|
Name |
Accession |
Description |
Interval |
E-value |
| 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 ... |
1009-1080 |
1.47e-44 |
|
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: 155.17 E-value: 1.47e-44
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907075650 1009 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1080
Cdd:cd09568 1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
|
|
| 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 ... |
800-870 |
3.98e-44 |
|
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: 153.87 E-value: 3.98e-44
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907075650 800 FAQWDGPTVVAWLELWLGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 870
Cdd:cd09562 1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
|
|
| 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 ... |
924-989 |
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 1907075650 924 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 989
Cdd:cd09565 1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
|
|
| SAM_liprin-kazrin_repeat2 |
cd09495 |
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ... |
928-987 |
2.11e-31 |
|
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and in adheren junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188894 Cd Length: 60 Bit Score: 117.25 E-value: 2.11e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 928 WIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 987
Cdd:cd09495 1 WWVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLVHLKVTSQLHHLSLKCGIHVLH 60
|
|
| SAM_liprin-kazrin_repeat1 |
cd09494 |
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
807-865 |
2.66e-27 |
|
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: 105.39 E-value: 2.66e-27
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907075650 807 TVVAWLELWLGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 865
Cdd:cd09494 1 RVCAWLEDFGLMP-MYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
|
|
| SAM_liprin-kazrin_repeat3 |
cd09496 |
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of ... |
1017-1078 |
4.65e-25 |
|
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: 99.15 E-value: 4.65e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907075650 1017 RVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNN 1078
Cdd:cd09496 1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETEFNN 62
|
|
| SAM_kazrin_repeat3 |
cd09570 |
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin ... |
1009-1080 |
1.12e-18 |
|
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: 81.33 E-value: 1.12e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907075650 1009 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1080
Cdd:cd09570 1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
|
|
| SAM_kazrin_repeat1 |
cd09564 |
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ... |
801-865 |
3.13e-17 |
|
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: 77.11 E-value: 3.13e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907075650 801 AQWDGPTVVAWLELWLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 865
Cdd:cd09564 2 SRWKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
|
|
| SAM_kazrin_repeat2 |
cd09567 |
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ... |
923-987 |
1.27e-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: 75.14 E-value: 1.27e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907075650 923 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 987
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 ... |
923-987 |
1.34e-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: 75.04 E-value: 1.34e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907075650 923 DMNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLrVHLKMVDSFHRTSLQYGIMCLK 987
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 ... |
1009-1080 |
1.76e-15 |
|
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.
Pssm-ID: 188968 Cd Length: 72 Bit Score: 72.10 E-value: 1.76e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907075650 1009 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1080
Cdd:cd09569 1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
177-440 |
3.02e-15 |
|
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: 81.26 E-value: 3.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 177 LLEKQNyEMAQMKERLTALSSRVGEVEQEAETARKDLikteemntkyqRDIRECYLQAMAQKEDMEERITTLEKRYLSAQ 256
Cdd:TIGR02168 672 ILERRR-EIEELEEKIEELEEKIAELEKALAELRKEL-----------EELEEELEQLRKELEELSRQISALRKDLARLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 257 RESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpevEAELAQRIAALTKAEERH---- 332
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL---KEELKALREALDELRAELtlln 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 333 ---GNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLHLKERMAALEEKNVLIQES 406
Cdd:TIGR02168 817 eeaANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELeelIEELESELEALLNERASLEEALALLRSEL 896
|
250 260 270
....*....|....*....|....*....|....
gi 1907075650 407 ENFRKNLEESLHDKERLAEEIEKLRSELDQMKMR 440
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKLAQLELR 930
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
27-386 |
1.03e-14 |
|
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: 79.33 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 27 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERS---LRMTVVKRQAQSPSGVSSEVEVLKAL 103
Cdd:TIGR02168 691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEveqLEERIAQLSKELTELEAEIEELEERL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 104 KSLFEHHKALDEKIVALREQnvhIQRkmVSSEGSTESEHLEGMEAGQKVHEKRLSNGSIDSTDDTSQIVELQELLEKQNY 183
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQ---IEQ--LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 184 EMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDI---RECYLQAMAQKEDMEERITTLEKRYLSAQresT 260
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALallRSELEELSEELRELESKRSELRRELEELR---E 922
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 261 SIHDMNDKLEnelankeailrQMEEKNRQLQERL-ELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNI---- 335
Cdd:TIGR02168 923 KLAQLELRLE-----------GLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVnlaa 991
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907075650 336 -------EERMRHLEGQLEeknqELQRARQR-----EKMNEEHNKRLSDTVDRLltesNERLQ 386
Cdd:TIGR02168 992 ieeyeelKERYDFLTAQKE----DLTEAKETleeaiEEIDREARERFKDTFDQV----NENFQ 1046
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
140-446 |
1.77e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.44 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 140 SEHLEGMEAGQKVHEKRLSNGSIDSTDDtsQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLikteem 219
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEA--ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE------ 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 220 ntkyqrdirecyLQAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQ 299
Cdd:COG1196 291 ------------YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 300 KLQQtmrKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREkmnEEHNKRLSDTVDRLLT 379
Cdd:COG1196 359 ELAE---AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL---ERLEEELEELEEALAE 432
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907075650 380 ESNERLQLHLKERmAALEEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSLIE 446
Cdd:COG1196 433 LEEEEEEEEEALE-EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
923-987 |
5.34e-14 |
|
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.
Pssm-ID: 425739 Cd Length: 64 Bit Score: 67.68 E-value: 5.34e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907075650 923 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 987
Cdd:pfam00536 1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
184-436 |
6.32e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.51 E-value: 6.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 184 EMAQMKERLTALSSRVGEVEQ-------EAETARK-DLIKTEEmntkyqrDIRECYLQAmAQKEDMEERITTLEKRYLSA 255
Cdd:COG1196 180 KLEATEENLERLEDILGELERqleplerQAEKAERyRELKEEL-------KELEAELLL-LKLRELEAELEELEAELEEL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 256 QREStsihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERhgnI 335
Cdd:COG1196 252 EAEL-------EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE---L 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 336 EERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLHLKERMAALEEKNVLIQESENFRKN 412
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAeeaLLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
250 260
....*....|....*....|....
gi 1907075650 413 LEESLHDKERLAEEIEKLRSELDQ 436
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEE 425
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
40-399 |
1.01e-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: 72.79 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 40 REQLLEKEEEISELKAERNNTRLLLEHLECLVsrHERSLRMTVVKRQAqspsgvsseVEVLKALKSLFEHHKALDEKIVA 119
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRL--DELSQELSDASRKI---------GEIEKEIEQLEQEEEKLKERLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 120 LREQNVHIQRKM--VSSEGSTESEHLEGMEAgqKVHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSS 197
Cdd:TIGR02169 742 LEEDLSSLEQEIenVKSELKELEARIEELEE--DLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 198 RVGEVEQEAETARKdlikteEMNTKyQRDIRECYLQAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLEN---ELA 274
Cdd:TIGR02169 820 KLNRLTLEKEYLEK------EIQEL-QEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDlkkERD 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 275 NKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAA----------LTKAEERHGNIEERMRhleg 344
Cdd:TIGR02169 893 ELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeeelsLEDVQAELQRVEEEIR---- 968
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1907075650 345 QLEEKNqelQRARQREkmnEEHNKRLSDTVDRLLTESNERLQlhLKERMAALEEK 399
Cdd:TIGR02169 969 ALEPVN---MLAIQEY---EEVLKRLDELKEKRAKLEEERKA--ILERIEEYEKK 1015
|
|
| SAM_liprin-beta1,2_repeat1 |
cd09563 |
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
800-864 |
1.14e-12 |
|
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: 63.79 E-value: 1.14e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907075650 800 FAQWDGPTVVAWL-ELWLGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQ 864
Cdd:cd09563 1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
191-436 |
2.48e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.63 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 191 RLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREC---YLQAMAQKEDMEERITTLEKRYLSAQREstsIHDMND 267
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELeekLEELRLEVSELEEEIEELQKELYALANE---ISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 268 KLENELANKEAILRQMEEKNRQLQE----RLELAEQKLQQTMRKAETLPEVEAELAQriaaLTKAEERHGNIEERMRHLE 343
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEEleskLDELAEELAELEEKLEELKEELESLEAE----LEELEAELEELESRLEELE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 344 GQLEEKNQELQRARQREKMNEEHNKRLSDTVDRlLTESNERLQLHLKERMAALEEKNV--LIQESENFRKNLEESLHDKE 421
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNNEIERLEARLER-LEDRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQEELE 457
|
250
....*....|....*
gi 1907075650 422 RLAEEIEKLRSELDQ 436
Cdd:TIGR02168 458 RLEEALEELREELEE 472
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
154-437 |
9.11e-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: 69.71 E-value: 9.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 154 EKRLSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREcylq 233
Cdd:TIGR02169 701 ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHK---- 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 234 amaqkedMEERITTLEKRYlsAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPE 313
Cdd:TIGR02169 777 -------LEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 314 VEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARqrekmnEEHNKRLSDTVDRL--LTESNERLQLHLKE 391
Cdd:TIGR02169 848 QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER------DELEAQLRELERKIeeLEAQIEKKRKRLSE 921
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1907075650 392 RMAALEEKNVLIQESENFRKNLEES---LHDKERLAEEIEKLRSELDQM 437
Cdd:TIGR02169 922 LKAKLEALEEELSEIEDPKGEDEEIpeeELSLEDVQAELQRVEEEIRAL 970
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
103-388 |
1.05e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.70 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 103 LKSLFEHHKALDEKIVALREQNVHIQRKMVSSEGS---TESEHLEgMEAGQKVHEKRLSNGSIDSTDDTSQIVELQELLE 179
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKleeLRLEVSE-LEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 180 KQNYEMAQMKERLTALSSRVGEVEQEAETARKdliKTEEMNTKYQrDIRECYLQAMAQKEDMEERITTLEKRYLSAQRES 259
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEE---KLEELKEELE-SLEAELEELEAELEELESRLEELEEQLETLRSKV 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 260 TSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKA--ETLPEVEAELAQRIAALTKAEERHGNIEE 337
Cdd:TIGR02168 389 AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqAELEELEEELEELQEELERLEEALEELRE 468
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1907075650 338 RMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLH 388
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
163-417 |
1.94e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.54 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 163 DSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEmNTKYQRDIREcylQAMAQKEDME 242
Cdd:TIGR02168 720 ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE-ELAEAEAEIE---ELEAQIEQLK 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 243 ERITTLEKRYLSAQRE----STSIHDMNDKLENELANKEAILRQME------EKNRQLQERLELAEQKLQQTMRKAET-L 311
Cdd:TIGR02168 796 EELKALREALDELRAEltllNEEAANLRERLESLERRIAATERRLEdleeqiEELSEDIESLAAEIEELEELIEELESeL 875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 312 PEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKE 391
Cdd:TIGR02168 876 EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE 955
|
250 260
....*....|....*....|....*.
gi 1907075650 392 RMAALEEKNVLIQESENFRKNLEESL 417
Cdd:TIGR02168 956 AEALENKIEDDEEEARRRLKRLENKI 981
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
28-444 |
4.58e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 67.37 E-value: 4.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 28 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLrmtvvkrqaQSPSGVSSEVEVLKALKSLF 107
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERR---------EELETLEAEIEDLRETIAET 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 108 EHHKA--------LDEKIVALREQNVHIQRKMVSSEGSTE--SEHLEGMEAGQKVHEKRLSNGSIDSTDDTSQIVELQEl 177
Cdd:PRK02224 271 EREREelaeevrdLRERLEELEEERDDLLAEAGLDDADAEavEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRE- 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 178 lekqnyEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEmntkyqrdirecylqamaQKEDMEERITTLEKRYLSAQR 257
Cdd:PRK02224 350 ------DADDLEERAEELREEAAELESELEEAREAVEDRRE------------------EIEELEEEIEELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 258 ESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQklqqtMRKAETLPEVEAEL--AQRIAALTKAEERHGNI 335
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA-----LLEAGKCPECGQPVegSPHVETIEEDRERVEEL 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 336 EERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLS--DTVDRLLTESNERLQlHLKERMAAL-EEKNVLIQESENFRKN 412
Cdd:PRK02224 481 EAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIE-EKRERAEELrERAAELEAEAEEKREA 559
|
410 420 430
....*....|....*....|....*....|..
gi 1907075650 413 LEESLHDKERLAEEIEKLRSELDQMKMRTGSL 444
Cdd:PRK02224 560 AAEAEEEAEEAREEVAELNSKLAELKERIESL 591
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
100-365 |
1.00e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 100 LKALKSLFEHHKALDEKIVALREQNVHIQRKMVSSEGSTESEHLEGMEAGQKVHEKRLSNGSIDS--------------- 164
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAelarleqdiarleer 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 165 -TDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEmntkyqrdirecylQAMAQKEDMEE 243
Cdd:COG1196 311 rRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE--------------ALLEAEAELAE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 244 RITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIA 323
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1907075650 324 ALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEE 365
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
25-332 |
9.92e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.15 E-value: 9.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 25 TFQEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLEclvsrherslrmtvvkrqaqspsgvsSEVEVLKALK 104
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ--------------------------KELYALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 105 SLFEHHKaldeKIVALREQNVHIQRKMVSSEGSTESEHLEgmEAGQKVHEKRlsngsidstddtSQIVELQELLEKQNYE 184
Cdd:TIGR02168 298 SRLEQQK----QILRERLANLERQLEELEAQLEELESKLD--ELAEELAELE------------EKLEELKEELESLEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 185 MAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRecylQAMAQKEDMEERITTLEKRyLSAQRESTSIHD 264
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE----RLEARLERLEDRRERLQQE-IEELLKKLEEAE 434
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907075650 265 MnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERH 332
Cdd:TIGR02168 435 L-KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENL 501
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
236-444 |
2.05e-09 |
|
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: 62.01 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 236 AQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAET----L 311
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENvkseL 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 312 PEVEAELAQRIAALTKAEERHGNIEERMRHleGQLEEKNQELqrarqrEKMNEEHnKRLSDTVDRLLTESNERLQL--HL 389
Cdd:TIGR02169 761 KELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAEL------SKLEEEV-SRIEARLREIEQKLNRLTLEkeYL 831
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907075650 390 KERMAALEEKNVLIQESEN-FRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSL 444
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKsIEKEIENLNGKKEELEEELEELEAALRDLESRLGDL 887
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
233-443 |
2.24e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.93 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 233 QAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLp 312
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 313 evEAELAQRIAALTK------------------AEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTV 374
Cdd:COG4942 103 --KEELAELLRALYRlgrqpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907075650 375 DRLLTEsNERLQLHLKERMAALEEKNvliQESENFRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGS 443
Cdd:COG4942 181 AELEEE-RAALEALKAERQKLLARLE---KELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
169-365 |
2.27e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 60.61 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 169 SQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIrecylqaMAQKEDMEERITTL 248
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI-------AEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 249 EKRYLSAQR------------ESTSIHDMNDKLEN----ELANKEAILRQMEEKNR--QLQERLELAEQKLQQTMRKAET 310
Cdd:COG3883 89 GERARALYRsggsvsyldvllGSESFSDFLDRLSAlskiADADADLLEELKADKAEleAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907075650 311 -LPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEE 365
Cdd:COG3883 169 aKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
156-444 |
2.49e-09 |
|
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: 61.62 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 156 RLSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLikteemntkyqRDIRECYLQAM 235
Cdd:TIGR02169 661 APRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKI-----------GEIEKEIEQLE 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 236 AQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLelAEQKLQQTMRKAETLPEVE 315
Cdd:TIGR02169 730 QEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEV 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 316 AELAQRIAALTKAEERhgnieermRHLEGQ-LEEKNQELQrarqrEKMNEEHNKRlsdtvdrlltESNERLQLHLKERMA 394
Cdd:TIGR02169 808 SRIEARLREIEQKLNR--------LTLEKEyLEKEIQELQ-----EQRIDLKEQI----------KSIEKEIENLNGKKE 864
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1907075650 395 ALEEKnvlIQESENFRKNLEESLHDkerLAEEIEKLRSELDQMKMRTGSL 444
Cdd:TIGR02169 865 ELEEE---LEELEAALRDLESRLGD---LKKERDELEAQLRELERKIEEL 908
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
173-444 |
3.17e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 173 ELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMntkyqrdirecylqamaqkedmEERITTLEKRy 252
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL----------------------KEEIEELEKE- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 253 lsaqrestsihdmNDKLENELANKEAILRQMEEKNRQLQERLELAEQK---LQQTMRKAETLPEVEAELAQRIAALTKAE 329
Cdd:PRK03918 247 -------------LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkeLKELKEKAEEYIKLSEFYEEYLDELREIE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 330 ERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDtvdrlLTESNERLQ--LHLKERMAALEEKnVLIQESE 407
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEE-----LEERHELYEeaKAKKEELERLKKR-LTGLTPE 387
|
250 260 270
....*....|....*....|....*....|....*..
gi 1907075650 408 NFRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSL 444
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL 424
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
201-438 |
3.36e-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: 61.23 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 201 EVEQEAETARKDLIKTEEMNTKYQRDIRECYLQA-MAQK-EDMEERITTLEKRYLSAQREStsihdmndkLENELANKEA 278
Cdd:TIGR02168 176 ETERKLERTRENLDRLEDILNELERQLKSLERQAeKAERyKELKAELRELELALLVLRLEE---------LREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 279 ILRQMEEKNRQLQERLELAEQKLQQTMRKaetlpevEAELAQRIAALTKAEERHGNIEERmrhLEGQLEEKNQELQRARQ 358
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLE-------VSELEEEIEELQKELYALANEISR---LEQQKQILRERLANLER 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 359 REKMNE---EHNKRLSDTVDRLLTESNERLQLhLKERMAALEEKnvlIQESENFRKNLEESLHDKErlaEEIEKLRSELD 435
Cdd:TIGR02168 317 QLEELEaqlEELESKLDELAEELAELEEKLEE-LKEELESLEAE---LEELEAELEELESRLEELE---EQLETLRSKVA 389
|
...
gi 1907075650 436 QMK 438
Cdd:TIGR02168 390 QLE 392
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
28-378 |
3.45e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 3.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 28 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLEclvsrherslrmtvvkrqaqspsgvssevevlkalkslf 107
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELR--------------------------------------- 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 108 EHHKALDEKIVALREQNVHIQRKmvssegstesehLEGMEAGQKVHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEMAQ 187
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAE------------LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 188 MKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITTLEKRYLSAQRESTSIHDMND 267
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 268 KLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGniEERMRHLEGQLE 347
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA--EAAARLLLLLEA 499
|
330 340 350
....*....|....*....|....*....|.
