|
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 ... |
934-999 |
1.11e-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: 1.11e-43
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568909610 934 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 999
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 ... |
826-896 |
2.35e-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: 2.35e-42
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568909610 826 FAQWDGPTVVSWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEMVSLT 896
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 ... |
1019-1090 |
4.98e-40 |
|
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: 142.07 E-value: 4.98e-40
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568909610 1019 DVLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALVLQIPTQSTQARQVMEREFNNLL 1090
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 ... |
938-997 |
1.35e-30 |
|
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and in adheren junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188894 Cd Length: 60 Bit Score: 114.94 E-value: 1.35e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 938 WIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 997
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 ... |
1027-1088 |
2.28e-26 |
|
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: 103.00 E-value: 2.28e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568909610 1027 QVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALVLQIPTQSTQARQVMEREFNN 1088
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 ... |
833-891 |
4.75e-25 |
|
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of the SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and adherens junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188893 Cd Length: 58 Bit Score: 98.84 E-value: 4.75e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 568909610 833 TVVSWLELWVGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQE 891
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 ... |
1019-1090 |
1.70e-19 |
|
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188969 Cd Length: 72 Bit Score: 83.65 E-value: 1.70e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568909610 1019 DVLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALVLQIPTQSTQARQVMEREFNNLL 1090
Cdd:cd09570 1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
|
|
| SAM_kazrin_repeat2 |
cd09567 |
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ... |
933-997 |
4.48e-16 |
|
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188966 Cd Length: 65 Bit Score: 73.60 E-value: 4.48e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568909610 933 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 997
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 ... |
933-997 |
5.16e-16 |
|
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta potentially is able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.
Pssm-ID: 188965 Cd Length: 63 Bit Score: 73.50 E-value: 5.16e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568909610 933 DMNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLrVHLKMVDSFHRTSLQYGIMCLK 997
Cdd:cd09566 1 KLDTHWV-LRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDL-LHLKVTSALHHASIRRGIQVLR 63
|
|
| SAM_liprin-beta1,2_repeat3 |
cd09569 |
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ... |
1019-1090 |
5.79e-16 |
|
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.
Pssm-ID: 188968 Cd Length: 72 Bit Score: 73.64 E-value: 5.79e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568909610 1019 DVLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALVLQIPTQSTQARQVMEREFNNLL 1090
Cdd:cd09569 1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
|
|
| SAM_kazrin_repeat1 |
cd09564 |
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ... |
827-891 |
1.18e-15 |
|
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrin contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved into interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188963 Cd Length: 70 Bit Score: 72.48 E-value: 1.18e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568909610 827 AQWDGPTVVSWLELWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQE 891
Cdd:cd09564 2 SRWKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
227-472 |
2.59e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.14 E-value: 2.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 227 RVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYL 306
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 307 AAQ----REATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAE 382
Cdd:COG1196 313 ELEerleELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 383 ERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSE----- 457
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAElleea 472
|
250 260
....*....|....*....|
gi 568909610 458 -----EIEKLRQEVDQLKGR 472
Cdd:COG1196 473 alleaALAELLEELAEAAAR 492
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
227-470 |
4.83e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 77.28 E-value: 4.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 227 RVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYL 306
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 307 AAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHG 386
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 387 NIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEV 466
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
....
gi 568909610 467 DQLK 470
Cdd:COG1196 494 LLLL 497
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
933-997 |
6.37e-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: 67.29 E-value: 6.37e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568909610 933 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 997
Cdd:pfam00536 1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
147-469 |
1.20e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.86 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 147 EVEVLKALKSLFEHHKALDEkVRERLRAALERVTTLEEQLAGAHQQVSALQ-QGAGIRDGVAEEEGTVdlgpkrlwKDDT 225
Cdd:TIGR02168 711 EEELEQLRKELEELSRQISA-LRKDLARLEAEVEQLEERIAQLSKELTELEaEIEELEERLEEAEEEL--------AEAE 781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 226 GRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRY 305
Cdd:TIGR02168 782 AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 306 LAAQREATSIHDLNDKLENELANkeslhrqceekarhLQELLEVAEQKLQQTMrkaETLPEVEAELSQRIAALTKAEERH 385
Cdd:TIGR02168 862 EELEELIEELESELEALLNERAS--------------LEEALALLRSELEELS---EELRELESKRSELRRELEELREKL 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 386 GNIEEHLRQLEGQLEEKNQelaRVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKER-------MAALEEKGRLSEE 458
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQE---RLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIkelgpvnLAAIEEYEELKER 1001
|
330
....*....|.
gi 568909610 459 IEKLRQEVDQL 469
Cdd:TIGR02168 1002 YDFLTAQKEDL 1012
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
159-492 |
6.90e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.43 E-value: 6.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 159 EHHKALDEKVRER-LRAALERVTTLEEQLAGAHQQVSALQQgagirdgvAEEEGTVDLgpkrlwKDDTGRVEELQGLLEK 237
Cdd:COG1196 213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEA--------ELEELEAEL------AELEAELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 238 QNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHD 317
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 318 LNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERhgnIEEHLRQLEG 397
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE---LEEALAELEE 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 398 QLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRlsEEIEKLRQEVDQLKGRGGPFV 477
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR--LLLLLEAEADYEGFLEGVKAA 513
|
330
....*....|....*
gi 568909610 478 DGIHSRSHVGSAADV 492
Cdd:COG1196 514 LLLAGLRGLAGAVAV 528
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
170-469 |
9.93e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.78 E-value: 9.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 170 ERLRAALERVT----TLEEQLAGAHQQVSALQQGAGIRdgvaEEEGTVDLgpkRLWkddTGRVEELQGLLEKQNYELSQA 245
Cdd:TIGR02168 182 ERTRENLDRLEdilnELERQLKSLERQAEKAERYKELK----AELRELEL---ALL---VLRLEELREELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 246 RERLVTLSATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRylaaqreatsihdlndkLENE 325
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER-----------------LANL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 326 LANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQE 405
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568909610 406 LARVRQREKMNEDHNKRLSDTVDRLLSESNERLQ-LHLKERMAALEEKGRLSEEIEKLRQEVDQL 469
Cdd:TIGR02168 395 IASLNNEIERLEARLERLEDRRERLQQEIEELLKkLEEAELKELQAELEELEEELEELQEELERL 459
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
20-472 |
2.83e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 2.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 20 ADAEANFEQLMVNMLDEREKLLESLRESQETLVATQSRLQDALHERDQLQRHLNSALpQEFATLTRELSMCREQLLEREE 99
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA-EELLEALRAAAELAAQLEELEE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 100 EISELKAERNNTRLLLEHLEclvSRHERSLRMTVVKRQAQSpsgvsSEVEVLKALKSLFEHHKALDEKVRERLRAALERV 179
Cdd:COG1196 408 AEEALLERLERLEEELEELE---EALAELEEEEEEEEEALE-----EAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 180 TTLEEQLAGAHQQVSALQQGAGIRDGVAEEEGTVDLgpKRLWKDDTGRVEELQGLLEKqnYELSQARERLVTLSATVTEL 259
Cdd:COG1196 480 AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL--LAGLRGLAGAVAVLIGVEAA--YEAALEAALAAALQNIVVED 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 260 EEDLGTARRDLIKSEE-------LSSKHQRDLREALAQKEDMEERITTLEkryLAAQREATSIHDLNDKLENELANKESL 332
Cdd:COG1196 556 DEVAAAAIEYLKAAKAgratflpLDKIRARAALAAALARGAIGAAVDLVA---SDLREADARYYVLGDTLLGRTLVAARL 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 333 HRQCEEKARHLQELLEV---AEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARV 409
Cdd:COG1196 633 EAALRRAVTLAGRLREVtleGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEA 712
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568909610 410 RQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGR 472
Cdd:COG1196 713 EEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
218-472 |
2.83e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 71.64 E-value: 2.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 218 KRLWKDDTGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEE----LSSKHQRDLREALAQKED 293
Cdd:TIGR02169 155 RRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERyqalLKEKREYEGYELLKEKEA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 294 MEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHL--QELLEVAEQ--KLQQTMRKAE-TLPEVE 368
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeEEQLRVKEKigELEAEIASLErSIAEKE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 369 AELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQ-----REKMN------EDHNKRLSDTVDRL------L 431
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEeyaelKEELEdlraelEEVDKEFAETRDELkdyrekL 394
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 568909610 432 SESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGR 472
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
19-409 |
1.88e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.93 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 19 GADAEANFEQLMVNML-----DEREKLLESL----------RESQETLVATQ---SRLQDALHERD-QLQR-HLNSALPQ 78
Cdd:TIGR02168 134 GKRSYSIIEQGKISEIieakpEERRAIFEEAagiskykerrKETERKLERTRenlDRLEDILNELErQLKSlERQAEKAE 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 79 EFATLTRELSmcREQLLEREEEISELKAERNNTRLLLEHLECLVSRHERSLRMTvvkrqaqspsgvSSEVEVLKALKSlf 158
Cdd:TIGR02168 214 RYKELKAELR--ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQEL------------EEKLEELRLEVS-- 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 159 EHHKALDEkVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGIRDGVAEEEGTVDLGPKRLWKDDTGRVEELQGLLEKQ 238
Cdd:TIGR02168 278 ELEEEIEE-LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESL 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 239 NYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATS---- 314
Cdd:TIGR02168 357 EAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaelk 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 315 -IHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKaetlpevEAELSQRIAALTKAEERHGNIEEHLR 393
Cdd:TIGR02168 437 eLQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE-------LAQLQARLDSLERLQENLEGFSEGVK 509
|
410
....*....|....*.
gi 568909610 394 QLEGQLEEKNQELARV 409
Cdd:TIGR02168 510 ALLKNQSGLSGILGVL 525
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
146-470 |
2.13e-11 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 68.23 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 146 SEVEVLKALKSLFEHHKALDEKVRERL--RAALERVTTLEEQLAGAHQQVSALQQGAGIRDGVAEEEGTVDLGPKRLWKD 223
Cdd:pfam17380 266 TENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 224 DTGRVEELQglLEKQNYELSQARERLVTLSAT-VTELEedlgtarRDLIKSEELSSKHQRDLREALAQKEDMEERittlE 302
Cdd:pfam17380 346 RERELERIR--QEERKRELERIRQEEIAMEISrMRELE-------RLQMERQQKNERVRQELEAARKVKILEEER----Q 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 303 KRYLAAQREATSIhdlndKLENELANKESLHRQCEEKARHLQELLEvAEQKLQQTMrkaETLPEVEAELSQRIAALTKAE 382
Cdd:pfam17380 413 RKIQQQKVEMEQI-----RAEQEEARQREVRRLEEERAREMERVRL-EEQERQQQV---ERLRQQEEERKRKKLELEKEK 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 383 ERHGNIEEHLRQ-LEGQLEEKNQELARVRQREKM----NEDHNKRLSDTVDRLLSESNERLQLHLKER-------MAALE 450
Cdd:pfam17380 484 RDRKRAEEQRRKiLEKELEERKQAMIEEERKRKLlekeMEERQKAIYEEERRREAEEERRKQQEMEERrriqeqmRKATE 563
|
330 340
....*....|....*....|
gi 568909610 451 EKGRLsEEIEKLRQEVDQLK 470
Cdd:pfam17380 564 ERSRL-EAMEREREMMRQIV 582
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
21-639 |
2.83e-11 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 68.22 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 21 DAEANFEQLMVNMLDErEKLLESLREsqeTLVATQSRLQDALHERDQLQ----RHLNSALPQEFATLTRELSMCREQLLE 96
Cdd:pfam15921 167 DSNTQIEQLRKMMLSH-EGVLQEIRS---ILVDFEEASGKKIYEHDSMStmhfRSLGSAISKILRELDTEISYLKGRIFP 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 97 REEEISELKAE-RNNTRLLLEH----LECLVSRHERSL-----RMTVVKRQAQSpsgVSSEVEV------------LKAL 154
Cdd:pfam15921 243 VEDQLEALKSEsQNKIELLLQQhqdrIEQLISEHEVEItglteKASSARSQANS---IQSQLEIiqeqarnqnsmyMRQL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 155 KSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHqqvSALQQGAGIRDGVAEEEGTVD-------------------- 214
Cdd:pfam15921 320 SDLESTVSQLRSELREAKRMYEDKIEELEKQLVLAN---SELTEARTERDQFSQESGNLDdqlqklladlhkrekelsle 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 215 -LGPKRLWKDDTG--------------------RVE--------ELQGLLEKQNYELSQARERLVTLSATVTELE----- 260
Cdd:pfam15921 397 kEQNKRLWDRDTGnsitidhlrrelddrnmevqRLEallkamksECQGQMERQMAAIQGKNESLEKVSSLTAQLEstkem 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 261 -----EDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQ 335
Cdd:pfam15921 477 lrkvvEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQ 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 336 CEEKARHLQELLEVAEQKLQ---QTMRKAETLPEVEAELSQRIaaltkaEERHGNIEEhLRQLEGQLEEKNQEL-ARVRQ 411
Cdd:pfam15921 557 MAEKDKVIEILRQQIENMTQlvgQHGRTAGAMQVEKAQLEKEI------NDRRLELQE-FKILKDKKDAKIRELeARVSD 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 412 RE----KMNEDHNKRLSDTVDRllseSNERLQLhLKERMAALEEKGRLSEEIEKLRQEVDQlkgrggpfvdgiHSRSHVG 487
Cdd:pfam15921 630 LElekvKLVNAGSERLRAVKDI----KQERDQL-LNEVKTSRNELNSLSEDYEVLKRNFRN------------KSEEMET 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 488 SAADVRFSLSTAthappglhrrysalrdESAKDWKPSPLPGVLGATTPAFDSdpeisdvdedepggLVGTQVDVISPGGH 567
Cdd:pfam15921 693 TTNKLKMQLKSA----------------QSELEQTRNTLKSMEGSDGHAMKV--------------AMGMQKQITAKRGQ 742
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568909610 568 SDA-QTLAMMLQEQLDAINQEIRMIQEEKE--STELRAEEIETRVTSGSMEALNLTQLRKRGSIPTSLTALSLAS 639
Cdd:pfam15921 743 IDAlQSKIQFLEEAMTNANKEKHFLKEEKNklSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKAS 817
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
227-470 |
4.30e-11 |
|
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: 67.40 E-value: 4.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 227 RVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEkRYL 306
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE-EDL 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 307 AAQREAtsIHDLNDKL-ENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALtkaEERH 385
Cdd:TIGR02169 775 HKLEEA--LNDLEARLsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL---KEQI 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 386 GNIEEHLRQLEGQLEEKNQELARVRQREKmneDHNKRLSDtvdrlLSESNERLQLHLKErmaALEEKGRLSEEIEKLRQE 465
Cdd:TIGR02169 850 KSIEKEIENLNGKKEELEEELEELEAALR---DLESRLGD-----LKKERDELEAQLRE---LERKIEELEAQIEKKRKR 918
|
....*
gi 568909610 466 VDQLK 470
Cdd:TIGR02169 919 LSELK 923
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
38-469 |
4.47e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 67.37 E-value: 4.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 38 EKLLESLRESQETLVATQSRLQDA-LHERdqlqrhLNsALPQEFATLTRElsmcreqllereeeISELKAERNNTRLLLE 116
Cdd:PRK02224 179 ERVLSDQRGSLDQLKAQIEEKEEKdLHER------LN-GLESELAELDEE--------------IERYEEQREQARETRD 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 117 HLECLVSRHERSLrmtvvkrqaqspsgvsSEVEVLKALKSLFEHHKALDEKVRERLRaalERVTTLEEQLAGAHQQVSAL 196
Cdd:PRK02224 238 EADEVLEEHEERR----------------EELETLEAEIEDLRETIAETEREREELA---EEVRDLRERLEELEEERDDL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 197 QQGAGIRDGVAEeegTVDLGPKRLWKDDtgrvEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEEL 276
Cdd:PRK02224 299 LAEAGLDDADAE---AVEARREELEDRD----EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 277 SSKHQRDLREALAQKEDMEERITTLEKRYLAAqreATSIHDLNDKLENELANKESLHRQCEEkarhlqelLEVAEQKLQQ 356
Cdd:PRK02224 372 LEEAREAVEDRREEIEELEEEIEELRERFGDA---PVDLGNAEDFLEELREERDELREREAE--------LEATLRTARE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 357 TMRKAETL------PEVEAEL--SQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQRekmnedhnKRLSDTVD 428
Cdd:PRK02224 441 RVEEAEALleagkcPECGQPVegSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL--------VEAEDRIE 512
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 568909610 429 RLLsESNERLQLHLKERMAALEEKgrlSEEIEKLRQEVDQL 469
Cdd:PRK02224 513 RLE-ERREDLEELIAERRETIEEK---RERAEELRERAAEL 549
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
247-473 |
1.11e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.09 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 247 ERLVTLSATVTELEEDLGTARRDLIKSEELSSKHQRdLREALAQKEDMEERITTLekRYLAAQREATSIHDLNDKLENEL 326
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLEPIRELAER-YAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 327 ANKESLHRQCEEKARHLQELLEVAEQKLQQtmRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQEL 406
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQIRG--NGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEF 382
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568909610 407 ARVRQRekmnedhnkrlsdtVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGRG 473
Cdd:COG4913 383 AALRAE--------------AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK 435
|
|
| SAM_liprin-beta1,2_repeat1 |
cd09563 |
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
826-890 |
1.19e-10 |
|
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta protein contain three copies (repeats) of SAM domain. They may form heterodimers with liprins-alpha through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta is potentially able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.
