMLSH-EGVLQEIRS---ILVDFEEASGKKIYEHDSMStmhfRSLGSAISKILRELDTEISYLKGRIFP 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 97 REEEISELKAE-RNNTRLLLEH----LECLVSRHERSL-----RMTVVKRQAQSpsgVSSEVEV------------LKAL 154
Cdd:pfam15921 243 VEDQLEALKSEsQNKIELLLQQhqdrIEQLISEHEVEItglteKASSARSQANS---IQSQLEIiqeqarnqnsmyMRQL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 155 KSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHqqvSALQQGAGVRDGAAEEEGTV----------------ELG-- 216
Cdd:pfam15921 320 SDLESTVSQLRSELREAKRMYEDKIEELEKQLVLAN---SELTEARTERDQFSQESGNLddqlqklladlhkrekELSle 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 217 ---PKRLWKEDTG-----------------RVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLG--TARRDLIKS- 273
Cdd:pfam15921 397 keqNKRLWDRDTGnsitidhlrrelddrnmEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSslTAQLESTKEm 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 274 -----EELSSKHQ---------RDLREALAQKEDMEE----RITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQ 335
Cdd:pfam15921 477 lrkvvEELTAKKMtlessertvSDLTASLQEKERAIEatnaEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQ 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 336 AEERHGNIEEHLRQLEG--QLEEKNQELARVRQREKMN---EDHNKRLSDTVDRLLSESNERLQLHLKERMAALE-EKGR 409
Cdd:pfam15921 557 MAEKDKVIEILRQQIENmtQLVGQHGRTAGAMQVEKAQlekEINDRRLELQEFKILKDKKDAKIRELEARVSDLElEKVK 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 410 L----SEE---IEKLRQEVDQLkgrggpfvdgvhsrshMGSAADVRFSLGTTTHAPPGVHRRYSALREEsaKDWETSPLP 482
Cdd:pfam15921 637 LvnagSERlraVKDIKQERDQL----------------LNEVKTSRNELNSLSEDYEVLKRNFRNKSEE--METTTNKLK 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 483 GMLAPAAGPAFDSDPEISDVdEDEPGGLVGSA-----DVVSPSGHSDA-QTLAMMLQEQLDAINEEIRMIQEEKE--STE 554
Cdd:pfam15921 699 MQLKSAQSELEQTRNTLKSM-EGSDGHAMKVAmgmqkQITAKRGQIDAlQSKIQFLEEAMTNANKEKHFLKEEKNklSQE 777
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 2017363566 555 LRAEEIETRVTSGSMEALNLKQLRKRGSIPTSLTALSLAS 594
Cdd:pfam15921 778 LSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKAS 817
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
164-428 |
3.02e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 164 LDEK-VRERLRAALERVTTL---EEQLAGAHQQVSALQQgagVRDGAAEeegtvelgpkrlWKEDTGRVEELQELLEKQN 239
Cdd:COG4913 218 LEEPdTFEAADALVEHFDDLeraHEALEDAREQIELLEP---IRELAER------------YAAARERLAELEYLRAALR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 240 FELSQARerlvtltttvteleedLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATsihdln 319
Cdd:COG4913 283 LWFAQRR----------------LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRL------ 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 320 DKLENELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQELARVRQRekmnedhnkrlsdtVDRLLSESNERLQLHLKE 399
Cdd:COG4913 341 EQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE--------------AAALLEALEEELEALEEA 406
|
250 260
....*....|....*....|....*....
gi 2017363566 400 RMAALEEKGRLSEEIEKLRQEVDQLKGRG 428
Cdd:COG4913 407 LAEAEAALRDLRRELRELEAEIASLERRK 435
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-427 |
5.75e-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: 60.46 E-value: 5.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 101 ISELKAERNNTRLLLEH-------LECLVSRHERSLRMtvVKRQAQSpsgvsseVEVLKALKS-LFEHHKALDEKVRERL 172
Cdd:TIGR02168 167 ISKYKERRKETERKLERtrenldrLEDILNELERQLKS--LERQAEK-------AERYKELKAeLRELELALLVLRLEEL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 173 RAALERvttLEEQLAGAHQQVSALQQGAGVRDGAAEEegtvelgpKRLWKedtGRVEELQELLEKQNFELSQARERLVTL 252
Cdd:TIGR02168 238 REELEE---LQEELKEAEEELEELTAELQELEEKLEE--------LRLEV---SELEEEIEELQKELYALANEISRLEQQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 253 TTTVTELEEDLgtaRRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQreatsihDLNDKLENELANKESL 332
Cdd:TIGR02168 304 KQILRERLANL---ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE-------AELEELEAELEELESR 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 333 HRQAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLS---------------DTVDRLLSESNERLQLHL 397
Cdd:TIGR02168 374 LEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQqeieellkkleeaelKELQAELEELEEELEELQ 453
|
330 340 350
....*....|....*....|....*....|
gi 2017363566 398 KERMAALEEKGRLSEEIEKLRQEVDQLKGR 427
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAERE 483
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
20-425 |
7.57e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 7.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 20 ADADANFEQLMVNMLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSALPQEFATLTRELSmcreqlleREE 99
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL--------LEA 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 100 EISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHH------KALDEKVRERLR 173
Cdd:COG1196 478 ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAleaalaAALQNIVVEDDE 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 174 AALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKrlwkedtGRVEELQELLEKQNFELSQARERLVTLT 253
Cdd:COG1196 558 VAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVD-------LVASDLREADARYYVLGDTLLGRTLVAA 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 254 TTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLH 333
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA 710
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 334 RQAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLlSESNERLQLhLKER--------MAALE 405
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL-EELERELER-LEREiealgpvnLLAIE 788
|
410 420
....*....|....*....|
gi 2017363566 406 EKGRLSEEIEKLRQEVDQLK 425
Cdd:COG1196 789 EYEELEERYDFLSEQREDLE 808
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
169-425 |
1.06e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.70 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 169 RERLRAALERVTTLEEQLAGAHQQVSALQQGAG-VRDGAAEEEGTVELGPKRlWKEDTGRVEELQELLEKQNFELSQARE 247
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDeLSQELSDASRKIGEIEKE-IEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 248 RLVTLTTTVTELEEDLGTARRDLIK-SEELSSKHQRDLREAL----AQKEDMEERITTLEKRYLAAQREATSIHDLNDKL 322
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEEDLHKlEEALNDLEARLSHSRIpeiqAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 323 ENELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKmneDHNKRLSDtvdrlLSESNERLQLHLKErma 402
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR---DLESRLGD-----LKKERDELEAQLRE--- 900
|
250 260
....*....|....*....|...
gi 2017363566 403 ALEEKGRLSEEIEKLRQEVDQLK 425
Cdd:TIGR02169 901 LERKIEELEAQIEKKRKRLSELK 923
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
782-848 |
3.36e-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: 3.36e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017363566 782 FAQWDGPTVVSWLELWvGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEM 848
Cdd:smart00454 1 VSQWSPESVADWLESI-GLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
898-953 |
7.01e-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: 7.01e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2017363566 898 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 953
Cdd:smart00454 11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
19-425 |
9.57e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 9.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 19 GADADANFEQLMVNML-----DEREKLLESL----------RESQETLAATQ---SRLQDAIHERD-QLQR-HLNSALPQ 78
Cdd:TIGR02168 134 GKRSYSIIEQGKISEIieakpEERRAIFEEAagiskykerrKETERKLERTRenlDRLEDILNELErQLKSlERQAEKAE 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 79 EFATLTRELSmcREQLLEREEEISELKAERNNTRLLLEHLECLVSRHERSLRMTvvkrqaqspsgvSSEVEVLKALKSlf 158
Cdd:TIGR02168 214 RYKELKAELR--ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQEL------------EEKLEELRLEVS-- 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 159 EHHKALDEkVRERLRAALERVTTLEEQLAGAHQQVSALQQGAgvrdgaAEEEGTVELGPKRLwkedtgrvEELQELLEKQ 238
Cdd:TIGR02168 278 ELEEEIEE-LQKELYALANEISRLEQQKQILRERLANLERQL------EELEAQLEELESKL--------DELAEELAEL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 239 NFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRylaaqreatsIHDL 318
Cdd:TIGR02168 343 EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR----------LERL 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 319 NDKLENELANKESLHRQAEErhgnieEHLRQLEGQLEEKNQELARVRQREkmnEDHNKRLSdTVDRLLSESNERLQL--- 395
Cdd:TIGR02168 413 EDRRERLQQEIEELLKKLEE------AELKELQAELEELEEELEELQEEL---ERLEEALE-ELREELEEAEQALDAaer 482
|
410 420 430
....*....|....*....|....*....|...