gi 1907075650 348 EKNQELQRARQREKMNEEHNKRLSDTVDRLL 378
Cdd:COG1196 500 EADYEGFLEGVKAALLLAGLRGLAGAVAVLI 530
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
166-590 |
3.77e-09 |
|
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: 61.24 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 166 DDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEmntkyqrdirecYLQAMAQKEDMEERI 245
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAER------------YQALLKEKREYEGYE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 246 TTLEKRYLSAQREstsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAelaqrIAAL 325
Cdd:TIGR02169 228 LLKEKEALERQKE---------AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ-----LRVK 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 326 TKAEERHGNIEErmrhLEGQLEEKNQELQRA-RQREKMNEEHNKRLSdtvdrlltesnerlqlhlkermaaleeknvliq 404
Cdd:TIGR02169 294 EKIGELEAEIAS----LERSIAEKERELEDAeERLAKLEAEIDKLLA--------------------------------- 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 405 ESENFRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSLieptisrthidtSTELRYSVGSLVDSQSDYRTTKVIRRPR 484
Cdd:TIGR02169 337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEV------------DKEFAETRDELKDYREKLEKLKREINEL 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 485 RGRMGVRRDEPKVKS--LGDHEwnrtQQIGVLGSHPFESDTEMSDIDDDDRETIFSSMDLLSPSGHSDAQTLAmmLQEQL 562
Cdd:TIGR02169 405 KRELDRLQEELQRLSeeLADLN----AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD--LKEEY 478
|
410 420
....*....|....*....|....*...
gi 1907075650 563 DAINKEIRLIQEEKESTELRAEEIENRV 590
Cdd:TIGR02169 479 DRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
28-327 |
3.84e-09 |
|
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: 61.24 E-value: 3.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 28 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLrmtvvkrqaqspsgvSSEVEVLKALKSLF 107
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL---------------HKLEEALNDLEARL 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 108 EHH--KALDEKIVALREQNVHIQRKMVSSEGSTESEHLEGMEAGQKVHEKRLSNGSIDSTDDT--SQIVELQELLEKQNY 183
Cdd:TIGR02169 789 SHSriPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSieKEIENLNGKKEELEE 868
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 184 EMAQMKERLTALSSRVGEVEQEAETARKDL----IKTEEMNTKYQRdIRECYLQAMAQKEDMEERITTLEKRYLSAQRES 259
Cdd:TIGR02169 869 ELEELEAALRDLESRLGDLKKERDELEAQLreleRKIEELEAQIEK-KRKRLSELKAKLEALEEELSEIEDPKGEDEEIP 947
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907075650 260 TSIHDMnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTK 327
Cdd:TIGR02169 948 EEELSL-EDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
800-866 |
3.98e-09 |
|
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: 53.84 E-value: 3.98e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907075650 800 FAQWDGPTVVAWLELwLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 866
Cdd:smart00454 1 VSQWSPESVADWLES-IGLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
25-444 |
4.19e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.82 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 25 TFQEFAALTKELNACREQLLEKEEEISELKAERNNTRL----LLEHLECLVSRHERSLRMTVVKRQAQSpsgvssevEVL 100
Cdd:PRK02224 270 TEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDAdaeaVEARREELEDRDEELRDRLEECRVAAQ--------AHN 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 101 KALKSLFEHHKALDEKIVALREQNVHIQRKMVSSEG--STESEHLEGMEAGQKVHEKRLSNGSIDSTDDTSQIVELQELL 178
Cdd:PRK02224 342 EEAESLREDADDLEERAEELREEAAELESELEEAREavEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREER 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 179 EKQNYEMAQMKERLTALSSRVGEVEQ--------EAETARKDLIKTEEMNTKYQR--DIRECYLQAMAQKEDMEERITTL 248
Cdd:PRK02224 422 DELREREAELEATLRTARERVEEAEAlleagkcpECGQPVEGSPHVETIEEDRERveELEAELEDLEEEVEEVEERLERA 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 249 EKrYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKA 328
Cdd:PRK02224 502 ED-LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSK 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 329 EERHGNIEERMRHLEGQL---EEKNQELQRARQREK----MNEEHNKRLSDTVDRL-----------LTESNERLQlHLK 390
Cdd:PRK02224 581 LAELKERIESLERIRTLLaaiADAEDEIERLREKREalaeLNDERRERLAEKRERKreleaefdearIEEAREDKE-RAE 659
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1907075650 391 ERMAALEEKnvlIQESENFRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSL 444
Cdd:PRK02224 660 EYLEQVEEK---LDELREERDDLQAEIGAVENELEELEELRERREALENRVEAL 710
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
25-436 |
9.09e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 9.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 25 TFQEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLEclvsrhERSLRMTVVKRQAQspsgvssEVEVLKALK 104
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE------EKVKELKELKEKAE-------EYIKLSEFY 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 105 SLFEHHKALDEKIVA-LREQNVHIQRKMvsSEGSTESEHLEGMEAGQKVHEKRLSNGSIDSTddtsqivELQELLEKQNy 183
Cdd:PRK03918 303 EEYLDELREIEKRLSrLEEEINGIEERI--KELEEKEERLEELKKKLKELEKRLEELEERHE-------LYEEAKAKKE- 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 184 EMAQMKERLTALSsrVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYlQAMAQKEDMEERITTLEKRYLSAQRESTSIH 263
Cdd:PRK03918 373 ELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITARIGELK-KEIKELKKAIEELKKAKGKCPVCGRELTEEH 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 264 DMN--DKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQ-----TMRK-AETLPEVEAELAQ-RIAALTKAEERHGN 334
Cdd:PRK03918 450 RKEllEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKeseliKLKElAEQLKELEEKLKKyNLEELEKKAEEYEK 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 335 IEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLsDTVDRLLTESNERLQLHLKERMAALEEKnvlIQESENFRK--- 411
Cdd:PRK03918 530 LKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKL-DELEEELAELLKELEELGFESVEELEER---LKELEPFYNeyl 605
|
410 420
....*....|....*....|....*
gi 1907075650 412 NLEESLHDKERLAEEIEKLRSELDQ 436
Cdd:PRK03918 606 ELKDAEKELEREEKELKKLEEELDK 630
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
34-437 |
9.49e-09 |
|
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: 59.98 E-value: 9.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 34 KELNACREQLLEKEEEISELKAERNNtrlLLEHLECLVSRHERSLRMTVVkrQAQSPSGVSSEVE-VLKALKSLFEHHKA 112
Cdd:TIGR00618 472 EQQLQTKEQIHLQETRKKAVVLARLL---ELQEEPCPLCGSCIHPNPARQ--DIDNPGPLTRRMQrGEQTYAQLETSEED 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 113 LDEKIVALREQNVHIQRKMVSSEGSTE------SEHLEGMEAGQKVHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEMA 186
Cdd:TIGR00618 547 VYHQLTSERKQRASLKEQMQEIQQSFSiltqcdNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQD 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 187 QMKERLTalssrvgEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITTLEKRYLSAQRESTSIHDM- 265
Cdd:TIGR00618 627 LQDVRLH-------LQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMl 699
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 266 ---NDKLENELANKEAILRQMEE-------KNRQLQERLELAEQKLQQTMRKAET-LPEVEAELAQRIAALTKAEERhgn 334
Cdd:TIGR00618 700 aqcQTLLRELETHIEEYDREFNEienasssLGSDLAAREDALNQSLKELMHQARTvLKARTEAHFNNNEEVTAALQT--- 776
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 335 iEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESENFRKNLE 414
Cdd:TIGR00618 777 -GAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYE 855
|
410 420
....*....|....*....|...
gi 1907075650 415 ESLHDKERLAEEIEKLRSELDQM 437
Cdd:TIGR00618 856 ECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
40-365 |
9.66e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.70 E-value: 9.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 40 REQLLEKEE-EISELKAERNNTRLLLEHLECLVSRHERSLRmtvvKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEkiv 118
Cdd:TIGR02169 214 QALLKEKREyEGYELLKEKEALERQKEAIERQLASLEEELE----KLTEEISELEKRLEEIEQLLEELNKKIKDLGE--- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 119 alrEQNVHIQRKMVSSEGSTESehlegMEAGQKVHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSR 198
Cdd:TIGR02169 287 ---EEQLRVKEKIGELEAEIAS-----LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 199 VGEVEQEAETARKDLiktEEMNTKYQRDIREcylqamaqKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEA 278
Cdd:TIGR02169 359 YAELKEELEDLRAEL---EEVDKEFAETRDE--------LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 279 ILRQMEEKNRQLQERLElaeqklqqtmRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQ 358
Cdd:TIGR02169 428 AIAGIEAKINELEEEKE----------DKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEA 497
|
....*..
gi 1907075650 359 REKMNEE 365
Cdd:TIGR02169 498 QARASEE 504
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
169-435 |
1.00e-08 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 58.93 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 169 SQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEemntkyqRDIRECYLQAMAQKEDMEER---I 245
Cdd:pfam19220 48 SRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLE-------AALREAEAAKEELRIELRDKtaqA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 246 TTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAAL 325
Cdd:pfam19220 121 EALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAEL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 326 TKAEERHgniEERMRHLEGQLEEKNQELQRA-RQREKMNEEHNKRLSDTVDRLLTESNerlqlhlkeRMAALEeknVLIQ 404
Cdd:pfam19220 201 ETQLDAT---RARLRALEGQLAAEQAERERAeAQLEEAVEAHRAERASLRMKLEALTA---------RAAATE---QLLA 265
|
250 260 270
....*....|....*....|....*....|.
gi 1907075650 405 ESENFRKNLEESLHDKERLAEEIEKLRSELD 435
Cdd:pfam19220 266 EARNQLRDRDEAIRAAERRLKEASIERDTLE 296
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
267-433 |
1.49e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 267 DKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtLPEVEAELA---QRIAALTKAEERHGNIEERMRHLE 343
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID-VASAEREIAeleAELERLDASSDDLAALEEQLEELE 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 344 GQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLT-------ESNERLQLHLKERMAALEEKNVLIQESENFRKNLEES 416
Cdd:COG4913 699 AELEELEEELDELKGEIGRLEKELEQAEEELDELQDrleaaedLARLELRALLEERFAAALGDAVERELRENLEERIDAL 778
|
170
....*....|....*..
gi 1907075650 417 LHDKERLAEEIEKLRSE 433
Cdd:COG4913 779 RARLNRAEEELERAMRA 795
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
134-419 |
1.57e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.38 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 134 SEGSTESEHLEGMEAGQKVHEKRLSNgSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARkdl 213
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKADEAKKAE-EKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR--- 1593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 214 ikTEEMNTKYQRdirECYLQAMAQKEDMEERITTLEKRylSAQRESTSIHDMNDKLENEL--------ANKEAILRQMEE 285
Cdd:PTZ00121 1594 --IEEVMKLYEE---EKKMKAEEAKKAEEAKIKAEELK--KAEEEKKKVEQLKKKEAEEKkkaeelkkAEEENKIKAAEE 1666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 286 KNRQLQERLELAE-QKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNE 364
Cdd:PTZ00121 1667 AKKAEEDKKKAEEaKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA 1746
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907075650 365 EHNKR---LSDTVDRLLTESNERLQLHLKERMAALEEKnvLIQESENFRKNLEESLHD 419
Cdd:PTZ00121 1747 EEAKKdeeEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE--LDEEDEKRRMEVDKKIKD 1802
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
163-441 |
1.69e-08 |
|
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: 59.03 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 163 DSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDI---RECYLQAMAQKE 239
Cdd:pfam01576 216 ESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLeseRAARNKAEKQRR 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 240 DMEERI------------TTLEKRYLSAQREsTSIHDMNDKLENELANKEAILRQMEEKNRQ----LQERLELAEQKLQQ 303
Cdd:pfam01576 296 DLGEELealkteledtldTTAAQQELRSKRE-QEVTELKKALEEETRSHEAQLQEMRQKHTQaleeLTEQLEQAKRNKAN 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 304 TMRKAETLPEVEAELAQRIAALTKAEerhGNIEERMRHLEGQLEEKNQELQRA-RQREKMNEEHNK-------------- 368
Cdd:pfam01576 375 LEKAKQALESENAELQAELRTLQQAK---QDSEHKRKKLEGQLQELQARLSESeRQRAELAEKLSKlqselesvssllne 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 369 ------RLSDTVDRL---LTESNERLQ------LHLKERMAALEEknvliqESENFRKNLEESLHDKERLAEEIEKLRSE 433
Cdd:pfam01576 452 aegkniKLSKDVSSLesqLQDTQELLQeetrqkLNLSTRLRQLED------ERNSLQEQLEEEEEAKRNVERQLSTLQAQ 525
|
....*...
gi 1907075650 434 LDQMKMRT 441
Cdd:pfam01576 526 LSDMKKKL 533
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
32-445 |
1.70e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.88 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 32 LTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHeRSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHK 111
Cdd:TIGR04523 171 LENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKN-KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEIS 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 112 ALDEKIVALREQNVHIQRKMV--SSEGSTESEHLEGMEAGQKVHEKRLSNGSIDSTDDTSQivELQELLEKQNYEMAQMK 189
Cdd:TIGR04523 250 NTQTQLNQLKDEQNKIKKQLSekQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNK--ELKSELKNQEKKLEEIQ 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 190 ERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREcylqamaqKEDMEERIttlekrylsaQRESTSIHDMNDKL 269
Cdd:TIGR04523 328 NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE--------KQNEIEKL----------KKENQSYKQEIKNL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 270 ENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKA----EERHGNIEERMRHLEGQ 345
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvkELIIKNLDNTRESLETQ 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 346 --------------LEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNErlqlhLKERMAALE----EKNVLIQESE 407
Cdd:TIGR04523 470 lkvlsrsinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS-----LKEKIEKLEsekkEKESKISDLE 544
|
410 420 430
....*....|....*....|....*....|....*...
gi 1907075650 408 NFRKNLEESLhDKERLAEEIEKLRSELDQMKMRTGSLI 445
Cdd:TIGR04523 545 DELNKDDFEL-KKENLEKEIDEKNKEIEELKQTQKSLK 581
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
238-437 |
1.84e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 238 KEDMEERITTLEKrYLSAQREstsIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAE 317
Cdd:PRK03918 171 IKEIKRRIERLEK-FIKRTEN---IEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 318 LAQRIAALTKAEERHGNIEERMRHLEGQ---LEEKNQELQRARQREKMNEEHNKRLSDTVDRL-----LTESNERLQLHL 389
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEieeLEEKVKELKELKEKAEEYIKLSEFYEEYLDELreiekRLSRLEEEINGI 326
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907075650 390 KERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQM 437
Cdd:PRK03918 327 EERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEL 374
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
41-440 |
2.20e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 41 EQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRmtVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKIVAL 120
Cdd:PRK03918 286 KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN--GIEERIKELEEKEERLEELKKKLKELEKRLEELEERHEL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 121 REQnvhIQRKMVSSEGstesehlegmeagqkvHEKRLSNGSIDstddtsQIVELQELLEKQNYEMaqmKERLTALSSRVG 200
Cdd:PRK03918 364 YEE---AKAKKEELER----------------LKKRLTGLTPE------KLEKELEELEKAKEEI---EEEISKITARIG 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 201 EVEQEAETARKDLIKTE-----------EMNTKYQRDIRECYLqamAQKEDMEERITTLEKRYLSAQRESTsihdmndKL 269
Cdd:PRK03918 416 ELKKEIKELKKAIEELKkakgkcpvcgrELTEEHRKELLEEYT---AELKRIEKELKEIEEKERKLRKELR-------EL 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 270 ENELANKEAI--LRQMEEKNRQLQERLE-LAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQL 346
Cdd:PRK03918 486 EKVLKKESELikLKELAEQLKELEEKLKkYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKL 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 347 EEKNQELQRA-RQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESEnfrknLEESLHDKERLAE 425
Cdd:PRK03918 566 DELEEELAELlKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEE-----LDKAFEELAETEK 640
|
410
....*....|....*
gi 1907075650 426 EIEKLRSELDQMKMR 440
Cdd:PRK03918 641 RLEELRKELEELEKK 655
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
45-449 |
2.43e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 45 EKEEEISELKAERNNTRLllehlECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKIVALREQN 124
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKA-----DAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAK 1437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 125 VHIQRKMVSSEGSTESEHLEGME-AGQKVHEKRLSNGSIDSTDDTSQIVELQELLE----------------KQNYEMAQ 187
Cdd:PTZ00121 1438 KKAEEAKKADEAKKKAEEAKKAEeAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEeakkkadeakkaaeakKKADEAKK 1517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 188 MKERLTALSSRVGEVEQEAETARK--DLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITTLEKRYLSAQRESTSIHDM 265
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKADEAKKaeEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEV 1597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 266 NDKLENELANKEAILRQMEE---------KNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIE 336
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEakikaeelkKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA 1677
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 337 ERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLltesnERLQLHLKERMAALEEknvLIQESENFRKNLEES 416
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA-----EELKKAEEENKIKAEE---AKKEAEEDKKKAEEA 1749
|
410 420 430
....*....|....*....|....*....|...