Pssm-ID: 188962 Cd Length: 64 Bit Score: 58.01 E-value: 1.19e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568909610 826 FAQWDGPTVVSWL-ELWVGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQ 890
Cdd:cd09563 1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
34-470 |
1.41e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.86 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 34 LDEREKLLESLRESQETLVATQSRLQDALHERDQLQRHLnSALPQEFATLTRELSmcreQLLEREEEISELKAERNNTRL 113
Cdd:PRK03918 278 LEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRL-SRLEEEINGIEERIK----ELEEKEERLEELKKKLKELEK 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 114 LLEHLEclvSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKAlDEKVRERLRAALERVTTLEEQLAGAHQQV 193
Cdd:PRK03918 353 RLEELE---ERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKA-KEEIEEEISKITARIGELKKEIKELKKAI 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 194 SALQQGAGI-----RDGVAEEEgtvdlgpKRLWKDDTGRVEELQGLLEKQNYELSQARERLVTLSaTVTELEEDLGTARR 268
Cdd:PRK03918 429 EELKKAKGKcpvcgRELTEEHR-------KELLEEYTAELKRIEKELKEIEEKERKLRKELRELE-KVLKKESELIKLKE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 269 --DLIKS--EELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDK---LENELANKES----LHRQCE 337
Cdd:PRK03918 501 laEQLKEleEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKlaeLEKKLDELEEelaeLLKELE 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 338 EKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQreKMNE 417
Cdd:PRK03918 581 ELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK--KYSE 658
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 568909610 418 DHNKRLSDTVDRL------LSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLK 470
Cdd:PRK03918 659 EEYEELREEYLELsrelagLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLE 717
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
159-468 |
1.50e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.93 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 159 EHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGIRDgvAEEEGTVDlgpkrlwkdDTGRVEELQGLLEKQ 238
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKK--AEEKKKAE---------EAKKAEEDKNMALRK 1582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 239 NYELSQARERLVTLSATVTELE-----EDLGTARRDLIKSEELSsKHQRDLREALAQKEDMEERITTLEKRYLAAQREAT 313
Cdd:PTZ00121 1583 AEEAKKAEEARIEEVMKLYEEEkkmkaEEAKKAEEAKIKAEELK-KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKI 1661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 314 SIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKlqqtmRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLR 393
Cdd:PTZ00121 1662 KAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA-----KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAK 1736
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568909610 394 QlEGQLEEKNQELARVRQREKmnedhnkrlsDTVDRLLSESNERLQLHLKERMAALEEKgrLSEEIEKLRQEVDQ 468
Cdd:PTZ00121 1737 K-EAEEDKKKAEEAKKDEEEK----------KKIAHLKKEEEKKAEEIRKEKEAVIEEE--LDEEDEKRRMEVDK 1798
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
227-474 |
1.96e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.47 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 227 RVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSSK---HQRDLREALAQKEDMEERITTLEK 303
Cdd:PRK03918 187 RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEieeLEKELESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 304 RylaaqreatsIHDLNDKLEnELANKESLHRQCEEKA---RHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTK 380
Cdd:PRK03918 267 R----------IEELKKEIE-ELEEKVKELKELKEKAeeyIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 381 AEERHGNIEEHLRQLE---GQLEEKNQELARVRQREKMNEDHNKRLSDtvdrllsESNERLQLHLKErmaALEEKGRLSE 457
Cdd:PRK03918 336 KEERLEELKKKLKELEkrlEELEERHELYEEAKAKKEELERLKKRLTG-------LTPEKLEKELEE---LEKAKEEIEE 405
|
250
....*....|....*..
gi 568909610 458 EIEKLRQEVDQLKGRGG 474
Cdd:PRK03918 406 EISKITARIGELKKEIK 422
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
20-439 |
2.34e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 20 ADAEANFEQLMVNMLDEREKLLESLRESQETLVATQSRLQDALHERDQLQRHLNSALPQEFATLTRELSmcreqlleREE 99
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL--------LEA 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 100 EISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHH------KALDEKVRERLR 173
Cdd:COG1196 478 ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAleaalaAALQNIVVEDDE 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 174 AALERVTTLEEQLAGAHQQVSALQQGAGIRDGVAEEEGTVDLGPkRLWKDDTGRVEELQGLLEKQNYELSQARERLVTLS 253
Cdd:COG1196 558 VAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAV-DLVASDLREADARYYVLGDTLLGRTLVAARLEAAL 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 254 ATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITtlekryLAAQREATSIHDLNDKLENELANKESLH 333
Cdd:COG1196 637 RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELE------ELAERLAEEELELEEALLAEEEEERELA 710
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 334 RQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEK---N----QEL 406
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvNllaiEEY 790
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 568909610 407 ARVRQR-EKMNEDHN------KRLSDTVDRLLSESNERLQ 439
Cdd:COG1196 791 EELEERyDFLSEQREdleearETLEEAIEEIDRETRERFL 830
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
229-407 |
5.35e-10 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 61.09 E-value: 5.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 229 EELQGLLEKQNY--ELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRyl 306
Cdd:COG1579 4 EDLRALLDLQELdsELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 307 aaQREATSIHDLNDkLENELANKESLHRQCEEKARHLQELLEVAEQKLQqtmrkaetlpEVEAELSQRIAALTKAEERHG 386
Cdd:COG1579 82 --LGNVRNNKEYEA-LQKEIESLKRRISDLEDEILELMERIEELEEELA----------ELEAELAELEAELEEKKAELD 148
|
170 180
....*....|....*....|.
gi 568909610 387 NIEEHLRQLEGQLEEKNQELA 407
Cdd:COG1579 149 EELAELEAELEELEAEREELA 169
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
36-418 |
6.05e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.93 E-value: 6.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 36 EREKLLESLRESQETLVATQSRLQDALHERDQLQRHLNSALpqEFATLTRELsmcreqlleREEEISELKAERNNTRLLL 115
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE--RYQALLKEK---------REYEGYELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 116 EHLECLVSRHERSLRMTVVKRQAQspsgvssEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSA 195
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISEL-------EKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 196 LQQGAgiRDGVAEE-EGTVDLGPKRLWKDD-TGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLiks 273
Cdd:TIGR02169 313 KEREL--EDAEERLaKLEAEIDKLLAEIEElEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL--- 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 274 eelsskhqRDLREALAQ-KEDMEERITTLEKRYLAAQREATSIHDLNdkleNELANKESLHRQCEEKARHLQELLEVAEQ 352
Cdd:TIGR02169 388 --------KDYREKLEKlKREINELKRELDRLQEELQRLSEELADLN----AAIAGIEAKINELEEEKEDKALEIKKQEW 455
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568909610 353 KLQQTmrkaetlpeveaelsqrIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNED 418
Cdd:TIGR02169 456 KLEQL-----------------AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
9-465 |
1.16e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 9 NEGDPLGPPHGADAEANFEQLmvnmlDEREKLLESLRESQETLVATQSRLQDALHERDQLQRHLNSA------------- 75
Cdd:COG4717 53 KEADELFKPQGRKPELNLKEL-----KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELreeleklekllql 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 76 --LPQEFATLTRELSMCREQLLEREEEISELKAERNNTRLLLEHLEclvsRHERSLRMTVVKRQAQSPSGVSSEVEVLKA 153
Cdd:COG4717 128 lpLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELA----ELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 154 LKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAH--QQVSALQQGAGIRDGVAEEEGTVDLGPKRLWKDD------T 225
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAAleERLKEARLLLLIAAALLALLGLGGSLLSLILTIAgvlflvL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 226 GRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRY 305
Cdd:COG4717 284 GLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 306 LAAQREATSIHDLND---KLENELANKESLHRQCEEkarhLQELLEVAEQKLqqtmrkAETLPEVEAELSQriAALTKAE 382
Cdd:COG4717 364 QLEELEQEIAALLAEagvEDEEELRAALEQAEEYQE----LKEELEELEEQL------EELLGELEELLEA--LDEEELE 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 383 ERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDhnkrlSDTVDRLLSEsnerlQLHLKERMAALEEKGR-------- 454
Cdd:COG4717 432 EELEELEEELEELEEELEELREELAELEAELEQLEE-----DGELAELLQE-----LEELKAELRELAEEWAalklalel 501
|
490
....*....|.
gi 568909610 455 LSEEIEKLRQE 465
Cdd:COG4717 502 LEEAREEYREE 512
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
267-472 |
1.33e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 267 RRDLIksEELS--SKHQRDLREALAQKEDMEERIT-------TLEKRY--LAAQRE-ATSIHDLNDKLEnELANKESLHR 334
Cdd:COG1196 157 RRAII--EEAAgiSKYKERKEEAERKLEATEENLErledilgELERQLepLERQAEkAERYRELKEELK-ELEAELLLLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 335 qceekARHLQELLEVAEQKLQQTMRKAETLpevEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREK 414
Cdd:COG1196 234 -----LRELEAELEELEAELEELEAELEEL---EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568909610 415 MNEDHNKRLSDTVDRL---LSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGR 472
Cdd:COG1196 306 RLEERRRELEERLEELeeeLAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
142-472 |
1.81e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 142 SGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQgagIRDGVAEEEGTVDlgpkrlw 221
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE---KVKELKELKEKAE------- 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 222 kddtgRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLgtarrdliksEELSSKHQRdLREALAQKEDMEERITTL 301
Cdd:PRK03918 294 -----EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI----------KELEEKEER-LEELKKKLKELEKRLEEL 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 302 EKRYLAAQrEATSIHDLNDKLENELANKESlhrqceEKarhLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKA 381
Cdd:PRK03918 358 EERHELYE-EAKAKKEELERLKKRLTGLTP------EK---LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKA 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 382 EER-----------HGNIEEHLRqlEGQLEEKNQELARVRQREKMNEDHNKRLSD---TVDRLLSESNERLQLH-LKERM 446
Cdd:PRK03918 428 IEElkkakgkcpvcGRELTEEHR--KELLEEYTAELKRIEKELKEIEEKERKLRKelrELEKVLKKESELIKLKeLAEQL 505
|
330 340 350
....*....|....*....|....*....|....*
gi 568909610 447 AALEEK---------GRLSEEIEKLRQEVDQLKGR 472
Cdd:PRK03918 506 KELEEKlkkynleelEKKAEEYEKLKEKLIKLKGE 540
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
26-472 |
1.92e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.24 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 26 FEQLMVNMLDER-EKLLESLRESQETLVATQSRLQDALHERDQLQRHLNSA-------LPQEFATLTREL---------- 87
Cdd:COG4913 285 FAQRRLELLEAElEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrleqLEREIERLERELeererrrarl 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 88 -SMCREQLLEREEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSP--SGVSSEVEVLKALKSLFEHHkal 164
Cdd:COG4913 365 eALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRelRELEAEIASLERRKSNIPAR--- 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 165 DEKVRERLRAAL---------------------------ERV-----TTL---EEQLAGAHQQVSALQQGAGIR-DGVae 208
Cdd:COG4913 442 LLALRDALAEALgldeaelpfvgelievrpeeerwrgaiERVlggfaLTLlvpPEHYAAALRWVNRLHLRGRLVyERV-- 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 209 eegtvdlgPKRLWKDDTGRVEElQGLLEKQNYELSQARERLVTLSATVTEL-----EEDLGTARRD-----LIKSEelSS 278
Cdd:COG4913 520 --------RTGLPDPERPRLDP-DSLAGKLDFKPHPFRAWLEAELGRRFDYvcvdsPEELRRHPRAitragQVKGN--GT 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 279 KHQRDLREALAQK----EDMEERITTLEKRYLAAQREAtsihdlnDKLENELANKESLHRQCEEKARHLQELLEV--AEQ 352
Cdd:COG4913 589 RHEKDDRRRIRSRyvlgFDNRAKLAALEAELAELEEEL-------AEAEERLEALEAELDALQERREALQRLAEYswDEI 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 353 KLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLS 432
Cdd:COG4913 662 DVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 568909610 433 ESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGR 472
Cdd:COG4913 742 LARLELRALLEERFAAALGDAVERELRENLEERIDALRAR 781
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
146-484 |
2.35e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 146 SEVEVLKALKSLFEHHKALDEkVRERLRAALERVTTLEEQLAGAHQQVSALqqgagiRDGVAEEEGTVDlgpkrlwkDDT 225
Cdd:TIGR02168 223 RELELALLVLRLEELREELEE-LQEELKEAEEELEELTAELQELEEKLEEL------RLEVSELEEEIE--------ELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 226 GRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRY 305
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 306 LAAqreatsiHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEerh 385
Cdd:TIGR02168 368 EEL-------ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE--- 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 386 gnieehlrqLEGQLEEKNQELARVRQREkmnEDHNKRLSDTVDRLLSESNERLQL-----HLKERMAALEekgRLSEEIE 460
Cdd:TIGR02168 438 ---------LQAELEELEEELEELQEEL---ERLEEALEELREELEEAEQALDAAerelaQLQARLDSLE---RLQENLE 502
|
330 340 350
....*....|....*....|....*....|.
gi 568909610 461 KLRQEV-------DQLKGRGGPFVDGIHSRS 484
Cdd:TIGR02168 503 GFSEGVkallknqSGLSGILGVLSELISVDE 533
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
34-469 |
2.62e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 34 LDEREKLLESLRESQETLVATQSRLQDALHERDQLQRHL-NSALPQEFATLTRELSMCREQLLEREEEISELKAERNNTR 112
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLqLLPLYQELEALEAELAELPERLEELEERLEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 113 LLLEHLEclvsRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAH-- 190
Cdd:COG4717 167 ELEAELA----ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAle 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 191 QQVSALQQGAGIRDGVAEEEGTVDLGPKRLWKDD------TGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLG 264
Cdd:COG4717 243 ERLKEARLLLLIAAALLALLGLGGSLLSLILTIAgvlflvLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELE 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 265 TARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLND---KLENELANKESLHRQCEEkar 341
Cdd:COG4717 323 ELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEagvEDEEELRAALEQAEEYQE--- 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 342 hLQELLEVAEQKLqqtmrkAETLPEVEAELSQriAALTKAEERHGNIEEHLRQLEGQLEEKNQELARvrqrekmnedhnk 421
Cdd:COG4717 400 -LKEELEELEEQL------EELLGELEELLEA--LDEEELEEELEELEEELEELEEELEELREELAE------------- 457
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 568909610 422 rlsdtvdrllsesnerlqlhLKERMAALEEKGRLSE---EIEKLRQEVDQL 469
Cdd:COG4717 458 --------------------LEAELEQLEEDGELAEllqELEELKAELREL 488
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
35-474 |
5.01e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.82 E-value: 5.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 35 DEREKLLESLRESQETLVA---TQSRLQDALHERDQLQRHLnSALPQEFATLTRELSMCREQLLEREEEISELKAERNNT 111
Cdd:PRK02224 227 EQREQARETRDEADEVLEEheeRREELETLEAEIEDLRETI-AETEREREELAEEVRDLRERLEELEEERDDLLAEAGLD 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 112 RL----LLEHLECLVSRHERSLRMTVVKRQAQSpsgvssevEVLKALKSLFEHHKALDEKVRErlraALERVTTLEEQLA 187
Cdd:PRK02224 306 DAdaeaVEARREELEDRDEELRDRLEECRVAAQ--------AHNEEAESLREDADDLEERAEE----LREEAAELESELE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 188 GAHQQVSALQ-QGAGIRDGVAEEEGTVDLGPKRLwkddtgrvEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTA 266
Cdd:PRK02224 374 EAREAVEDRReEIEELEEEIEELRERFGDAPVDL--------GNAEDFLEELREERDELREREAELEATLRTARERVEEA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 267 RR---------------------DLIKSEELSSKHQRDLREALAQKEDMEERITTLEKrYLAAQREATSIHDLNDKLENE 325
Cdd:PRK02224 446 EAlleagkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIERLEERREDLEEL 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 326 LANKESL----HRQCEEKARHLQELLEVAEQK---LQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLrqleGQ 398
Cdd:PRK02224 525 IAERRETieekRERAEELRERAAELEAEAEEKreaAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLL----AA 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 399 LEEKNQELARVRQREK----MNEDHNKRLSDTVDR---LLSESNE-RLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLK 470
Cdd:PRK02224 601 IADAEDEIERLREKREalaeLNDERRERLAEKRERkreLEAEFDEaRIEEAREDKERAEEYLEQVEEKLDELREERDDLQ 680
|
....