gi 2017363566 396 ---HLKERMAALEekgRLSEEIEKLRQEVDQLK 425
Cdd:TIGR02168 483 elaQLQARLDSLE---RLQENLEGFSEGVKALL 512
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
35-364 |
2.41e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 35 DEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSALpQEFATLTRELSMCREQLLEREEEISELKAERNNTRLL 114
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL-AELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 115 LEHLECLVSRHERSLRMTVVKRQAqspsgvsSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVS 194
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEE-------AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 195 ALQQGAGVRDGAAEEEGTVELGPKRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSE 274
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 275 ELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQAEERHGNIEEHLRQLEGQL 354
Cdd:COG1196 485 ELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIE 564
|
330
....*....|
gi 2017363566 355 EEKNQELARV 364
Cdd:COG1196 565 YLKAAKAGRA 574
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
265-425 |
2.51e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 265 TARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLND---------KLENELANKESLHRQ 335
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllplyqeleALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 336 AEERHgnieEHLRQLEGQLEEKNQELARVRQREkmnEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIE 415
Cdd:COG4717 151 LEERL----EELRELEEELEELEAELAELQEEL---EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170
....*....|
gi 2017363566 416 KLRQEVDQLK 425
Cdd:COG4717 224 ELEEELEQLE 233
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
32-425 |
3.77e-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: 54.74 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 32 NMLDEREKLLesLRESQETLaatQSRLQDAIHERDQLqrhlnsalpqefATLTRELSMCReqllereeeiSELKAERNNT 111
Cdd:pfam15921 98 NELHEKQKFY--LRQSVIDL---QTKLQEMQMERDAM------------ADIRRRESQSQ----------EDLRNQLQNT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 112 RLLLEHLECLVSR--HERSLRMTVVKRQAQSPSGVSSEVEVL------KALKSLFEHH-------KALDEKVRERLRAAL 176
Cdd:pfam15921 151 VHELEAAKCLKEDmlEDSNTQIEQLRKMMLSHEGVLQEIRSIlvdfeeASGKKIYEHDsmstmhfRSLGSAISKILRELD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 177 ERVTTLEEQLAGAHQQVSALQqgagvrdgaAEEEGTVELgpkrLWKEDTGRVE--------ELQELLEKQNFELSQARER 248
Cdd:pfam15921 231 TEISYLKGRIFPVEDQLEALK---------SESQNKIEL----LLQQHQDRIEqlisehevEITGLTEKASSARSQANSI 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 249 LVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREAlaqKEDMEERITTLEKRYLAAQREATSIHDLNDKLENElan 328
Cdd:pfam15921 298 QSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREA---KRMYEDKIEELEKQLVLANSELTEARTERDQFSQE--- 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 329 keslhrqaeerHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNER---------------- 392
Cdd:pfam15921 372 -----------SGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRnmevqrleallkamks 440
|
410 420 430
....*....|....*....|....*....|....
gi 2017363566 393 -LQLHLKERMAALEEKGRLSEEIEKLRQEVDQLK 425
Cdd:pfam15921 441 eCQGQMERQMAAIQGKNESLEKVSSLTAQLESTK 474
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
281-427 |
6.68e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 6.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 281 QRDLREALAQKEDMEERITTLEKRYLAAQREATS-------------IHDLNDKLENELANKESLhRQAEERHGNIEEHL 347
Cdd:COG4913 623 EEELAEAEERLEALEAELDALQERREALQRLAEYswdeidvasaereIAELEAELERLDASSDDL-AALEEQLEELEAEL 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 348 RQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGR 427
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRAR 781
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
262-427 |
7.07e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 7.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 262 DLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQAEERHG 341
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 342 NIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKR---LSDTVDRL--LSESNERLQLHLKERMAALEEKGRLSEEIEK 416
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEieeLEEKVKELkeLKEKAEEYIKLSEFYEEYLDELREIEKRLSR 318
|
170
....*....|.
gi 2017363566 417 LRQEVDQLKGR 427
Cdd:PRK03918 319 LEEEINGIEER 329
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
229-419 |
7.89e-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: 7.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 229 EELQELLEKQNF--ELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRyl 306
Cdd:COG1579 4 EDLRALLDLQELdsELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 307 aaQREATSIHDLNDkLENELAnkeslhrQAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLL 386
Cdd:COG1579 82 --LGNVRNNKEYEA-LQKEIE-------SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL 151
|
170 180 190
....*....|....*....|....*....|....
gi 2017363566 387 SESNERLQLHLKERMAALEE-KGRLSEEIEKLRQ 419
Cdd:COG1579 152 AELEAELEELEAEREELAAKiPPELLALYERIRK 185
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
142-425 |
1.01e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 142 SGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALqqgagvrdgaaeeegtvelgpkrlw 221
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL------------------------- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 222 KEDTGRVEELQElLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKS-EELSSKHQRdLREALAQKEDMEERITT 300
Cdd:PRK03918 279 EEKVKELKELKE-KAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERiKELEEKEER-LEELKKKLKELEKRLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 301 LEKRYLAAQREATSIHDLN-----------DKLENELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQELARVRQ--- 366
Cdd:PRK03918 357 LEERHELYEEAKAKKEELErlkkrltgltpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakg 436
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 367 -----REKMNEDHNKRLSDTVDRLLSESNERLQ------LHLKERMAALEEKGRLSEEIEKLRQEVDQLK 425
Cdd:PRK03918 437 kcpvcGRELTEEHRKELLEEYTAELKRIEKELKeieekeRKLRKELRELEKVLKKESELIKLKELAEQLK 506
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
218-427 |
1.49e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.76 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 218 KRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEE----LSSKHQRDLREALAQKED 293
Cdd:TIGR02169 155 RRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERyqalLKEKREYEGYELLKEKEA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 294 MEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQAEERHGNI-EEHLRQLEGQLEEKNQELARVRQREKMNE 372
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKE 314
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017363566 373 DHNKRLSDTVDRLLSESNErlqlhLKERMAALE--------EKGRLSEEIEKLRQEVDQLKGR 427
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDK-----LLAEIEELEreieeerkRRDKLTEEYAELKEELEDLRAE 372
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
33-425 |
1.52e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 33 MLDEREKLLESL-------RESQETLAATQsRLQDAIHERDQLQRHLNSALPQEFATLTRELSMCREQLLEREEEISELK 105
Cdd:PRK02224 242 VLEEHEERREELetleaeiEDLRETIAETE-REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 106 AERNNTRLLLEHLECLVSRHER---SLRMTVVKRQAQSPSGVSS----EVEVLKALKSLFEHHKALDEkVRERLRAALER 178
Cdd:PRK02224 321 DRDEELRDRLEECRVAAQAHNEeaeSLREDADDLEERAEELREEaaelESELEEAREAVEDRREEIEE-LEEEIEELRER 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 179 VTTLEEQLAGAHQQVSALQQGagvRDGAAEEEGTVELGpkrlWKEDTGRVEELQELLEK-------QNFELSQARERLVT 251
Cdd:PRK02224 400 FGDAPVDLGNAEDFLEELREE---RDELREREAELEAT----LRTARERVEEAEALLEAgkcpecgQPVEGSPHVETIEE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 252 LTTTVTELEEDLGTARRDLiksEELSSKHQR--DLREALAQKEDMEERITTLEKRY------LAAQRE-ATSIHDLNDKL 322
Cdd:PRK02224 473 DRERVEELEAELEDLEEEV---EEVEERLERaeDLVEAEDRIERLEERREDLEELIaerretIEEKRErAEELRERAAEL 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 323 ENELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQE---LARVRQREKMNEDHNKRLSDTVDRL--LSESNERLQLHL 397
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERiesLERIRTLLAAIADAEDEIERLREKReaLAELNDERRERL 629
|
410 420 430
....*....|....*....|....*....|..
