|
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 ... |
1086-1157 |
2.41e-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: 154.40 E-value: 2.41e-44
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907075611 1086 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1157
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 ... |
877-947 |
4.01e-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: 4.01e-44
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907075611 877 FAQWDGPTVVAWLELWLGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 947
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 ... |
1001-1066 |
1.36e-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: 1.36e-43
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907075611 1001 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 1066
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 ... |
1005-1064 |
2.60e-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: 116.86 E-value: 2.60e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 1005 WIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1064
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 ... |
884-942 |
2.86e-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: 2.86e-27
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907075611 884 TVVAWLELWLGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 942
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 ... |
1094-1155 |
5.91e-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: 98.77 E-value: 5.91e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907075611 1094 RVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNN 1155
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 ... |
1086-1157 |
1.33e-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: 80.95 E-value: 1.33e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907075611 1086 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1157
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 ... |
878-942 |
4.13e-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: 76.72 E-value: 4.13e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907075611 878 AQWDGPTVVAWLELWLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 942
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 ... |
1000-1064 |
1.62e-16 |
|
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188966 Cd Length: 65 Bit Score: 74.75 E-value: 1.62e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907075611 1000 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1064
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 ... |
1000-1064 |
2.01e-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: 74.65 E-value: 2.01e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907075611 1000 DMNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLrVHLKMVDSFHRTSLQYGIMCLK 1064
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 ... |
1086-1157 |
2.01e-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: 2.01e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907075611 1086 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1157
Cdd:cd09569 1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
251-514 |
4.66e-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: 80.49 E-value: 4.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 251 LLEKQNyEMAQMKERLTALSSRVGEVEQEAETARKDLikteemntkyqRDIRECYLQAMAQKEDMEERITTLEKRYLSAQ 330
Cdd:TIGR02168 672 ILERRR-EIEELEEKIEELEEKIAELEKALAELRKEL-----------EELEEELEQLRKELEELSRQISALRKDLARLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 331 RESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpevEAELAQRIAALTKAEERH---- 406
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL---KEELKALREALDELRAELtlln 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 407 ---GNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLHLKERMAALEEKNVLIQES 480
Cdd:TIGR02168 817 eeaANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELeelIEELESELEALLNERASLEEALALLRSEL 896
|
250 260 270
....*....|....*....|....*....|....
gi 1907075611 481 ENFRKNLEESLHDKERLAEEIEKLRSELDQMKMR 514
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKLAQLELR 930
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-460 |
2.63e-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: 78.17 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 101 PEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERS---LRMTVVKRQAQSPSGVSSEVEVLKAL 177
Cdd:TIGR02168 691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEveqLEERIAQLSKELTELEAEIEELEERL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 178 KSLFEHHKALDEKIVALREQnvhIQRkmVSSEGSTESEHLEGMEAGQKVHEKRLSNGSIDSTDDTSQIVELQELLEKQNY 257
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQ---IEQ--LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 258 EMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDI---RECYLQAMAQKEDMEERITTLEKRYLSAQresT 334
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALallRSELEELSEELRELESKRSELRRELEELR---E 922
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 335 SIHDMNDKLEnelankeailrQMEEKNRQLQERL-ELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNI---- 409
Cdd:TIGR02168 923 KLAQLELRLE-----------GLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVnlaa 991
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907075611 410 -------EERMRHLEGQLEeknqELQRARQR-----EKMNEEHNKRLSDTVDRLltesNERLQ 460
Cdd:TIGR02168 992 ieeyeelKERYDFLTAQKE----DLTEAKETleeaiEEIDREARERFKDTFDQV----NENFQ 1046
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
214-520 |
2.70e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.05 E-value: 2.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 214 SEHLEGMEAGQKVHEKRLSNGSIDSTDDtsQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLikteem 293
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEA--ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE------ 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 294 ntkyqrdirecyLQAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQ 373
Cdd:COG1196 291 ------------YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 374 KLQQtmrKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREkmnEEHNKRLSDTVDRLLT 453
Cdd:COG1196 359 ELAE---AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL---ERLEEELEELEEALAE 432
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907075611 454 ESNERLQLHLKERmAALEEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSLIE 520
Cdd:COG1196 433 LEEEEEEEEEALE-EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
1000-1064 |
6.66e-14 |
|
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.