gi 568909610 471 GRGG 474
Cdd:PRK02224 681 AEIG 684
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
166-476 |
5.42e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 60.74 E-value: 5.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 166 EKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAG-------IRDGVAEEEGTVDLGPKRLwkddTGRVEELQGLLEKQ 238
Cdd:PRK04863 379 EENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIqyqqavqALERAKQLCGLPDLTADNA----EDWLEEFQAKEQEA 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 239 NYELSQARERLVTLSATVTELEEDLGTARRdlIKSEELSSKHQRDLREALAQKEdmeerittlEKRYLAAQREAtsihdl 318
Cdd:PRK04863 455 TEELLSLEQKLSVAQAAHSQFEQAYQLVRK--IAGEVSRSEAWDVARELLRRLR---------EQRHLAEQLQQ------ 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 319 ndkLENELANKESLHRQceekARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQ 398
Cdd:PRK04863 518 ---LRMRLSELEQRLRQ----QQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQ 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 399 LEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESN---ERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGRGGP 475
Cdd:PRK04863 591 LQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQdvtEYMQQLLERERELTVERDELAARKQALDEEIERLSQPGGS 670
|
.
gi 568909610 476 F 476
Cdd:PRK04863 671 E 671
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
261-475 |
6.20e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 6.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 261 EDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKA 340
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 341 RHLQEL----------LEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAE---ERHGNIEEHLRQLEGQLEEKNQELA 407
Cdd:PRK03918 238 EEIEELekeleslegsKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKekaEEYIKLSEFYEEYLDELREIEKRLS 317
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568909610 408 RVRQREKMNEDHNKRLSDTVDRLlsESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGRGGP 475
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERL--EELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTG 383
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
163-414 |
1.83e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 59.20 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 163 ALDEKVRERLRAALERVTTLEEQLAgahQQVSALQQGAGIRDGVAEEEGTVD--LGPKRLWKDDT--GRVEELqgllEKQ 238
Cdd:COG3096 829 AFAPDPEAELAALRQRRSELERELA---QHRAQEQQLRQQLDQLKEQLQLLNklLPQANLLADETlaDRLEEL----REE 901
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 239 NYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELsskhQRDLREALAQKEDMEERITTLEkrYLAAQREATSIHD- 317
Cdd:COG3096 902 LDAAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQL----QADYLQAKEQQRRLKQQIFALS--EVVQRRPHFSYEDa 975
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 318 ---------LNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQ--QTMR--KAETLPEVEAELSQ-RIAALTKAEE 383
Cdd:COG3096 976 vgllgensdLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLAslKSSRdaKQQTLQELEQELEElGVQADAEAEE 1055
|
250 260 270
....*....|....*....|....*....|.
gi 568909610 384 RhgnIEEHLRQLEGQLeekNQELARVRQREK 414
Cdd:COG3096 1056 R---ARIRRDELHEEL---SQNRSRRSQLEK 1080
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
246-472 |
2.25e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.54 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 246 RERLVTLSATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENE 325
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 326 LANKESLHR-------QCEEKARHLQELLE-----VAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLR 393
Cdd:TIGR02169 753 IENVKSELKelearieELEEDLHKLEEALNdlearLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 394 QLEGQLEEKNQEL-ARVRQREKMNEDHNKRLSDTVDRLlsesnERLQLHLKErmaALEEKGRLSEEIEKLRQEVDQLKGR 472
Cdd:TIGR02169 833 KEIQELQEQRIDLkEQIKSIEKEIENLNGKKEELEEEL-----EELEAALRD---LESRLGDLKKERDELEAQLRELERK 904
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
241-465 |
2.80e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 241 ELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREatsIHDLND 320
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE---LEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 321 KLENELANKESLHRQCEEKarhlqelLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERhgnieehLRQLEGQLE 400
Cdd:COG4942 105 ELAELLRALYRLGRQPPLA-------LLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE-------LAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568909610 401 EKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQE 465
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
229-430 |
4.12e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 4.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 229 EELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYlAA 308
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL-AE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 309 QREATSIHDLNDKLENELANKESLhrQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERhgnI 388
Cdd:COG4942 109 LLRALYRLGRQPPLALLLSPEDFL--DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE---L 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568909610 389 EEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRL 430
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
826-892 |
5.12e-08 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 50.76 E-value: 5.12e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568909610 826 FAQWDGPTVVSWLELWvGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEM 892
Cdd:smart00454 1 VSQWSPESVADWLESI-GLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
272-470 |
7.56e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 7.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 272 KSEELSSKHQRDLREALAQKEDMEERIttlekrylaaqREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAE 351
Cdd:COG4717 54 EADELFKPQGRKPELNLKELKELEEEL-----------KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 352 QKLQQTMRKAEtLPEVEAELSQRIAALTKAEERHgnieEHLRQLEGQLEEKNQELARVRQREkmnEDHNKRLSDTVDRLL 431
Cdd:COG4717 123 KLLQLLPLYQE-LEALEAELAELPERLEELEERL----EELRELEEELEELEAELAELQEEL---EELLEQLSLATEEEL 194
|
170 180 190
....*....|....*....|....*....|....*....
gi 568909610 432 SESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLK 470
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
234-470 |
7.78e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.57 E-value: 7.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 234 LLEKQNyELSQARERLVTLSATVTELEEDLGTARRDliKSEELSSKHQRDLREALAQKEDMEERITTLEKrylaaqreat 313
Cdd:TIGR04523 269 LSEKQK-ELEQNNKKIKELEKQLNQLKSEISDLNNQ--KEQDWNKELKSELKNQEKKLEEIQNQISQNNK---------- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 314 SIHDLND---KLENELANKES----LHRQCEEKARHLQELLEVAEQKLQQTmrkaETLPEVEAELSQRIaalTKAEERHG 386
Cdd:TIGR04523 336 IISQLNEqisQLKKELTNSESenseKQRELEEKQNEIEKLKKENQSYKQEI----KNLESQINDLESKI---QNQEKLNQ 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 387 NIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLS--DTVDRLLSESNERLQLHLKERMAALEekgrlsEEIEKLRQ 464
Cdd:TIGR04523 409 QKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTnqDSVKELIIKNLDNTRESLETQLKVLS------RSINKIKQ 482
|
....*.
gi 568909610 465 EVDQLK 470
Cdd:TIGR04523 483 NLEQKQ 488
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
177-469 |
8.70e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 8.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 177 ERVTTLEEQLAGAHQQVSALQQGAGIRDGVAEEEGTVDlgpkRLWKddtgRVEELQGLLEKQNYELSQARERLVTLSATV 256
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIE----RLEE----RREDLEELIAERRETIEEKRERAEELRERA 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 257 TELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKrylaaqreatsIHDLNDKLENELANKESLhrqc 336
Cdd:PRK02224 547 AELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER-----------IRTLLAAIADAEDEIERL---- 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 337 EEKARHLQELLEVAEQKLQQtmrKAETLPEVEAELSQriAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMN 416
Cdd:PRK02224 612 REKREALAELNDERRERLAE---KRERKRELEAEFDE--ARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAV 686
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 568909610 417 EDHNKRLSDtvdrllsesnerlqlhLKERMAALEEKgrlSEEIEKLRQEVDQL 469
Cdd:PRK02224 687 ENELEELEE----------------LRERREALENR---VEALEALYDEAEEL 720
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
61-409 |
8.83e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 8.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 61 ALHERDQLQRHLNSALpQEFATLTRELSMCREQLLEREEEISELKAERNNTRLLLEHLeclvsrheRSLRMTVVKRQAQS 140
Cdd:COG1196 230 LLLKLRELEAELEELE-AELEELEAELEELEAELAELEAELEELRLELEELELELEEA--------QAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 141 PSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGIRDGVAEEEGTVDLGPKRL 220
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 221 WKDDTGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITT 300
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 301 LEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEE-KARHLQELLEVAEQKLQQTMRKAE----TLPEVEAELSQRI 375
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEaEADYEGFLEGVKAALLLAGLRGLAgavaVLIGVEAAYEAAL 540
|
330 340 350
....*....|....*....|....*....|....
gi 568909610 376 AALTKAEERHGNIEEHLRQLEGQLEEKNQELARV 409
Cdd:COG1196 541 EAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRA 574
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
942-997 |
9.77e-08 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 49.99 E-value: 9.77e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 568909610 942 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 997
Cdd:smart00454 11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
183-470 |
1.24e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 56.28 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 183 EEQLAGAHQQVSALQQGAGIRDGVAEEEGTV-----DLGPKRLWKDDTGRVEELQGLLEKQNYELSQARERLVTLSATVT 257
Cdd:pfam15921 162 EDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIlvdfeEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIF 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 258 ELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEerITTLEKRYLAAQREATSIHDLNDKLENELANKESLHrqce 337
Cdd:pfam15921 242 PVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVE--ITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMY---- 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 338 ekARHLQELLEVAEQkLQQTMRKA-----ETLPEVEAELSQRIAALTKAE-------ERHGNIEEHLRQLEGQLEEKNQE 405
Cdd:pfam15921 316 --MRQLSDLESTVSQ-LRSELREAkrmyeDKIEELEKQLVLANSELTEARterdqfsQESGNLDDQLQKLLADLHKREKE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 406 LARVRQREKMNEDHNKRLSDTVDRLLSESNER-----------------LQLHLKERMAALEEKGRLSEEIEKLRQEVDQ 468
Cdd:pfam15921 393 LSLEKEQNKRLWDRDTGNSITIDHLRRELDDRnmevqrleallkamkseCQGQMERQMAAIQGKNESLEKVSSLTAQLES 472
|
..
gi 568909610 469 LK 470
Cdd:pfam15921 473 TK 474
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
253-469 |
2.16e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 253 SATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREatsIHDLNDKLENELANKESL 332
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE---LAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 333 HRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQR 412
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568909610 413 EKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQL 469
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
37-470 |
2.29e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 55.23 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 37 REKLLESLRESQETLVATQSRLQDALHERDQLQRHLNsalpQEFATLTRELSmcrEQLLEREEEISELKAERNNTRlllE 116
Cdd:pfam12128 253 LESAELRLSHLHFGYKSDETLIASRQEERQETSAELN----QLLRTLDDQWK---EKRDELNGELSAADAAVAKDR---S 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 117 HLECLVSRHERSLRMTVVKR---QAQSPSgVSSEVEVL-KALKSLFEHHK-------ALDEKVRERLRAALERVT----- 180
Cdd:pfam12128 323 ELEALEDQHGAFLDADIETAaadQEQLPS-WQSELENLeERLKALTGKHQdvtakynRRRSKIKEQNNRDIAGIKdklak 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 181 ---TLEEQLAGAHQQVSAL------QQGAGIRDGVAEEEGTVD-LGPKRLWKDDTGRVEELQGLLEKQNYELSQARERLV 250
Cdd:pfam12128 402 ireARDRQLAVAEDDLQALeselreQLEAGKLEFNEEEYRLKSrLGELKLRLNQATATPELLLQLENFDERIERAREEQE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 251 TLSATVTELEEDLGTARRdliKSEELSSKHQRDLREALAQKEDMEERITTLEKRylaaqrEATSIHDLNDKLEN------ 324
Cdd:pfam12128 482 AANAEVERLQSELRQARK---RRDQASEALRQASRRLEERQSALDELELQLFPQ------AGTLLHFLRKEAPDweqsig 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 325 ELANKESLHR---QCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKA----EERHGNIEEHLRQLEG 397
Cdd:pfam12128 553 KVISPELLHRtdlDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEAlqsaREKQAAAEEQLVQANG 632
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568909610 398 QLEEKNQELARVRQREKMNEDHNKRLSDtvdrllsesnERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLK 470
Cdd:pfam12128 633 ELEKASREETFARTALKNARLDLRRLFD----------EKQSEKDKKNKALAERKDSANERLNSLEAQLKQLD 695
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
284-464 |
2.40e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.00 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 284 LREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEvaeqklqqtmrKAET 363
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG-----------NVRN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 364 LPEVEAeLSQRIAALtkaEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLK 443
Cdd:COG1579 88 NKEYEA-LQKEIESL---KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
170 180
....*....|....*....|..
gi 568909610 444 ERMAALEE-KGRLSEEIEKLRQ 464
Cdd:COG1579 164 EREELAAKiPPELLALYERIRK 185
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
20-472 |
2.54e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 20 ADAEANFEQLMVNMLDEREKLleslRESQETLVATQSRLQDALHERDQLQRHLNSALPQEfATLTRELSmcreqllEREE 99
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAEL----EELEAELEELESRLEELEEQLETLRSKVAQLELQI-ASLNNEIE-------RLEA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 100 EISELKAERNNTRLLLEHLECLVSRHERS-LRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRE------RL 172
Cdd:TIGR02168 408 RLERLEDRRERLQQEIEELLKKLEEAELKeLQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAaerelaQL 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 173 RAALERVTTLEEQLAGAHQQVSAL----QQGAGIRDGVAE----EEG-----TVDLGPKR---LWKDDTGRVEELQGLLE 236
Cdd:TIGR02168 488 QARLDSLERLQENLEGFSEGVKALlknqSGLSGILGVLSElisvDEGyeaaiEAALGGRLqavVVENLNAAKKAIAFLKQ 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 237 KQN-----YELSQARERL--VTLSATVTELEEDLGTARrDLIKSEELSSK-------HQR---DLREALAQ--KEDMEER 297
Cdd:TIGR02168 568 NELgrvtfLPLDSIKGTEiqGNDREILKNIEGFLGVAK-DLVKFDPKLRKalsyllgGVLvvdDLDNALELakKLRPGYR 646
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 298 ITTLE-----KRYLAAQREATSIHDLNDKlENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELS 372
Cdd:TIGR02168 647 IVTLDgdlvrPGGVITGGSAKTNSSILER-RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS 725
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 373 QRIAA----LTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSD---TVDRLLSESNERLQLhLKER 445
Cdd:TIGR02168 726 RQISAlrkdLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAeieELEAQIEQLKEELKA-LREA 804
|
490 500
....*....|....*....|....*...
gi 568909610 446 MAALE-EKGRLSEEIEKLRQEVDQLKGR 472
Cdd:TIGR02168 805 LDELRaELTLLNEEAANLRERLESLERR 832
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
33-380 |
2.98e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.07 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 33 MLDEREKLLESLRESQETLVATQSRLQDALHERDQLQRHLNsALPQEFATLTRELSMCREQLLEREEEISELKAErnntr 112
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE-QLEQEEEKLKERLEELEEDLSSLEQEIENVKSE----- 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 113 llLEHLECLVSRHERSLrmtvVKRQAQ--------SPSGVSsevEVLKALKSLFEHHKALDEKVRErLRAALERVTTLEE 184
Cdd:TIGR02169 760 --LKELEARIEELEEDL----HKLEEAlndlearlSHSRIP---EIQAELSKLEEEVSRIEARLRE-IEQKLNRLTLEKE 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 185 QLAGAHQQvsALQQGAGIRDGVAEEEGTVDlgpkrlwkDDTGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLG 264
Cdd:TIGR02169 830 YLEKEIQE--LQEQRIDLKEQIKSIEKEIE--------NLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 265 TARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQ 344
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQ 979
|
330 340 350
....*....|....*....|....*....|....*.