gi 2017363566 398 K---ERMAALEEKgrLSEE-IEKLRQEVDQLK 425
Cdd:PRK02224 630 AekrERKRELEAE--FDEArIEEAREDKERAE 659
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
34-425 |
1.88e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 52.53 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 34 LDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSALPQEFATLTRELSmcrEQLLEREEEISELKAERNNTRl 113
Cdd:pfam12128 246 LQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWK---EKRDELNGELSAADAAVAKDR- 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 114 llEHLECLVSRHERSLRMTVVKR---QAQSPSgVSSEVEVL-KALKSLFEHHK-------ALDEKVRERLRAALERVT-- 180
Cdd:pfam12128 322 --SELEALEDQHGAFLDADIETAaadQEQLPS-WQSELENLeERLKALTGKHQdvtakynRRRSKIKEQNNRDIAGIKdk 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 181 ------TLEEQLAGAHQQVSAL------QQGAGVRDGAAEEEGTVE-LGPKRLWKEDTGRVEELQELLEKQNFELSQARE 247
Cdd:pfam12128 399 lakireARDRQLAVAEDDLQALeselreQLEAGKLEFNEEEYRLKSrLGELKLRLNQATATPELLLQLENFDERIERARE 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 248 RLVTLTTTVTELEEDLGTARRdliKSEELSSKHQR------DLREALAQKEDM-------------------EERITTLE 302
Cdd:pfam12128 479 EQEAANAEVERLQSELRQARK---RRDQASEALRQasrrleERQSALDELELQlfpqagtllhflrkeapdwEQSIGKVI 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 303 KRYL---------------------------AAQREATSIHDLNDKLENELANKESLHRQAEERHGNIEEHLRQLEGQLE 355
Cdd:pfam12128 556 SPELlhrtdldpevwdgsvggelnlygvkldLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELE 635
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 356 EKNQELARVRQREKMNEDHNKRLSDtvdrllsesnERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLK 425
Cdd:pfam12128 636 KASREETFARTALKNARLDLRRLFD----------EKQSEKDKKNKALAERKDSANERLNSLEAQLKQLD 695
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
229-426 |
3.00e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 229 EELQELL-EKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTL-EKRYL 306
Cdd:TIGR02169 211 ERYQALLkEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 307 AAQREATSIHDLNDKLENELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLL 386
Cdd:TIGR02169 291 RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLR 370
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2017363566 387 SesneRLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKG 426
Cdd:TIGR02169 371 A----ELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
267-425 |
3.29e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 267 RRDLIksEELS--SKHQRDLREALAQKEDMEERITTLE--------------------KRYLAAQREATsIHDLN----- 319
Cdd:COG1196 157 RRAII--EEAAgiSKYKERKEEAERKLEATEENLERLEdilgelerqleplerqaekaERYRELKEELK-ELEAEllllk 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 320 -DKLENELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQELARVRQR-EKMNEDHNKRLSDtvdrlLSESNERLQLHL 397
Cdd:COG1196 234 lRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELElEEAQAEEYELLAE-----LARLEQDIARLE 308
|
170 180
....*....|....*....|....*...
gi 2017363566 398 KERMAALEEKGRLSEEIEKLRQEVDQLK 425
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELE 336
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
34-407 |
4.25e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 34 LDEREKLLESLRESQETLAATQSRLQDAIherDQLQRHLNSALPQEFATLTRELSMCREQLLEREEEISELKAERNNTRL 113
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEEL---EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 114 LLEHLECLVSRHER--------------SLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERV 179
Cdd:COG4717 228 ELEQLENELEAAALeerlkearlllliaAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEEL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 180 TTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKRLWKEDTGRVEELQEllekqnfELSQARERLVTLTTTVTEL 259
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE-------ELQLEELEQEIAALLAEAG 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 260 EEDLGTARRDLIKSEElsskhQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDkLENELANKESLHRQAEER 339
Cdd:COG4717 381 VEDEEELRAALEQAEE-----YQELKEELEELEEQLEELLGELEELLEALDEEELEEELEE-LEEELEELEEELEELREE 454
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 340 HGNIEEHLRQLE--GQLEEKNQELARVRQREKMNEDHNKRLsDTVDRLLSESNERLQlhlKERMAALEEK 407
Cdd:COG4717 455 LAELEAELEQLEedGELAELLQELEELKAELRELAEEWAAL-KLALELLEEAREEYR---EERLPPVLER 520
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
31-423 |
4.43e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.88 E-value: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 31 VNMLDEREKLL-ESLRESQETLAATQSRLQDAiheRDQLQRHLNS--ALPQEFATLTRELSMCREQLLEREEE------- 100
Cdd:pfam05483 270 ANQLEEKTKLQdENLKELIEKKDHLTKELEDI---KMSLQRSMSTqkALEEDLQIATKTICQLTEEKEAQMEElnkakaa 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 101 ----ISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgvsSEVEVLKALKS-----LFEHHKALDEKvrER 171
Cdd:pfam05483 347 hsfvVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS-----SELEEMTKFKNnkeveLEELKKILAED--EK 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 172 LRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKRLWKEDtgrVEELQELLEKQ---NFELSQARER 248
Cdd:pfam05483 420 LLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKE---VEDLKTELEKEklkNIELTAHCDK 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 249 LVTLTTTVTELEEDLgtarrdlikSEELSsKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHD----------- 317
Cdd:pfam05483 497 LLLENKELTQEASDM---------TLELK-KHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREefiqkgdevkc 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 318 LNDKLENELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQELARVRQR----EKMNEDHNKRLSD---TVDRL---LS 387
Cdd:pfam05483 567 KLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQEnkalKKKGSAENKQLNAyeiKVNKLeleLA 646
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2017363566 388 ESNERLQLHLKERMAALEEKG----RLSEEIEKLRQEVDQ 423
Cdd:pfam05483 647 SAKQKFEEIIDNYQKEIEDKKiseeKLLEEVEKAKAIADE 686
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
976-1047 |
5.88e-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: 5.88e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363566 976 VLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHntlalILQIPTQNTQARQVMEREFNNLLA 1047
Cdd:smart00454 1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEED-----LKELGITKLGHRKKILKAIQKLKE 67
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
227-430 |
6.72e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 6.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 227 RVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYL 306
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 307 AAQREATSIHDLNDKLENELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQELARVRQreKMNEDHNKRLSDTVDRLL 386
Cdd:COG4372 112 ELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ--ELQALSEAEAEQALDELL 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2017363566 387 SESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGRGGP 430
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233
|
|
| SAM_superfamily |
cd09487 |
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
898-949 |
7.31e-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: 7.31e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2017363566 898 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGI 949
Cdd:cd09487 4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
274-425 |
7.31e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 7.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 274 EELSSKHQRDLREALAQKEDMEERITTLEKRYlaaqREATSIHDLNDKLENELANKESLHRQAEERHGNIEE---HLRQL 350
Cdd:PRK03918 570 EELAELLKELEELGFESVEELEERLKELEPFY----NEYLELKDAEKELEREEKELKKLEEELDKAFEELAEtekRLEEL 645
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363566 351 EGQLEEKNQELARVRQREKMNEdhNKRLSDTVDRLLSESnERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLK 425
Cdd:PRK03918 646 RKELEELEKKYSEEEYEELREE--YLELSRELAGLRAEL-EELEKRREEIKKTLEKLKEELEEREKAKKELEKLE 717
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
159-423 |
8.33e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 8.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 159 EHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDgaAEEEGTVElgPKRLWKEDTG----RVEELQEL 234
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKK--AEEKKKAE--EAKKAEEDKNmalrKAEEAKKA 1589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 235 LEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEE-------LSSKHQRDLREALAQKEDMEERITTLEKRYLA 307
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEekkkveqLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK 1669
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 308 AQREATSIHDLNDKLENELANKESLHRQAEER------HGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDT 381
Cdd:PTZ00121 1670 AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAkkaeelKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA 1749
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2017363566 382 ---------VDRLLSESNERLQLHLKERMAALEEKgrLSEEIEKLRQEVDQ 423
Cdd:PTZ00121 1750 kkdeeekkkIAHLKKEEEKKAEEIRKEKEAVIEEE--LDEEDEKRRMEVDK 1798
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
34-425 |
8.89e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 8.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 34 LDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNS---------ALPQEFATLTRELSMCREQLLEREEEISEL 104
Cdd:PRK03918 240 IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkelkEKAEEYIKLSEFYEEYLDELREIEKRLSRL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 105 KAERNNTRLLLEHLECLVSR-HERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALD-----EKVRERLRAALER 178
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERlEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLtgltpEKLEKELEELEKA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 179 VTTLEEQLAGAHQQVSALQQGAGVRDGAAEE----EGTVELGPKRLWKEDTGRV-EELQELLEKQNFELSQARERLVTLT 253
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKKAIEElkkaKGKCPVCGRELTEEHRKELlEEYTAELKRIEKELKEIEEKERKLR 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 254 TTVTELEEDLGTARR--------DLIKS--EELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLE 323
Cdd:PRK03918 480 KELRELEKVLKKESEliklkelaEQLKEleEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLA 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 324 NELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLlsesnERLQLHLKErmaA 403
Cdd:PRK03918 560 ELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKEL-----KKLEEELDK---A 631
|
410 420
....*....|....*....|..