gi 1907075650 417 LHDKERlAEEIEKLRSELDQMKMRTGSLIEPTI 449
Cdd:PTZ00121 1750 KKDEEE-KKKIAHLKKEEEKKAEEIRKEKEAVI 1781
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
30-435 |
2.87e-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: 58.43 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 30 AALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRH---------ERSLRmtvVKRQAQSpsgvssevEVL 100
Cdd:COG3096 781 AAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVGGHlavafapdpEAELA---ALRQRRS--------ELE 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 101 KALKSLFEHHKALDEKIVALREQnVHIQRKMVSSEGSTESEHLEgmeagQKVHEKRlsngsidstddtsqiVELQELLEK 180
Cdd:COG3096 850 RELAQHRAQEQQLRQQLDQLKEQ-LQLLNKLLPQANLLADETLA-----DRLEELR---------------EELDAAQEA 908
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 181 QNYeMAQMKERLTalssrvgEVEQEAETARKDLIKTEEMntkyQRDirecYLQAMAQKEDMEERITTLEkrYLSAQREST 260
Cdd:COG3096 909 QAF-IQQHGKALA-------QLEPLVAVLQSDPEQFEQL----QAD----YLQAKEQQRRLKQQIFALS--EVVQRRPHF 970
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 261 SIHD----------MNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAAL----- 325
Cdd:COG3096 971 SYEDavgllgensdLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELgvqad 1050
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 326 TKAEERhgnIEERMRHLEGQL----EEKNQ-ELQRARQREKMnEEHNKRLSDtVDRLLTESNERLQLHLKERMAALEekn 400
Cdd:COG3096 1051 AEAEER---ARIRRDELHEELsqnrSRRSQlEKQLTRCEAEM-DSLQKRLRK-AERDYKQEREQVVQAKAGWCAVLR--- 1122
|
410 420 430
....*....|....*....|....*....|....*
gi 1907075650 401 vLIQESenfrkNLEESLHDKERLAEEIEKLRSELD 435
Cdd:COG3096 1123 -LARDN-----DVERRLHRRELAYLSADELRSMSD 1151
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
170-384 |
5.92e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.31 E-value: 5.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 170 QIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITTLe 249
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 250 krYLSAQRESTSI----HDMNDkLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAAL 325
Cdd:COG4942 114 --YRLGRQPPLALllspEDFLD-AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907075650 326 TKAEERHgniEERMRHLEGQLEEKNQELQRARQREkmneehnKRLSDTVDRLLTESNER 384
Cdd:COG4942 191 EALKAER---QKLLARLEKELAELAAELAELQQEA-------EELEALIARLEAEAAAA 239
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
121-435 |
6.50e-08 |
|
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: 57.11 E-value: 6.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 121 REQNVHIQRKMVSSEGSTESEHLEGMEAG-QKVH-EKRLSNGSIDSTDDTSQIVELQEllEKQNYEMAQMKERLTALSSR 198
Cdd:pfam01576 90 RSQQLQNEKKKMQQHIQDLEEQLDEEEAArQKLQlEKVTTEAKIKKLEEDILLLEDQN--SKLSKERKLLEERISEFTSN 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 199 VGEVEQEAETARKDLIKTEEMNTKYQRDIRECylqamaqkedmEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEA 278
Cdd:pfam01576 168 LAEEEEKAKSLSKLKNKHEAMISDLEERLKKE-----------EKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 279 ILRQMEEKNRQLQERLE---LAEQKLQQTMRKAET-LPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEK----- 349
Cdd:pfam01576 237 QLAKKEEELQAALARLEeetAQKNNALKKIRELEAqISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTldtta 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 350 -NQELQRARQRE--------------------KMNEEHNKRLSDTVDRLltESNERLQLHLKERMAALEEKNVLI----- 403
Cdd:pfam01576 317 aQQELRSKREQEvtelkkaleeetrsheaqlqEMRQKHTQALEELTEQL--EQAKRNKANLEKAKQALESENAELqaelr 394
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1907075650 404 ------QESENFRKNLEESLHD-----------KERLAEEIEKLRSELD 435
Cdd:pfam01576 395 tlqqakQDSEHKRKKLEGQLQElqarlseserqRAELAEKLSKLQSELE 443
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
28-438 |
7.42e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 7.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 28 EFAALTKELNACREQLLE---KEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALK 104
Cdd:PRK03918 315 RLSRLEEEINGIEERIKEleeKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELE 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 105 SLFEHHKALDEKIvalreqnvhiqRKMVSSEGSTESEHLEGMEAGQKVHEKR----LSNGSIDSTDDTSQIVELQELLEK 180
Cdd:PRK03918 395 ELEKAKEEIEEEI-----------SKITARIGELKKEIKELKKAIEELKKAKgkcpVCGRELTEEHRKELLEEYTAELKR 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 181 QNYEMAQMKERLTALSSRVGEVEQEAETARK---------DLIKTEEMNTKYQRDIREcylQAMAQKEDMEERITTLEKR 251
Cdd:PRK03918 464 IEKELKEIEEKERKLRKELRELEKVLKKESEliklkelaeQLKELEEKLKKYNLEELE---KKAEEYEKLKEKLIKLKGE 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 252 YLSAQRESTSIHDMNDK---LENELANKEA----ILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAA 324
Cdd:PRK03918 541 IKSLKKELEKLEELKKKlaeLEKKLDELEEelaeLLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKE 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 325 LTKAEERHGNIEERMRHLEGQLEEKNQELQRARQreKMNEEHNKRLSDTVDRLltesnERLQLHLKERMAALEEknvLIQ 404
Cdd:PRK03918 621 LKKLEEELDKAFEELAETEKRLEELRKELEELEK--KYSEEEYEELREEYLEL-----SRELAGLRAELEELEK---RRE 690
|
410 420 430
....*....|....*....|....*....|....
gi 1907075650 405 ESENFRKNLEESLHDKERLAEEIEKLRSELDQMK 438
Cdd:PRK03918 691 EIKKTLEKLKEELEEREKAKKELEKLEKALERVE 724
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
33-431 |
8.48e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 56.98 E-value: 8.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 33 TKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMtvVKRQAQSPSGVS------------------ 94
Cdd:TIGR00606 411 AQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKF--VIKELQQLEGSSdrileldqelrkaerels 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 95 -----SEVEVLKA-LKSLFEHHKALDEKIVALREQNVHIQRKmVSSEGSTESEHLEGMEAGQKVHE--KRLSNGSIDSTD 166
Cdd:TIGR00606 489 kaeknSLTETLKKeVKSLQNEKADLDRKLRKLDQEMEQLNHH-TTTRTQMEMLTKDKMDKDEQIRKikSRHSDELTSLLG 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 167 DTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREcylqaMAQKEDMEERIT 246
Cdd:TIGR00606 568 YFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFD-----VCGSQDEESDLE 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 247 TLEKRYLSAQRESTSIH---DMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAET-LPEVEAELA--- 319
Cdd:TIGR00606 643 RLKEEIEKSSKQRAMLAgatAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDkLKSTESELKkke 722
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 320 -QRIAALTKAEERHGNIEERMRHLEgQLEEKNQELQRARQREKMNEEHNKRLSDTV-------DRLLTESN--ERLQLHL 389
Cdd:TIGR00606 723 kRRDEMLGLAPGRQSIIDLKEKEIP-ELRNKLQKVNRDIQRLKNDIEEQETLLGTImpeeesaKVCLTDVTimERFQMEL 801
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1907075650 390 KERMAALEEKNVLIQESE------NFRKNLEESLHDKERLAEEIEKLR 431
Cdd:TIGR00606 802 KDVERKIAQQAAKLQGSDldrtvqQVNQEKQEKQHELDTVVSKIELNR 849
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
932-987 |
9.02e-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: 9.02e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907075650 932 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 987
Cdd:smart00454 11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
255-435 |
1.08e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.20 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 255 AQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGN 334
Cdd:PRK02224 197 EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 335 IEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNErlqlhLKERmaaLEEKNVLIQESENFRKNLE 414
Cdd:PRK02224 277 LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEE-----LRDR---LEECRVAAQAHNEEAESLR 348
|
170 180
....*....|....*....|.
gi 1907075650 415 ESLHDKERLAEEIEKLRSELD 435
Cdd:PRK02224 349 EDADDLEERAEELREEAAELE 369
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
248-440 |
1.14e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 248 LEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTK 327
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 328 AEERHgNIEERMRHLEGQLEE---KNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKErmaaleeknvLIQ 404
Cdd:COG4717 131 YQELE-ALEAELAELPERLEEleeRLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD----------LAE 199
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907075650 405 ESENFRKNLEESLHDKERLAEEIEKLRSELDQMKMR 440
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
166-434 |
2.21e-07 |
|
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: 55.36 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 166 DDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVE-QEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEER 244
Cdd:pfam02463 159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKlQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 245 ITTLEKRYLSAQRESTSihdMNDKLENELANKEAILRQMEEKNR--QLQERLELAEQKLQQTMRKAETLPEVEAELAQRI 322
Cdd:pfam02463 239 IDLLQELLRDEQEEIES---SKQEIEKEEEKLAQVLKENKEEEKekKLQEEELKLLAKEEEELKSELLKLERRKVDDEEK 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 323 AA-----LTKAEERHGNIEERMRHLEGQLEEKN---QELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMA 394
Cdd:pfam02463 316 LKesekeKKKAEKELKKEKEEIEELEKELKELEikrEAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE 395
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1907075650 395 ALEEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSEL 434
Cdd:pfam02463 396 ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEE 435
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
27-440 |
2.45e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 27 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSL---RMTVVKRQAQSPSGVSSEVEVLKAL 103
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELaeaEEELEELAEELLEALRAAAELAAQL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 104 KSLFEHHKALDEKIVALREQNVHIQRKMVSSEGS--TESEHLEGMEAGQKVHEKRLSNGSIDSTDDTSQIVELQELLEKQ 181
Cdd:COG1196 403 EELEEAEEALLERLERLEEELEELEEALAELEEEeeEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 182 NYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTE------------EMNTKYQRDIRECYLQAMAQK-----EDMEER 244
Cdd:COG1196 483 LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGlrglagavavliGVEAAYEAALEAALAAALQNIvveddEVAAAA 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 245 ITTLEKRYLS----------AQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEV 314
Cdd:COG1196 563 IEYLKAAKAGratflpldkiRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTL 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 315 EAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQRE-KMNEEHNKRLSDTVDRLLTESNERLQLHLKERM 393
Cdd:COG1196 643 AGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLaEEELELEEALLAEEEEERELAEAEEERLEEELE 722
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1907075650 394 AALEEKNVLIQESENFRKNLEESLHDKERLAEE------IEKLRSELDQMKMR 440
Cdd:COG1196 723 EEALEEQLEAEREELLEELLEEEELLEEEALEElpeppdLEELERELERLERE 775
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
280-438 |
3.24e-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: 54.00 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 280 LRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKaeeRHGNIEERMRHLEGQLEEKNQELQRARQR 359
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR---RIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 360 EKMNEEHNKRLSDTVDRL--------------LTESNERLQLH---LKERMAALEEKNVLIQESENFRKNLEESLHDKER 422
Cdd:COG4942 99 LEAQKEELAELLRALYRLgrqpplalllspedFLDAVRRLQYLkylAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170
....*....|....*.
gi 1907075650 423 LAEEIEKLRSELDQMK 438
Cdd:COG4942 179 LLAELEEERAALEALK 194
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
30-445 |
3.99e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 30 AALTKELNACREQL---LEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVvkrqaqspSGVSSEVEVLKALKSL 106
Cdd:PRK03918 168 GEVIKEIKRRIERLekfIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL--------EKLEKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 107 FE-----------HHKALDEKIVALREQNVHIQRKM-VSSEGSTESEHLEG-------MEAGQKVHEKRLSNGSIDSTDD 167
Cdd:PRK03918 240 IEelekeleslegSKRKLEEKIRELEERIEELKKEIeELEEKVKELKELKEkaeeyikLSEFYEEYLDELREIEKRLSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 168 TSQIVELQELLEKqnyemaqmkerLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRdirecYLQAMAQKEDMEERIT- 246
Cdd:PRK03918 320 EEEINGIEERIKE-----------LEEKEERLEELKKKLKELEKRLEELEERHELYEE-----AKAKKEELERLKKRLTg 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 247 ----TLEKRYLSAQRESTSIHDMNDKLENELANkeaiLRQMEEKNRQLQERLELAEQKLQQTMR------KAETLPEVEA 316
Cdd:PRK03918 384 ltpeKLEKELEELEKAKEEIEEEISKITARIGE----LKKEIKELKKAIEELKKAKGKCPVCGRelteehRKELLEEYTA 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 317 ELAQRIAALTKAEERHGNIEERMRHLEGQLEeKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLhLKERMAAL 396
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLK-KESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEK-LKEKLIKL 537
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1907075650 397 EEKnvliqesenfRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSLI 445
Cdd:PRK03918 538 KGE----------IKSLKKELEKLEELKKKLAELEKKLDELEEELAELL 576
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
1010-1081 |
5.21e-07 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 48.06 E-value: 5.21e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907075650 1010 VLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDEnfdysSLALLLQIPTQNTQARQILEREYNNLLA 1081
Cdd:smart00454 1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLT-----SEEDLKELGITKLGHRKKILKAIQKLKE 67
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
27-430 |
6.24e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 6.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 27 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQaqspsgVSSEVEVLKALKSL 106
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAE------LAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 107 FEHHKALDEKIVALREQNVHIQRKMVSSEGSTESEHLEGMEagqkvhekrlsngsidstDDTSQIVELQELLEKQNYEMA 186
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ------------------DLAEELEELQQRLAELEEELE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 187 QMKERLTALSSRVGEVEQEAETARKDLIKTEEMNT--------------------------------------KYQRDIR 228
Cdd:COG4717 217 EAQEELEELEEELEQLENELEAAALEERLKEARLLlliaaallallglggsllsliltiagvlflvlgllallFLLLARE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 229 ECYLQAMAQKEDMEERITTLEKRYLSAQRESTSI-HDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK 307
Cdd:COG4717 297 KASLGKEAEELQALPALEELEEEELEELLAALGLpPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 308 AETLPEVEAELAQRIAALTKAEErhgnIEERMRHLEGQLEEKNQELQRARQREKmNEEHNKRLSDTVDRLLTESNERLQL 387
Cdd:COG4717 377 AEAGVEDEEELRAALEQAEEYQE----LKEELEELEEQLEELLGELEELLEALD-EEELEEELEELEEELEELEEELEEL 451
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1907075650 388 HlkERMAALEEKnvlIQESENfRKNLEESLHDKERLAEEIEKL 430
Cdd:COG4717 452 R--EELAELEAE---LEQLEE-DGELAELLQELEELKAELREL 488
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
272-429 |
7.93e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 53.24 E-value: 7.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 272 ELANKEAIlRQMEEKNRQLQERLELAEQKLQQTMRKAETlpEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ 351
Cdd:PRK12704 34 KEAEEEAK-RILEEAKKEAEAIKKEALLEAKEEIHKLRN--EFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 352 ELQRARQREKMNEEHNKRLSDTVDRLLTESNERLqlhlkERMAAL---EEKNVLIQESEnfrknlEESLHDKERLAEEIE 428
Cdd:PRK12704 111 ELEKKEKELEQKQQELEKKEEELEELIEEQLQEL-----ERISGLtaeEAKEILLEKVE------EEARHEAAVLIKEIE 179
|
.
gi 1907075650 429 K 429
Cdd:PRK12704 180 E 180
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
232-437 |
8.07e-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: 53.43 E-value: 8.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 232 LQAMAQKEDMEERITTLEKRY----LSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQK------L 301
Cdd:TIGR00618 183 LMEFAKKKSLHGKAELLTLRSqlltLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQlkkqqlL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 302 QQTMRKAETLPEVEAELAQRIAALTKAE--ERHGNIEERMRHLEGQLEEKNQELQ-RARQREKMNEEHNKRLSDTVDRLL 378
Cdd:TIGR00618 263 KQLRARIEELRAQEAVLEETQERINRARkaAPLAAHIKAVTQIEQQAQRIHTELQsKMRSRAKLLMKRAAHVKQQSSIEE 342
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907075650 379 TESNERLQLHLKERMAALEEKNVLIQESENFRKNLEESLH----DKERLAEEIEKLRSELDQM 437
Cdd:TIGR00618 343 QRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHtlqqQKTTLTQKLQSLCKELDIL 405
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
170-440 |
8.69e-07 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 52.23 E-value: 8.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 170 QIVELQELLEKQNYEMAQMKERLTALssrvgeVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITTLE 249
Cdd:pfam13868 81 QIEEREQKRQEEYEEKLQEREQMDEI------VERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREED 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 250 KRYLSAQREstsihdMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAE 329
Cdd:pfam13868 155 ERILEYLKE------KAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 330 ERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEknvLIQESE-N 408
Cdd:pfam13868 229 KKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEK---QIEEREeQ 305
|
250 260 270
....*....|....*....|....*....|..
gi 1907075650 409 FRKNLEESLHDKERLAEEIEKLRSELDQMKMR 440
Cdd:pfam13868 306 RAAEREEELEEGERLREEEAERRERIEEERQK 337
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
168-446 |
8.94e-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: 53.43 E-value: 8.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 168 TSQIVELQELLEKQNYemAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKyqrdIRECYLQAMAQKEDMEERITT 247
Cdd:TIGR00618 273 RAQEAVLEETQERINR--ARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAK----LLMKRAAHVKQQSSIEEQRRL 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 248 LEkrylSAQRESTSIHDMNDKlenELANKEAILRQMEEKN--RQLQERLELAEQKLQQTMRKAETLPE----VEAELAQR 321
Cdd:TIGR00618 347 LQ----TLHSQEIHIRDAHEV---ATSIREISCQQHTLTQhiHTLQQQKTTLTQKLQSLCKELDILQReqatIDTRTSAF 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 322 IAALTKAEERHGNIEERMRHLEGQ----------LEEKNQELQRARQR---EKMNEEHNKRLSDTVDRLLTESNERLQLH 388
Cdd:TIGR00618 420 RDLQGQLAHAKKQQELQQRYAELCaaaitctaqcEKLEKIHLQESAQSlkeREQQLQTKEQIHLQETRKKAVVLARLLEL 499
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907075650 389 ------LKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSLIE 446
Cdd:TIGR00618 500 qeepcpLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKE 563
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
184-414 |
1.09e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 52.82 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 184 EMAQMKE--RLTALSSRVGE-VEQEAETARKDLIKTEEMNTKYQRDIRECYL----QAMAQKEDM----EERITTLEKRY 252
Cdd:pfam17380 373 EISRMREleRLQMERQQKNErVRQELEAARKVKILEEERQRKIQQQKVEMEQiraeQEEARQREVrrleEERAREMERVR 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 253 LSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQtmRKAETLPE------VEAELAQRIAALT 326
Cdd:pfam17380 453 LEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEE--RKQAMIEEerkrklLEKEMEERQKAIY 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 327 KAEERHGNIEERMRHLEgqLEEknqelqRARQREKMneehnkrlsdtvdRLLTESNERLQLHLKERmaaleEKNVLIQES 406
Cdd:pfam17380 531 EEERRREAEEERRKQQE--MEE------RRRIQEQM-------------RKATEERSRLEAMERER-----EMMRQIVES 584
|
....*...