gi 568909610 345 ELLEVAEqKLQQTMRKAETLPEVEAELSQRIAALTK 380
Cdd:TIGR02169 980 EYEEVLK-RLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
169-410 |
4.42e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 4.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 169 RERLRAALERVTTLEEQLAGAHQQVSALQQGAGIRDGVAE-EEGTVDLGPkrlWKDDTGRVEELQGLLEKQNYELSQARE 247
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAELDALQERREALQRLAEySWDEIDVAS---AEREIAELEAELERLDASSDDLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 248 RLVTLSATVTELEEDLGTARRDLIKSEelssKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELA 327
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLE----KELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELR 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 328 nkeslhRQCEEKARHLQELLEVAEQKLQQTMRK---------------AETLPEVEAELSQ-----------RIA-ALTK 380
Cdd:COG4913 769 ------ENLEERIDALRARLNRAEEELERAMRAfnrewpaetadldadLESLPEYLALLDRleedglpeyeeRFKeLLNE 842
|
250 260 270
....*....|....*....|....*....|....*
gi 568909610 381 AEER-----HGNIEEHLRQLEGQLEEKNQELARVR 410
Cdd:COG4913 843 NSIEfvadlLSKLRRAIREIKERIDPLNDSLKRIP 877
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
112-351 |
5.20e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 5.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 112 RLLLEHLECLVSRHERslrMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVR-----ERLRAALERVTTLEEQL 186
Cdd:COG4913 228 DALVEHFDDLERAHEA---LEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRlwfaqRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 187 AGAHQQVSALQQGagiRDGVAEEEGTVDlgpKRLWKDDTGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTA 266
Cdd:COG4913 305 ARLEAELERLEAR---LDALREELDELE---AQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 267 RRDLiksEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLE--------NELANKESLHRQCEE 338
Cdd:COG4913 379 AEEF---AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLErrksnipaRLLALRDALAEALGL 455
|
250
....*....|....*.
gi 568909610 339 KARHLQ---ELLEVAE 351
Cdd:COG4913 456 DEAELPfvgELIEVRP 471
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
38-468 |
5.37e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.20 E-value: 5.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 38 EKLLESLRESQETLVATQ---SRLQDALHERDQLQRHLNSALPQEfATLTRELSmcreqllereeEISELKAERNNTRll 114
Cdd:TIGR00618 225 EKELKHLREALQQTQQSHaylTQKREAQEEQLKKQQLLKQLRARI-EELRAQEA-----------VLEETQERINRAR-- 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 115 leHLECLVsrhERSLRMTVVKRQAQspsgvssevevlkalkslfEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVS 194
Cdd:TIGR00618 291 --KAAPLA---AHIKAVTQIEQQAQ-------------------RIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 195 ALQ-QGAGIRDGVAEEEGTvdlgpkrLWKDDTGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGT------AR 267
Cdd:TIGR00618 347 LQTlHSQEIHIRDAHEVAT-------SIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATidtrtsAF 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 268 RDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHdlnDKLENELANKESLHRQCEEK-ARHLQEL 346
Cdd:TIGR00618 420 RDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSL---KEREQQLQTKEQIHLQETRKkAVVLARL 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 347 LEVAEQklQQTMRKAETLPEVEAELSQRIAALT----KAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKR 422
Cdd:TIGR00618 497 LELQEE--PCPLCGSCIHPNPARQDIDNPGPLTrrmqRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSI 574
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 568909610 423 LSDTVDRLLSESNERLQL-----HLKERMAALEEKGRLSEEIEKLRQEVDQ 468
Cdd:TIGR00618 575 LTQCDNRSKEDIPNLQNItvrlqDLTEKLSEAEDMLACEQHALLRKLQPEQ 625
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
35-470 |
5.45e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 5.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 35 DEREKLLESLRESQETLVATQSRLQDALHERDQLqrhlNSALPQefatLTRELSMcreqLLEREEEISELKAERNNTRLL 114
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEVLREINEI----SSELPE----LREELEK----LEKEVKELEELKEEIEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 115 LEHLECLVSRHERSLRMTV-----VKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGA 189
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEerieeLKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 190 HQQVSALQQG-----------AGIRDGVAEEEGTVdlgpkRLWKDDTGRVEELQGLLEK-QNYELSQARERLVTLSATVT 257
Cdd:PRK03918 327 EERIKELEEKeerleelkkklKELEKRLEELEERH-----ELYEEAKAKKEELERLKKRlTGLTPEKLEKELEELEKAKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 258 ELEEDLG--TARRDLIKSE-----------------------ELSSKHQRDL-REALAQKEDMEERITTLEKRYLAAQRE 311
Cdd:PRK03918 402 EIEEEISkiTARIGELKKEikelkkaieelkkakgkcpvcgrELTEEHRKELlEEYTAELKRIEKELKEIEEKERKLRKE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 312 ATsihdlndKLENELANKESLHRQCE--EKARHLQELLE-VAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNI 388
Cdd:PRK03918 482 LR-------ELEKVLKKESELIKLKElaEQLKELEEKLKkYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEEL 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 389 EEHLRQLEGQLEEKNQELARVRQR----------------EKMNEDHNK--RLSDTVDRLLSESnERLQLHLKERMAALE 450
Cdd:PRK03918 555 KKKLAELEKKLDELEEELAELLKEleelgfesveeleerlKELEPFYNEylELKDAEKELEREE-KELKKLEEELDKAFE 633
|
490 500
....*....|....*....|
gi 568909610 451 EKGRLSEEIEKLRQEVDQLK 470
Cdd:PRK03918 634 ELAETEKRLEELRKELEELE 653
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
34-380 |
7.85e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 7.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 34 LDEREKLLESLRESQETLVATQSRLQDALherDQLQRHLNSALPQEFATLTRELSMCREQLLEREEEISELKAERNNTRL 113
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEEL---EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 114 LLEHLECLVSRHER--------------SLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERV 179
Cdd:COG4717 228 ELEQLENELEAAALeerlkearlllliaAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEEL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 180 TTLEEQLAGAHQQVSALQQGAGIRDGVAEEEGTVDLGPKRLWKDDTGRVEELQGLLEKQNYELSQAR------------- 246
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAllaeagvedeeel 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 247 ERLVTLSATVTELEEDLGTARRDL--IKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLEN 324
Cdd:COG4717 388 RAALEQAEEYQELKEELEELEEQLeeLLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE 467
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568909610 325 --ELANKESLHRQCEEKARHLQE---LLEVAEQKLQQTMRKA--ETLPEVEAELSQRIAALTK 380
Cdd:COG4717 468 dgELAELLQELEELKAELRELAEewaALKLALELLEEAREEYreERLPPVLERASEYFSRLTD 530
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
18-471 |
8.75e-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: 53.58 E-value: 8.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 18 HGADAEANFEQLMVNMLDEREKLLESLRESQETLVATQSRLQDALHERDQLQR---HLNSALPQEFATL---TRELSMCR 91
Cdd:pfam15921 318 QLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQesgNLDDQLQKLLADLhkrEKELSLEK 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 92 EQLLE-------REEEISELKAERNNTRLLLEHLECLVsrheRSLRMTVVKRQAQSPSGVSSEVEVLKALKSLfehhKAL 164
Cdd:pfam15921 398 EQNKRlwdrdtgNSITIDHLRRELDDRNMEVQRLEALL----KAMKSECQGQMERQMAAIQGKNESLEKVSSL----TAQ 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 165 DEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGagirdgVAEEEGTVDLGPKRLWKDDTG---RVEELQGLLEKQNYe 241
Cdd:pfam15921 470 LESTKEMLRKVVEELTAKKMTLESSERTVSDLTAS------LQEKERAIEATNAEITKLRSRvdlKLQELQHLKNEGDH- 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 242 LSQARERLVTLSATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERIT----TLEKRYLAAQREATSIHD 317
Cdd:pfam15921 543 LRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINdrrlELQEFKILKDKKDAKIRE 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 318 LNDKLENELANKESLHRQCEEKARHLQELlevaEQKLQQTMRKAETLPEVEAELSQRIAAL-----TKAEErhgnIEEHL 392
Cdd:pfam15921 623 LEARVSDLELEKVKLVNAGSERLRAVKDI----KQERDQLLNEVKTSRNELNSLSEDYEVLkrnfrNKSEE----METTT 694
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 393 RQLEGQLEEKNQELARVRQREKMNEDHN-----------KRLS---DTVDRLLSESN---ERLQLHLKERMAALEEKGRL 455
Cdd:pfam15921 695 NKLKMQLKSAQSELEQTRNTLKSMEGSDghamkvamgmqKQITakrGQIDALQSKIQfleEAMTNANKEKHFLKEEKNKL 774
|
490
....*....|....*.
gi 568909610 456 SEEIEKLRQEVDQLKG 471
Cdd:pfam15921 775 SQELSTVATEKNKMAG 790
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
281-470 |
1.03e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 281 QRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRK 360
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 361 AETLpevEAELSQRIAALTK------------------AEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKR 422
Cdd:COG4942 99 LEAQ---KEELAELLRALYRlgrqpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568909610 423 LSDTVDRlLSESNERLQLHLKERMAALEekgRLSEEIEKLRQEVDQLK 470
Cdd:COG4942 176 LEALLAE-LEEERAALEALKAERQKLLA---RLEKELAELAAELAELQ 219
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
272-478 |
1.63e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.83 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 272 KSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAE 351
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 352 QKLQQTMRKAETLpevEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRL- 430
Cdd:COG4372 101 EELESLQEEAEEL---QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALs 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568909610 431 LSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGRGGPFVD 478
Cdd:COG4372 178 EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKD 225
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
135-470 |
1.64e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 135 KRQAQSPSGVSSEVEVLKALKSLFEHHKALDE--KVRERLRAALERVTTLEEQlagahQQVSALQQGAgirdgvaEEEGT 212
Cdd:PTZ00121 1417 KKKADEAKKKAEEKKKADEAKKKAEEAKKADEakKKAEEAKKAEEAKKKAEEA-----KKADEAKKKA-------EEAKK 1484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 213 VDLGPKRLwKDDTGRVEELQGLLE--KQNYELSQARERLVTLSATVTELEEDLGTARR--------DLIKSEELssKHQR 282
Cdd:PTZ00121 1485 ADEAKKKA-EEAKKKADEAKKAAEakKKADEAKKAEEAKKADEAKKAEEAKKADEAKKaeekkkadELKKAEEL--KKAE 1561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 283 DLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKlqqtmRKAE 362
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK-----KKVE 1636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 363 TLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDtvdrllsESNERLQLHL 442
Cdd:PTZ00121 1637 QLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE-------EAKKAEELKK 1709
|
330 340 350
....*....|....*....|....*....|..
gi 568909610 443 KErmaalEEKGRLSEEIEKLRQE----VDQLK 470
Cdd:PTZ00121 1710 KE-----AEEKKKAEELKKAEEEnkikAEEAK 1736
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
20-484 |
1.68e-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: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 20 ADAEANFEQLMvnMLDEREKLLESLRESQETLVATQSRLQDALHERDQLQRHLNSALPQEFATLTRELSMCREQLLEREE 99
Cdd:pfam12128 454 NQATATPELLL--QLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFP 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 100 EISELKAE-RNNTRLLLEHLECLVSR---HERSLRMTVVKRQAQSPS---GVSSEVEVLKALKSLFeHHKALDEK---VR 169
Cdd:pfam12128 532 QAGTLLHFlRKEAPDWEQSIGKVISPellHRTDLDPEVWDGSVGGELnlyGVKLDLKRIDVPEWAA-SEEELRERldkAE 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 170 ERLRAALERVTTLEEQLAGAHQQVSALQqgAGIRDGVAEEEGTvDLGPKRLwkddTGRVEELQGLLEKQ-NYELSQARER 248
Cdd:pfam12128 611 EALQSAREKQAAAEEQLVQANGELEKAS--REETFARTALKNA-RLDLRRL----FDEKQSEKDKKNKAlAERKDSANER 683
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 249 LVTLSATVTELEEDLGTA----RRDLIkseELSSKHQRDLREALAQKEDMEERI-TTLEKRYLAAQREATSIHDLNDkle 323
Cdd:pfam12128 684 LNSLEAQLKQLDKKHQAWleeqKEQKR---EARTEKQAYWQVVEGALDAQLALLkAAIAARRSGAKAELKALETWYK--- 757
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 324 NELANK--------------ESLHRQCEEKARHLQELLE----VAEQKLQQTMRKAETLPEVEAELsqriaaltkaeerh 385
Cdd:pfam12128 758 RDLASLgvdpdviaklkreiRTLERKIERIAVRRQEVLRyfdwYQETWLQRRPRLATQLSNIERAI-------------- 823
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 386 gnieehlRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSE---------------SNERLQLHLKERMAALE 450
Cdd:pfam12128 824 -------SELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGlrcemsklatlkedaNSEQAQGSIGERLAQLE 896
|
490 500 510
....*....|....*....|....*....|....*
gi 568909610 451 E-KGRLSEEIEKLRQEVDQLKGrggpfVDGIHSRS 484
Cdd:pfam12128 897 DlKLKRDYLSESVKKYVEHFKN-----VIADHSGS 926
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
281-468 |
1.96e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 281 QRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELankESLHRQCEEKARHLQELLEVAEQKLQQTMRK 360
Cdd:COG3883 22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI---DKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 361 AETLPEVEA--------ELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLS 432
Cdd:COG3883 99 GGSVSYLDVllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 568909610 433 ESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQ 468
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
264-472 |
2.24e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 264 GTARRDLIKSEELSskhqRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHL 343
Cdd:TIGR02169 667 LFSRSEPAELQRLR----ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 344 QELLEVAEQKLqqTMRKAEtLPEVEAELSQRIAALTKAEERHGNIEEHL-----RQLEGQLEEKNQELARVRQR-----E 413
Cdd:TIGR02169 743 EEDLSSLEQEI--ENVKSE-LKELEARIEELEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEARlreieQ 819
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568909610 414 KMNEDHNKR--LSDTVDRLLSESNErLQLHLKERMAALEE----KGRLSEEIEKLRQEVDQLKGR 472
Cdd:TIGR02169 820 KLNRLTLEKeyLEKEIQELQEQRID-LKEQIKSIEKEIENlngkKEELEEELEELEAALRDLESR 883
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
20-465 |
2.90e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 20 ADAEANFEQLMVNMLDEREKLLESLRESQETLVATQSRLQDALHERDQLQRHLN------SALPQEFATLTRELSMCREQ 93
Cdd:COG4913 376 PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAslerrkSNIPARLLALRDALAEALGL 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 94 LLEREEEISEL------------KAER----NNTRLLLEH------LECLVSRH-ERSLRMTVVKRQAQSPSGVSSEVEV 150
Cdd:COG4913 456 DEAELPFVGELievrpeeerwrgAIERvlggFALTLLVPPehyaaaLRWVNRLHlRGRLVYERVRTGLPDPERPRLDPDS 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 151 LkALKSLFEHHKALDEkVRERL--RAALERVTTlEEQLAGAHQQVSAlqqgagirdgvaeeEGTVDLGPKRLWKDDTGRV 228
Cdd:COG4913 536 L-AGKLDFKPHPFRAW-LEAELgrRFDYVCVDS-PEELRRHPRAITR--------------AGQVKGNGTRHEKDDRRRI 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 229 eelqglleKQNYEL-SQARERLVTLSATVTELEEDLGTARRDLIKSEELsSKHQRDLREALAQKEDMEERittlEKRYLA 307
Cdd:COG4913 599 --------RSRYVLgFDNRAKLAALEAELAELEEELAEAEERLEALEAE-LDALQERREALQRLAEYSWD----EIDVAS 665
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 308 AQREatsIHDLNDKLENELANKESLhrqceekaRHLQELLEVAEQKLQqtmrkaetlpEVEAELSQRIAALTKAEERHGN 387
Cdd:COG4913 666 AERE---IAELEAELERLDASSDDL--------AALEEQLEELEAELE----------ELEEELDELKGEIGRLEKELEQ 724
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568909610 388 IEEHLRQLEGQLEEKnQELARVRQREKMNEDHNKRLSDTVDRLLSESNERlqlhlkERMAALEEKGRLSEEIEKLRQE 465
Cdd:COG4913 725 AEEELDELQDRLEAA-EDLARLELRALLEERFAAALGDAVERELRENLEE------RIDALRARLNRAEEELERAMRA 795
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
235-472 |
3.34e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.67 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 235 LEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREAts 314
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 315 ihdlnDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGnIEEHLRQ 394
Cdd:COG4372 118 -----EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQA-LDELLKE 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568909610 395 LEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGR 472
Cdd:COG4372 192 ANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILV 269