gi 2017363566 404 LEEKGRLSEEIEKLRQEVDQLK 425
Cdd:PRK03918 632 FEELAETEKRLEELRKELEELE 653
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
976-1046 |
9.10e-06 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 44.18 E-value: 9.10e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017363566 976 VLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALdeNFDHNTLAlilQIPTQNTQARQVMEREFNNLL 1046
Cdd:pfam07647 1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK---RLGITSVGHRRKILKKIQELK 66
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
163-427 |
1.52e-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: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 163 ALDEKVRERLRAALERVTTLEEQLAgahQQVSALQQGAGVRDGAAEEEGTVE--LGPKRLWKEDT--GRVEELQELLEkq 238
Cdd:COG3096 829 AFAPDPEAELAALRQRRSELERELA---QHRAQEQQLRQQLDQLKEQLQLLNklLPQANLLADETlaDRLEELREELD-- 903
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 239 nfELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELsskhQRDLREALAQKEDMEERITTLEkrYLAAQREATSIHD- 317
Cdd:COG3096 904 --AAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQL----QADYLQAKEQQRRLKQQIFALS--EVVQRRPHFSYEDa 975
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 318 ---------LNDKLENELANKESLHRQAEERhgnieehLRQLEGQLEEKNQELA----RVRQREKMNEDHNKRLSDTVDR 384
Cdd:COG3096 976 vgllgensdLNEKLRARLEQAEEARREAREQ-------LRQAQAQYSQYNQVLAslksSRDAKQQTLQELEQELEELGVQ 1048
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2017363566 385 LLSESNERLQLHLKERMAAL-EEKGRLSeEIEKLRQ----EVDQLKGR 427
Cdd:COG3096 1049 ADAEAEERARIRRDELHEELsQNRSRRS-QLEKQLTrceaEMDSLQKR 1095
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
32-425 |
2.08e-05 |
|
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: 48.81 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 32 NMLDEREKLLESLRESQETLAATQsRLQDAIHERDQLQRHLNSALPQEfATLTRELSmcreqllereeEISELKAERNNT 111
Cdd:TIGR00618 223 VLEKELKHLREALQQTQQSHAYLT-QKREAQEEQLKKQQLLKQLRARI-EELRAQEA-----------VLEETQERINRA 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 112 RllleHLECLVsrhERSLRMTVVKRQAQspsgvssevevlkalkslfEHHKALDEKVRERLRAALERVTTLEEQLAGAHQ 191
Cdd:TIGR00618 290 R----KAAPLA---AHIKAVTQIEQQAQ-------------------RIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 192 QVSA---LQQGAGVRDGAAEEEGTVELGPKRlwKEDTGRVEELQELLEKQNfELSQARERLVTLTTTVTELEEDLGTARR 268
Cdd:TIGR00618 344 RRLLqtlHSQEIHIRDAHEVATSIREISCQQ--HTLTQHIHTLQQQKTTLT-QKLQSLCKELDILQREQATIDTRTSAFR 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 269 DLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHdlnDKLENELANKESLHRQAEERHGNIEEHL- 347
Cdd:TIGR00618 421 DLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSL---KEREQQLQTKEQIHLQETRKKAVVLARLl 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 348 ------RQLEGQLEEKNQEL----------ARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKG--- 408
Cdd:TIGR00618 498 elqeepCPLCGSCIHPNPARqdidnpgpltRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSIltq 577
|
410 420
....*....|....*....|
gi 2017363566 409 ---RLSEEIEKLRQEVDQLK 425
Cdd:TIGR00618 578 cdnRSKEDIPNLQNITVRLQ 597
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
149-370 |
2.48e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 149 EVLKALKSLFEHHKALDEkVRERLRAALERVTTLEEQLAGAHQQVSALQQgagvrdgaaeeegtvelgpkrlwkedtgRV 228
Cdd:COG1579 4 EDLRALLDLQELDSELDR-LEHRLKELPAELAELEDELAALEARLEAAKT----------------------------EL 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 229 EELQELLEKQNFELSQARERLVtltttvteleedlgtarrdliKSEEL--SSKHQRDLREALAQKEDMEERITTLEKRYL 306
Cdd:COG1579 55 EDLEKEIKRLELEIEEVEARIK---------------------KYEEQlgNVRNNKEYEALQKEIESLKRRISDLEDEIL 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363566 307 AAQREAtsihdlnDKLENELANKESLHRQAEERhgnIEEHLRQLEGQLEEKNQELARVR-QREKM 370
Cdd:COG1579 114 ELMERI-------EELEEELAELEAELAELEAE---LEEKKAELDEELAELEAELEELEaEREEL 168
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
235-420 |
3.38e-05 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 47.50 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 235 LEKQNFELSQARErlvtlttTVTELEEDLGTARRDLIKSEEL-SSKHQRD--LREALAQKEDME--------------ER 297
Cdd:pfam15905 127 LEKQLLELTRVNE-------LLKAKFSEDGTQKKMSSLSMELmKLRNKLEakMKEVMAKQEGMEgklqvtqknlehskGK 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 298 ITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQAEErhgnIEEHLRQLEGQLEEKNQELARVRQREKMNEDHN-- 375
Cdd:pfam15905 200 VAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEK----YKLDIAQLEELLKEKNDEIESLKQSLEEKEQELsk 275
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2017363566 376 ---------KRLSDTVDRLLSESNERLQLHLKErMAALEEKGRL-SEEIEKLRQE 420
Cdd:pfam15905 276 qikdlnekcKLLESEKEELLREYEEKEQTLNAE-LEELKEKLTLeEQEHQKLQQK 329
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
227-430 |
4.13e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 227 RVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSK---HQRDLREALAQKEDMEERITTLEK 303
Cdd:PRK03918 187 RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEieeLEKELESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 304 RYLAAQREatsIHDLNDKLE--NELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDT 381
Cdd:PRK03918 267 RIEELKKE---IEELEEKVKelKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL 343
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2017363566 382 VDRLLSesnerlqlhLKERMAALEEKGRLSEEIEKLRQEVDQLKGRGGP 430
Cdd:PRK03918 344 KKKLKE---------LEKRLEELEERHELYEEAKAKKEELERLKKRLTG 383
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
223-429 |
5.24e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 5.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 223 EDTGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEelssKHQRDLREALAQKEDMEErittLE 302
Cdd:PRK03918 221 EELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK----KEIEELEEKVKELKELKE----KA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 303 KRYLAAQREATSIHDLNDKLENELANKESLHRQAEERHGNIEE---HLRQLEGQLEEKNQELARVRQREKMNEDhNKRLS 379
Cdd:PRK03918 293 EEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEkeeRLEELKKKLKELEKRLEELEERHELYEE-AKAKK 371
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2017363566 380 DTVDRLLSESNERLQLHLKERMAALEE-KGRLSEEIEKLRQEVDQLKGRGG 429
Cdd:PRK03918 372 EELERLKKRLTGLTPEKLEKELEELEKaKEEIEEEISKITARIGELKKEIK 422
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
229-420 |
5.48e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 229 EELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRY--- 305
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELael 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 306 -LAAQR-----------EATSIHDLNDKLENELANKESLHRQAEERHGNIEEhLRQLEGQLEEKNQELARVRQREKMNED 373
Cdd:COG4942 110 lRALYRlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE-LAALRAELEAERAELEALLAELEEERA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2017363566 374 HNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQE 420
Cdd:COG4942 189 ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
33-421 |
5.61e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 5.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 33 MLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLN------SALPQEFATLTRELSMCREQLLEREEEISELKA 106
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEqleqeeEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 107 ERNNTRLLLEHLECLVSRHERSLRMTVVKrqaqspsgvssevEVLKALKSLFEHHKALDEKVRErLRAALERVTTLEEQL 186
Cdd:TIGR02169 766 RIEELEEDLHKLEEALNDLEARLSHSRIP-------------EIQAELSKLEEEVSRIEARLRE-IEQKLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 187 AGAHQQvsALQQGAGVRDGAAEEEGTVElgpkrlwkEDTGRVEELQELLEKQnfelsQARERlvtltttvteleeDLGTA 266
Cdd:TIGR02169 832 EKEIQE--LQEQRIDLKEQIKSIEKEIE--------NLNGKKEELEEELEEL-----EAALR-------------DLESR 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 267 RRDLikseelsskhQRDLREALAQKEDMEERITTLEkryLAAQREATSIHDLNDKLEN---ELANKESLHRQAEERHGNi 343
Cdd:TIGR02169 884 LGDL----------KKERDELEAQLRELERKIEELE---AQIEKKRKRLSELKAKLEAleeELSEIEDPKGEDEEIPEE- 949
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 344 EEHLRQLEGQLEEKNQELarvRQREKMN-------EDHNKRLSDtvdrlLSESNERLQlhlKERMAALEekgrLSEEIEK 416
Cdd:TIGR02169 950 ELSLEDVQAELQRVEEEI---RALEPVNmlaiqeyEEVLKRLDE-----LKEKRAKLE---EERKAILE----RIEEYEK 1014
|
....*
gi 2017363566 417 LRQEV 421
Cdd:TIGR02169 1015 KKREV 1019
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
281-425 |
7.43e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 7.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 281 QRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQE 360
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 361 LARVRQR--------EKMNED-------HNKRLSDTVDRL--LSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQ 423
Cdd:COG4942 99 LEAQKEElaellralYRLGRQpplalllSPEDFLDAVRRLqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
..