gi 1907075650 407 ENFRKNLE 414
Cdd:pfam17380 585 EKARAEYE 592
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
27-509 |
1.25e-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: 52.92 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 27 QEFAALTKELNacrEQLLEKEEEISELKAERNNTRLLL--------EHLECLVSRHERSLRMTVVKR---QAQSPSgVSS 95
Cdd:pfam12128 279 EERQETSAELN---QLLRTLDDQWKEKRDELNGELSAAdaavakdrSELEALEDQHGAFLDADIETAaadQEQLPS-WQS 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 96 EVEVL-KALKSLFEHHKALDEKIVALREQnvhiqrkmVSSEGSTEsehLEGMEAGQ-KVHEKRLSNGSIDSTDDTSQIVE 173
Cdd:pfam12128 355 ELENLeERLKALTGKHQDVTAKYNRRRSK--------IKEQNNRD---IAGIKDKLaKIREARDRQLAVAEDDLQALESE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 174 LQELLEKQNYEMAQMKERLtalSSRVGE--VEQEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITTLEKR 251
Cdd:pfam12128 424 LREQLEAGKLEFNEEEYRL---KSRLGElkLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKR 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 252 YLSAQRESTSIHDMNDKLENELA-----------------NKEAIL-RQMEEK--NRQLQERLELAEQKLQQTMRKAETL 311
Cdd:pfam12128 501 RDQASEALRQASRRLEERQSALDelelqlfpqagtllhflRKEAPDwEQSIGKviSPELLHRTDLDPEVWDGSVGGELNL 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 312 -------------------PEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSD 372
Cdd:pfam12128 581 ygvkldlkridvpewaaseEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFD 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 373 TVDRL---LTESNERLQLHLKERMAALE-EKNVLIQESENF-----RKNLEESLHDKERLAEEIEKLRSELDQMKmrTGS 443
Cdd:pfam12128 661 EKQSEkdkKNKALAERKDSANERLNSLEaQLKQLDKKHQAWleeqkEQKREARTEKQAYWQVVEGALDAQLALLK--AAI 738
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907075650 444 LIEPTISRTHIDT-STELRYSVGSL-VDSQSDYRTTKVIRRPRRGRMGVRRDEPKVKSLgdHEWNRTQ 509
Cdd:pfam12128 739 AARRSGAKAELKAlETWYKRDLASLgVDPDVIAKLKREIRTLERKIERIAVRRQEVLRY--FDWYQET 804
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
233-407 |
1.43e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 233 QAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAilrQMEEKNRQLQERLELAEQKLQQTMRKAETLP 312
Cdd:COG3883 27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA---EIAEAEAEIEERREELGERARALYRSGGSVS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 313 EVEA--------ELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNER 384
Cdd:COG3883 104 YLDVllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL 183
|
170 180
....*....|....*....|...
gi 1907075650 385 LQLHLKERMAALEEKNVLIQESE 407
Cdd:COG3883 184 LAQLSAEEAAAEAQLAELEAELA 206
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
169-452 |
1.68e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.83 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 169 SQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRecylQAMAQKEDMEERITTL 248
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE----SLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 249 EKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMrkaetlpevEAELAQRIAALTKA 328
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS---------EAEAEQALDELLKE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 329 EERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESEN 408
Cdd:COG4372 192 ANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEK 271
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1907075650 409 FRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSLIEPTISRT 452
Cdd:COG4372 272 DTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALED 315
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
170-348 |
1.71e-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: 50.69 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 170 QIVELQELLEkqnyEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAmaqkEDMEERITTLE 249
Cdd:COG1579 8 ALLDLQELDS----ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI----EEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 250 KR---------YLSAQRESTSIHDMNDKLEnelankEAILRQMEEKNrQLQERLELAEQKLQQtmrKAETLPEVEAELAQ 320
Cdd:COG1579 80 EQlgnvrnnkeYEALQKEIESLKRRISDLE------DEILELMERIE-ELEEELAELEAELAE---LEAELEEKKAELDE 149
|
170 180
....*....|....*....|....*...
gi 1907075650 321 RIAALTKAEERhgnIEERMRHLEGQLEE 348
Cdd:COG1579 150 ELAELEAELEE---LEAEREELAAKIPP 174
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
152-432 |
2.64e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.88 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 152 VHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDL------IKTEEMNTKYQR 225
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLnlvqtaLRQQEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 226 DIRECYLQAMAQKE-------------------------------DMEERITTLEKR---YLSAQRESTSIHDMNDKLEN 271
Cdd:PRK04863 356 DLEELEERLEEQNEvveeadeqqeenearaeaaeeevdelksqlaDYQQALDVQQTRaiqYQQAVQALERAKQLCGLPDL 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 272 ELANKEAILRQMEEKNRQLQERLELAEQKLQ-------------QTMRKAetLPEVEAELAQRIA--ALTKAEErHGNIE 336
Cdd:PRK04863 436 TADNAEDWLEEFQAKEQEATEELLSLEQKLSvaqaahsqfeqayQLVRKI--AGEVSRSEAWDVAreLLRRLRE-QRHLA 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 337 ERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDrllteSNERLQLHLKERMAALEEknvLIQESENFRKNLEES 416
Cdd:PRK04863 513 EQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLD-----DEDELEQLQEELEARLES---LSESVSEARERRMAL 584
|
330
....*....|....*.
gi 1907075650 417 LHDKERLAEEIEKLRS 432
Cdd:PRK04863 585 RQQLEQLQARIQRLAA 600
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
27-362 |
3.32e-06 |
|
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: 50.84 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 27 QEFAALTKELNA-------CREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQA--QSPSGVSSEV 97
Cdd:pfam19220 69 RELAGLTRRLSAaegeleeLVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRAleEENKALREEA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 98 EVLKALKSLFEHHKALDEKIVALREQNVHIQRKMVSSEGSTESEHlegmEAGQKVHEKRLSNGSIDSTDDTSQIVELQEL 177
Cdd:pfam19220 149 QAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAEL----TRRLAELETQLDATRARLRALEGQLAAEQAE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 178 LEK----QNYEMAQMKERLTALSSRVgeveqEAETARkdLIKTEEMNTkyqrdirecylQAMAQKEDMEERITTLEKRYL 253
Cdd:pfam19220 225 RERaeaqLEEAVEAHRAERASLRMKL-----EALTAR--AAATEQLLA-----------EARNQLRDRDEAIRAAERRLK 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 254 SAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLElaeqklqqTMRKAetlpeveaeLAQRIAALTKAEERHG 333
Cdd:pfam19220 287 EASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAE--------MLTKA---------LAAKDAALERAEERIA 349
|
330 340 350
....*....|....*....|....*....|....*.
gi 1907075650 334 NIEERMRHLEGQ-------LEEKNQELQRARQREKM 362
Cdd:pfam19220 350 SLSDRIAELTKRfeveraaLEQANRRLKEELQRERA 385
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
27-457 |
3.72e-06 |
|
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: 51.59 E-value: 3.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 27 QEFAA-LTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQ------AQSPSGVSSEVEV 99
Cdd:TIGR00606 694 QEFISdLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQkvnrdiQRLKNDIEEQETL 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 100 LKALKSLFEHHKALDEKIVALreQNVHIQRKMVSSEGSTESEHLEGMEAGQKVHEKRLSNGSIDSTDDT--SQIVELQEL 177
Cdd:TIGR00606 774 LGTIMPEEESAKVCLTDVTIM--ERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTvvSKIELNRKL 851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 178 LEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTkyqrDIRECYLQAMAQKEDMEERITTLEKrylSAQR 257
Cdd:TIGR00606 852 IQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELST----EVQSLIREIKDAKEQDSPLETFLEK---DQQE 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 258 ESTSIHDMNDklENELANKEaiLRQMEEKNRQLQERLELAEQKLQQTmrKAETLPEVEAELAQRIAALTKAEERHGNIEE 337
Cdd:TIGR00606 925 KEELISSKET--SNKKAQDK--VNDIKEKVKNIHGYMKDIENKIQDG--KDDYLKQKETELNTVNAQLEECEKHQEKINE 998
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 338 RMRHLEGQLEEKNQE---LQRARQREKMNEEHnKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESENF----- 409
Cdd:TIGR00606 999 DMRLMRQDIDTQKIQerwLQDNLTLRKRENEL-KEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLalgrq 1077
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1907075650 410 RKNLEESLHDKERLAEEI-----EKLRSELDQMKMRTGSLIEPTISRTHIDTS 457
Cdd:TIGR00606 1078 KGYEKEIKHFKKELREPQfrdaeEKYREMMIVMRTTELVNKDLDIYYKTLDQA 1130
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
147-340 |
3.83e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 147 EAGQKVHEKRLSNGSIDSTDDT----SQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAetarkdlikTEEMNTK 222
Cdd:COG3206 193 EAEAALEEFRQKNGLVDLSEEAklllQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDAL---------PELLQSP 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 223 YQRDIRECYLQAMAQKEDMEERITTLEKRYLSAQREstsIHDMNDKLENELankEAILRQMEEKNRQLQERLELAEQKLQ 302
Cdd:COG3206 264 VIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ---IAALRAQLQQEA---QRILASLEAELEALQAREASLQAQLA 337
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907075650 303 QTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMR 340
Cdd:COG3206 338 QLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
104-600 |
3.86e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 51.27 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 104 KSLFEHHKALDEKIVALREQNVHIQRKMvsSEGSTESEHLEGMEAGQKVHEKRLSNGSIDSTDDTSQIVELQE-LLEKQN 182
Cdd:pfam15921 92 RRLNESNELHEKQKFYLRQSVIDLQTKL--QEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEdMLEDSN 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 183 YEMAQMKERLTALSSRVGEVEQE----AETARKDLIKTEEMNTKYQRDIRECyLQAMAQKEDME-----ERITTLEKRYL 253
Cdd:pfam15921 170 TQIEQLRKMMLSHEGVLQEIRSIlvdfEEASGKKIYEHDSMSTMHFRSLGSA-ISKILRELDTEisylkGRIFPVEDQLE 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 254 SAQRESTS-----IHDMNDKLENELANKEAILRQMEEKN-------RQLQERLEL-AEQKLQQTMRKAETLPEVEAELAQ 320
Cdd:pfam15921 249 ALKSESQNkiellLQQHQDRIEQLISEHEVEITGLTEKAssarsqaNSIQSQLEIiQEQARNQNSMYMRQLSDLESTVSQ 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 321 RIAALTKAEERHgniEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLT-------------ESNERL-- 385
Cdd:pfam15921 329 LRSELREAKRMY---EDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLAdlhkrekelslekEQNKRLwd 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 386 -----QLHLKERMAALEEKNVLIQESENFRKNLEE-----------SLHDKERLAEEIEKLRSELDQMKMRTGSLIEPTI 449
Cdd:pfam15921 406 rdtgnSITIDHLRRELDDRNMEVQRLEALLKAMKSecqgqmerqmaAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELT 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 450 SRTHIDTSTELRYS--VGSLVDSQSDYRTTKVIRRPRRGRMGVRRDEPK-VKSLGDHEWNRTQQIGVLGSHPFESDTEMS 526
Cdd:pfam15921 486 AKKMTLESSERTVSdlTASLQEKERAIEATNAEITKLRSRVDLKLQELQhLKNEGDHLRNVQTECEALKLQMAEKDKVIE 565
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907075650 527 DIddddRETIFSSMDLLSPSGHSDA--QTLAMMLQEQLDAINKEIRLIQEEKESTELRAEEIENRVASVSLEGLNL 600
Cdd:pfam15921 566 IL----RQQIENMTQLVGQHGRTAGamQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKL 637
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
42-399 |
3.95e-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: 51.26 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 42 QLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSL-RMTVVKRQAQSPSGvsSEVEVLKALKSLFEHHKALDEKIVAL 120
Cdd:pfam05483 385 ELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLdEKKQFEKIAEELKG--KEQELIFLLQAREKEIHDLEIQLTAI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 121 REQNVHIQRKMVSSEGSTESEHLEGMEAGQKVHEKRLSNGSI--DSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSR 198
Cdd:pfam05483 463 KTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELtqEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEK 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 199 VGEVEQEAETARKDLI-KTEEMNTKY------QRDIRECYLQAMAQKEDMEERITTLEKRYLSAQRESTSIHDMN----- 266
Cdd:pfam05483 543 EMNLRDELESVREEFIqKGDEVKCKLdkseenARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENkalkk 622
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 267 ----------------DKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETL--------PEVEAELAQRI 322
Cdd:pfam05483 623 kgsaenkqlnayeikvNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIadeavklqKEIDKRCQHKI 702
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 323 AALTKAEERHGN-----IEERMRHLeGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLT---ESNERLQLHLKERMA 394
Cdd:pfam05483 703 AEMVALMEKHKHqydkiIEERDSEL-GLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEiekEEKEKLKMEAKENTA 781
|
....*
gi 1907075650 395 ALEEK 399
Cdd:pfam05483 782 ILKDK 786
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
97-443 |
4.17e-06 |
|
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: 51.11 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 97 VEVLKALKSLFEHHKALDEKIVALREQNVHIQRKMVSSEGSTESEHLEGMEAGQKVHEKRLSNGSIDST-DDTSQIVEL- 174
Cdd:COG5185 183 GLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTsDKLEKLVEQn 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 175 QELLEKQNYEMAQMKERLTALSS-----------RVGEVEQEAETAR-----KDLIKTEEMNTKYQRDIRECYLQAMAQK 238
Cdd:COG5185 263 TDLRLEKLGENAESSKRLNENANnlikqfentkeKIAEYTKSIDIKKateslEEQLAAAEAEQELEESKRETETGIQNLT 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 239 EDMEERITTLEKRYLSAQRESTSIHDMND------KLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLP 312
Cdd:COG5185 343 AEIEQGQESLTENLEAIKEEIENIVGEVElsksseELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQI 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 313 E--------VEAELAQRIAALTKAEERhgnIEERMRHLEGQLEEKNQELQRARQRE--KMNEEHNKRLSDTVDRLLT--E 380
Cdd:COG5185 423 EelqrqieqATSSNEEVSKLLNELISE---LNKVMREADEESQSRLEEAYDEINRSvrSKKEDLNEELTQIESRVSTlkA 499
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907075650 381 SNERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKERlaEEIEKLRSELDQMKMRTGS 443
Cdd:COG5185 500 TLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILAL--ENLIPASELIQASNAKTDG 560
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
25-397 |
4.61e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 51.27 E-value: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 25 TFQEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKrQAQSPSGVSSEVEVLKALK 104
Cdd:pfam15921 459 SLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAE-ITKLRSRVDLKLQELQHLK 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 105 SLFEH-------------HKALDEKIVALREQNVHIQRKMVSSEGSTESE-HLEGMEAGQKVHEKRLSNGSIDSTDDT-- 168
Cdd:pfam15921 538 NEGDHlrnvqtecealklQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAmQVEKAQLEKEINDRRLELQEFKILKDKkd 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 169 SQIVELQELLEKQNYEMAQM----KERLTALSSRVGEVEQ---EAETARKDLIKTEEMNTKYQRDIREcylqamaQKEDM 241
Cdd:pfam15921 618 AKIRELEARVSDLELEKVKLvnagSERLRAVKDIKQERDQllnEVKTSRNELNSLSEDYEVLKRNFRN-------KSEEM 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 242 EERITTLEKRYLSAQRE----STSIHDMNDKLENELANKEAILRQMEEKNRQ---LQERLELAEQKLQQTMRKAETLPEV 314
Cdd:pfam15921 691 ETTTNKLKMQLKSAQSEleqtRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQidaLQSKIQFLEEAMTNANKEKHFLKEE 770
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 315 EAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMneehnkRLSDTVDRLLTESNERLQLHLKERMA 394
Cdd:pfam15921 771 KNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASL------QFAECQDIIQRQEQESVRLKLQHTLD 844
|
...
gi 1907075650 395 ALE 397
Cdd:pfam15921 845 VKE 847
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
283-436 |
4.91e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.15 E-value: 4.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 283 MEEKNRQLqERLELAEQKLQQTMRKAETLP----EVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQ 358
Cdd:COG1579 2 MPEDLRAL-LDLQELDSELDRLEHRLKELPaelaELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 359 R--------------------EKMNEEHNKRLSDTVDRLltESNERLQLHLKERMAALEEKnvLIQESENFRKNLEESLH 418
Cdd:COG1579 81 QlgnvrnnkeyealqkeieslKRRISDLEDEILELMERI--EELEEELAELEAELAELEAE--LEEKKAELDEELAELEA 156
|
170
....*....|....*...
gi 1907075650 419 DKERLAEEIEKLRSELDQ 436
Cdd:COG1579 157 ELEELEAEREELAAKIPP 174
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
32-429 |
5.19e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.79 E-value: 5.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 32 LTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTvvKRQAQSpsgVSSEVEVLKALKSLfEHHK 111
Cdd:TIGR04523 237 KQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKEL--EKQLNQ---LKSEISDLNNQKEQ-DWNK 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 112 ALDEKIVALREQNVHIQRKMVSSEGSTES--EHLEGMEagQKVHEKRLSNGSIDStddtsQIVELQELLEKQNYEMAQMK 189
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQlnEQISQLK--KELTNSESENSEKQR-----ELEEKQNEIEKLKKENQSYK 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 190 ERLTALSSRVGEVE-----QEAETARKDL-IKTEEMN----TKYQRDIRECYLQAMAQKEDMEERITTLEKRY--LSAQR 257
Cdd:TIGR04523 384 QEIKNLESQINDLEskiqnQEKLNQQKDEqIKKLQQEkellEKEIERLKETIIKNNSEIKDLTNQDSVKELIIknLDNTR 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 258 ES--TSIHDMNDKLENELANKEAILRQMEEKNRQLqerLELAEQKLQqtmrkaetLPEVEAELAQRIAALTKAEErhgNI 335
Cdd:TIGR04523 464 ESleTQLKVLSRSINKIKQNLEQKQKELKSKEKEL---KKLNEEKKE--------LEEKVKDLTKKISSLKEKIE---KL 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 336 EERMRHLEGQLEEKNQELqrarqrEKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESENFRKNLEE 415
Cdd:TIGR04523 530 ESEKKEKESKISDLEDEL------NKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIK 603
|
410
....*....|....
gi 1907075650 416 SLHDKERLAEEIEK 429
Cdd:TIGR04523 604 EIEEKEKKISSLEK 617
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
239-440 |
5.77e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 5.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 239 EDMEERITTLE------KRYLSAQRESTSIHDMNDKLEnelankeaiLRQMEEKNRQLQERLELAEQKLQQTMRKAETLP 312
Cdd:COG4913 245 EDAREQIELLEpirelaERYAAARERLAELEYLRAALR---------LWFAQRRLELLEAELEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 313 EVEAELAQRIAALTKAEERHGNIEErmrhleGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKER 392
Cdd:COG4913 316 ARLDALREELDELEAQIRGNGGDRL------EQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEA 389
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907075650 393 MAALEEknvLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQMKMR 440
Cdd:COG4913 390 AALLEA---LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
242-398 |
5.85e-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: 5.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 242 EERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLElaeqKLQQTMRKAETLPEVEAeLAQR 321
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK----KYEEQLGNVRNNKEYEA-LQKE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907075650 322 IAALtkaEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEE 398
Cdd:COG1579 98 IESL---KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| SAM_superfamily |
cd09487 |
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
932-983 |
6.05e-06 |
|
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.