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
31-452 |
5.22e-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: 5.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 31 VNMLDEREKLL-ESLRESQETLVATQSRLQD-------------ALHERDQLQRHLNSALPQEFATLTRELSmcrEQLLE 96
Cdd:pfam05483 270 ANQLEEKTKLQdENLKELIEKKDHLTKELEDikmslqrsmstqkALEEDLQIATKTICQLTEEKEAQMEELN---KAKAA 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 97 REEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgvsSEVEVLKALKS-----LFEHHKALDEKvrER 171
Cdd:pfam05483 347 HSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS-----SELEEMTKFKNnkeveLEELKKILAED--EK 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 172 LRAALERVTTLEEQLAGAHQQVSALQQGAGIRDGVAEEEGTVDLGPKRLWkddTGRVEELQGLLEKQ------------- 238
Cdd:pfam05483 420 LLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHY---LKEVEDLKTELEKEklknieltahcdk 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 239 ----NYELSQ---------------------ARERLV----TLSATVTELEEDLGTARRDLI-----------KSEELSS 278
Cdd:pfam05483 497 llleNKELTQeasdmtlelkkhqediinckkQEERMLkqieNLEEKEMNLRDELESVREEFIqkgdevkckldKSEENAR 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 279 KHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLN---------------------DKLENELANKESLHRQCE 337
Cdd:pfam05483 577 SIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENkalkkkgsaenkqlnayeikvNKLELELASAKQKFEEII 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 338 EKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRI--AALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKM 415
Cdd:pfam05483 657 DNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIdkRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQE 736
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 568909610 416 NEDHNK----RLSDTVDRLLS---------ESNERLQLHLKERMAALEEK 452
Cdd:pfam05483 737 QSSAKAaleiELSNIKAELLSlkkqleiekEEKEKLKMEAKENTAILKDK 786
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
227-371 |
5.87e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.77 E-value: 5.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 227 RVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEEL--SSKHQRDLREALAQKEDMEERITTLEKR 304
Cdd:COG1579 32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgNVRNNKEYEALQKEIESLKRRISDLEDE 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568909610 305 YLAAQREATSIHDLNDKLENELANKEslhRQCEEKARHLQELLEVAEQKLQQTMRKAETL-PEVEAEL 371
Cdd:COG1579 112 ILELMERIEELEEELAELEAELAELE---AELEEKKAELDEELAELEAELEELEAEREELaAKIPPEL 176
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
227-411 |
7.97e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 7.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 227 RVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEElsskhqrdlrEALAQKEDMEERITTLEKRYL 306
Cdd:COG3883 24 ELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA----------EIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 307 AAQR------------EATSIHDLNDKLEN----ELANKESLHRQCEEKAR--HLQELLEVAEQKLQQTMRKAET-LPEV 367
Cdd:COG3883 94 ALYRsggsvsyldvllGSESFSDFLDRLSAlskiADADADLLEELKADKAEleAKKAELEAKLAELEALKAELEAaKAEL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568909610 368 EAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQ 411
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
31-468 |
9.41e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.90 E-value: 9.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 31 VNMLDEREKLLESLRESQETLVATQSRLQDALHERDQLQ-------------RHLNSALPQEFATLTRELSMCREQLLER 97
Cdd:PRK01156 321 INKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEgyemdynsylksiESLKKKIEEYSKNIERMSAFISEILKIQ 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 98 EEEISELKAERNNTRLLLEHLECLVSRHERSLRmtvvkrqaqspSGVSSEVEVLKALKSLFEHHKAL-------DEKVRE 170
Cdd:PRK01156 401 EIDPDAIKKELNEINVKLQDISSKVSSLNQRIR-----------ALRENLDELSRNMEMLNGQSVCPvcgttlgEEKSNH 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 171 RLRAALERVTTLEEQLAGAHQQVSALQQGagIRDGVAEEEgtvdlgpkRLWKDDTGRVEELQGLLEKQNYELSQARERLV 250
Cdd:PRK01156 470 IINHYNEKKSRLEEKIREIEIEVKDIDEK--IVDLKKRKE--------YLESEEINKSINEYNKIESARADLEDIKIKIN 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 251 TLSATVTELE-----------EDLGTARRDLIKSeeLSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLN 319
Cdd:PRK01156 540 ELKDKHDKYEeiknrykslklEDLDSKRTSWLNA--LAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYI 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 320 D----KLENELANKESLHRQCEEKARHLQELLEvaeqklqqtmrKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQL 395
Cdd:PRK01156 618 DksirEIENEANNLNNKYNEIQENKILIEKLRG-----------KIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKS 686
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568909610 396 EGQLEEKNQELARVRQREKMNEDHNKRLSDTVdrllSESNERLQlHLKERMAALEEKGRLSEEIEK------LRQEVDQ 468
Cdd:PRK01156 687 RKALDDAKANRARLESTIEILRTRINELSDRI----NDINETLE-SMKKIKKAIGDLKRLREAFDKsgvpamIRKSASQ 760
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
27-469 |
9.41e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.97 E-value: 9.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 27 EQLMVNMLDEREKLLE-SLRESQETLVATQSRL-QDALHERDQLQ-RHLNSALPQEFATLTRELSMCREQLLEREEEISE 103
Cdd:TIGR00618 408 EQATIDTRTSAFRDLQgQLAHAKKQQELQQRYAeLCAAAITCTAQcEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETR 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 104 LKAERNNTRLLLEHLECLVsrhERSLRMTVVKRQAQSPSGVSSEvEVLKALKSLFEHHKALdEKVRERLRAALERVTTLE 183
Cdd:TIGR00618 488 KKAVVLARLLELQEEPCPL---CGSCIHPNPARQDIDNPGPLTR-RMQRGEQTYAQLETSE-EDVYHQLTSERKQRASLK 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 184 EQLAGAHQQVSALQQ-----GAGIRDGVAEEEGTVDLGPKRLWKDDTGRVEELQGLLEKQ----NYELS----QARERLV 250
Cdd:TIGR00618 563 EQMQEIQQSFSILTQcdnrsKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQpeqdLQDVRlhlqQCSQELA 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 251 TLSATVTELEEDLG------TARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDlNDKLEN 324
Cdd:TIGR00618 643 LKLTALHALQLTLTqervreHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEE-YDREFN 721
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 325 ELANKESLHRQceekarHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEG----QLE 400
Cdd:TIGR00618 722 EIENASSSLGS------DLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQffnrLRE 795
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568909610 401 EKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQL 469
Cdd:TIGR00618 796 EDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQL 864
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
1020-1090 |
9.83e-06 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 44.18 E-value: 9.83e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568909610 1020 VLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALdeNFDHNTLAlvlQIPTQSTQARQVMEREFNNLL 1090
Cdd:pfam07647 1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK---RLGITSVGHRRKILKKIQELK 66
|
|
| SAM_superfamily |
cd09487 |
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
942-993 |
1.08e-05 |
|
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.
Pssm-ID: 188886 [Multi-domain] Cd Length: 56 Bit Score: 43.77 E-value: 1.08e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 568909610 942 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGI 993
Cdd:cd09487 4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
30-415 |
1.12e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 49.30 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 30 MVNMLDEREKLLESLRESQETLVATQSRLQDALHERDQLQRHLNS------ALPQEFATLTRELSmcreqllereeeisE 103
Cdd:pfam19220 15 MADRLEDLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQeraaygKLRRELAGLTRRLS--------------A 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 104 LKAERNNTRLLLEHLECLVSRHER---SLRMTVVKRQAQSPS---GVSSEVEVLKALKslfEHHKALdekvRERLRAALE 177
Cdd:pfam19220 81 AEGELEELVARLAKLEAALREAEAakeELRIELRDKTAQAEAlerQLAAETEQNRALE---EENKAL----REEAQAAEK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 178 RVTTLEEQLAGAHQqvsalqqgagiRDGVAEEEGTVdlgpkrlwkddtgrveeLQGLLEKQNYELSQarerlvtLSATVT 257
Cdd:pfam19220 154 ALQRAEGELATARE-----------RLALLEQENRR-----------------LQALSEEQAAELAE-------LTRRLA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 258 ELEEDLGTARRDLIKSE----ELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLH 333
Cdd:pfam19220 199 ELETQLDATRARLRALEgqlaAEQAERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAI 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 334 RQCEEKARH--------------LQELLEVAEQKLQQTMRKAETLPEVEAELSQRIA----ALTKAEERHGNIEEHLRQL 395
Cdd:pfam19220 279 RAAERRLKEasierdtlerrlagLEADLERRTQQFQEMQRARAELEERAEMLTKALAakdaALERAEERIASLSDRIAEL 358
|
410 420
....*....|....*....|....*..
gi 568909610 396 EGQ-------LEEKNQELARVRQREKM 415
Cdd:pfam19220 359 TKRfeveraaLEQANRRLKEELQRERA 385
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
227-465 |
1.68e-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: 48.27 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 227 RVEELQGLLEKQNYELSQA-RERLvTLSATVTELEEDLgtarRDLIKSEE-LSSKHQRDLREALAQKEDMEerITTLEKR 304
Cdd:pfam15905 95 RLQALEEELEKVEAKLNAAvREKT-SLSASVASLEKQL----LELTRVNElLKAKFSEDGTQKKMSSLSME--LMKLRNK 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 305 YLAAQREATsihDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEER 384
Cdd:pfam15905 168 LEAKMKEVM---AKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 385 hgnieehLRQLEGQLEEKNQELARVRQREKMNEDHN-----------KRLSDTVDRLLSESNERLQLHLKErMAALEEKG 453
Cdd:pfam15905 245 -------IAQLEELLKEKNDEIESLKQSLEEKEQELskqikdlnekcKLLESEKEELLREYEEKEQTLNAE-LEELKEKL 316
|
250
....*....|...
gi 568909610 454 RL-SEEIEKLRQE 465
Cdd:pfam15905 317 TLeEQEHQKLQQK 329
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
235-470 |
2.52e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.81 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 235 LEKQNYELSQARERLVTLSATVTELEEDLgtarrdliKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATS 314
Cdd:pfam02463 171 KKEALKKLIEETENLAELIIDLEELKLQE--------LKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 315 IHDLNDK------------LENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIaaLTKAE 382
Cdd:pfam02463 243 QELLRDEqeeiesskqeieKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEK--LKESE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 383 ERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKL 462
Cdd:pfam02463 321 KEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELK 400
|
....*...
gi 568909610 463 RQEVDQLK 470
Cdd:pfam02463 401 SEEEKEAQ 408
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
1020-1091 |
2.96e-05 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 43.05 E-value: 2.96e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568909610 1020 VLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHntlalVLQIPTQSTQARQVMEREFNNLLA 1091
Cdd:smart00454 1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEED-----LKELGITKLGHRKKILKAIQKLKE 67
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
165-470 |
3.49e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.12 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 165 DEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGIRDGVAEEEGTVDlgpkrlwkDDTGRVEELQGLLEKQNYELSQ 244
Cdd:TIGR00606 790 DVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELD--------TVVSKIELNRKLIQDQQEQIQH 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 245 ARERLVTLSATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLEN 324
Cdd:TIGR00606 862 LKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQD 941
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 325 ELankESLHRQCEEKARHLQELLE-VAEQKLQQTMRKaetlpevEAELSQRIAALTKAEERHGNIEEHLRQLEgqleekn 403
Cdd:TIGR00606 942 KV---NDIKEKVKNIHGYMKDIENkIQDGKDDYLKQK-------ETELNTVNAQLEECEKHQEKINEDMRLMR------- 1004
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568909610 404 QELARVRQREKMNEDHNKRLsdTVDRLLSESNERLQLHLKE--RMAALEEKgrlsEEIEKLRQEVDQLK 470
Cdd:TIGR00606 1005 QDIDTQKIQERWLQDNLTLR--KRENELKEVEEELKQHLKEmgQMQVLQMK----QEHQKLEENIDLIK 1067
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
135-472 |
3.72e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 135 KRQAQSPSGVSSEVEVL-KALKSLFEHHKALDEKvRERLRAALERVTTLEEQLAGAHQQVSALQQGAGIRDGVAEEEGTv 213
Cdd:COG4717 60 KPQGRKPELNLKELKELeEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 214 dlgpKRLWKDDTGRVEELqgllEKQNYELSQARERLVTLSATVTELEEDLGTARRDLikseelSSKHQRDLREALAQKED 293
Cdd:COG4717 138 ----EAELAELPERLEEL----EERLEELRELEEELEELEAELAELQEELEELLEQL------SLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 294 MEERITTLEKRYLAAQREATSIHDLNDKLENE------------------------------------------------ 325
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENEleaaaleerlkearlllliaaallallglggsllsliltiagvlflvl 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 326 ---------LANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVE-AELSQRIAALTKAEERHGNIEEHLRQL 395
Cdd:COG4717 284 gllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSpEELLELLDRIEELQELLREAEELEEEL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 396 E-GQLEEKNQEL-------------ARVRQREKMNEDhNKRLSDTVDRLLSESNERLQLHLKERMAALEEK-GRLSEEIE 460
Cdd:COG4717 364 QlEELEQEIAALlaeagvedeeelrAALEQAEEYQEL-KEELEELEEQLEELLGELEELLEALDEEELEEElEELEEELE 442
|
410
....*....|..
gi 568909610 461 KLRQEVDQLKGR 472
Cdd:COG4717 443 ELEEELEELREE 454
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
230-470 |
4.06e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.71 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 230 ELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERIttlekrylaaQ 309
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKEN----------Q 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 310 REATSIHDLNDK---LENELANKESLHRQCEEKARHLQ---ELLEVAEQKLQQTMRKAETlpEVEaELSQRIAALTKAEE 383
Cdd:TIGR04523 381 SYKQEIKNLESQindLESKIQNQEKLNQQKDEQIKKLQqekELLEKEIERLKETIIKNNS--EIK-DLTNQDSVKELIIK 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 384 RHGNIEEHLRQ----LEGQ-------LEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNErlqlhLKERMAALE-- 450
Cdd:TIGR04523 458 NLDNTRESLETqlkvLSRSinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS-----LKEKIEKLEse 532
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 568909610 451 -----------------------------EKGRLSEEIEKLRQEVDQLK 470
Cdd:TIGR04523 533 kkekeskisdledelnkddfelkkenlekEIDEKNKEIEELKQTQKSLK 581
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
281-472 |
4.47e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 4.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 281 QRDLREALAQKEDMEERIttlekrylaaqrEATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRK 360
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEK------------EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEER 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 361 AETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQL 440
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDR 329
|
170 180 190
....*....|....*....|....*....|..
gi 568909610 441 HLKERMAAleekGRLSEEIEKLRQEVDQLKGR 472
Cdd:PRK02224 330 LEECRVAA----QAHNEEAESLREDADDLEER 357
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
227-469 |
5.89e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 47.26 E-value: 5.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 227 RVEELQGLLEKQNYELSQARERLVtlsatvtELEEDLGTAR-----RDLIKSEELSSKHQRDLREA----LAQKEDMEER 297
Cdd:COG5185 276 SSKRLNENANNLIKQFENTKEKIA-------EYTKSIDIKKateslEEQLAAAEAEQELEESKRETetgiQNLTAEIEQG 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 298 ITTLEKRYLAAQREATSIHDLND------KLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAEtlpeveael 371
Cdd:COG5185 349 QESLTENLEAIKEEIENIVGEVElsksseELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAAD--------- 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 372 sqriaalTKAEERHGNIEEHLRQLEgQLEEKNQELAR--VRQREKMNEDHNKRLSDTVDRLLSE-------SNERLQlHL 442
Cdd:COG5185 420 -------RQIEELQRQIEQATSSNE-EVSKLLNELISelNKVMREADEESQSRLEEAYDEINRSvrskkedLNEELT-QI 490
|
250 260 270
....*....|....*....|....*....|..