gi 2017363566 424 LK 425
Cdd:COG4942 179 LL 180
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
229-427 |
1.11e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 229 EELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRyLAA 308
Cdd:TIGR02169 691 SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR-IEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 309 QREAtsIHDLNDKLeNELANKESLHR--QAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLL 386
Cdd:TIGR02169 770 LEED--LHKLEEAL-NDLEARLSHSRipEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK 846
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2017363566 387 SESNER-------------LQLHLKERMAAL----EEKGRLSEEIEKLRQEVDQLKGR 427
Cdd:TIGR02169 847 EQIKSIekeienlngkkeeLEEELEELEAALrdleSRLGDLKKERDELEAQLRELERK 904
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
285-420 |
1.13e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 285 REALAQKEDMEerittlekryLAAQREatsIHDLNDKLENELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQELARV 364
Cdd:PRK12704 49 KEAEAIKKEAL----------LEAKEE---IHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKK 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 365 RQREKMNEDHNKRLSDTVDRLLSESNERLqlhlkERMAAL---EEKGRLSEEIE-KLRQE 420
Cdd:PRK12704 116 EKELEQKQQELEKKEEELEELIEEQLQEL-----ERISGLtaeEAKEILLEKVEeEARHE 170
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
28-373 |
1.13e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 28 QLMVNMLDEREKLLESLRESQETLAATQSRLQDAihERDQLQRHLNSALPQEfATLTRELSMCREQLLEREEEISELKAE 107
Cdd:TIGR02169 190 DLIIDEKRQQLERLRREREKAERYQALLKEKREY--EGYELLKEKEALERQK-EAIERQLASLEEELEKLTEEISELEKR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 108 RNNTRLLLEHLECLVSRhERSLRMTVVKRQAQSpsgVSSEVEVLK-ALKSLFEHHKALDEKVR---ERLRAALERVTTLE 183
Cdd:TIGR02169 267 LEEIEQLLEELNKKIKD-LGEEEQLRVKEKIGE---LEAEIASLErSIAEKERELEDAEERLAkleAEIDKLLAEIEELE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 184 EQLAGAHQQVSALQqgAGVRDGAAEEEGTVElgpkrlwkedtgRVEELQELLEKQNFELSQARERlvtltttVTELEEDL 263
Cdd:TIGR02169 343 REIEEERKRRDKLT--EEYAELKEELEDLRA------------ELEEVDKEFAETRDELKDYREK-------LEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 264 GTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREatsIHDLNDKLENELANKESlhrqAEERHGNI 343
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE---IKKQEWKLEQLAADLSK----YEQELYDL 474
|
330 340 350
....*....|....*....|....*....|
gi 2017363566 344 EEHLRQLEGQLEEKNQELARVRQREKMNED 373
Cdd:TIGR02169 475 KEEYDRVEKELSKLQRELAEAEAQARASEE 504
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
222-427 |
1.20e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 222 KEDTGRVEELQELLEKQNFELSQARERLVTLTTTvteleedLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTL 301
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENR-------LDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 302 EKRYLAAQREATSIHDLNDKLENELANKESLHRQAEERHGNIEEHL-----RQLEGQLEEKNQELARVRQR-----EKMN 371
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEARlreieQKLN 822
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363566 372 EDHNKR--LSDTVDRLLSESNErLQLHLKERMAALEE----KGRLSEEIEKLRQEVDQLKGR 427
Cdd:TIGR02169 823 RLTLEKeyLEKEIQELQEQRID-LKEQIKSIEKEIENlngkKEELEEELEELEAALRDLESR 883
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
42-427 |
1.31e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 42 ESLRESQETLAATQSRLQDAIHE-RDQLQRHLNSA----------------LPQEFATLTRELSMCREQLLEREEEISEL 104
Cdd:PRK02224 310 EAVEARREELEDRDEELRDRLEEcRVAAQAHNEEAeslredaddleeraeeLREEAAELESELEEAREAVEDRREEIEEL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 105 KAERNNTRL-----------LLEHLECLVSRHERslrmtVVKRQAQSPSGVSSEVEVLKALKSLFEHHKA-------LDE 166
Cdd:PRK02224 390 EEEIEELRErfgdapvdlgnAEDFLEELREERDE-----LREREAELEATLRTARERVEEAEALLEAGKCpecgqpvEGS 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 167 KVRERLRAALERVTTLEEQLAGAHQQVSALQQgagvRDGAAEEEGTVELGPKRLwKEdtgRVEELQELLEKQNFELSQAR 246
Cdd:PRK02224 465 PHVETIEEDRERVEELEAELEDLEEEVEEVEE----RLERAEDLVEAEDRIERL-EE---RREDLEELIAERRETIEEKR 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 247 ERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEK-RYLAAQRE--ATSIHDLNDKLE 323
Cdd:PRK02224 537 ERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERiRTLLAAIAdaEDEIERLREKRE 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 324 NeLANKESLHRqaeERHGNIEEHLRQLEGQLEEKNQELArvRQREKMNEDHNKRLSDTVDRLLSESNErlqlhLKERMAA 403
Cdd:PRK02224 617 A-LAELNDERR---ERLAEKRERKRELEAEFDEARIEEA--REDKERAEEYLEQVEEKLDELREERDD-----LQAEIGA 685
|
410 420
....*....|....*....|....
gi 2017363566 404 LEEKgrlSEEIEKLRQEVDQLKGR 427
Cdd:PRK02224 686 VENE---LEELEELRERREALENR 706
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
38-427 |
1.69e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 38 EKLLESLRESQETLAATQSRLQDA-IHERdqlqrhLNsALPQEFATLTRElsmcreqllereeeISELKAERNNTRLLLE 116
Cdd:PRK02224 179 ERVLSDQRGSLDQLKAQIEEKEEKdLHER------LN-GLESELAELDEE--------------IERYEEQREQARETRD 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 117 HLECLVSRHERSLrmtvvkrqaqspsgvsSEVEVLKALKSLFEHHKALDEKVRERLRaalERVTTLEEQLAGAHQQVSAL 196
Cdd:PRK02224 238 EADEVLEEHEERR----------------EELETLEAEIEDLRETIAETEREREELA---EEVRDLRERLEELEEERDDL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 197 QQGAGVRDGAAEeegtvelgpkrlwkedtgRVEELQELLEKQNFELsqarerlvtltttvteleedlgtaRRDLIKSEEL 276
Cdd:PRK02224 299 LAEAGLDDADAE------------------AVEARREELEDRDEEL------------------------RDRLEECRVA 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 277 SSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQAEERHGNIEEHLRQLEGQLEE 356
Cdd:PRK02224 337 AQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEE 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 357 KNQELARVRQREKMNEDHNKRLSDTVdrllsESNERLQLHLK-----------ERMAALEE----KGRLSEEIEKLRQEV 421
Cdd:PRK02224 417 LREERDELREREAELEATLRTARERV-----EEAEALLEAGKcpecgqpvegsPHVETIEEdrerVEELEAELEDLEEEV 491
|
....*.