Pssm-ID: 188886 [Multi-domain] Cd Length: 56 Bit Score: 44.54 E-value: 6.05e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1907075650 932 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGI 983
Cdd:cd09487 4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
170-358 |
6.23e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 6.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 170 QIVELQELLEKQNyEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEemntkyQRDIRECYLQAMAQKEDMEERITTLE 249
Cdd:COG4913 250 QIELLEPIRELAE-RYAAARERLAELEYLRAALRLWFAQRRLELLEAE------LEELRAELARLEAELERLEARLDALR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 250 KRYLSAQREstsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQkLQQTMRKAE-TLPEVEAELAQRI----AA 324
Cdd:COG4913 323 EELDELEAQ---------IRGNGGDRLEQLEREIERLERELEERERRRAR-LEALLAALGlPLPASAEEFAALRaeaaAL 392
|
170 180 190
....*....|....*....|....*....|....
gi 1907075650 325 LTKAEERHGNIEERMRHLEGQLEEKNQELQRARQ 358
Cdd:COG4913 393 LEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
168-461 |
6.44e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 6.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 168 TSQIVELQELLEKQNYEMAQMKERLTALS--SRVGEVEQEAETARKDLIKTEEMntkyqrdiRECYLQAMAQKEDMEERI 245
Cdd:COG4913 623 EEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAE--------LERLDASSDDLAALEEQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 246 TTLEKRYlsaqrestsihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlPEVEAELAQRIAAL 325
Cdd:COG4913 695 EELEAEL--------------EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR--LELRALLEERFAAA 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 326 tKAEERHGNIEERmrhLEGQLEEKNQELQRARQR-EKMNEEHNKRLSDTVDRLLT--ESNERLQLHLK----ERMAALEE 398
Cdd:COG4913 759 -LGDAVERELREN---LEERIDALRARLNRAEEElERAMRAFNREWPAETADLDAdlESLPEYLALLDrleeDGLPEYEE 834
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907075650 399 K--NVLIQESENFRKNLEESLHDKERLAEE-IEKLRSELDQMKMRTGSLIEPTISRTHIDTSTELR 461
Cdd:COG4913 835 RfkELLNENSIEFVADLLSKLRRAIREIKErIDPLNDSLKRIPFGPGRYLRLEARPRPDPEVREFR 900
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
185-376 |
8.06e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 8.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 185 MAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITTLEKRYLSAQRESTSIHD 264
Cdd:COG1196 632 LEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 265 MNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNI--------- 335
Cdd:COG1196 712 AEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPVnllaieeye 791
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907075650 336 --EERMRHLEGQLEeknqELQRARQR-----EKMNEEHNKRLSDTVDR 376
Cdd:COG1196 792 elEERYDFLSEQRE----DLEEARETleeaiEEIDRETRERFLETFDA 835
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
27-438 |
8.09e-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: 50.35 E-value: 8.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 27 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAqspsgVSSEVEVLKALK-S 105
Cdd:TIGR00618 386 QQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAA-----ITCTAQCEKLEKiH 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 106 LFEHHKALDEKIVALRE-QNVHIQRKMVSSEGSTESEHLEGME---AGQKVHEKRLSNGSIDSTDDTSQIVELQELLEKQ 181
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTkEQIHLQETRKKAVVLARLLELQEEPcplCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQL 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 182 NYEMAQMKERLTALSSRVGEVEQEAETARKDLIK--------TEEMN--TKYQRDIREcYLQAMAQKEDMEERITTLEKR 251
Cdd:TIGR00618 541 ETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSIltqcdnrsKEDIPnlQNITVRLQD-LTEKLSEAEDMLACEQHALLR 619
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 252 YLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQtMRKAETLPEVEAELAQRIAALTKAEER 331
Cdd:TIGR00618 620 KLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLP-KELLASRQLALQKMQSEKEQLTYWKEM 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 332 HGNIEERMRHLEGQLEEKNQELQR------------ARQREKMNEEHNK--RLSDTVDRLLTESNERLQLHLKERMAALE 397
Cdd:TIGR00618 699 LAQCQTLLRELETHIEEYDREFNEienassslgsdlAAREDALNQSLKElmHQARTVLKARTEAHFNNNEEVTAALQTGA 778
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1907075650 398 EKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQMK 438
Cdd:TIGR00618 779 ELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDIL 819
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
49-386 |
8.88e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.90 E-value: 8.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 49 EISELKAERNNTRLLLEHLECLVSRherslrmtVVKRQAQSPSGVSSEV-EVLKALKSLFEHHKALDEKIVALREQNVHI 127
Cdd:PRK01156 371 SIESLKKKIEEYSKNIERMSAFISE--------ILKIQEIDPDAIKKELnEINVKLQDISSKVSSLNQRIRALRENLDEL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 128 QRKMVSSEGSTESEhLEGMEAGQKVHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSrvGEVEQ--- 204
Cdd:PRK01156 443 SRNMEMLNGQSVCP-VCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLES--EEINKsin 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 205 ---EAETARKDL--------------IKTEEMNTKYQ-------RDIRECYLQAMAQKEDMEerITTLEKRYLSAQREST 260
Cdd:PRK01156 520 eynKIESARADLedikikinelkdkhDKYEEIKNRYKslkledlDSKRTSWLNALAVISLID--IETNRSRSNEIKKQLN 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 261 SIHDMNDKLENELANKEA----ILRQMEEKNRQLQERLELAEQK--LQQTMR-KAETLPEVEAELAQRIAALTKAEERHG 333
Cdd:PRK01156 598 DLESRLQEIEIGFPDDKSyidkSIREIENEANNLNNKYNEIQENkiLIEKLRgKIDNYKKQIAEIDSIIPDLKEITSRIN 677
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1907075650 334 NIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVdrllTESNERLQ 386
Cdd:PRK01156 678 DIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRI----NDINETLE 726
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
257-434 |
9.51e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 9.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 257 RESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQ--QTMRKAETLPEVEAELAQRIAALTKAEERHGN 334
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 335 IEERMRHLEGQLEEKNQELQRARQRekMNEEHNKRLSDTVDRLltesnERLQlhlkERMAALEEKNVLIQESENFRKNLE 414
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQ--LSLATEEELQDLAEEL-----EELQ----QRLAELEEELEEAQEELEELEEEL 229
|
170 180
....*....|....*....|
gi 1907075650 415 ESLHDKERLAEEIEKLRSEL 434
Cdd:COG4717 230 EQLENELEAAALEERLKEAR 249
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
270-436 |
1.05e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 270 ENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlpEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEK 349
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN---ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 350 NQELQRARQREKMNEE--HNKRLSDTVDRL-----LTESNERLQLHLKERMAALEEKnvliqesenfRKNLEESLHDKER 422
Cdd:COG3883 92 ARALYRSGGSVSYLDVllGSESFSDFLDRLsalskIADADADLLEELKADKAELEAK----------KAELEAKLAELEA 161
|
170
....*....|....
gi 1907075650 423 LAEEIEKLRSELDQ 436
Cdd:COG3883 162 LKAELEAAKAELEA 175
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
116-307 |
1.79e-05 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 46.82 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 116 KIVALREQNVHIQRKMvsSEGSTESEHLEGMeagQKVHEKRLSNgsIDSTDDtsqivELQELLEKQNYEMAQMKERLTAL 195
Cdd:pfam15619 12 KIKELQNELAELQSKL--EELRKENRLLKRL---QKRQEKALGK--YEGTES-----ELPQLIARHNEEVRVLRERLRRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 196 SSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREcylQAMAQKEDMEERITTLEKRYLSAQREstsIHDMNDKLEN---- 271
Cdd:pfam15619 80 QEKERDLERKLKEKEAELLRLRDQLKRLEKLSED---KNLAEREELQKKLEQLEAKLEDKDEK---IQDLERKLELenks 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907075650 272 ---ELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK 307
Cdd:pfam15619 154 frrQLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKERE 192
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
24-434 |
2.12e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 24 YTFQEFAALTKELNACREQLLEKEEE----ISELKAERNNTRLLLEHLEclvsrhERSLRMTVVKRQAQSPSGVSSEVEV 99
Cdd:PRK03918 384 LTPEKLEKELEELEKAKEEIEEEISKitarIGELKKEIKELKKAIEELK------KAKGKCPVCGRELTEEHRKELLEEY 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 100 LKALKSLFEHHKALDEKIVALREQNVHIQRKMV-SSEGSTESEHLEgmeagqkvhekrlsngsidstddtsQIVELQELL 178
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKkESELIKLKELAE-------------------------QLKELEEKL 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 179 EKQNYEMAQMKER-LTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREcylqamaqKEDMEERITTLEKRYLSAQR 257
Cdd:PRK03918 513 KKYNLEELEKKAEeYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKK--------LDELEEELAELLKELEELGF 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 258 EstSIHDMNDKLE---------NELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlpeveaELAQRIAALTK- 327
Cdd:PRK03918 585 E--SVEELEERLKelepfyneyLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE-------ELRKELEELEKk 655
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 328 -AEERHGNIEERMRHLEGQLEEKNQELqrarqrekmneEHNKRLSDTVDRLLTEsnerlqlhLKERMAALEEKnvlIQES 406
Cdd:PRK03918 656 ySEEEYEELREEYLELSRELAGLRAEL-----------EELEKRREEIKKTLEK--------LKEELEEREKA---KKEL 713
|
410 420
....*....|....*....|....*...
gi 1907075650 407 ENFRKNLEeslhDKERLAEEIEKLRSEL 434
Cdd:PRK03918 714 EKLEKALE----RVEELREKVKKYKALL 737
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
269-446 |
2.18e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 269 LENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEE 348
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 349 KNQELQRARQREKMNEEHNKRLSDtvdrlLTESNERLQlHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIE 428
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEE-----LEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIE 327
|
170
....*....|....*...
gi 1907075650 429 KLRSELDQMKMRTGSLIE 446
Cdd:PRK03918 328 ERIKELEEKEERLEELKK 345
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
145-438 |
2.19e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 145 GMEAGQKVHEKRLSNGSIdSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQ 224
Cdd:COG4372 1 GDRLGEKVGKARLSLFGL-RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 225 RDIRecylQAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQT 304
Cdd:COG4372 80 EELE----ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 305 MRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNER 384
Cdd:COG4372 156 EEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1907075650 385 LQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQMK 438
Cdd:COG4372 236 SALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALE 289
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
266-370 |
2.22e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.67 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 266 NDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAEL---AQRIA--ALTKAEERHGNIEERMR 340
Cdd:PRK00409 515 KEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLleeAEKEAqqAIKEAKKEADEIIKELR 594
|
90 100 110
....*....|....*....|....*....|...
gi 1907075650 341 HLE--GQLEEKNQELQRARQR-EKMNEEHNKRL 370
Cdd:PRK00409 595 QLQkgGYASVKAHELIEARKRlNKANEKKEKKK 627
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
169-331 |
2.50e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 169 SQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARK-------DLIKTEEMNTKYQ------RDIREcYLQAM 235
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKeikrlelEIEEVEARIKKYEeqlgnvRNNKE-YEALQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 236 AQKEDMEERITTLEKRYLsaqrestsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQtmRKAETLPEVE 315
Cdd:COG1579 96 KEIESLKRRISDLEDEIL--------------ELMERIEELEEELAELEAELAELEAELEEKKAELDE--ELAELEAELE 159
|
170
....*....|....*.
gi 1907075650 316 AELAQRIAALTKAEER 331
Cdd:COG1579 160 ELEAEREELAAKIPPE 175
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
47-443 |
3.26e-05 |
|
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: 48.28 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 47 EEEISELKAERNNTRLLLEHLECLVsrHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEhhkALDEKIVALrEQNVH 126
Cdd:pfam10174 177 GEEDWERTRRIAEAEMQLGHLEVLL--DQKEKENIHLREELHRRNQLQPDPAKTKALQTVIE---MKDTKISSL-ERNIR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 127 ---IQRKMVSSEGSTES----EHLEGMEAgQKVHEKRLSNgSIDSTDD-----TSQIVELQ---ELLEKQNYEMAQ---- 187
Cdd:pfam10174 251 dleDEVQMLKTNGLLHTedreEEIKQMEV-YKSHSKFMKN-KIDQLKQelskkESELLALQtklETLTNQNSDCKQhiev 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 188 MKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREC------------YLQAM-------------------A 236
Cdd:pfam10174 329 LKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLteekstlageirDLKDMldvkerkinvlqkkienlqE 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 237 QKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAIL-RQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVE 315
Cdd:pfam10174 409 QLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIeRLKEQREREDRERLEELESLKKENKDLKEKVSALQ 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 316 AELAQRIAALTKAEERHGN-------IEERMRHLEGQLEEKNQE-------LQRARQRE---KMNEEHNKRLS---DTVD 375
Cdd:pfam10174 489 PELTEKESSLIDLKEHASSlassglkKDSKLKSLEIAVEQKKEEcsklenqLKKAHNAEeavRTNPEINDRIRlleQEVA 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 376 RLLTESN------ERLQLHLKE----------RMAALEE-------------KNVLIQESENFRKN---LEESLHDK--- 420
Cdd:pfam10174 569 RYKEESGkaqaevERLLGILREvenekndkdkKIAELESltlrqmkeqnkkvANIKHGQQEMKKKGaqlLEEARRREdnl 648
|
490 500 510
....*....|....*....|....*....|..
gi 1907075650 421 ---------ERLAEEIEKLRSELDQMKMRTGS 443
Cdd:pfam10174 649 adnsqqlqlEELMGALEKTRQELDATKARLSS 680
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
323-438 |
4.24e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.55 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 323 AALTKAEERHGNIEER-----MRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLlTESNERLQLHLK-----ER 392
Cdd:COG2433 380 EALEELIEKELPEEEPeaereKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEK-DERIERLERELSearseER 458
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1907075650 393 MAALEEKNVLIQESENfrKNLEESLHDKErlaEEIEKLRSELDQMK 438
Cdd:COG2433 459 REIRKDREISRLDREI--ERLERELEEER---ERIEELKRKLERLK 499
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
173-432 |
4.45e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.02 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 173 ELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLikteemnTKYQRDIRE------CYLQAMAQKEDMEERit 246
Cdd:COG3096 358 ELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQL-------ADYQQALDVqqtraiQYQQAVQALEKARAL-- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 247 tLEKRYLSAqrestsihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETL----PEVEAELA-QR 321
Cdd:COG3096 429 -CGLPDLTP-----------ENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVckiaGEVERSQAwQT 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 322 IAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDrllteSNERLQLHLKERMAALEEknv 401
Cdd:COG3096 497 ARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLD-----AAEELEELLAELEAQLEE--- 568
|
250 260 270
....*....|....*....|....*....|.
gi 1907075650 402 LIQESENFRKNLEESLHDKERLAEEIEKLRS 432
Cdd:COG3096 569 LEEQAAEAVEQRSELRQQLEQLRARIKELAA 599
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
115-438 |
4.78e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 47.54 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 115 EKIVALREQNVHIQRK----MVSSE--GSTESEHLEGM--EAGQKVHEKRLSNG-SIDSTDDT-----SQIVELQELLEK 180
Cdd:pfam06160 92 EELLDDIEEDIKQILEeldeLLESEekNREEVEELKDKyrELRKTLLANRFSYGpAIDELEKQlaeieEEFSQFEELTES 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 181 QNYEMA-----QMKERLTALSSRVGEVEQEAETARKDLikTEEMNtkyqrDIRECYLQAMAQKEDMEErittlekryLSA 255
Cdd:pfam06160 172 GDYLEArevleKLEEETDALEELMEDIPPLYEELKTEL--PDQLE-----ELKEGYREMEEEGYALEH---------LNV 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 256 QRESTSIHDMNDKLENELANKEaiLRQMEEKNRQLQERLElaeqKLQQTMRKaetlpEVEAELaqriaaltKAEERHGNI 335
Cdd:pfam06160 236 DKEIQQLEEQLEENLALLENLE--LDEAEEALEEIEERID----QLYDLLEK-----EVDAKK--------YVEKNLPEI 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 336 EERMRHLEGQLEEKNQELQRARQREKMNEEH-------NKRLsDTVDRLLTESNERLQLH------LKERMAALEEKNVL 402
Cdd:pfam06160 297 EDYLEHAEEQNKELKEELERVQQSYTLNENElervrglEKQL-EELEKRYDEIVERLEEKevayseLQEELEEILEQLEE 375
|
330 340 350
....*....|....*....|....*....|....*...
gi 1907075650 403 IQES-ENFRKNLeESLHDKERLA-EEIEKLRSELDQMK 438
Cdd:pfam06160 376 IEEEqEEFKESL-QSLRKDELEArEKLDEFKLELREIK 412
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
210-433 |
4.83e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 47.77 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 210 RKDLIKTEEMNTKYQRDI-RECYLQAMAQKEDMEERITTLEKRYLSAQREstsihdmndklenelanKEAILRQMEEKNR 288
Cdd:COG5022 809 RKEYRSYLACIIKLQKTIkREKKLRETEEVEFSLKAEVLIQKFGRSLKAK-----------------KRFSLLKKETIYL 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 289 QLQERLELAEQK---LQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIE-----ERMRHLEGQLEEKNQELQRARQRE 360
Cdd:COG5022 872 QSAQRVELAERQlqeLKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENlefktELIARLKKLLNNIDLEEGPSIEYV 951
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907075650 361 KmNEEHNKRLsdTVDRLLTESNERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSE 433
Cdd:COG5022 952 K-LPELNKLH--EVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKEL 1021
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
96-429 |
4.96e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 96 EVEVLKALKSLFEHHKALDEKIVALREQNVHIQRKMVSSEGSteseHLEGMEAGQKVHEKRLSNgSIDSTDDTSQIVELQ 175
Cdd:PTZ00121 1222 DAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMA----HFARRQAAIKAEEARKAD-ELKKAEEKKKADEAK 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 176 ELLEKQNYE----MAQMKERLTALSSRVGEVEQEAETARKdliKTEEmnTKYQRDIRECYLQAMAQK-EDMEERITTLEK 250
Cdd:PTZ00121 1297 KAEEKKKADeakkKAEEAKKADEAKKKAEEAKKKADAAKK---KAEE--AKKAAEAAKAEAEAAADEaEAAEEKAEAAEK 1371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 251 RYLSAQREStsihDMNDKLENELANKEAILRQMEEKNRQLQE--RLELAEQKLQQTMRKAETLPEVEaELAQRIAALTKA 328
Cdd:PTZ00121 1372 KKEEAKKKA----DAAKKKAEEKKKADEAKKKAEEDKKKADElkKAAAAKKKADEAKKKAEEKKKAD-EAKKKAEEAKKA 1446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 329 EERHGNIEERMRHLEgqLEEKNQELQRARQREKMNEEhnKRLSDTVDRLLTESNERLQlhlkERMAALEEKnvliQESEN 408
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEE--AKKKAEEAKKADEAKKKAEE--AKKADEAKKKAEEAKKKAD----EAKKAAEAK----KKADE 1514
|
330 340
....*....|....*....|.