gi 568909610 443 KERMAAL-----EEKGRLSEEIEKLRQEVDQL 469
Cdd:COG5185 491 ESRVSTLkatleKLRAKLERQLEGVRSKLDQV 522
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
320-470 |
6.34e-05 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 45.44 E-value: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 320 DKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAEtlPEVEAELSQRIAALTKAEERHG-----------NI 388
Cdd:pfam04012 39 VKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGN--EELAREALAEKKSLEKQAEALEtqlaqqrsaveQL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 389 EEHLRQLEGQLEEKNQELARVRQREKMNEdHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEK---LRQE 465
Cdd:pfam04012 117 RKQLAALETKIQQLKAKKNLLKARLKAAK-AQEAVQTSLGSLSTSSATDSFERIEEKIEEREARADAAAELASavdLDAK 195
|
....*
gi 568909610 466 VDQLK 470
Cdd:pfam04012 196 LEQAG 200
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
164-412 |
7.80e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 7.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 164 LDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQG-AGIRdgvaEEEGTVDLGPKRlwKDDTGRVEELQGllekqnyEL 242
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAAlEEFR----QKNGLVDLSEEA--KLLLQQLSELES-------QL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 243 SQARERLVTLSATVTELEEDLGTARRDLikSEELSSKHQRDLREALAQkedMEERITTLEKRYLAAQREATSihdlndkL 322
Cdd:COG3206 229 AEARAELAEAEARLAALRAQLGSGPDAL--PELLQSPVIQQLRAQLAE---LEAELAELSARYTPNHPDVIA-------L 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 323 ENELANKEslhrqceekarhlQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEK 402
Cdd:COG3206 297 RAQIAALR-------------AQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVA 363
|
250
....*....|
gi 568909610 403 NQELARVRQR 412
Cdd:COG3206 364 RELYESLLQR 373
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
166-476 |
1.16e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.48 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 166 EKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAG----IRDGVAEEEGTVDLgPKRLWKDDTGRVEELQGLLEKQNYE 241
Cdd:COG3096 378 AEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIqyqqAVQALEKARALCGL-PDLTPENAEDYLAAFRAKEQQATEE 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 242 LSQARERLVTLSATVTELEEDLGTARRdlIKSE-ELSSKHQRdLREALAQKEdmeerittlEKRYLAAQREAtsihdlnd 320
Cdd:COG3096 457 VLELEQKLSVADAARRQFEKAYELVCK--IAGEvERSQAWQT-ARELLRRYR---------SQQALAQRLQQ-------- 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 321 kLENELANKEslhrQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLE 400
Cdd:COG3096 517 -LRAQLAELE----QRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLR 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 401 EKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNE----RLQLHLKERMAALEEKgRLSEEIEKLRQEVDQLKGRGGPF 476
Cdd:COG3096 592 ARIKELAARAPAWLAAQDALERLREQSGEALADSQEvtaaMQQLLEREREATVERD-ELAARKQALESQIERLSQPGGAE 670
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
258-470 |
1.33e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 45.26 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 258 ELEEDLGTARRDLI-KSEELSSKHQRDLREALAQkeDMEERITTLE-------KRYLAAQREATSIHDLNDK-------- 321
Cdd:cd16269 94 KLMEQLEEKKEEFCkQNEEASSKRCQALLQELSA--PLEEKISQGSysvpggyQLYLEDREKLVEKYRQVPRkgvkaeev 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 322 LENELANKESlhrqcEEKArHLQ--ELLEVAEQKLQQTMRKAETLpEVEAELSQRIAALT--KAEERHGNIEEHLRQLEG 397
Cdd:cd16269 172 LQEFLQSKEA-----EAEA-ILQadQALTEKEKEIEAERAKAEAA-EQERKLLEEQQRELeqKLEDQERSYEEHLRQLKE 244
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568909610 398 QLEEKNQelarvrqrekmnedhnkrlsdtvdRLLSESNERLQLHLKErMAALEEKGrLSEEIEKLRQEVDQLK 470
Cdd:cd16269 245 KMEEERE------------------------NLLKEQERALESKLKE-QEALLEEG-FKEQAELLQEEIRSLK 291
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
154-417 |
1.35e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 154 LKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQgagirdgvaeeegtvdlgpkrlwkddtgRVEELQG 233
Cdd:COG4372 15 LFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQARE----------------------------ELEQLEE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 234 LLEKQNYELSQARERLVTLsatvteleedlgtaRRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREAT 313
Cdd:COG4372 67 ELEQARSELEQLEEELEEL--------------NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 314 SIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMrkaetlpevEAELSQRIAALTKAEERHGNIEEHLR 393
Cdd:COG4372 133 QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS---------EAEAEQALDELLKEANRNAEKEEELA 203
|
250 260
....*....|....*....|....
gi 568909610 394 QLEGQLEEKNQELARVRQREKMNE 417
Cdd:COG4372 204 EAEKLIESLPRELAEELLEAKDSL 227
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
105-464 |
1.40e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 105 KAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALkslfEHHKALDEKVRERLRAALERVTTLEE 184
Cdd:PTZ00121 1244 KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD----EAKKAEEKKKADEAKKKAEEAKKADE 1319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 185 qlagAHQQVSALQQGAGIRDGVAEEEGTVDLGPK---RLWKDDTGRVEELQGLLEKQNYELSQARERLVTLSATVTELEE 261
Cdd:PTZ00121 1320 ----AKKKAEEAKKKADAAKKKAEEAKKAAEAAKaeaEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE 1395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 262 DLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREAtsiHDLNDKLEnELANKESLHRQCEEKaR 341
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA---DEAKKKAE-EAKKAEEAKKKAEEA-K 1470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 342 HLQELLEVAEQKlqqtmRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNK 421
Cdd:PTZ00121 1471 KADEAKKKAEEA-----KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK 1545
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 568909610 422 RLSDTVDRL--LSESNERLQLHLKERmaALEEKGRLSEEIEKLRQ 464
Cdd:PTZ00121 1546 KKADELKKAeeLKKAEEKKKAEEAKK--AEEDKNMALRKAEEAKK 1588
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
169-465 |
1.52e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.63 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 169 RERLRAALERVTTLEEQLAGAHQQVSALQQGAGIRDGVAEEEGTVDLGPKRLWKDDTGRVEE-----LQGLLEKQNYELS 243
Cdd:pfam02029 12 RRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREErrqkrLQEALERQKEFDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 244 QARE--RLVTLSATVTELEEDLGTARRDLIKSEELSSK-----------HQRDLREALAQ---KEDMEERITTLEKRYLA 307
Cdd:pfam02029 92 TIADekESVAERKENNEEEENSSWEKEEKRDSRLGRYKeeeteirekeyQENKWSTEVRQaeeEGEEEEDKSEEAEEVPT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 308 AQREATSIHDLNDKLENELA--NKESLHRQ---CEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAE 382
Cdd:pfam02029 172 ENFAKEEVKDEKIKKEKKVKyeSKVFLDQKrghPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 383 ErhgnieehLRQLEGQLEEKNQELARVRQREKMNE-DHNKRLSDTVDRLLSESNERLQLHLKERMAALEE-KGRLSEEIE 460
Cdd:pfam02029 252 E--------LRRRRQEKESEEFEKLRQKQQEAELElEELKKKREERRKLLEEEEQRRKQEEAERKLREEEeKRRMKEEIE 323
|
....*
gi 568909610 461 KLRQE 465
Cdd:pfam02029 324 RRRAE 328
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
301-472 |
1.63e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 301 LEKRYLAAQREATSIHDLNDKLE-NELANKESLHRQCEEKARHLQELlevaEQKLQQTMRKAETLPEVEAELSQRIAALT 379
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNlKELKELEEELKEAEEKEEEYAEL----QEELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 380 KAEERHGNIEEhLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEI 459
Cdd:COG4717 123 KLLQLLPLYQE-LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
170
....*....|...
gi 568909610 460 EKLRQEVDQLKGR 472
Cdd:COG4717 202 EELQQRLAELEEE 214
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
178-454 |
1.77e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.66 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 178 RVTTLEEQLAGAHQQVSALQQGAGIRDGVAEEEGTVDLGPKRLWKddtGRVEELQGLLEKQNYELSQARERLVTLS---- 253
Cdd:pfam07888 28 RAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWE---RQRRELESRVAELKEELRQSREKHEELEekyk 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 254 ------------------------ATVTELEEDLGT-ARRDLIKSEELSSKHQRdLREALAQKEDMEERITTLEKRYLAA 308
Cdd:pfam07888 105 elsasseelseekdallaqraaheARIRELEEDIKTlTQRVLERETELERMKER-AKKAGAQRKEEEAERKQLQAKLQQT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 309 QREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQK---LQQTMRKAETLPEVeAELSQRIAALTKAEER- 384
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKeaeNEALLEELRSLQER-LNASERKVEGLGEELSs 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 385 ------HGNIEEH-----LRQLEGQLEEKN-----------QELARVRQREKMNEDHNKRLSDTVDRLlsesNERLQLHL 442
Cdd:pfam07888 263 maaqrdRTQAELHqarlqAAQLTLQLADASlalregrarwaQERETLQQSAEADKDRIEKLSAELQRL----EERLQEER 338
|
330
....*....|..
gi 568909610 443 KERMAALEEKGR 454
Cdd:pfam07888 339 MEREKLEVELGR 350
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
313-423 |
2.65e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.20 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 313 TSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRI-----AALTKAEERHGN 387
Cdd:PRK00409 509 KLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAekeaqQAIKEAKKEADE 588
|
90 100 110
....*....|....*....|....*....|....*....
gi 568909610 388 IEEHLRQLE--GQLEEKNQELARVRQR-EKMNEDHNKRL 423
Cdd:PRK00409 589 IIKELRQLQkgGYASVKAHELIEARKRlNKANEKKEKKK 627
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
228-470 |
3.30e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 44.84 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 228 VEELQGLLEKqnYELSQARERLVTLSATVTELEEDLGTARR---DLIKSEELSSKHQRDLREalaqkedmeeRITTLEKR 304
Cdd:pfam06160 69 LFEAEELNDK--YRFKKAKKALDEIEELLDDIEEDIKQILEeldELLESEEKNREEVEELKD----------KYRELRKT 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 305 YLAaQREA--TSIhdlnDKLENELANKESLHRQCEE--------KARhlqELLEVAEQKLQQTMRKAETLPEVEAELSQR 374
Cdd:pfam06160 137 LLA-NRFSygPAI----DELEKQLAEIEEEFSQFEEltesgdylEAR---EVLEKLEEETDALEELMEDIPPLYEELKTE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 375 I-AALTKAEE------------RHGNIEEHLRQLEGQLEE-----KNQELARVrqrEKMNEDHNKRLSDTVDRLLSESNE 436
Cdd:pfam06160 209 LpDQLEELKEgyremeeegyalEHLNVDKEIQQLEEQLEEnlallENLELDEA---EEALEEIEERIDQLYDLLEKEVDA 285
|
250 260 270
....*....|....*....|....*....|....
gi 568909610 437 RLQLHlkermaalEEKGRLSEEIEKLRQEVDQLK 470
Cdd:pfam06160 286 KKYVE--------KNLPEIEDYLEHAEEQNKELK 311
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
257-472 |
3.54e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.96 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 257 TELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERIT--TLEKRYLAAQREATSIHDLNDKLENELANKESLHR 334
Cdd:pfam02463 156 LEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQelKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLN 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 335 QCEEKARHLQELLEVAEQKLQQTmrkaetLPEVEAELSQRIAALTKAEER-HGNIEEHLRQLEGQLEEKNQELARVRQRE 413
Cdd:pfam02463 236 EERIDLLQELLRDEQEEIESSKQ------EIEKEEEKLAQVLKENKEEEKeKKLQEEELKLLAKEEEELKSELLKLERRK 309
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568909610 414 KMNEDhNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGR 472
Cdd:pfam02463 310 VDDEE-KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEK 367
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
281-470 |
4.37e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 44.30 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 281 QRDLREALAQKEDMEERITTLekRYLAAQREATSIHDLND-KLENE---LANKESLHRQCEEKARHLQELLEVAEQKLQQ 356
Cdd:COG0497 171 KKELEELRADEAERARELDLL--RFQLEELEAAALQPGEEeELEEErrrLSNAEKLREALQEALEALSGGEGGALDLLGQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 357 TMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQRekMNEDHN--KRLSDTVDRLLSes 434
Cdd:COG0497 249 ALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEER--LALLRRlaRKYGVTVEELLA-- 324
|
170 180 190
....*....|....*....|....*....|....*.
gi 568909610 435 nerLQLHLKERMAALEEkgrLSEEIEKLRQEVDQLK 470
Cdd:COG0497 325 ---YAEELRAELAELEN---SDERLEELEAELAEAE 354
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
283-470 |
4.45e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 44.29 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 283 DLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMR--- 359
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRlet 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 360 -------KAETLPEVEAELSQRIAALTKAEE------------RHGNieEHLRQLEGQLE---EKNQELARVRQREKMNE 417
Cdd:pfam05622 81 arddyriKCEELEKEVLELQHRNEELTSLAEeaqalkdemdilRESS--DKVKKLEATVEtykKKLEDLGDLRRQVKLLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 418 DHN----------------------------KRLSDTVDRLLSESN--ERLQL---HLKERMAALE-EKGRLSEEIEKLR 463
Cdd:pfam05622 159 ERNaeymqrtlqleeelkkanalrgqletykRQVQELHGKLSEESKkaDKLEFeykKLEEKLEALQkEKERLIIERDTLR 238
|
....*..
gi 568909610 464 QEVDQLK 470
Cdd:pfam05622 239 ETNEELR 245
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
135-470 |
5.66e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 43.98 E-value: 5.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 135 KRQAQSPSGVSSEV-EVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGIRdgvAEEEGTv 213
Cdd:pfam09731 88 QVKIPRQSGVSSEVaEEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAIQ---AVKAHT- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 214 DLGPKRLWKDDTGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSeelsSKHQRDLREALAQKED 293
Cdd:pfam09731 164 DSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPK----LPEHLDNVEEKVEKAQ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 294 MEERITTLEKRYLAA-----QREATSIHD---LNDKLENELANKE------SLHRQCEEKARHLQELLEVAEQKLQQTMR 359
Cdd:pfam09731 240 SLAKLVDQYKELVASerivfQQELVSIFPdiiPVLKEDNLLSNDDlnsliaHAHREIDQLSKKLAELKKREEKHIERALE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 360 KA-ETLPEVEAELSQRIaaltkaeerhgniEEHLRQLEGQLEEKNQElARVRQREKM-----------NEDHNKRLSDTV 427
Cdd:pfam09731 320 KQkEELDKLAEELSARL-------------EEVRAADEAQLRLEFER-EREEIRESYeeklrtelerqAEAHEEHLKDVL 385
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 568909610 428 DRLLSESNERLQLHLKERMAalEEKGRLSEEIEKLRQEVDQLK 470
Cdd:pfam09731 386 VEQEIELQREFLQDIKEKVE--EERAGRLLKLNELLANLKGLE 426
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
235-469 |
5.85e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.40 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 235 LEKQNYELSQARERLVTLSATVTELEEDlgtaRRDLikSEELSSKHQRDLrEALAQKEDMEERITTLEKRYLAAQREATS 314
Cdd:pfam01576 358 LEELTEQLEQAKRNKANLEKAKQALESE----NAEL--QAELRTLQQAKQ-DSEHKRKKLEGQLQELQARLSESERQRAE 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 315 IHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAAL----TKAEERHGNIEE 390
Cdd:pfam01576 431 LAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLederNSLQEQLEEEEE 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 391 HLRQLEGQLEEKNQELARVRQreKMNEDhnkrlSDTVDrLLSESNERLQLHLKERMAALEEKGRLSEEIEK----LRQEV 466
Cdd:pfam01576 511 AKRNVERQLSTLQAQLSDMKK--KLEED-----AGTLE-ALEEGKKRLQRELEALTQQLEEKAAAYDKLEKtknrLQQEL 582
|
...
gi 568909610 467 DQL 469
Cdd:pfam01576 583 DDL 585
|
|
| SAM_STIM-1,2-like |
cd09504 |
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ... |
829-887 |
6.99e-04 |
|
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like (Stromal interaction molecule) proteins is a putative protein-protein interaction domain. STIM1 and STIM2 human proteins are type I transmembrane proteins. The N-terminal part of them includes "hidden" EF-hand and SAM domains. This region is responsible for sensing changes in store-operated and basal cytoplasmic Ca2+ levels and initiates oligomerization. "Hidden" EF hand and SAM domains have a stable intramolecular association, and the SAM domain is a component that regulates stability within STIM proteins. Destabilization of the EF-SAM association during Ca2+ depletion leads to partial unfolding and aggregation (homooligomerization), thus activating the store-operated Ca2+ entry. Immunoprecipitation analysis indicates that STIM1 and STIM2 can form co-precipitable oligomeric associations in vivo. It was suggested that STIM1 and STIM2 are involved in opposite regulation of store operated channels in plasma membrane.