Pssm-ID: 425739 Cd Length: 64 Bit Score: 67.29 E-value: 6.66e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907075611 1000 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1064
Cdd:pfam00536 1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
258-510 |
9.57e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.13 E-value: 9.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 258 EMAQMKERLTALSSRVGEVEQ-------EAETARK-DLIKTEEmntkyqrDIRECYLQAmAQKEDMEERITTLEKRYLSA 329
Cdd:COG1196 180 KLEATEENLERLEDILGELERqleplerQAEKAERyRELKEEL-------KELEAELLL-LKLRELEAELEELEAELEEL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 330 QREStsihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERhgnI 409
Cdd:COG1196 252 EAEL-------EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE---L 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 410 EERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLHLKERMAALEEKNVLIQESENFRKN 486
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAeeaLLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
250 260
....*....|....*....|....
gi 1907075611 487 LEESLHDKERLAEEIEKLRSELDQ 510
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEE 425
|
|
| SAM_liprin-beta1,2_repeat1 |
cd09563 |
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
877-941 |
1.29e-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: 1.29e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907075611 877 FAQWDGPTVVAWL-ELWLGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQ 941
Cdd:cd09563 1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
114-473 |
1.55e-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: 72.41 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 114 REQLLEKEEEISELKAERNNTRLLLEHLECLVsrHERSLRMTVVKRQAqspsgvsseVEVLKALKSLFEHHKALDEKIVA 193
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRL--DELSQELSDASRKI---------GEIEKEIEQLEQEEEKLKERLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 194 LREQNVHIQRKM--VSSEGSTESEHLEGMEAgqKVHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSS 271
Cdd:TIGR02169 742 LEEDLSSLEQEIenVKSELKELEARIEELEE--DLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 272 RVGEVEQEAETARKdlikteEMNTKyQRDIRECYLQAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLEN---ELA 348
Cdd:TIGR02169 820 KLNRLTLEKEYLEK------EIQEL-QEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDlkkERD 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 349 NKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAA----------LTKAEERHGNIEERMRHLEG 418
Cdd:TIGR02169 893 ELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeeelsLEDVQAELQRVEEEIRALEP 972
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1907075611 419 QLEEKNQELqrarqrekmnEEHNKRLSDTVDRLLTESNERLQlhLKERMAALEEK 473
Cdd:TIGR02169 973 VNMLAIQEY----------EEVLKRLDELKEKRAKLEEERKA--ILERIEEYEKK 1015
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
49-462 |
1.64e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.40 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 49 LRETQESLslaqQRLQDVIYDR----DSLQRQLNSA-----LPQDIESLtggltgskgadppEFAALTKELNACREQLLE 119
Cdd:TIGR02168 181 LERTRENL----DRLEDILNELerqlKSLERQAEKAerykeLKAELREL-------------ELALLVLRLEELREELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 120 KEEEISELKAERNNTRLLLEHLECLVSRHErsLRMTVVKRQAQSpsgVSSEVEVLKALKSLFEHHKaldeKIVALREQNV 199
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELR--LEVSELEEEIEE---LQKELYALANEISRLEQQK----QILRERLANL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 200 HIQRKMVSsegsTESEHLEgmeagqkvhekrlsngsidstddtSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQE 279
Cdd:TIGR02168 315 ERQLEELE----AQLEELE------------------------SKLDELAEELAELEEKLEELKEELESLEAELEELEAE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 280 AEtarkdlikteEMNTKYqrdirecylqamaqkEDMEERITTLEKRYLSAQRESTSIhdmndklENELANKEAILRQMEE 359
Cdd:TIGR02168 367 LE----------ELESRL---------------EELEEQLETLRSKVAQLELQIASL-------NNEIERLEARLERLED 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 360 KNRQLQERLELAEQKLQQTMRKA--ETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMN 437
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEAELKElqAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
|
410 420
....*....|....*....|....*
gi 1907075611 438 EEHNKRLSDTVDRLLTESNERLQLH 462
Cdd:TIGR02168 495 ERLQENLEGFSEGVKALLKNQSGLS 519
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
265-510 |
3.46e-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: 71.24 E-value: 3.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 265 RLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREC---YLQAMAQKEDMEERITTLEKRYLSAQREstsIHDMND 341
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELeekLEELRLEVSELEEEIEELQKELYALANE---ISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 342 KLENELANKEAILRQMEEKNRQLQE----RLELAEQKLQQTMRKAETLPEVEAELAQriaaLTKAEERHGNIEERMRHLE 417