gi 1907075650 409 FRKNLEESLHDKERLAEEIEK 429
Cdd:PTZ00121 1515 AKKAEEAKKADEAKKAEEAKK 1535
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
238-444 |
5.58e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.60 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 238 KEDMEERITTLEKRYLSAQRESTSIHDmndkLENELANKEAILRQmEEKNRQLQERLELAEQKLQQTMRKAETLPEVEA- 316
Cdd:PRK11281 38 EADVQAQLDALNKQKLLEAEDKLVQQD----LEQTLALLDKIDRQ-KEETEQLKQQLAQAPAKLRQAQAELEALKDDNDe 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 317 ELAQRIAALTkaeerhgnieerMRHLEGQLEEKNQELQRARqrekmneehnKRLSDTVDRLLTESN--ERLQlhlkermA 394
Cdd:PRK11281 113 ETRETLSTLS------------LRQLESRLAQTLDQLQNAQ----------NDLAEYNSQLVSLQTqpERAQ-------A 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1907075650 395 ALEEKNVLIQESENFRKNLEESlhDKERLAEEIEKLRSELD----QMKMRTGSL 444
Cdd:PRK11281 164 ALYANSQRLQQIRNLLKGGKVG--GKALRPSQRVLLQAEQAllnaQNDLQRKSL 215
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
27-444 |
8.20e-05 |
|
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: 47.04 E-value: 8.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 27 QEFAALTKELNA-CREQLlekEEEISELKAERNNtrllLEHLECLVSRHERS---LRMTVVKRQAQSPSGVSSEVEVLKA 102
Cdd:pfam15921 429 QRLEALLKAMKSeCQGQM---ERQMAAIQGKNES----LEKVSSLTAQLESTkemLRKVVEELTAKKMTLESSERTVSDL 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 103 LKSLFEHHKALDEKIVALREQNVHIQRKMVSSEG-STESEHLEGMEAGQKVHEKRLSngsidstdDTSQIVE-LQELLEK 180
Cdd:pfam15921 502 TASLQEKERAIEATNAEITKLRSRVDLKLQELQHlKNEGDHLRNVQTECEALKLQMA--------EKDKVIEiLRQQIEN 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 181 QNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREcyLQAMAQKEDMEE-RITTLEKRYLSAQREs 259
Cdd:pfam15921 574 MTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRE--LEARVSDLELEKvKLVNAGSERLRAVKD- 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 260 tsIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAET-LPEVEAELAQRIAALTKAEERHGNIEER 338
Cdd:pfam15921 651 --IKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMqLKSAQSELEQTRNTLKSMEGSDGHAMKV 728
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 339 MRHLEGQLEEKNQELQRARQREKMNEEhnkrlsdtvdrLLTESNerlqlhlKERMAALEEKNVLIQEsenfrknLEESLH 418
Cdd:pfam15921 729 AMGMQKQITAKRGQIDALQSKIQFLEE-----------AMTNAN-------KEKHFLKEEKNKLSQE-------LSTVAT 783
|
410 420
....*....|....*....|....*.
gi 1907075650 419 DKERLAEEIEKLRSELDQMKMRTGSL 444
Cdd:pfam15921 784 EKNKMAGELEVLRSQERRLKEKVANM 809
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
249-430 |
8.66e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 8.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 249 EKRYLSAQREStsihdmndkLENELANkeaiLRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKA 328
Cdd:PRK04863 507 EQRHLAEQLQQ---------LRMRLSE----LEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSES 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 329 EERHGNIEERMRHLEGQLEEKNQELQRARQrekmnEEHNkrLSDTVDRLLTESNERLqlhlkERMAALEE--KNVLIQES 406
Cdd:PRK04863 574 VSEARERRMALRQQLEQLQARIQRLAARAP-----AWLA--AQDALARLREQSGEEF-----EDSQDVTEymQQLLERER 641
|
170 180
....*....|....*....|....
gi 1907075650 407 EnFRKNLEESLHDKERLAEEIEKL 430
Cdd:PRK04863 642 E-LTVERDELAARKQALDEEIERL 664
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
30-439 |
9.33e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 46.71 E-value: 9.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 30 AALTKELNACREQLLEKEEEIS-------ELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRqAQSPSGVSSEVEVLKA 102
Cdd:pfam01576 225 AELQAQIAELRAQLAKKEEELQaalarleEETAQKNNALKKIRELEAQISELQEDLESERAAR-NKAEKQRRDLGEELEA 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 103 LKSLFEH---HKALDEKIVALREQNVHIQRKMVSSEGstesehlegmeagqKVHEKRLSNGSIDSTddtSQIVELQELLE 179
Cdd:pfam01576 304 LKTELEDtldTTAAQQELRSKREQEVTELKKALEEET--------------RSHEAQLQEMRQKHT---QALEELTEQLE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 180 KQNYEMAQMKERLTALSSRVGEVEQEAETarkdlIKTEEMNTKYQRDIRECYLQamaqkedmeeritTLEKRYLSAQRES 259
Cdd:pfam01576 367 QAKRNKANLEKAKQALESENAELQAELRT-----LQQAKQDSEHKRKKLEGQLQ-------------ELQARLSESERQR 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 260 TSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMrkaETLPEveaELAQRIAALTKAEErhgnIEERM 339
Cdd:pfam01576 429 AELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQ---ELLQE---ETRQKLNLSTRLRQ----LEDER 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 340 RHLEGQLEEknqELQRARQREKMNEEHNKRLSDTVDRLLTESnerlqlhlkERMAALEE-KNVLIQESENFRKNLEESLH 418
Cdd:pfam01576 499 NSLQEQLEE---EEEAKRNVERQLSTLQAQLSDMKKKLEEDA---------GTLEALEEgKKRLQRELEALTQQLEEKAA 566
|
410 420
....*....|....*....|.
gi 1907075650 419 DKERLAEEIEKLRSELDQMKM 439
Cdd:pfam01576 567 AYDKLEKTKNRLQQELDDLLV 587
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
27-446 |
9.62e-05 |
|
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: 46.59 E-value: 9.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 27 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTvvKRQAQSpsgVSSEVEVLKA-LKS 105
Cdd:TIGR02168 337 EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL--ELQIAS---LNNEIERLEArLER 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 106 LFEHHKALDEKIVALREQNVHIQRKMVSSEGSTESEHLEGMEAGQKVHEKRLSNGSidstddtSQIVELQELLEKQNYEM 185
Cdd:TIGR02168 412 LEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELR-------EELEEAEQALDAAEREL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 186 AQMKERLTALSSRVGEVEQEAETARK----------------DLIKTEEmntKYQRDIrECYLQAMAQ------KEDMEE 243
Cdd:TIGR02168 485 AQLQARLDSLERLQENLEGFSEGVKAllknqsglsgilgvlsELISVDE---GYEAAI-EAALGGRLQavvvenLNAAKK 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 244 RITTLEKrylsAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTM------------------ 305
Cdd:TIGR02168 561 AIAFLKQ----NELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALsyllggvlvvddldnale 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 306 -----RKAETLPEVEAELAQRIAALTKAEERHGN-----------IEERMRHLEGQLEEKNQELQRAR-QREKMNEEHNK 368
Cdd:TIGR02168 637 lakklRPGYRIVTLDGDLVRPGGVITGGSAKTNSsilerrreieeLEEKIEELEEKIAELEKALAELRkELEELEEELEQ 716
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 369 --RLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESENF-------RKNLEESLHDKERLAEEIEKLRSELDQMKM 439
Cdd:TIGR02168 717 lrKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELeaeieelEERLEEAEEELAEAEAEIEELEAQIEQLKE 796
|
....*..
gi 1907075650 440 RTGSLIE 446
Cdd:TIGR02168 797 ELKALRE 803
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
28-288 |
9.77e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 9.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 28 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRhERSLRMTVVKRQAQSpsgVSSEVEVLK-ALKSL 106
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKD-LGEEEQLRVKEKIGE---LEAEIASLErSIAEK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 107 FEHHKALDEKIVALREQNVHIQRKMVSSEGSTESEHL-------EGMEAGQKVHEKRLSNGSIDSTDDTS--QIVELQEL 177
Cdd:TIGR02169 314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKrrdklteEYAELKEELEDLRAELEEVDKEFAETrdELKDYREK 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 178 LEKQNYEMAQMK-------ERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEeritTLEK 250
Cdd:TIGR02169 394 LEKLKREINELKreldrlqEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS----KYEQ 469
|
250 260 270
....*....|....*....|....*....|....*...
gi 1907075650 251 RYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNR 288
Cdd:TIGR02169 470 ELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVR 507
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
802-866 |
1.04e-04 |
|
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: 41.49 E-value: 1.04e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907075650 802 QWDGPTVVAWLElWLGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQEM 866
Cdd:pfam00536 2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
288-485 |
1.06e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 46.24 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 288 RQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERmrhlegqlEEKNQELQRARQREKMNEEHN 367
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRER--------EELQREEERLVQKEEQLDARA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 368 KRLSDTVDRLLTESN----ERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHD--KERLAEEIEKLRSELD-QMKMR 440
Cdd:PRK12705 98 EKLDNLENQLEEREKalsaRELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAelEEEKAQRVKKIEEEADlEAERK 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907075650 441 TGSLIEPTISRTHIDTSTELRYSVgslVDSQSDYRTTKVIRRPRR 485
Cdd:PRK12705 178 AQNILAQAMQRIASETASDLSVSV---VPIPSDAMKGRIIGREGR 219
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
268-438 |
1.16e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 268 KLENELANKEAILRQMEEKNRQLQERLELAEQKLQqtmrkaetlpEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLE 347
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLE----------AAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 348 E-KNQELQRARQREKmnEEHNKRLSDTVDRLLtesnerlqlhlkERMAALEEKNVLIQESENFRKNLEESL-HDKERLAE 425
Cdd:COG1579 84 NvRNNKEYEALQKEI--ESLKRRISDLEDEIL------------ELMERIEELEEELAELEAELAELEAELeEKKAELDE 149
|
170
....*....|...
gi 1907075650 426 EIEKLRSELDQMK 438
Cdd:COG1579 150 ELAELEAELEELE 162
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
1010-1080 |
1.20e-04 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 41.10 E-value: 1.20e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907075650 1010 VLVWSNDRVIRWIQAIGLREYANNILESGVHG--SLIALDENFdysslalLLQIPTQNTQARQILEREYNNLL 1080
Cdd:pfam07647 1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGaeLLLRLTLED-------LKRLGITSVGHRRKILKKIQELK 66
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
199-397 |
1.30e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 199 VGEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITTLEKryLSAQREstsihdmndKLENELANKEA 278
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEE--LEEELE---------ELEAELEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 279 ILRQME--EKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHL--------EGQLEE 348
Cdd:COG4717 117 ELEKLEklLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELleqlslatEEELQD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907075650 349 KNQELQRARQREKMNEEHNKRLSDTVDRLLTE----SNERLQLHLKERMAALE 397
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEEEleqlENELEAAALEERLKEAR 249
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
173-358 |
1.39e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 173 ELQELlEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAmaQKEDMEERITTLEKRY 252
Cdd:COG4717 79 ELKEA-EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEA--ELAELPERLEELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 253 LSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETlpeveaelaqriaALTKAEERH 332
Cdd:COG4717 156 EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEE-------------ELEEAQEEL 222
|
170 180
....*....|....*....|....*...
gi 1907075650 333 GNIEERMRHLEGQLE--EKNQELQRARQ 358
Cdd:COG4717 223 EELEEELEQLENELEaaALEERLKEARL 250
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
173-359 |
1.57e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 45.84 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 173 ELQELLEKQNyEMAQMKERLT-------ALSSRVGEVEQ-EAEtaRKDLIKTEEMntkyQRDIRECYlQAMAQKED-MEE 243
Cdd:COG0497 173 ELEELRADEA-ERARELDLLRfqleeleAAALQPGEEEElEEE--RRRLSNAEKL----REALQEAL-EALSGGEGgALD 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 244 RITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQ---ERLELAEQKLQ---QTMRK----AETLPE 313
Cdd:COG0497 245 LLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEfdpERLEEVEERLAllrRLARKygvtVEELLA 324
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907075650 314 VEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQR 359
Cdd:COG0497 325 YAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKK 370
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
210-437 |
1.74e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.89 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 210 RKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITTLEKRYlsaQRESTSIHDMND---KLENELANKEAILRQMEEK 286
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQL---DRESDRNQELQKrirLLEKREAEAEEALREQAEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 287 NRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHgnieermrhlEGQLEEKNQELQRARQR------- 359
Cdd:pfam05557 78 NRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRA----------ELELQSTNSELEELQERldllkak 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 360 ----EKMNEEHNKRLSdtvdrLLTESNERLQ----------------LHLKERMAALEEKNVLIQESENFRKNLEESLHD 419
Cdd:pfam05557 148 aseaEQLRQNLEKQQS-----SLAEAEQRIKelefeiqsqeqdseivKNSKSELARIPELEKELERLREHNKHLNENIEN 222
|
250
....*....|....*...
gi 1907075650 420 KERLAEEIEKLRSELDQM 437
Cdd:pfam05557 223 KLLLKEEVEDLKRKLERE 240
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
173-405 |
1.76e-04 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 44.71 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 173 ELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYlQAMAQKEDMEERITTLEKR- 251
Cdd:pfam06008 27 QLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAK-ELAEAIKNLIDNIKEINEKv 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 252 -YLSAQRESTSihdmNDKLENELANKEAILRQMeeKNRQLQERLELAEQKLqqtmRKAETLPEVEAELAQRIAALTKAee 330
Cdd:pfam06008 106 aTLGENDFALP----SSDLSRMLAEAQRMLGEI--RSRDFGTQLQNAEAEL----KAAQDLLSRIQTWFQSPQEENKA-- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 331 rhgnIEERMRHLEGQLEEKNQELQ--------RARQREKMNEEHNKRLSDTVDRLLT--ESNERLQLHLKERMAALEEKN 400
Cdd:pfam06008 174 ----LANALRDSLAEYEAKLSDLRellreaaaKTRDANRLNLANQANLREFQRKKEEvsEQKNQLEETLKTARDSLDAAN 249
|
....*
gi 1907075650 401 VLIQE 405
Cdd:pfam06008 250 LLLQE 254
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
30-440 |
1.77e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 30 AALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMtvvkrqaqspsgvssevevlkalkslfeh 109
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV----------------------------- 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 110 hKALDEKIVALREQnvhiqrkmvssegstesehLEGMEAGQkvhekrlsngsidstddtSQIVELQELLEKQNYEMAQMK 189
Cdd:COG4913 664 -ASAEREIAELEAE-------------------LERLDASS------------------DDLAALEEQLEELEAELEELE 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 190 ERLTALSSRVGEVEQEAETARKDLIKTEEMntkyqrdirecyLQAMAQKEDMEERiTTLEKRYLSAQRestsihdmnDKL 269
Cdd:COG4913 706 EELDELKGEIGRLEKELEQAEEELDELQDR------------LEAAEDLARLELR-ALLEERFAAALG---------DAV 763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 270 ENELAnkeailRQMEEKNRQLQERLELAEQKLQQTMRKA-ETLPEVEAELAQRIAALTKAEERHGNIEERmrhlegQLEE 348
Cdd:COG4913 764 ERELR------ENLEERIDALRARLNRAEEELERAMRAFnREWPAETADLDADLESLPEYLALLDRLEED------GLPE 831
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 349 KNQELQRARQR----------EKMNEEHN---KRLsDTVDRLLTESN----ERLQLHLKERM--AALEEKNVLIQESEN- 408
Cdd:COG4913 832 YEERFKELLNEnsiefvadllSKLRRAIReikERI-DPLNDSLKRIPfgpgRYLRLEARPRPdpEVREFRQELRAVTSGa 910
|
410 420 430
....*....|....*....|....*....|..
gi 1907075650 409 FRKNLEESLHDKERLAEEIEKLRSELDQMKMR 440
Cdd:COG4913 911 SLFDEELSEARFAALKRLIERLRSEEEESDRR 942
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
291-429 |
2.45e-04 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 42.29 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 291 QERLELAEQKLQQtmrkaetLPEVEAELAQRIAALTKaeeRHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRL 370
Cdd:pfam12718 13 QERAEELEEKVKE-------LEQENLEKEQEIKSLTH---KNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNENLTRKI 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907075650 371 sdtvdRLLTESNERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIEK 429
Cdd:pfam12718 83 -----QLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEE 136
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
135-433 |
4.12e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 4.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 135 EGSTESEHLEGMEAGQKVHEKRLSNGSiDSTDDTSQIVELQELLE-KQNYEMAQMKERLTALSSRVGEVEQEAETARKdl 213
Cdd:PTZ00121 1143 EEARKAEDAKRVEIARKAEDARKAEEA-RKAEDAKKAEAARKAEEvRKAEELRKAEDARKAEAARKAEEERKAEEARK-- 1219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 214 iKTEEMNTKYQRDIRECYLQAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENelANKEAILRQMEEKNRQLQER 293
Cdd:PTZ00121 1220 -AEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE--ARKADELKKAEEKKKADEAK 1296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 294 LELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLE---GQLEEKNQELQRARQREKMNEEHNKRL 370
Cdd:PTZ00121 1297 KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEaakAEAEAAADEAEAAEEKAEAAEKKKEEA 1376
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907075650 371 SDTVDRLLTESNE-RLQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKE--RLAEEIEKLRSE 433
Cdd:PTZ00121 1377 KKKADAAKKKAEEkKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEekKKADEAKKKAEE 1442
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
200-455 |
4.20e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.58 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 200 GEVEQEAETARKDLIKTEE--MNTKYQRDIRECYLQAMAQKEDMEERITTLEKRYLSAQREstsihDMNDKLENELANKE 277
Cdd:pfam02463 142 GKIEIIAMMKPERRLEIEEeaAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKL-----KEQAKKALEYYQLK 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 278 AILRQMEEKNRQLQERLELAEQK---------LQQTMRKAETLPEVEAELAQRIAALTKAEER-HGNIEERMRHLEGQLE 347
Cdd:pfam02463 217 EKLELEEEYLLYLDYLKLNEERIdllqellrdEQEEIESSKQEIEKEEEKLAQVLKENKEEEKeKKLQEEELKLLAKEEE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 348 EKNQELQRARQREKMNEEhNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEI 427
Cdd:pfam02463 297 ELKSELLKLERRKVDDEE-KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEEL 375
|
250 260
....*....|....*....|....*...
gi 1907075650 428 EKLRSELDQMKMRTGSLIEPTISRTHID 455
Cdd:pfam02463 376 LAKKKLESERLSSAAKLKEEELELKSEE 403
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
267-441 |
4.32e-04 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 42.82 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 267 DKLENELANKEAILRQME------------EKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIaaltkaEERHGN 334
Cdd:cd00176 10 DELEAWLSEKEELLSSTDygddlesveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI------QERLEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 335 IEERMRHLEGQLEEKNQELQRARQREKMNEEH---NKRLSDTVDRLLTESN-------ERLQLHLKERMAALEEKNVLIQ 404
Cdd:cd00176 84 LNQRWEELRELAEERRQRLEEALDLQQFFRDAddlEQWLEEKEAALASEDLgkdlesvEELLKKHKELEEELEAHEPRLK 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907075650 405 ESENFRKNLEESLH--DKERLAEEIEKLRSELDQMKMRT 441
Cdd:cd00176 164 SLNELAEELLEEGHpdADEEIEEKLEELNERWEELLELA 202
|
|
| SAM_STIM-1,2-like |
cd09504 |
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ... |
803-861 |
4.96e-04 |
|
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like (Stromal interaction molecule) proteins is a putative protein-protein interaction domain. STIM1 and STIM2 human proteins are type I transmembrane proteins. The N-terminal part of them includes "hidden" EF-hand and SAM domains. This region is responsible for sensing changes in store-operated and basal cytoplasmic Ca2+ levels and initiates oligomerization. "Hidden" EF hand and SAM domains have a stable intramolecular association, and the SAM domain is a component that regulates stability within STIM proteins. Destabilization of the EF-SAM association during Ca2+ depletion leads to partial unfolding and aggregation (homooligomerization), thus activating the store-operated Ca2+ entry. Immunoprecipitation analysis indicates that STIM1 and STIM2 can form co-precipitable oligomeric associations in vivo. It was suggested that STIM1 and STIM2 are involved in opposite regulation of store operated channels in plasma membrane.