gi 2017363566 422 DQLKGR 427
Cdd:PRK02224 492 EEVEER 497
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
30-414 |
1.91e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 30 MVNMLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSAlPQEFATLTRELSmcreqLLEREEEISELKAERN 109
Cdd:PRK03918 389 LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKA-KGKCPVCGRELT-----EEHRKELLEEYTAELK 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 110 NTRLLLEHLECLVSRHERSLRMtvVKRQAQSPSGVSSEVEVLKALKSLFEHHKALD-----------EKVRERLRAALER 178
Cdd:PRK03918 463 RIEKELKEIEEKERKLRKELRE--LEKVLKKESELIKLKELAEQLKELEEKLKKYNleelekkaeeyEKLKEKLIKLKGE 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 179 VTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTV-----ELGPKRLwKEDTGRVEELQELLEKQNfELSQARERLVTLT 253
Cdd:PRK03918 541 IKSLKKELEKLEELKKKLAELEKKLDELEEELAELlkeleELGFESV-EELEERLKELEPFYNEYL-ELKDAEKELEREE 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 254 TTvteleedLGTARRDLIKSEElsskhqrDLREALAQKEDMEERITTLEKRYlaAQREATSIHDLNDKLENELANKESLH 333
Cdd:PRK03918 619 KE-------LKKLEEELDKAFE-------ELAETEKRLEELRKELEELEKKY--SEEEYEELREEYLELSRELAGLRAEL 682
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 334 RQAEERHGNIEEHLRQLEGQLEEknqelaRVRQREKMnEDHNKRLSDTVDrlLSESNERLQLHLKERmaALEEKGRLSEE 413
Cdd:PRK03918 683 EELEKRREEIKKTLEKLKEELEE------REKAKKEL-EKLEKALERVEE--LREKVKKYKALLKER--ALSKVGEIASE 751
|
.
gi 2017363566 414 I 414
Cdd:PRK03918 752 I 752
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
16-427 |
2.16e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 16 PPHGADADA---NFEQLM---VNMLDEREK--LLESLRESQETLAATQSRLQDAIHERDQLQ----RHLNSALPQEFATL 83
Cdd:COG4913 221 PDTFEAADAlveHFDDLErahEALEDAREQieLLEPIRELAERYAAARERLAELEYLRAALRlwfaQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 84 TRELSMCREQLLEREEEISELKAERNNTRLL--------LEHLECLVSRHERSLRMTVVKRQA----------QSPSGVS 145
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEAQirgnggdrLEQLEREIERLERELEERERRRARleallaalglPLPASAE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 146 SEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAG------------------------ 201
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSniparllalrdalaealgldeael 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 202 --------VRDGAAEEEGTVE--LGPKRL--------------WKE--------DTGRVEELQE-----------LLEKQ 238
Cdd:COG4913 461 pfvgelieVRPEEERWRGAIErvLGGFALtllvppehyaaalrWVNrlhlrgrlVYERVRTGLPdperprldpdsLAGKL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 239 NFELSQARERLVTLTTTVTE-----LEEDLGTARRD-----LIKSEelSSKHQRDLREALAQK----EDMEERITTLEKR 304
Cdd:COG4913 541 DFKPHPFRAWLEAELGRRFDyvcvdSPEELRRHPRAitragQVKGN--GTRHEKDDRRRIRSRyvlgFDNRAKLAALEAE 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 305 YLAAQREatsIHDLNDKLEnELANKESLHRQAEERHGNIEEH------LRQLEGQLEEKNQELARVRQRekmnedhnkrl 378
Cdd:COG4913 619 LAELEEE---LAEAEERLE-ALEAELDALQERREALQRLAEYswdeidVASAEREIAELEAELERLDAS----------- 683
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2017363566 379 SDTVDRL---LSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGR 427
Cdd:COG4913 684 SDDLAALeeqLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
104-427 |
3.48e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.81 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 104 LKAERNNTRLLLEHLECLVSRHERSLRmtvvkRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLraaLERVTTLE 183
Cdd:pfam10174 343 LQTEVDALRLRLEEKESFLNKKTKQLQ-----DLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENL---QEQLRDKD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 184 EQLAGAHQQVSALQQGAGVRDGA--------AEEEGTVELGPKRLWKEDTGRVEELqELLEKQNFELSQARERLVTLTTT 255
Cdd:pfam10174 415 KQLAGLKERVKSLQTDSSNTDTAlttleealSEKERIIERLKEQREREDRERLEEL-ESLKKENKDLKEKVSALQPELTE 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 256 VTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDK---LENELANK--E 330
Cdd:pfam10174 494 KESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRirlLEQEVARYkeE 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 331 SLHRQAE-ERHGNIeehLRQLEGQLEEKNQELA-----RVRQ-REKMNEDHNKRLSDTVDRllSESNERLQLHLKERMAA 403
Cdd:pfam10174 574 SGKAQAEvERLLGI---LREVENEKNDKDKKIAeleslTLRQmKEQNKKVANIKHGQQEMK--KKGAQLLEEARRREDNL 648
|
330 340 350
....*....|....*....|....*....|..
gi 2017363566 404 --------LEEkgrLSEEIEKLRQEVDQLKGR 427
Cdd:pfam10174 649 adnsqqlqLEE---LMGALEKTRQELDATKAR 677
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
262-425 |
4.04e-04 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 43.13 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 262 DLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERIT-TLEKRYLAAQREA-TSIHDLndklENELANKESLHRQAEER 339
Cdd:pfam04012 37 ELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQaALTKGNEELAREAlAEKKSL----EKQAEALETQLAQQRSA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 340 HGNIEEHLRQLEGQLEEKNQELARVRQREKMNEdHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEK--- 416
Cdd:pfam04012 113 VEQLRKQLAALETKIQQLKAKKNLLKARLKAAK-AQEAVQTSLGSLSTSSATDSFERIEEKIEEREARADAAAELASavd 191
|
....*....