Pssm-ID: 188903 Cd Length: 74 Bit Score: 39.24 E-value: 6.99e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568909610 829 WDGPTVVSWLELWVGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNALHRLKLRL 887
Cdd:cd09504 5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
247-406 |
7.04e-04 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 41.87 E-value: 7.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 247 ERLVTLSATVTELEEDLGTARRDLIkseELSSKHQRDLREALAQK-EDMEERITTlekrYLAAQRE--ATSIHDLNDKLE 323
Cdd:pfam01442 4 DSLDELSTYAEELQEQLGPVAQELV---DRLEKETEALRERLQKDlEEVRAKLEP----YLEELQAklGQNVEELRQRLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 324 NELankESLHRQCEEKARHLQELLEVAEQKLQQTMRK---------AETLPEVEAELSQRIAAL-----TKAEERHGNIE 389
Cdd:pfam01442 77 PYT---EELRKRLNADAEELQEKLAPYGEELRERLEQnvdalrarlAPYAEELRQKLAERLEELkeslaPYAEEVQAQLS 153
|
170
....*....|....*..
gi 568909610 390 EHLRQLEGQLEEKNQEL 406
Cdd:pfam01442 154 QRLQELREKLEPQAEDL 170
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
172-360 |
7.08e-04 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 42.20 E-value: 7.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 172 LRAALERVTTLEEQLAGAHQQVSALQqgagirdgvaEEEGTVdlgpKRLWKDDT-------GRVEELQGLLEKQNYELSQ 244
Cdd:pfam15619 6 LSARLHKIKELQNELAELQSKLEELR----------KENRLL----KRLQKRQEkalgkyeGTESELPQLIARHNEEVRV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 245 ARERLVTLSATVTELEEDLGTARRDLIKSEElSSKHQRDLREA--LAQKEDMEERITTLEKRYLAAQREatsIHDLNDKL 322
Cdd:pfam15619 72 LRERLRRLQEKERDLERKLKEKEAELLRLRD-QLKRLEKLSEDknLAEREELQKKLEQLEAKLEDKDEK---IQDLERKL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568909610 323 EN-------ELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRK 360
Cdd:pfam15619 148 ELenksfrrQLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKERE 192
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
241-412 |
7.29e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.53 E-value: 7.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 241 ELSQARERLVTLSATVTELEEDLG--TARRDLIKS---------------EELSSKHQR-----DLREALAQ-KEDMEER 297
Cdd:COG0497 159 EYREAYRAWRALKKELEELRADEAerARELDLLRFqleeleaaalqpgeeEELEEERRRlsnaeKLREALQEaLEALSGG 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 298 ITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQ----------ELLEVAEQKLQ---QTMRK---- 360
Cdd:COG0497 239 EGGALDLLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRryldslefdpERLEEVEERLAllrRLARKygvt 318
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568909610 361 AETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQR 412
Cdd:COG0497 319 VEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKK 370
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
106-411 |
7.60e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.06 E-value: 7.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 106 AERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPsgvssevEVLKALKSLFehhKALDEKVRERLRAALERVTTLEEQ 185
Cdd:pfam12128 247 QQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQ-------ETSAELNQLL---RTLDDQWKEKRDELNGELSAADAA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 186 LAGAHQQVSALQQGAGIRDGVAEEEGTVDLGPKRLWKDDTGRVEE-LQGLLEKQN--YELSQARERLVT--LSATVTELE 260
Cdd:pfam12128 317 VAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEErLKALTGKHQdvTAKYNRRRSKIKeqNNRDIAGIK 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 261 EDLGTARRDLIKSEELSSKHQRDLREALaqKEDMEERITTLEKrylAAQREATSIHDLNDKLENELANKESLHRQceeka 340
Cdd:pfam12128 397 DKLAKIREARDRQLAVAEDDLQALESEL--REQLEAGKLEFNE---EEYRLKSRLGELKLRLNQATATPELLLQL----- 466
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568909610 341 RHLQELLEVAEQKLQQTMRKAETLpeveaelsQRiaALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQ 411
Cdd:pfam12128 467 ENFDERIERAREEQEAANAEVERL--------QS--ELRQARKRRDQASEALRQASRRLEERQSALDELEL 527
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
286-411 |
8.29e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 8.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 286 EALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLEnELANKEslhrQCEEKARHLQELLEVAEQKLQQTMRKAETLP 365
Cdd:PRK11281 33 GDLPTEADVQAQLDALNKQKLLEAEDKLVQQDLEQTLA-LLDKID----RQKEETEQLKQQLAQAPAKLRQAQAELEALK 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 568909610 366 EVEA-ELSQRIAALTkaeerhgnieehLRQLEGQLEEKNQELARVRQ 411
Cdd:PRK11281 108 DDNDeETRETLSTLS------------LRQLESRLAQTLDQLQNAQN 142
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
367-470 |
8.74e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 8.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 367 VEAELSQRIAALTKAEERHGNIEEHlrQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLlSESNERLQLHLKERM 446
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKE--HEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEK-DERIERLERELSEAR 454
|
90 100
....*....|....*....|....
gi 568909610 447 AALEEKGRLSEEIEKLRQEVDQLK 470
Cdd:COG2433 455 SEERREIRKDREISRLDREIERLE 478
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
21-469 |
9.44e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 9.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 21 DAEANFEQLmvnmLDEREKLLESLRESQETLVATQSRLQdalHERDQLQRhlnsalpqefatltrelsmcreqllereeE 100
Cdd:PRK04863 551 DDEDELEQL----QEELEARLESLSESVSEARERRMALR---QQLEQLQA-----------------------------R 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 101 ISELKAERNNTRLLLEHLECLvsrherslrmtvvkrQAQSPSGVSSEVEVLKALKSLFEHHKALdEKVRERLRAALERvt 180
Cdd:PRK04863 595 IQRLAARAPAWLAAQDALARL---------------REQSGEEFEDSQDVTEYMQQLLEREREL-TVERDELAARKQA-- 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 181 tLEEqlagahqQVSALQQGAGIRD----GVAEEEGTVDLGpkRLWKD----DTGRVEELQGLLEKQNY--ELSQARERLV 250
Cdd:PRK04863 657 -LDE-------EIERLSQPGGSEDprlnALAERFGGVLLS--EIYDDvsleDAPYFSALYGPARHAIVvpDLSDAAEQLA 726
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 251 TLSATVTEL---EEDLGTARRDLIKSEELSSK-----HQRDLR------EALAQKEDMEERITTL-EKRYLAAQREATS- 314
Cdd:PRK04863 727 GLEDCPEDLyliEGDPDSFDDSVFSVEELEKAvvvkiADRQWRysrfpeVPLFGRAAREKRIEQLrAEREELAERYATLs 806
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 315 --------------------------------IHDLNDK---LENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMR 359
Cdd:PRK04863 807 fdvqklqrlhqafsrfigshlavafeadpeaeLRQLNRRrveLERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNL 886
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 360 KA-ETLPEVEAELSQRIAALTKAE---ERHGNieeHLRQLEGQ---LEEKNQELARVRQR----EKMNEDHNKR---LSD 425
Cdd:PRK04863 887 LAdETLADRVEEIREQLDEAEEAKrfvQQHGN---ALAQLEPIvsvLQSDPEQFEQLKQDyqqaQQTQRDAKQQafaLTE 963
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 568909610 426 TVDR-----------LLSESNErLQLHLKERMAALEEKGRlsEEIEKLRQEVDQL 469
Cdd:PRK04863 964 VVQRrahfsyedaaeMLAKNSD-LNEKLRQRLEQAEQERT--RAREQLRQAQAQL 1015
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
38-340 |
1.00e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 43.35 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 38 EKLLESLRESQE-TLVATQSRLQ------DALHERDQLQRHLNsalpqefaTLTRELSmcreqllEREEEISELKAERNN 110
Cdd:PLN02939 131 EDLVGMIQNAEKnILLLNQARLQaledleKILTEKEALQGKIN--------ILEMRLS-------ETDARIKLAAQEKIH 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 111 TRLLLEHLEclvsrherSLRMTVVKRQAQSPSGVSSEVEVLKALKslfEHHKALDEKVrERLRAALERVTTLEEQLAGAH 190
Cdd:PLN02939 196 VEILEEQLE--------KLRNELLIRGATEGLCVHSLSKELDVLK---EENMLLKDDI-QFLKAELIEVAETEERVFKLE 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 191 QQVSALQqgAGIRD----GVAEEEGTVDLGPKR---LWKddtgRVEELQGLLEKQNYELSQArerlvtlsATVTELEEDL 263
Cdd:PLN02939 264 KERSLLD--ASLREleskFIVAQEDVSKLSPLQydcWWE----KVENLQDLLDRATNQVEKA--------ALVLDQNQDL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 264 gtarRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQRE--------ATSIHDLNDKLENelANKESLHRQ 335
Cdd:PLN02939 330 ----RDKVDKLEASLKEANVSKFSSYKVELLQQKLKLLEERLQASDHEihsyiqlyQESIKEFQDTLSK--LKEESKKRS 403
|
....*
gi 568909610 336 CEEKA 340
Cdd:PLN02939 404 LEHPA 408
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
53-430 |
1.01e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.42 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 53 ATQSRLQDALHERDQLQ------RHLNSALPQEFATLTRELSMCREQLLEREEEISELKAERNNTRLLLEHLECLVSRHE 126
Cdd:TIGR00618 525 PLTRRMQRGEQTYAQLEtseedvYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLS 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 127 RSLRMTVVKRQAQSpsgVSSEVEVLKALKSLFEHHKAldekvrERLRAALERVTTLEEQLAGAHQQVSALqqgagirdgv 206
Cdd:TIGR00618 605 EAEDMLACEQHALL---RKLQPEQDLQDVRLHLQQCS------QELALKLTALHALQLTLTQERVREHAL---------- 665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 207 aeeegTVDLGPKRLWKDDTGRVEELQGLLEkqnyELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSSKHQRDLR- 285
Cdd:TIGR00618 666 -----SIRVLPKELLASRQLALQKMQSEKE----QLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAa 736
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 286 --EALAQ--KEDMEERITTLEKRYLAAQR---EATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTm 358
Cdd:TIGR00618 737 reDALNQslKELMHQARTVLKARTEAHFNnneEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSD- 815
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568909610 359 rKAETLPEVEAELSQRIAALTKAEERHGNIEEhLRQLEGQLEEKNQELARVRQREKmnedhnkRLSDTVDRL 430
Cdd:TIGR00618 816 -EDILNLQCETLVQEEEQFLSRLEEKSATLGE-ITHQLLKYEECSKQLAQLTQEQA-------KIIQLSDKL 878
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
272-383 |
1.09e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 272 KSEELSSKHQRDLREALAQKEDMEERittLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAE 351
Cdd:PRK12704 65 EIHKLRNEFEKELRERRNELQKLEKR---LLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQL 141
|
90 100 110
....*....|....*....|....*....|....*...
gi 568909610 352 QKLQQTMR------KAETLPEVEAELSQRIAALTKAEE 383
Cdd:PRK12704 142 QELERISGltaeeaKEILLEKVEEEARHEAAVLIKEIE 179
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
269-486 |
1.21e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 269 DLIKSE-ELSSKHQRDLREALAQkedmeeRITTLEKRYLAAQREATSIHDLNDKLENELANkesLHRQCEEKARHLQEL- 346
Cdd:PHA02562 191 DHIQQQiKTYNKNIEEQRKKNGE------NIARKQNKYDELVEEAKTIKAEIEELTDELLN---LVMDIEDPSAALNKLn 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 347 -------LEVAE-QKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNED 418
Cdd:PHA02562 262 taaakikSKIEQfQKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLE 341
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568909610 419 HNKRLSdTVDRLLS---ESNERLQLHLKErmaALEEKGRLSEEIEKLRQEVDQLKGRGGPFVDGIHSRSHV 486
Cdd:PHA02562 342 LKNKIS-TNKQSLItlvDKAKKVKAAIEE---LQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRGIV 408
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
227-472 |
1.45e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.89 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 227 RVEELQGLLEKQNYELSQARERLVTLSA-------TVTELEEDLGTARRDLiksEELSSKHQRDLREALAQKEDMEERIT 299
Cdd:pfam10174 402 KIENLQEQLRDKDKQLAGLKERVKSLQTdssntdtALTTLEEALSEKERII---ERLKEQREREDRERLEELESLKKENK 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 300 TLEKRYLAAQREAT----SIHDLNDK---LENELANKESLHRQCE---EKARHLQELLEVAEQKLQQTMRKAETLPEV-- 367
Cdd:pfam10174 479 DLKEKVSALQPELTekesSLIDLKEHassLASSGLKKDSKLKSLEiavEQKKEECSKLENQLKKAHNAEEAVRTNPEInd 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 368 -----EAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELA-----RVRQ-REKMNEDHNKRLSDTVDRllSESNE 436
Cdd:pfam10174 559 rirllEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAeleslTLRQmKEQNKKVANIKHGQQEMK--KKGAQ 636
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 568909610 437 RLQLHLKERMAA--------LEEkgrLSEEIEKLRQEVDQLKGR 472
Cdd:pfam10174 637 LLEEARRREDNLadnsqqlqLEE---LMGALEKTRQELDATKAR 677
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
228-470 |
1.87e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 228 VEELQGLLEKQNYELSQARERLVTLSATVTELEEdlgtARRDLI-KSEELSSKhqrdLREALAQKEDMEERITTLEKRYL 306
Cdd:COG1340 10 LEELEEKIEELREEIEELKEKRDELNEELKELAE----KRDELNaQVKELREE----AQELREKRDELNEKVKELKEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 307 AAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELlevaeQKLQQTMrkaETLPEVEAELSQRIAALTK-AEERh 385
Cdd:COG1340 82 ELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERL-----EWRQQTE---VLSPEEEKELVEKIKELEKeLEKA- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 386 gnieEHLRQLEGQLEEKNQELARVRQREkmnEDHNKRLSDTVDRLLSESNERLQLhLKERMAALEEKGRLSEEIEKLRQE 465
Cdd:COG1340 153 ----KKALEKNEKLKELRAELKELRKEA---EEIHKKIKELAEEAQELHEEMIEL-YKEADELRKEADELHKEIVEAQEK 224
|
....*
gi 568909610 466 VDQLK 470
Cdd:COG1340 225 ADELH 229
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
828-892 |
1.88e-03 |
|
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.
Pssm-ID: 425739 Cd Length: 64 Bit Score: 37.63 E-value: 1.88e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568909610 828 QWDGPTVVSWLElWVGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNALHRLKLRLAIQEM 892
Cdd:pfam00536 2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
218-470 |
2.12e-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: 42.31 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 218 KRLWKDDTGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLgtarrDLIKSEELSSKHQR-DLREALAQKEDMEE 296
Cdd:TIGR04523 137 KKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEK-----LNIQKNIDKIKNKLlKLELLLSNLKKKIQ 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 297 RITTLEKRYLAAQREATSIHDLNDKLENELANKeslhrqceekarhlQELLEVAEQKLQQTMrkaETLPEVEAELSQRIA 376
Cdd:TIGR04523 212 KNKSLESQISELKKQNNQLKDNIEKKQQEINEK--------------TTEISNTQTQLNQLK---DEQNKIKKQLSEKQK 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 377 ALTKAEERHGNIEEHLRQLEGQLE----EKNQELAR-----VRQREKMNEDHNKRLSDTvDRLLSESNERLQLHLKERMA 447
Cdd:TIGR04523 275 ELEQNNKKIKELEKQLNQLKSEISdlnnQKEQDWNKelkseLKNQEKKLEEIQNQISQN-NKIISQLNEQISQLKKELTN 353
|
250 260
....*....|....*....|...