Pssm-ID: 188903 Cd Length: 74 Bit Score: 39.62 E-value: 4.96e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907075650 803 WDGPTVVAWLELWLGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNPLHRLKLRL 861
Cdd:cd09504 5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
174-440 |
5.06e-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: 44.12 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 174 LQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLiktEEMNTKYQRDIRECYLQAMAQKEDMEErittLEKRYL 253
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQW---ERQRRELESRVAELKEELRQSREKHEE----LEEKYK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 254 SAQRESTSIHdmndklenelANKEAILRQMEEKNRQLQErLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEE-RH 332
Cdd:pfam07888 105 ELSASSEELS----------EEKDALLAQRAAHEARIRE-LEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEaER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 333 GNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLH--LKERMAALEEK-NVLIQES 406
Cdd:pfam07888 174 KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLtqkLTTAHRKEAENeaLLEELRSLQERlNASERKV 253
|
250 260 270
....*....|....*....|....*....|....
gi 1907075650 407 ENFRKNLEESLHDKERLAEEIEKLRSELDQMKMR 440
Cdd:pfam07888 254 EGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQ 287
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
201-431 |
5.35e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.06 E-value: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 201 EVEQEAET-----ARKDLIKTEEMNTKYQRDIRECyLQAMA----QKEDMEERITTLEKRYLSAQRE----STSIHDMND 267
Cdd:PRK04778 90 EAEELNDKfrfrkAKHEINEIESLLDLIEEDIEQI-LEELQelleSEEKNREEVEQLKDLYRELRKSllanRFSFGPALD 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 268 KLENELANKEAILRQMEEKN-----RQLQERLELAEQKLQQTMRKAETLPEVEAELAQRI-AALTKAEE----------- 330
Cdd:PRK04778 169 ELEKQLENLEEEFSQFVELTesgdyVEAREILDQLEEELAALEQIMEEIPELLKELQTELpDQLQELKAgyrelveegyh 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 331 -RHGNIEERMRHLEGQLEEKNQELQR---ARQREKmNEEHNKRLSDTVDRLLTEsnerlqlhlkerMAAleeKNVLIQES 406
Cdd:PRK04778 249 lDHLDIEKEIQDLKEQIDENLALLEEldlDEAEEK-NEEIQERIDQLYDILERE------------VKA---RKYVEKNS 312
|
250 260
....*....|....*....|....*
gi 1907075650 407 ENFRKNLEESLHDKERLAEEIEKLR 431
Cdd:PRK04778 313 DTLPDFLEHAKEQNKELKEEIDRVK 337
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
267-434 |
5.88e-04 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 42.74 E-value: 5.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 267 DKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlPEVEAELAQRIAALTKAEERHG-----------NI 335
Cdd:pfam04012 39 VKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGN--EELAREALAEKKSLEKQAEALEtqlaqqrsaveQL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 336 EERMRHLEGQLEEKNQE-------LQRARQREKMNEehnkrlsdTVDRLLTESNERLQLHLKERMAALEEKNVLIQESEn 408
Cdd:pfam04012 117 RKQLAALETKIQQLKAKknllkarLKAAKAQEAVQT--------SLGSLSTSSATDSFERIEEKIEEREARADAAAELA- 187
|
170 180
....*....|....*....|....*.
gi 1907075650 409 FRKNLEESLHDKERLAEEIEKLRSEL 434
Cdd:pfam04012 188 SAVDLDAKLEQAGIQMEVSEDVLARL 213
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
105-438 |
8.01e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.56 E-value: 8.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 105 SLFEHHKALDEKIVALREQNVHIQRKMVSSEG------STESEHLEGMEAGQK-VHEKRLSNGSIdSTDDTSQIVELQEL 177
Cdd:pfam05483 68 SDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAelkqkeNKLQENRKIIEAQRKaIQELQFENEKV-SLKLEEEIQENKDL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 178 LEKQN---YEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDME-------ERITT 247
Cdd:pfam05483 147 IKENNatrHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHfklkedhEKIQH 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 248 LEKRYL----SAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK----AETLPEVEAELA 319
Cdd:pfam05483 227 LEEEYKkeinDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKkdhlTKELEDIKMSLQ 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 320 QRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLH---LKERMAAL 396
Cdd:pfam05483 307 RSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNedqLKIITMEL 386
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1907075650 397 EEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQMK 438
Cdd:pfam05483 387 QKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFE 428
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
174-359 |
8.06e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 8.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 174 LQELLEKQNyemAQMKERLTALSSRVGEVEQEAETARKDLIK----------TEEMNTKYQR--DIRECYLQAMAQKEDM 241
Cdd:COG3206 162 LEQNLELRR---EEARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdlSEEAKLLLQQlsELESQLAEARAELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 242 EERITTLEKRYLSAQRESTSI--HDMNDKLENELANKEAILRQMEEKN-------RQLQERLELAEQKLQQTMRKA---- 308
Cdd:COG3206 239 EARLAALRAQLGSGPDALPELlqSPVIQQLRAQLAELEAELAELSARYtpnhpdvIALRAQIAALRAQLQQEAQRIlasl 318
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907075650 309 ----ETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQR 359
Cdd:COG3206 319 eaelEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQR 373
|
|
| PRK03992 |
PRK03992 |
proteasome-activating nucleotidase; Provisional |
391-449 |
1.14e-03 |
|
proteasome-activating nucleotidase; Provisional
Pssm-ID: 179699 [Multi-domain] Cd Length: 389 Bit Score: 42.51 E-value: 1.14e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 391 ERMAALEEKNV-LIQESENFRKNLEESLHDKERLAEEIEKLRSELDqmKMRTGSLIEPTI 449
Cdd:PRK03992 1 ERLEALEERNSeLEEQIRQLELKLRDLEAENEKLERELERLKSELE--KLKSPPLIVATV 58
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
277-430 |
1.15e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.40 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 277 EAILRQMEEKNRQLQERLELAE---QKLQQTMRKAETLPEVEAELAQRIAALtkaEERHGNIEERMRHLEGQLEEKNQEL 353
Cdd:COG3096 518 RAQLAELEQRLRQQQNAERLLEefcQRIGQQLDAAEELEELLAELEAQLEEL---EEQAAEAVEQRSELRQQLEQLRARI 594
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907075650 354 QRARQREKMNEEHNKRLSdtvdRLLTESNERLQlHLKERMAALEEknVLIQESEnFRKNLEESLHDKERLAEEIEKL 430
Cdd:COG3096 595 KELAARAPAWLAAQDALE----RLREQSGEALA-DSQEVTAAMQQ--LLERERE-ATVERDELAARKQALESQIERL 663
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
175-357 |
1.27e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 41.66 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 175 QELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLikteEMNTKYQRDIRECylqamaqkEDMEERITTLEKRYLS 254
Cdd:cd00176 64 EQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRL----EEALDLQQFFRDA--------DDLEQWLEEKEAALAS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 255 aqrestsihdmnDKLENELANKEAILRQMEEknrqLQERLELAEQKLQQTMRKAETLPEveaelAQRIAALTKAEERHGN 334
Cdd:cd00176 132 ------------EDLGKDLESVEELLKKHKE----LEEELEAHEPRLKSLNELAEELLE-----EGHPDADEEIEEKLEE 190
|
170 180
....*....|....*....|...
gi 1907075650 335 IEERMRHLEGQLEEKNQELQRAR 357
Cdd:cd00176 191 LNERWEELLELAEERQKKLEEAL 213
|
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
149-513 |
1.49e-03 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 42.81 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 149 GQKVHEK--RLSNGSID----STDDTSQIVELQELLEKQNYEMAQMKERLTALS-SRVGEVEQE---AETARKDLIKTEe 218
Cdd:COG5192 415 GKAIAEEtsREDELSFDdsdvSTSDENEDVDFTGKKGAINNEDESDNEEVAFDSdSQFDESEGNlrwKEGLASKLAYSQ- 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 219 mNTKYQRDIREC-YLQAMAQKEDMEERittlekrylsaQRESTSIHDMNDKLENElanKEAILRQMEEKNRQLQERLE-L 296
Cdd:COG5192 494 -SGKRGRNIQKIfYDESLSPEECIEEY-----------KGESAKSSESDLVVQDE---PEDFFDVSKVANESISSNHEkL 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 297 AEQKLQQTMRKAETLPEVEAELAQriAALTKAEERHgniEErmrhLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDR 376
Cdd:COG5192 559 MESEFEELKKKWSSLAQLKSRFQK--DATLDSIEGE---EE----LIQDDEKGNFEDLEDEENSSDNEMEESRGSSVTAE 629
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 377 LLTESNERLQLHLKERMAALEEK---NVLIQESENFRKN-LEESLHDKERLAEEIEKLRSELDQM---------KMRTGS 443
Cdd:COG5192 630 NEESADEVDYETEREENARKKEElrgNFELEERGDPEKKdVDWYTEEKRKIEEQLKINRSEFETMvpesrvvieGYRAGR 709
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907075650 444 LIEPTISRTHIDTSTELRYS----VGSLVDSQSDYRTTKV-IRRPRRGRMGVRRDEPKVKSLGdheWNRTQQIGV 513
Cdd:COG5192 710 YVRIVLSHVPLEFVDEFNSRypivLGGLLPAEKEMGIVQGrIKRHRWHKKILKTNDPLIFSVG---WRRFQSIPV 781
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
78-596 |
1.64e-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: 42.73 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 78 LRMTVVKRQAQSPSG------VSSEVEVLKALKSLFEHHKA----LDEKIVALREQNVHIQRKMVSSEGSTESEHLEGME 147
Cdd:TIGR00606 222 IRDQITSKEAQLESSreivksYENELDPLKNRLKEIEHNLSkimkLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 148 AGQKVHEKRLSNGSidstDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVG------EVEQEAETARKDLIKTEEMNT 221
Cdd:TIGR00606 302 QLNDLYHNHQRTVR----EKERELVDCQRELEKLNKERRLLNQEKTELLVEQGrlqlqaDRHQEHIRARDSLIQSLATRL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 222 K---YQRDI---RECYLQAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLE 295
Cdd:TIGR00606 378 EldgFERGPfseRQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELK 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 296 LAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEErHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNkRLSDTVD 375
Cdd:TIGR00606 458 FVIKELQQLEGSSDRILELDQELRKAERELSKAEK-NSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLN-HHTTTRT 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 376 RLLTESNERLQLHLKERMAALEEKNVLIQESENF--RKNLEESLH----DKERLAEEIEKLRSELDQMKMRTGSLIEPTI 449
Cdd:TIGR00606 536 QMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFpnKKQLEDWLHskskEINQTRDRLAKLNKELASLEQNKNHINNELE 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 450 SRTHIDTSTELR-YSVGSLVDSQSDY-RTTKVIRRPRRGRMGVRRDEPKVKSLGDHEWNRTQQIGVLGSHPFESDTEMSD 527
Cdd:TIGR00606 616 SKEEQLSSYEDKlFDVCGSQDEESDLeRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQE 695
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907075650 528 IDDDdretiFSSMDLLSPSGHSDAQTLAMMLQEQLDAINKEIRLIQEEKESTELRAEEIENRVASVSLE 596
Cdd:TIGR00606 696 FISD-----LQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRD 759
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
219-438 |
1.79e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.37 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 219 MNTKYQRDIrecyLQAMAQKEDMEERITTLEKRYLSAQREstsihdmndkLENELANKEAILRQMEEKNRQLQErleLAE 298
Cdd:COG0497 138 LDPDAQREL----LDAFAGLEELLEEYREAYRAWRALKKE----------LEELRADEAERARELDLLRFQLEE---LEA 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 299 QKLQqtmrkaetlPEVEAELAQRIAALTKAEERHGNIEERMRHLEGqlEEKN--QELQRARQR-EKMnEEHNKRLSDTVD 375
Cdd:COG0497 201 AALQ---------PGEEEELEEERRRLSNAEKLREALQEALEALSG--GEGGalDLLGQALRAlERL-AEYDPSLAELAE 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 376 RL------LTESNERLQLHLK------ERMAALEEK-----------NVLIQESENFRKNLEESLHDKERLAEEIEKLRS 432
Cdd:COG0497 269 RLesalieLEEAASELRRYLDslefdpERLEEVEERlallrrlarkyGVTVEELLAYAEELRAELAELENSDERLEELEA 348
|
....*.
gi 1907075650 433 ELDQMK 438
Cdd:COG0497 349 ELAEAE 354
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
272-584 |
1.97e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.42 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 272 ELANKEAILRQMEEKNRQLQERLELAEQklqQTMRKAETlpeveaelaQRIAALTKAEERHGniEERMRHLEG-QLEEKN 350
Cdd:pfam17380 294 EKMEQERLRQEKEEKAREVERRRKLEEA---EKARQAEM---------DRQAAIYAEQERMA--MERERELERiRQEERK 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 351 QELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHL----------KERMAALEEKNVLIQ----ESENFRKNL--- 413
Cdd:pfam17380 360 RELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELeaarkvkileEERQRKIQQQKVEMEqiraEQEEARQREvrr 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 414 --EESLHDKERLAEE-------IEKLRSELDQMKMRTGSLIEPTISRTHIDtstELRYSVgslVDSQSDYRTTKVIRRPR 484
Cdd:pfam17380 440 leEERAREMERVRLEeqerqqqVERLRQQEEERKRKKLELEKEKRDRKRAE---EQRRKI---LEKELEERKQAMIEEER 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 485 RGRMGVRRDEPKVKSLGDHEWNRTQQigvlgshpfesDTEMSDIDDDDRETIFSSMDLLSPSghsdaqtlammlQEQLDA 564
Cdd:pfam17380 514 KRKLLEKEMEERQKAIYEEERRREAE-----------EERRKQQEMEERRRIQEQMRKATEE------------RSRLEA 570
|
330 340
....*....|....*....|
gi 1907075650 565 INKEIRLIQEEKESTELRAE 584
Cdd:pfam17380 571 MEREREMMRQIVESEKARAE 590
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
111-461 |
2.07e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 111 KALDEKIVALREQNVHIQRKmvSSEGSTESEHLEGMEAGQKVHEKRLsngsidstDDTSQIVELQELLEkqnyEMAQMKE 190
Cdd:COG4717 74 KELEEELKEAEEKEEEYAEL--QEELEELEEELEELEAELEELREEL--------EKLEKLLQLLPLYQ----ELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 191 RLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLE 270
Cdd:COG4717 140 ELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 271 NELANKEAILRQMEEKNRQLQERLELAEQK-----------LQQTMRKAETLPEVEAELAQRIAAL--------TKAEER 331
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEERLKEARlllliaaallaLLGLGGSLLSLILTIAGVLFLVLGLlallflllAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 332 HGNIEERMRHLEGQLEEKNQELQRARQREKMNEEhnkrLSDTVDRLLTESNERLQLHLKERMAALEEknVLIQESENFRK 411
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPD----LSPEELLELLDRIEELQELLREAEELEEE--LQLEELEQEIA 373
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907075650 412 NL--------EESLHDKERLAEEIEKLRSELDQMKMRTGSLIEPTISRTHIDTSTELR 461
Cdd:COG4717 374 ALlaeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE 431
|
|
| pepcterm_ChnLen |
TIGR03007 |
polysaccharide chain length determinant protein, PEP-CTERM locus subfamily; Members of this ... |
147-320 |
2.10e-03 |
|
polysaccharide chain length determinant protein, PEP-CTERM locus subfamily; Members of this protein family belong to the family of polysaccharide chain length determinant proteins (pfam02706). All are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria, and are found near the epsH homolog that is the putative exosortase gene. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 274386 [Multi-domain] Cd Length: 498 Bit Score: 41.96 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 147 EAGQKVHEKRLSNG---SIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDL-----IKTEE 218
Cdd:TIGR03007 179 AAENRLKAFKQENGgilPDQEGDYYSEISEAQEELEAARLELNEAIAQRDALKRQLGGEEPVLLAGSSVAnseldGRIEA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 219 MNTKYQrDIRECYLQAMAQKEDMEERITTLEKRYLSA-------QRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQ 291
Cdd:TIGR03007 259 LEKQLD-ALRLRYTDKHPDVIATKREIAQLEEQKEEEgsaknggPERGEIANPVYQQLQIELAEAEAEIASLEARVAELT 337
|
170 180
....*....|....*....|....*....