gi 2017363566 417 LRQEVDQLK 425
Cdd:pfam04012 192 LDAKLEQAG 200
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
33-407 |
5.49e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.33 E-value: 5.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 33 MLDEREKLLESLRESQETLAATQSRLQDAIHerdqlqrhLNSALPQEFATLTRELSMCREQLLEREEEISELKAERNNTR 112
Cdd:pfam05483 413 ILAEDEKLLDEKKQFEKIAEELKGKEQELIF--------LLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEK 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 113 LllEHLECLVSRHERSLRMtvvKRQAQSPSGVSSEvevLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQ 192
Cdd:pfam05483 485 L--KNIELTAHCDKLLLEN---KELTQEASDMTLE---LKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREE 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 193 VsaLQQGAGVR---DGAAEEEGTVE---LGPKRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTA 266
Cdd:pfam05483 557 F--IQKGDEVKcklDKSEENARSIEyevLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAY 634
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 267 RRDLIKSE-ELSSKHQRdLREALA--QKEDMEERITtlEKRYLAAQREATSIHDLNDKLENELaNKESLHRQAEERhGNI 343
Cdd:pfam05483 635 EIKVNKLElELASAKQK-FEEIIDnyQKEIEDKKIS--EEKLLEEVEKAKAIADEAVKLQKEI-DKRCQHKIAEMV-ALM 709
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2017363566 344 EEHLRQLEGQLEEKNQELARVRQREKmnEDHNKR------LSDTVDRLLS---------ESNERLQLHLKERMAALEEK 407
Cdd:pfam05483 710 EKHKHQYDKIIEERDSELGLYKNKEQ--EQSSAKaaleieLSNIKAELLSlkkqleiekEEKEKLKMEAKENTAILKDK 786
|
|
| SAM_STIM-1,2-like |
cd09504 |
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ... |
785-843 |
5.86e-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: 5.86e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363566 785 WDGPTVVSWLELWVGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNALHRLKLRL 843
Cdd:cd09504 5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
266-427 |
7.00e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.50 E-value: 7.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 266 ARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKR---YLAAQREATSIHDLNDK--LENELANKESLHRQAEERH 340
Cdd:COG1842 35 MEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKarlALEKGREDLAREALERKaeLEAQAEALEAQLAQLEEQV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 341 GNIEEHLRQLEGQLEEKNQELARVRQREKMNEdHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEK---L 417
Cdd:COG1842 115 EKLKEALRQLESKLEELKAKKDTLKARAKAAK-AQEKVNEALSGIDSDDATSALERMEEKIEEMEARAEAAAELAAgdsL 193
|
170
....*....|
gi 2017363566 418 RQEVDQLKGR 427
Cdd:COG1842 194 DDELAELEAD 203
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
13-439 |
7.72e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.67 E-value: 7.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 13 RLGPPHGADADANFEQLMVNMLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSALPQEFATLTRELSMCRE 92
Cdd:pfam12128 445 RLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDE 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 93 QLLEREEEISELKA-ERNNTRLLLEHLECLVSR---HERSLRMTVVKRQAQSPS---GVSSEVEVLKALKSLFeHHKALD 165
Cdd:pfam12128 525 LELQLFPQAGTLLHfLRKEAPDWEQSIGKVISPellHRTDLDPEVWDGSVGGELnlyGVKLDLKRIDVPEWAA-SEEELR 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 166 E---KVRERLRAALERVTTLEEQLAGAHQQVSALQqgAGVRDGAAEEEGTvELGPKRLWKEDTGRVEELQELLEKQNFEL 242
Cdd:pfam12128 604 ErldKAEEALQSAREKQAAAEEQLVQANGELEKAS--REETFARTALKNA-RLDLRRLFDEKQSEKDKKNKALAERKDSA 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 243 SQARERLVTLTTTVTELEEDLGTARRDliKSEELSSKHQRDLREALAQKEDMEERI-TTLEKRYLAAQRE---------- 311
Cdd:pfam12128 681 NERLNSLEAQLKQLDKKHQAWLEEQKE--QKREARTEKQAYWQVVEGALDAQLALLkAAIAARRSGAKAElkaletwykr 758
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 312 ---------------ATSIHDLNDKLENELANKE-------------SLHRQA-EERHGNIEEHLRQLEGQLEEKNQELA 362
Cdd:pfam12128 759 dlaslgvdpdviaklKREIRTLERKIERIAVRRQevlryfdwyqetwLQRRPRlATQLSNIERAISELQQQLARLIADTK 838
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 363 RVRQREKMNEDHNKRLSDTVDRLLSE---------------SNERLQLHLKERMAALEE-KGRLSEEIEKLRQEVDQLKG 426
Cdd:pfam12128 839 LRRAKLEMERKASEKQQVRLSENLRGlrcemsklatlkedaNSEQAQGSIGERLAQLEDlKLKRDYLSESVKKYVEHFKN 918
|
490
....*....|...
gi 2017363566 427 rggpfVDGVHSRS 439
Cdd:pfam12128 919 -----VIADHSGS 926
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
315-425 |
9.11e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 9.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 315 IHDLNDKLENELANKESLHRQAEERHGN-IEEHLRQLEGQLEEknqeLarvrqrekmnEDHNKRLSDTVDRLlSESNERL 393
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTeEEEEIRRLEEQVER----L----------EAEVEELEAELEEK-DERIERL 446
|
90 100 110
....*....|....*....|....*....|..
gi 2017363566 394 QLHLKERMAALEEKGRLSEEIEKLRQEVDQLK 425
Cdd:COG2433 447 ERELSEARSEERREIRKDREISRLDREIERLE 478
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
232-425 |
1.14e-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: 42.83 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 232 QELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQRE 311
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 312 atsIHDLNDKLENELANKESLHR--------------QAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKR 377
Cdd:COG4942 99 ---LEAQKEELAELLRALYRLGRqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2017363566 378 LSDTVDRlLSESNERLQLHLKERMAALEekgRLSEEIEKLRQEVDQLK 425
Cdd:COG4942 176 LEALLAE-LEEERAALEALKAERQKLLA---RLEKELAELAAELAELQ 219
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
272-425 |
1.44e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 272 KSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREatsIHDLNDK---LENELANKESLHRQAEERHGNIEEHLR 348
Cdd:TIGR04523 402 NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE---IKDLTNQdsvKELIIKNLDNTRESLETQLKVLSRSIN 478
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017363566 349 QLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNErlqlhLKERMAALE-EKGRLSEEIEKLRQEVDQLK 425
Cdd:TIGR04523 479 KIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS-----LKEKIEKLEsEKKEKESKISDLEDELNKDD 551
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
59-420 |
1.48e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.80 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 59 QDAIHERDQ---LQRHLNSALPQEFATLTRELSMCREQLLEREEEISELKAER----NNTRLLLEHLECL--VSRHERSL 129
Cdd:pfam17380 281 QKAVSERQQqekFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAaiyaEQERMAMERERELerIRQEERKR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 130 RMTVVKRQAqspsgVSSEVEVLKALKSLFEHHKALDEKVRERLRAAlERVTTLEEQlagahQQVSALQQGAGVRDGAAEE 209
Cdd:pfam17380 361 ELERIRQEE-----IAMEISRMRELERLQMERQQKNERVRQELEAA-RKVKILEEE-----RQRKIQQQKVEMEQIRAEQ 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 210 EgtvelgpkrlwkedTGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEelssKHQRDlreala 289
Cdd:pfam17380 430 E--------------EARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELE----KEKRD------ 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 290 QKEDMEERITTLEKRyLAAQREATsihdLNDKLENELANKESLHRQ---AEERHGNIEEHLRQLEGQLEEknqelaRVRQ 366
Cdd:pfam17380 486 RKRAEEQRRKILEKE-LEERKQAM----IEEERKRKLLEKEMEERQkaiYEEERRREAEEERRKQQEMEE------RRRI 554
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2017363566 367 REKMnedhnkrlsdtvdRLLSESNERLQLHLKERmaaleEKGRLSEEIEKLRQE 420
Cdd:pfam17380 555 QEQM-------------RKATEERSRLEAMERER-----EMMRQIVESEKARAE 590
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
320-424 |
1.53e-03 |
|
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: 42.90 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 320 DKLENELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKE 399
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSE 323
|
90 100
....*....|....*....|....*.
gi 2017363566 400 RMAALEEKGR-LSEEIEKLRQEVDQL 424
Cdd:pfam12128 324 LEALEDQHGAfLDADIETAAADQEQL 349
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
784-848 |
1.55e-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: 1.55e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363566 784 QWDGPTVVSWLElWVGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNALHRLKLRLAIQEM 848
Cdd:pfam00536 2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
898-953 |
1.64e-03 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 38.02 E-value: 1.64e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2017363566 898 EWLPSLGLPQYRSYFMECLVD-ARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 953
Cdd:pfam07647 11 DWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLK-RLGITSVGHRRKILKKIQELK 66
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
294-423 |
1.82e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.58 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 294 MEERITTLEKRYLAAQREATSIHDLNDKLEN---ELANKESLHRQAEE---RHGNIEEHLRQLEGQLEEKNQELARVRQR 367
Cdd:PRK01156 624 IENEANNLNNKYNEIQENKILIEKLRGKIDNykkQIAEIDSIIPDLKEitsRINDIEDNLKKSRKALDDAKANRARLEST 703
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363566 368 EKMNEDHNKRLSDTVdrllSESNERLQlHLKERMAALEEKGRLSEEIEK------LRQEVDQ 423
Cdd:PRK01156 704 IEILRTRINELSDRI----NDINETLE-SMKKIKKAIGDLKRLREAFDKsgvpamIRKSASQ 760
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
81-392 |
2.14e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 81 ATLTRELSMCREQLLEREEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgVSSEVE-------VLKA 153
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAE---LEAELErldassdDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 154 LKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKRLWKEDTGRVEELQE 233
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 234 LLEKQNFELSQARERLVTLTTTV--------TELEEDLGT---------ARRDLIKSEELsSKHQRDLREALaqKEDMEE 296
Cdd:COG4913 770 NLEERIDALRARLNRAEEELERAmrafnrewPAETADLDAdleslpeylALLDRLEEDGL-PEYEERFKELL--NENSIE 846
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 297 RITTLEKRYLAAQREATS-IHDLNDKLEN-ELANKESLHRQAEERHGnieEHLRQLEGQLEEKNqeLARVRQREKMNEDH 374
Cdd:COG4913 847 FVADLLSKLRRAIREIKErIDPLNDSLKRiPFGPGRYLRLEARPRPD---PEVREFRQELRAVT--SGASLFDEELSEAR 921
|
330
....*....|....*...