gi 568909610 448 ALEEKGRLSEEIEKLRQEVDQLK 470
Cdd:TIGR04523 354 SESENSEKQRELEEKQNEIEKLK 376
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
33-468 |
2.15e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.12 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 33 MLDEREKLLESLRESQETLVATQSRLQDALherDQLQRHLNsALPQEFATLTRELSMCREQLLEREEEISELKAERNNTR 112
Cdd:pfam10174 360 FLNKKTKQLQDLTEEKSTLAGEIRDLKDML---DVKERKIN-VLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTD 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 113 LLLEHLECLVSRHERslrmtvvkrqaqspsgvsseveVLKALKslfeHHKALDEKVRerlraaLERVTTLEEQLAGAHQQ 192
Cdd:pfam10174 436 TALTTLEEALSEKER----------------------IIERLK----EQREREDRER------LEELESLKKENKDLKEK 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 193 VSALQQGAGIRDGVAEE--EGTVDLGPKRLWKDDtgRVEELQGLLEKQNYELSQARERL-----VTLSATVT-ELEEDLG 264
Cdd:pfam10174 484 VSALQPELTEKESSLIDlkEHASSLASSGLKKDS--KLKSLEIAVEQKKEECSKLENQLkkahnAEEAVRTNpEINDRIR 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 265 TARRDLIKSEELSSKHQRD-------LREALAQKEDMEERITTLEKRYLAAQREATSihdlndklenELANKEslHRQCE 337
Cdd:pfam10174 562 LLEQEVARYKEESGKAQAEverllgiLREVENEKNDKDKKIAELESLTLRQMKEQNK----------KVANIK--HGQQE 629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 338 EKARHLQELLEVAEQKlqqtmrKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQ--REKM 415
Cdd:pfam10174 630 MKKKGAQLLEEARRRE------DNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAerRKQL 703
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 568909610 416 NEdhnkRLSDTVDRLLSESNER------LQLHLKERMAALEEKGRLSEEIEKLRQEVDQ 468
Cdd:pfam10174 704 EE----ILEMKQEALLAAISEKdanialLELSSSKKKKTQEEVMALKREKDRLVHQLKQ 758
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
942-997 |
2.16e-03 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 37.63 E-value: 2.16e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 568909610 942 EWLPSLGLPQYRSYFMECLVD-ARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 997
Cdd:pfam07647 11 DWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLK-RLGITSVGHRRKILKKIQELK 66
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
149-470 |
2.20e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.26 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 149 EVLKALKSLFEHHKALDEKVRERLR------AALERVTTLEEQLAGAHQQVSALQQG------AGIRDGVAEEEGTVDLG 216
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKkqqllkQLRARIEELRAQEAVLEETQERINRArkaaplAAHIKAVTQIEQQAQRI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 217 PKRLWKDDTGRVEELQ--GLLEKQNYELSQARERLVTLSATVTELEE--DLGTARRDlIKSEELSSKHQrdLREALAQKE 292
Cdd:TIGR00618 313 HTELQSKMRSRAKLLMkrAAHVKQQSSIEEQRRLLQTLHSQEIHIRDahEVATSIRE-ISCQQHTLTQH--IHTLQQQKT 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 293 DMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQ-QTMRKAE------TLP 365
Cdd:TIGR00618 390 TLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQcEKLEKIHlqesaqSLK 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 366 EVEAELSQRiAALTKAEERHGNIEEHL--------RQLEGQLEEKNQEL----------ARVRQREKMNEDHNKRLSDTV 427
Cdd:TIGR00618 470 EREQQLQTK-EQIHLQETRKKAVVLARllelqeepCPLCGSCIHPNPARqdidnpgpltRRMQRGEQTYAQLETSEEDVY 548
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 568909610 428 DRLLSESNERLQLHLKERMAALEEKG------RLSEEIEKLRQEVDQLK 470
Cdd:TIGR00618 549 HQLTSERKQRASLKEQMQEIQQSFSIltqcdnRSKEDIPNLQNITVRLQ 597
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
235-465 |
2.64e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 235 LEKQNYELSQARERLvtlSATVTELEEDLgtarRDLIKSE---ELSSKHQRDLREALaqkedmEERITTLEKRYLAAQRE 311
Cdd:TIGR04523 417 LQQEKELLEKEIERL---KETIIKNNSEI----KDLTNQDsvkELIIKNLDNTRESL------ETQLKVLSRSINKIKQN 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 312 AtsihdlnDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLpevEAELSQRIAALTKAEERHGNIEEH 391
Cdd:TIGR04523 484 L-------EQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKL---ESEKKEKESKISDLEDELNKDDFE 553
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568909610 392 LR--QLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNErlqlhLKERMAALEEK-GRLSEEIEKLRQE 465
Cdd:TIGR04523 554 LKkeNLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKD-----LIKEIEEKEKKiSSLEKELEKAKKE 625
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
272-474 |
2.82e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 41.76 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 272 KSEELSSKHQRDLREALAQKEdMEERITTLEKRylAAQREATSIHDLNDKLenelanKESLHRQCEEKARHLQELLEVAE 351
Cdd:PLN03229 555 KAEKLKAEINKKFKEVMDRPE-IKEKMEALKAE--VASSGASSGDELDDDL------KEKVEKMKKEIELELAGVLKSMG 625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 352 QKLQQTMRKAETLPEVEA--ELSQRIAALTkaEERHGNIEEHLR--QLEGQLEEKNQELARVrqrekmnedhnkrlSDTV 427
Cdd:PLN03229 626 LEVIGVTKKNKDTAEQTPppNLQEKIESLN--EEINKKIERVIRssDLKSKIELLKLEVAKA--------------SKTP 689
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568909610 428 DRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGRGG 474
Cdd:PLN03229 690 DVTEKEKIEALEQQIKQKIAEALNSSELKEKFEELEAELAAARETAA 736
|
|
| SAM_Neurabin-like |
cd09512 |
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ... |
1020-1059 |
2.86e-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: 2.86e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 568909610 1020 VLVWTNDQVVHWVQSIGLRDYAGNLHESGVHG-ALLALDEN 1059
Cdd:cd09512 4 VSEWSVQQVCQWLMGLGLEQYIPEFTANNIDGqQLLQLDSS 44
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
273-410 |
3.06e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.10 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 273 SEELSSKHQR---------DLREALA----QKEDMEERITTLEKRYLAAQREatsihdlNDKLENELANKESLHRQCEEK 339
Cdd:PRK09039 45 SREISGKDSAldrlnsqiaELADLLSlerqGNQDLQDSVANLRASLSAAEAE-------RSRLQALLAELAGAGAAAEGR 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568909610 340 ARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAAL--------TKAEERHGNIEEHLRQLEGQLEEKNQELARVR 410
Cdd:PRK09039 118 AGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALeaaldaseKRDRESQAKIADLGRRLNVALAQRVQELNRYR 196
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
31-374 |
3.30e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 31 VNMLDEREKLLESLRESQETLVATQSRLQDALHERDQLQrhlnsalpqefatltrelsmcreqllEREEEISELKAERNN 110
Cdd:PRK02224 467 VETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLV--------------------------EAEDRIERLEERRED 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 111 -TRLLLEHLECLvsrHERSLRMTVVKRQAQspsgvssevevlkALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGA 189
Cdd:PRK02224 521 lEELIAERRETI---EEKRERAEELRERAA-------------ELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAEL 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 190 HQQVSALQQgagIRDGVAEEEgtvdlgpkrlwkDDTGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARrd 269
Cdd:PRK02224 585 KERIESLER---IRTLLAAIA------------DAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEAR-- 647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 270 likSEELSSKHQRdlreALAQKEDMEERITTLEKRYLAAQREATSIhdlndklENELANKESL---HRQCEEKARHLQEL 346
Cdd:PRK02224 648 ---IEEAREDKER----AEEYLEQVEEKLDELREERDDLQAEIGAV-------ENELEELEELrerREALENRVEALEAL 713
|
330 340
....*....|....*....|....*...
gi 568909610 347 LEVAEQkLQQTMRkaetlpEVEAELSQR 374
Cdd:PRK02224 714 YDEAEE-LESMYG------DLRAELRQR 734
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
229-353 |
3.74e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 41.58 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 229 EELQGL-LEKQNYE--LSQARERLVTLSATVTELEEDLGTARRDLIKSEELSSKhqrdlreALAQKEDMEERITTLEKRY 305
Cdd:pfam05911 688 EEFEQLkSEKENLEveLASCTENLESTKSQLQESEQLIAELRSELASLKESNSL-------AETQLKCMAESYEDLETRL 760
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 568909610 306 LAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQK 353
Cdd:pfam05911 761 TELEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQEQLERNEKK 808
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
309-470 |
3.74e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 309 QREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNI 388
Cdd:COG4372 20 PKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 389 EEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERlqlhlKERMAALEEKG-RLSEEIEKLRQEVD 467
Cdd:COG4372 100 QEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER-----EEELKELEEQLeSLQEELAALEQELQ 174
|
...
gi 568909610 468 QLK 470
Cdd:COG4372 175 ALS 177
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
177-472 |
4.31e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 177 ERVTTLEEQLAGAHQQVSALQQGAGirdgvaEEEGTVDLGPKRLWKDDTGRvEELQGLLEKQNYELSQARERLVTLSATV 256
Cdd:pfam01576 159 ERISEFTSNLAEEEEKAKSLSKLKN------KHEAMISDLEERLKKEEKGR-QELEKAKRKLEGESTDLQEQIAELQAQI 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 257 TELeedlgtaRRDLIKSEElsskhqrDLREALAQKEDMEERITTLEKRYlaaqREATS-IHDLNDKLENELANKESLHRQ 335
Cdd:pfam01576 232 AEL-------RAQLAKKEE-------ELQAALARLEEETAQKNNALKKI----RELEAqISELQEDLESERAARNKAEKQ 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 336 CeekaRHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEE----HLRQLEGQ-LEEKNQELARVR 410
Cdd:pfam01576 294 R----RDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEaqlqEMRQKHTQaLEELTEQLEQAK 369
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568909610 411 qREKMNEDHNKRlsdtvdRLLSESNErLQLHLKERMAAleeKGRLSEEIEKLRQEVDQLKGR 472
Cdd:pfam01576 370 -RNKANLEKAKQ------ALESENAE-LQAELRTLQQA---KQDSEHKRKKLEGQLQELQAR 420
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
152-326 |
4.43e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 40.01 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 152 KALKSLFEHHKALDEkvRERLRAALE--------RVTTLEEQLAGAhqqvsalqqgagirdgvaeeegtvdlgpKRLWKD 223
Cdd:pfam00261 61 EALEKLEEAEKAADE--SERGRKVLEnralkdeeKMEILEAQLKEA----------------------------KEIAEE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 224 DTGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTAR---RDLIKSEELSSKHQRDLREALaqkEDMEERITT 300
Cdd:pfam00261 111 ADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGnnlKSLEASEEKASEREDKYEEQI---RFLTEKLKE 187
|
170 180
....*....|....*....|....*.
gi 568909610 301 LEKRYLAAQREATSIHDLNDKLENEL 326
Cdd:pfam00261 188 AETRAEFAERSVQKLEKEVDRLEDEL 213
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
343-470 |
5.19e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 343 LQELLEVAEQKLQQTMRKAETLPEVE-AELSQRIAALtkaEERHGNIEEHLRQLEGQLEEKNQELARVRQR---EKMNED 418
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERElTEEEEEIRRL---EEQVERLEAEVEELEAELEEKDERIERLERElseARSEER 458
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 568909610 419 HNKRLSDTVDRLLSEsNERLQLHLKErmaaleekgrLSEEIEKLRQEVDQLK 470
Cdd:COG2433 459 REIRKDREISRLDRE-IERLERELEE----------ERERIEELKRKLERLK 499
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
347-470 |
6.37e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 6.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 347 LEVAEQKLQQTMRKAETlpeVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQR-EKMNEDHNKRL-- 423
Cdd:COG3883 18 IQAKQKELSELQAELEA---AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEiEERREELGERAra 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568909610 424 --------------------SDTVDRL-----LSESNERLQLHLKERMAALEE-KGRLSEEIEKLRQEVDQLK 470
Cdd:COG3883 95 lyrsggsvsyldvllgsesfSDFLDRLsalskIADADADLLEELKADKAELEAkKAELEAKLAELEALKAELE 167
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
166-423 |
7.73e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 7.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 166 EKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAgirDGVAEEEGTVDLgpkrlWKDDT--GRVEELqgllEKQNYELS 243
Cdd:PRK04863 840 RQLNRRRVELERALADHESQEQQQRSQLEQAKEGL---SALNRLLPRLNL-----LADETlaDRVEEI----REQLDEAE 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 244 QARERLVTLSATVTELEEDLGTARRDLIKSEELsskhQRDLREALAQKEDMEERITTL----EKR----YLAAQREATSI 315
Cdd:PRK04863 908 EAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQL----KQDYQQAQQTQRDAKQQAFALtevvQRRahfsYEDAAEMLAKN 983
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 316 HDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALT---------KAEERHG 386
Cdd:PRK04863 984 SDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGvpadsgaeeRARARRD 1063
|
250 260 270
....*....|....*....|....*....|....*...
gi 568909610 387 NIEEHLRQLEGQleeKNQ-ELARVRQREKMNEdHNKRL 423
Cdd:PRK04863 1064 ELHARLSANRSR---RNQlEKQLTFCEAEMDN-LTKKL 1097
|
|
| SAM_SARM1-like_repeat1 |
cd09501 |
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
942-986 |
7.80e-03 |
|
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of SARM1-like adaptor proteins is a protein-protein interaction domain. SARM1-like proteins contain two tandem SAM domains. SARM1-like proteins are involved in TLR (Toll-like receptor) signaling. They are responsible for targeted localization of the whole protein to post-synaptic regions of axons. In humans SARM1 expression is detected in kidney and liver.
Pssm-ID: 188900 [Multi-domain] Cd Length: 69 Bit Score: 36.13 E-value: 7.80e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 568909610 942 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHR 986
Cdd:cd09501 11 TWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLR 55
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
376-472 |
8.62e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.04 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 376 AALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRL-------LSESNERLQLHLKERMAA 448
Cdd:COG1842 16 ALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWeekarlaLEKGREDLAREALERKAE 95
|
90 100 110
....*....|....*....|....*....|..
gi 568909610 449 LEEK--------GRLSEEIEKLRQEVDQLKGR 472
Cdd:COG1842 96 LEAQaealeaqlAQLEEQVEKLKEALRQLESK 127
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
28-473 |
9.15e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.09 E-value: 9.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 28 QLMVNMLDEREKLLESLRESQETLVATQSRLQDALHERDQLQRHLNSALPQEFATLTRELSMCREQLLEREEEISELKAE 107
Cdd:pfam05483 183 QVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 108 RNNTRLLLEHLECLVSRHERSLRMTVVKRQAqspsgVSSEVEVLK-ALKSLFEHHKALDEKvrerLRAALERVTTLEEQl 186
Cdd:pfam05483 263 LEESRDKANQLEEKTKLQDENLKELIEKKDH-----LTKELEDIKmSLQRSMSTQKALEED----LQIATKTICQLTEE- 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 187 agAHQQVSALQQGAGIRDGVAEEEGTVDLGPKRLWKDDTGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTA 266
Cdd:pfam05483 333 --KEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEEL 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 267 RRDLIKSEEL--SSKHQRDLREALAQKEdmEERITTLEKRylaaQREatsIHDLNDKLENELANKESLHRQCEEKARHLQ 344
Cdd:pfam05483 411 KKILAEDEKLldEKKQFEKIAEELKGKE--QELIFLLQAR----EKE---IHDLEIQLTAIKTSEEHYLKEVEDLKTELE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 345 -------ELLEVAEQKLQQTMRKAETLPEVEAELSQR---IAALTKAEERH----GNIEEHLRQLEGQLEEKNQELARVR 410
Cdd:pfam05483 482 keklkniELTAHCDKLLLENKELTQEASDMTLELKKHqedIINCKKQEERMlkqiENLEEKEMNLRDELESVREEFIQKG 561
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568909610 411 QREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGRG 473
Cdd:pfam05483 562 DEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKG 624
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
149-472 |
9.25e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.42 E-value: 9.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 149 EVLKALKSLFEHHKALD--EKVRERLRAALERVttLEEQLAGAHQQVSALQQGAGiRDGVAEEEGTVDLGPK-------- 218
Cdd:TIGR00606 259 HNLSKIMKLDNEIKALKsrKKQMEKDNSELELK--MEKVFQGTDEQLNDLYHNHQ-RTVREKERELVDCQREleklnker 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 219 RLWKDDTGRVEELQGLLEKQ---NYELSQARERLVTLSATVTELEedlgTARRDLIKSEELSSKHQRDLREALAQKEDME 295
Cdd:TIGR00606 336 RLLNQEKTELLVEQGRLQLQadrHQEHIRARDSLIQSLATRLELD----GFERGPFSERQIKNFHTLVIERQEDEAKTAA 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 296 ERITTLEKRYLAAQREATSIHDLNDKLENELANKEslhrqceEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRI 375
Cdd:TIGR00606 412 QLCADLQSKERLKQEQADEIRDEKKGLGRTIELKK-------EILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAE 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909610 376 AALTKAEE----------------RHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNkrlsdTVDRLLSESNERLQ 439
Cdd:TIGR00606 485 RELSKAEKnsltetlkkevkslqnEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKM-----DKDEQIRKIKSRHS 559
|
330 340 350
....*....|....*....|....*....|...
gi 568909610 440 LHLKERMAALEEKGRLSEEIEKLRQEVDQLKGR 472
Cdd:TIGR00606 560 DELTSLLGYFPNKKQLEDWLHSKSKEINQTRDR 592
|
|
| |