gi 1907075650 292 ERLElaeqklqQTMRKAETLPEVEAELAQ 320
Cdd:TIGR03007 338 ARIE-------RLESLLRTIPEVEAELTQ 359
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
932-987 |
2.14e-03 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 37.63 E-value: 2.14e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907075650 932 EWLPSLGLPQYRSYFMECLVD-ARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 987
Cdd:pfam07647 11 DWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLK-RLGITSVGHRRKILKKIQELK 66
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
280-393 |
2.27e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 280 LRQMEEKNRQLQ-ERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQ 358
Cdd:COG0542 413 LDELERRLEQLEiEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEK 492
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907075650 359 R----EKMNEEHNKRLSDTVD-----------------RLLTESNERLqLHLKERM 393
Cdd:COG0542 493 ElaelEEELAELAPLLREEVTeediaevvsrwtgipvgKLLEGEREKL-LNLEEEL 547
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
173-370 |
2.36e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 41.56 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 173 ELQELLEKQNYEMAQMKERLTALSSRvgEVEQEAETARKDLIKTEEmntKYQRDIREcylQAMAQKEDMEERITTLEKRY 252
Cdd:pfam15558 35 EELRRRDQKRQETLERERRLLLQQSQ--EQWQAEKEQRKARLGREE---RRRADRRE---KQVIEKESRWREQAEDQENQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 253 LSAQRESTSIHDMNDKLENE--LANKEAILRQMEEKNR-QLQERLELAEQKLQQ--------------------TMRKAE 309
Cdd:pfam15558 107 RQEKLERARQEAEQRKQCQEqrLKEKEEELQALREQNSlQLQERLEEACHKRQLkereeqkkvqennlsellnhQARKVL 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907075650 310 TLPEVEAELAQRIAAL----TKAEERH-GNIEERMRHLEGQLEEKNQELQRARQR-EKMNEEHNKRL 370
Cdd:pfam15558 187 VDCQAKAEELLRRLSLeqslQRSQENYeQLVEERHRELREKAQKEEEQFQRAKWRaEEKEEERQEHK 253
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
288-428 |
2.49e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 40.64 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 288 RQLQERLELAEQKLQQTMRKAETLP----------------EVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ 351
Cdd:pfam12072 27 AKIGSAEELAKRIIEEAKKEAETKKkealleakeeihklraEAERELKERRNELQRQERRLLQKEETLDRKDESLEKKEE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 352 ELQRARQREKMNEEHNKRLSDTVDRLLTESNERLqlhlkERMAAL---EEKNVLIQESEnfrknlEESLHDKERLAEEIE 428
Cdd:pfam12072 107 SLEKKEKELEAQQQQLEEKEEELEELIEEQRQEL-----ERISGLtseEAKEILLDEVE------EELRHEAAVMIKEIE 175
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
30-370 |
2.52e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 30 AALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHerslrmtvvkrqaqspSGVSSEVEVLKALKSLFEH 109
Cdd:PRK04863 782 AAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSH----------------LAVAFEADPEAELRQLNRR 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 110 HKALDEKIVALREQNVHIQRKMVSSEgstesehlEGMEAGQKVhekrlsNGSIDSTDDTSQIVELQELLEkQNYEMAQMK 189
Cdd:PRK04863 846 RVELERALADHESQEQQQRSQLEQAK--------EGLSALNRL------LPRLNLLADETLADRVEEIRE-QLDEAEEAK 910
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 190 ERLTALSSRVGEVEQEAETARKDliktEEMNTKYQRDirecYLQAMAQKEDMEERITTL----EKR----YLSAQRESTS 261
Cdd:PRK04863 911 RFVQQHGNALAQLEPIVSVLQSD----PEQFEQLKQD----YQQAQQTQRDAKQQAFALtevvQRRahfsYEDAAEMLAK 982
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 262 IHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALT-----KAEERhgnIE 336
Cdd:PRK04863 983 NSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGvpadsGAEER---AR 1059
|
330 340 350
....*....|....*....|....*....|....*....
gi 1907075650 337 ERMRHLEGQL----EEKNQ-ELQRARQREKMNEEhNKRL 370
Cdd:PRK04863 1060 ARRDELHARLsanrSRRNQlEKQLTFCEAEMDNL-TKKL 1097
|
|
| BAR_SNX7 |
cd07666 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 7; BAR domains are dimerization, lipid ... |
178-373 |
2.66e-03 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 7; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. The specific function of SNX7 is still unknown. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153350 Cd Length: 243 Bit Score: 41.04 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 178 LEKQNYEMAQMKERLTALSSRVGE-VEQEAETARKDLIKTEEMNtkyqrDIREcYLQAMAQK----EDMEERITTLEKRY 252
Cdd:cd07666 14 LTAQAWELSSHKKQGPGLLSRMGQtVKAVASSVRGVKNRPEEFT-----EMNE-YVEAFSQKinvlDKISQRIYKEQREY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 253 LSAQRESTSIHDMNDKLENELANK--------EAILRQMEEKNRQLQERLE-------LAEQKLQQTMRKAEtlpEVEAE 317
Cdd:cd07666 88 FEELKEYGPIYTLWSASEEELADSlkgmasciDRCCKATDKRMKGLSEQLLpviheyvLYSETLMGVIKRRD---QIQAE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907075650 318 LAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDT 373
Cdd:cd07666 165 LDSKVEALANKKADRDLLKEEIEKLEDKVECANNALKADWERWKQNMQTDLRSAFT 220
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
160-347 |
3.71e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 40.82 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 160 GSIDSTDDTSQIVELQELLEKQNYEMAQM---------KERLTALSSRVGEVEQEAETARKDLikteemnTKYQRDIrec 230
Cdd:cd22656 82 AQNAGGTIDSYYAEILELIDDLADATDDEeleeakktiKALLDDLLKEAKKYQDKAAKVVDKL-------TDFENQT--- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 231 ylqaMAQKEDMEERITTLEKRYlsaQRESTSIHDMN-DKLENELAN-KEAILRQMEEKNRQLQERLELAEQKLQQTMRKA 308
Cdd:cd22656 152 ----EKDQTALETLEKALKDLL---TDEGGAIARKEiKDLQKELEKlNEEYAAKLKAKIDELKALIADDEAKLAAALRLI 224
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907075650 309 ETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLE 347
Cdd:cd22656 225 ADLTAADTDLDNLLALIGPAIPALEKLQGAWQAIATDLD 263
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
32-437 |
3.84e-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: 41.70 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 32 LTKELNACREQL---LEKEEEISELKAERNNTRLLLEH-LECLVSRHERSLRmTVVKRQAQSPSGVSSEVEVLKALKSLF 107
Cdd:pfam01576 297 LGEELEALKTELedtLDTTAAQQELRSKREQEVTELKKaLEEETRSHEAQLQ-EMRQKHTQALEELTEQLEQAKRNKANL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 108 EHHKAldekivALREQNVHIQRKMVS-SEGSTESEHlegmeaGQKVHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEma 186
Cdd:pfam01576 376 EKAKQ------ALESENAELQAELRTlQQAKQDSEH------KRKKLEGQLQELQARLSESERQRAELAEKLSKLQSE-- 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 187 qmkerLTALSSRVGEVEQEAETARKDLIKTEEMntkyQRDIRECYLQAMAQKEDMEERITTLEKrylsaqrESTSIHDMn 266
Cdd:pfam01576 442 -----LESVSSLLNEAEGKNIKLSKDVSSLESQ----LQDTQELLQEETRQKLNLSTRLRQLED-------ERNSLQEQ- 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 267 dkLENELANKEAILRQMEEKNRQLQErlelAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERM----RHL 342
Cdd:pfam01576 505 --LEEEEEAKRNVERQLSTLQAQLSD----MKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLektkNRL 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 343 EGQLEEKNQELQRARQREKMNEEHNKRLsdtvDRLLTESNERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKER 422
Cdd:pfam01576 579 QQELDDLLVDLDHQRQLVSNLEKKQKKF----DQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEE 654
|
410
....*....|....*
gi 1907075650 423 LAEEIEKLRSELDQM 437
Cdd:pfam01576 655 LERTNKQLRAEMEDL 669
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
210-429 |
4.08e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 210 RKDLIKTEEMNTKYQRDIRECYLQAM------------AQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKE 277
Cdd:PTZ00121 1044 EKDIIDEDIDGNHEGKAEAKAHVGQDeglkpsykdfdfDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKK 1123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 278 A-ILRQMEEKN-----RQLQERLELAEQKLQQTMRKAETLPEVE----AELAQRIAALTKAEERHGNIE----ERMRHLE 343
Cdd:PTZ00121 1124 AeDARKAEEARkaedaRKAEEARKAEDAKRVEIARKAEDARKAEearkAEDAKKAEAARKAEEVRKAEElrkaEDARKAE 1203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 344 G----------------QLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAAL--EEKnvliQE 405
Cdd:PTZ00121 1204 AarkaeeerkaeearkaEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIkaEEA----RK 1279
|
250 260
....*....|....*....|....
gi 1907075650 406 SENFRKNLEESLHDKERLAEEIEK 429
Cdd:PTZ00121 1280 ADELKKAEEKKKADEAKKAEEKKK 1303
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
255-432 |
4.18e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 41.28 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 255 AQRESTSIHDMNDKLENELAnkEAILRQMEEKNRQLQERLELAEQKLQQTMRKaetlpEVEAELAQRIAALTKaeerhgn 334
Cdd:pfam09731 314 IERALEKQKEELDKLAEELS--ARLEEVRAADEAQLRLEFEREREEIRESYEE-----KLRTELERQAEAHEE------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 335 ieermrHLEGQLEEKNQELQRARQR---EKMNEEHNKRLSDtVDRLLTESNERLQLhLKERMAALEEKN---VLIQESEN 408
Cdd:pfam09731 380 ------HLKDVLVEQEIELQREFLQdikEKVEEERAGRLLK-LNELLANLKGLEKA-TSSHSEVEDENRkaqQLWLAVEA 451
|
170 180
....*....|....*....|....*.
gi 1907075650 409 FRKNLEESLHDKER--LAEEIEKLRS 432
Cdd:pfam09731 452 LRSTLEDGSADSRPrpLVRELKALKE 477
|
|
| SAM_superfamily |
cd09487 |
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
808-865 |
4.19e-03 |
|
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: 36.45 E-value: 4.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907075650 808 VVAWLElWLGMPaWYVAACRANVKSGAIMSALSDTEIQrEIGISNPLHRLKLRLAIQE 865
Cdd:cd09487 2 VAEWLE-SLGLE-QYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAIQR 56
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
236-357 |
5.45e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.33 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 236 AQKEDMEERITTLEKRYLSAQREstsihdmNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVE 315
Cdd:PRK09039 74 QGNQDLQDSVANLRASLSAAEAE-------RSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQI 146
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1907075650 316 AELAQRIAAL--------TKAEERHGNIEERMRHLEGQLEEKNQELQRAR 357
Cdd:PRK09039 147 AALRRQLAALeaaldaseKRDRESQAKIADLGRRLNVALAQRVQELNRYR 196
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
147-336 |
5.77e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 147 EAGQKVHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEE-----MNT 221
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREelgerARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 222 KYQRDIRECYL-------------------------------QAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLE 270
Cdd:COG3883 95 LYRSGGSVSYLdvllgsesfsdfldrlsalskiadadadlleELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907075650 271 NELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIE 336
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
169-325 |
6.37e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 39.12 E-value: 6.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 169 SQIVELQELLEKQNYEMA-------QMKERLTALSSRVGEVEQEAETARKDliKTEEMNTKYQRDIRECYLQAMA-QKED 240
Cdd:pfam13851 33 EEIAELKKKEERNEKLMSeiqqenkRLTEPLQKAQEEVEELRKQLENYEKD--KQSLKNLKARLKVLEKELKDLKwEHEV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 241 MEERITTLEKRY--LSAQREStSIHDMNDKLENE---LANK-EAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEV 314
Cdd:pfam13851 111 LEQRFEKVERERdeLYDKFEA-AIQDVQQKTGLKnllLEKKlQALGETLEKKEAQLNEVLAAANLDPDALQAVTEKLEDV 189
|
170
....*....|.
gi 1907075650 315 EAELAQRIAAL 325
Cdd:pfam13851 190 LESKNQLIKDL 200
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
272-440 |
6.76e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.46 E-value: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 272 ELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ 351
Cdd:PRK12705 40 QEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSAREL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 352 EL--QRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESENfRKNLEESLhdkERLAEEIEK 429
Cdd:PRK12705 120 ELeeLEKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKA-QNILAQAM---QRIASETAS 195
|
170
....*....|....*..
gi 1907075650 430 LRS------ELDQMKMR 440
Cdd:PRK12705 196 DLSvsvvpiPSDAMKGR 212
|
|
| SAM_SARM1-like_repeat1 |
cd09501 |
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
932-976 |
6.86e-03 |
|
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of SARM1-like adaptor proteins is a protein-protein interaction domain. SARM1-like proteins contain two tandem SAM domains. SARM1-like proteins are involved in TLR (Toll-like receptor) signaling. They are responsible for targeted localization of the whole protein to post-synaptic regions of axons. In humans SARM1 expression is detected in kidney and liver.
Pssm-ID: 188900 [Multi-domain] Cd Length: 69 Bit Score: 36.51 E-value: 6.86e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1907075650 932 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHR 976
Cdd:cd09501 11 TWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLR 55
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
26-292 |
7.42e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.66 E-value: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 26 FQEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLEclvsrherSLRMTVVKRQAQSPSGVSSEVEVLKALKs 105
Cdd:PLN02939 162 LTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLE--------KLRNELLIRGATEGLCVHSLSKELDVLK- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 106 lfEHHKALDEKIVALREQNVHIQrKMVSSEGSTESEHlEGMEAGQKVHEKRLsngsIDSTDDTSQIVELQ-ELLEKQNYE 184
Cdd:PLN02939 233 --EENMLLKDDIQFLKAELIEVA-ETEERVFKLEKER-SLLDASLRELESKF----IVAQEDVSKLSPLQyDCWWEKVEN 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 185 MAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQamaqkEDMEERITTLEKRYlsaQRESTSIHD 264
Cdd:PLN02939 305 LQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVSKFSSYKV-----ELLQQKLKLLEERL---QASDHEIHS 376
|
250 260 270
....*....|....*....|....*....|
gi 1907075650 265 MNDKLENELANKEAILRQM--EEKNRQLQE 292
Cdd:PLN02939 377 YIQLYQESIKEFQDTLSKLkeESKKRSLEH 406
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
269-436 |
7.49e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 39.59 E-value: 7.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 269 LENELANKEAILRQmEEKNRQLQERLELAEQKLQQTMRKAETL-----------------PEVEAELAQRIAALTKAEER 331
Cdd:pfam12795 22 LQQALSLLDKIDAS-KQRAAAYQKALDDAPAELRELRQELAALqakaeaapkeilaslslEELEQRLLQTSAQLQELQNQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 332 HGNIEERMRHLEGQLEEKNQELQRARQREkmnEEHNKRLSDTVDRLLTESNERlQLHLKERMAALEEKNVLI---QESEN 408
Cdd:pfam12795 101 LAQLNSQLIELQTRPERAQQQLSEARQRL---QQIRNRLNGPAPPGEPLSEAQ-RWALQAELAALKAQIDMLeqeLLSNN 176
|
170 180 190
....*....|....*....|....*....|...
gi 1907075650 409 FRKNLEESLHD-----KERLAEEIEKLRSELDQ 436
Cdd:pfam12795 177 NRQDLLKARRDlltlrIQRLEQQLQALQELLNE 209
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
197-320 |
7.50e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.04 E-value: 7.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 197 SRVGEVEQEAETARKDLIKTEEMNTKYQRDIRecylQAMAQKEDMEERITTLEKRYlSAQRESTSIHDMNDKLENELAnk 276
Cdd:COG1842 91 ERKAELEAQAEALEAQLAQLEEQVEKLKEALR----QLESKLEELKAKKDTLKARA-KAAKAQEKVNEALSGIDSDDA-- 163
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1907075650 277 EAILRQMEEKNRQLQERL----ELAEQK-LQQTMRKAETLPEVEAELAQ 320
Cdd:COG1842 164 TSALERMEEKIEEMEARAeaaaELAAGDsLDDELAELEADSEVEDELAA 212
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
262-452 |
8.37e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 262 IHDMndkLENELANK-EAILRQMEEKNRQLQERLELAEQKLQQtmrkaetLPEVEAELAQRIAALTKAEERHGNIEERMR 340
Cdd:COG4717 43 IRAM---LLERLEKEaDELFKPQGRKPELNLKELKELEEELKE-------AEEKEEEYAELQEELEELEEELEELEAELE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 341 HLEGQLEEKNQELQRARQREKMnEEHNKRLSDtvdrlltesnerlqlhLKERMAALEEKnvliqesenfRKNLEESLHDK 420
Cdd:COG4717 113 ELREELEKLEKLLQLLPLYQEL-EALEAELAE----------------LPERLEELEER----------LEELRELEEEL 165
|
170 180 190
....*....|....*....|....*....|..
gi 1907075650 421 ERLAEEIEKLRSELDQMKMRTGSLIEPTISRT 452
Cdd:COG4717 166 EELEAELAELQEELEELLEQLSLATEEELQDL 197
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
163-438 |
9.09e-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: 9.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 163 DSTDDTSQIVE--------LQELLEKQNY---EMAQMKERLTALSSRVGEVEQEAETARKDLIK-TEEMNTKYQRDIREC 230
Cdd:pfam05483 265 ESRDKANQLEEktklqdenLKELIEKKDHltkELEDIKMSLQRSMSTQKALEEDLQIATKTICQlTEEKEAQMEELNKAK 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 231 YLQAMAQKEdMEERITTLEKRYLSAQRestsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAET 310
Cdd:pfam05483 345 AAHSFVVTE-FEATTCSLEELLRTEQQ----------RLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKI 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075650 311 LPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQlEEKNQELQRARQREKMNEEH-NKRLSDTVDRLLTESNERLQLHL 389
Cdd:pfam05483 414 LAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAR-EKEIHDLEIQLTAIKTSEEHyLKEVEDLKTELEKEKLKNIELTA 492
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907075650 390 KERMAALEEKNvLIQESENFRKNLEESLHD-------KERLAEEIEKLRSELDQMK 438
Cdd:pfam05483 493 HCDKLLLENKE-LTQEASDMTLELKKHQEDiinckkqEERMLKQIENLEEKEMNLR 547
|
|
| |