gi 2017363566 375 NKRLSDTVDRLLSESNER 392
Cdd:COG4913 922 FAALKRLIERLRSEEEES 939
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
227-420 |
2.20e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 227 RVEELQELLEKQNFELSQARERLVTLTTTVTELEeDLGTARRDLIKSEELsskhQRDLREALAQKEDMEE---RITTLEK 303
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERREALQ-RLAEYSWDEIDVASA----EREIAELEAELERLDAssdDLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 304 RYLAAQREAtsihdlnDKLENELANKESLHRQAEERHGNIEEHLRQLEGQLEEKnQELARVRQREKMNEDHNKRLSDTVD 383
Cdd:COG4913 693 QLEELEAEL-------EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA-EDLARLELRALLEERFAAALGDAVE 764
|
170 180 190
....*....|....*....|....*....|....*..
gi 2017363566 384 RLLSESNERlqlhlkERMAALEEKGRLSEEIEKLRQE 420
Cdd:COG4913 765 RELRENLEE------RIDALRARLNRAEEELERAMRA 795
|
|
| SAM_Neurabin-like |
cd09512 |
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ... |
976-1015 |
2.24e-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: 2.24e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2017363566 976 VLVWTNDQVVHWVQSIGLRDYAGNLHESGVHG-ALLALDEN 1015
Cdd:cd09512 4 VSEWSVQQVCQWLMGLGLEQYIPEFTANNIDGqQLLQLDSS 44
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
267-425 |
2.88e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 41.65 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 267 RRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQ---REATSIHDLNDKLENELAN----KESLHRQAEER 339
Cdd:pfam05557 26 KRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEealREQAELNRLKKKYLEALNKklneKESQLADAREV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 340 HGNIEEHLRQLEGQLEEKNQELARVR-QREKMNEDHN---KRLSDtvdrlLSESNERLQLHLKERMAALEEKGRLSEEIE 415
Cdd:pfam05557 106 ISCLKNELSELRRQIQRAELELQSTNsELEELQERLDllkAKASE-----AEQLRQNLEKQQSSLAEAEQRIKELEFEIQ 180
|
170
....*....|
gi 2017363566 416 KLRQEVDQLK 425
Cdd:pfam05557 181 SQEQDSEIVK 190
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
166-379 |
3.60e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 166 EKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAgvrdgaaeEEGTVELgpkrlwKEDTGRVEELQELLEKQNFELSQA 245
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEY--------NELQAEL------EALQAEIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 246 RERlvtltttvteleedLGTARRDLIKSEELSSkhqrdLREALAQKEDMEE---RITTLEKRYLAAQREATSIHDLNDKL 322
Cdd:COG3883 85 REE--------------LGERARALYRSGGSVS-----YLDVLLGSESFSDfldRLSALSKIADADADLLEELKADKAEL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2017363566 323 ENELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLS 379
Cdd:COG3883 146 EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
279-425 |
4.11e-03 |
|
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: 40.64 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 279 KHQRDLREALAQKEDMEERI-------TTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQAEERHgniEEHLRQLE 351
Cdd:cd16269 167 KAEEVLQEFLQSKEAEAEAIlqadqalTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSY---EEHLRQLK 243
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2017363566 352 GQLEEKNQelarvrqrekmnedhnkrlsdtvdRLLSESNERLQLHLKErMAALEEKGrLSEEIEKLRQEVDQLK 425
Cdd:cd16269 244 EKMEEERE------------------------NLLKEQERALESKLKE-QEALLEEG-FKEQAELLQEEIRSLK 291
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
269-424 |
4.40e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 269 DLIKSE-ELSSKHQRDLREALAQkedmeeRITTLEKRYLAAQREATSIHDLNDKLENELANkesLHRQAEERHGNIEEhL 347
Cdd:PHA02562 191 DHIQQQiKTYNKNIEEQRKKNGE------NIARKQNKYDELVEEAKTIKAEIEELTDELLN---LVMDIEDPSAALNK-L 260
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017363566 348 RQLEGQLEEKNQELARVrqrEKMNEDHNkrLSDTVDRLLSESNERLQlHLKERMAALEEKGR-LSEEIEKLRQEVDQL 424
Cdd:PHA02562 261 NTAAAKIKSKIEQFQKV---IKMYEKGG--VCPTCTQQISEGPDRIT-KIKDKLKELQHSLEkLDTAIDELEEIMDEF 332
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
124-420 |
4.46e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 41.01 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 124 RHERSLRMTVvkRQAQSPSGVSSEVEVLKAlKSLFEHHKAL----------DEKVRERL-RAALERVTTLEEQLAGAHQQ 192
Cdd:pfam02029 13 RRAREERRRQ--KEEEEPSGQVTESVEPNE-HNSYEEDSELkpsgqggldeEEAFLDRTaKREERRQKRLQEALERQKEF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 193 VSALQQgagVRDGAAEEEGTVELGPKRLW-KEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLI 271
Cdd:pfam02029 90 DPTIAD---EKESVAERKENNEEEENSSWeKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 272 KSEELSSKHQRDLREALAQKED--MEERITTLEKRYL----AAQREATSIHDLNDKLENELANKESLHRQAEERHGNIE- 344
Cdd:pfam02029 167 EEVPTENFAKEEVKDEKIKKEKkvKYESKVFLDQKRGhpevKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEa 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 345 ----EHLRQLEGQLEEKNQELARVRQREKMNE-DHNKRLSDTVDRLLSESNERLQLHLKERMAALEE-KGRLSEEIEKLR 418
Cdd:pfam02029 247 eqklEELRRRRQEKESEEFEKLRQKQQEAELElEELKKKREERRKLLEEEEQRRKQEEAERKLREEEeKRRMKEEIERRR 326
|
..
gi 2017363566 419 QE 420
Cdd:pfam02029 327 AE 328
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
280-431 |
5.24e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 280 HQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQAEERHGNIEEHLRQLEGQLeeknQ 359
Cdd:PRK04863 521 RLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARI----Q 596
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363566 360 ELARVRQREKMNEDHNKRLSDTVDRLLSESN---ERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGRGGPF 431
Cdd:PRK04863 597 RLAARAPAWLAAQDALARLREQSGEEFEDSQdvtEYMQQLLERERELTVERDELAARKQALDEEIERLSQPGGSE 671
|
|
| SAM_SARM1-like_repeat1 |
cd09501 |
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
898-942 |
6.16e-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: 6.16e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2017363566 898 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHR 942
Cdd:cd09501 11 TWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLR 55
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
302-425 |
8.19e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 8.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 302 EKRYLAAQREATSIHDlNDKLENELANKESLhRQAEERhgnIEEHLRQLEGQLEEKNQELA----RVRQREkmnEDHNKR 377
Cdd:PRK12704 30 EAKIKEAEEEAKRILE-EAKKEAEAIKKEAL-LEAKEE---IHKLRNEFEKELRERRNELQklekRLLQKE---ENLDRK 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2017363566 378 LsdtvdrllsESNERLQLHLKERMAALEEKgrlSEEIEKLRQEVDQLK 425
Cdd:PRK12704 102 L---------ELLEKREEELEKKEKELEQK---QQELEKKEEELEELI 137
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
343-425 |
8.74e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.04 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363566 343 IEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRL-------LSESNERLQLHLKERMAALEEK-GRLSEEI 414
Cdd:COG1842 28 LDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWeekarlaLEKGREDLAREALERKAELEAQaEALEAQL 107
|
90
....*....|.
gi 2017363566 415 EKLRQEVDQLK 425
Cdd:COG1842 108 AQLEEQVEKLK 118
|
|
| |