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEEleskLDELAEELAELEEKLEELKEELESLEAE----LEELEAELEELESRLEELE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 418 GQLEEKNQELQRARQREKMNEEHNKRLSDTVDRlLTESNERLQLHLKERMAALEEKNV--LIQESENFRKNLEESLHDKE 495
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNNEIERLEARLER-LEDRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQEELE 457
|
250
....*....|....*
gi 1907075611 496 RLAEEIEKLRSELDQ 510
Cdd:TIGR02168 458 RLEEALEELREELEE 472
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
228-511 |
1.13e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 69.71 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 228 EKRLSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREcylq 307
Cdd:TIGR02169 701 ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHK---- 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 308 amaqkedMEERITTLEKRYlsAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPE 387
Cdd:TIGR02169 777 -------LEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 388 VEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARqrekmnEEHNKRLSDTVDRL--LTESNERLQLHLKE 465
Cdd:TIGR02169 848 QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER------DELEAQLRELERKIeeLEAQIEKKRKRLSE 921
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1907075611 466 RMAALEEKNVLIQESENFRKNLEES---LHDKERLAEEIEKLRSELDQM 511
Cdd:TIGR02169 922 LKAKLEALEEELSEIEDPKGEDEEIpeeELSLEDVQAELQRVEEEIRAL 970
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
237-491 |
2.85e-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: 68.16 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 237 DSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEmNTKYQRDIREcylQAMAQKEDME 316
Cdd:TIGR02168 720 ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE-ELAEAEAEIE---ELEAQIEQLK 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 317 ERITTLEKRYLSAQRE----STSIHDMNDKLENELANKEAILRQME------EKNRQLQERLELAEQKLQQTMRKAET-L 385
Cdd:TIGR02168 796 EELKALREALDELRAEltllNEEAANLRERLESLERRIAATERRLEdleeqiEELSEDIESLAAEIEELEELIEELESeL 875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 386 PEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKE 465
Cdd:TIGR02168 876 EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE 955
|
250 260
....*....|....*....|....*.
gi 1907075611 466 RMAALEEKNVLIQESENFRKNLEESL 491
Cdd:TIGR02168 956 AEALENKIEDDEEEARRRLKRLENKI 981
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
40-508 |
3.97e-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: 67.77 E-value: 3.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 40 DERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQdIESLTGGLTGSKGadppEFAALTKELNACREQLLE 119
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE-LESLEAELEELEA----ELEELESRLEELEEQLET 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 120 KEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEV--------EVLKALKSLFEHHKALDEKI 191
Cdd:TIGR02168 384 LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELkelqaeleELEEELEELQEELERLEEAL 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 192 VALREQNVHIQRKMVSSEGSTES------------EHLEGMEAGQK--VHEKRLSNGSIDS------------------- 238
Cdd:TIGR02168 464 EELREELEEAEQALDAAERELAQlqarldslerlqENLEGFSEGVKalLKNQSGLSGILGVlselisvdegyeaaieaal 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 239 --------TDDTSQIVELQELLEKQNYEMAQMKE----RLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRecYL 306
Cdd:TIGR02168 544 ggrlqavvVENLNAAKKAIAFLKQNELGRVTFLPldsiKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALS--YL 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 307 -------------QAMAQKEDMEERITTLE-----KRYLSAQRESTSIHDMNDKlENELANKEAILRQMEEKNRQLQERL 368
Cdd:TIGR02168 622 lggvlvvddldnaLELAKKLRPGYRIVTLDgdlvrPGGVITGGSAKTNSSILER-RREIEELEEKIEELEEKIAELEKAL 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 369 ELAEQKLQQTMRKAETLPEVEAELAQRIAA----LTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRL 444
Cdd:TIGR02168 701 AELRKELEELEEELEQLRKELEELSRQISAlrkdLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA 780
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907075611 445 SD---TVDRLLTESNERLQLhLKERMAALEEK----NVLIQESENFRKNLEESLHDKERLAEEIEKLRSEL 508
Cdd:TIGR02168 781 EAeieELEAQIEQLKEELKA-LREALDELRAEltllNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
102-518 |
8.98e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.60 E-value: 8.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 102 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLrmtvvkrqaQSPSGVSSEVEVLKALKSLF 181
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERR---------EELETLEAEIEDLRETIAET 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 182 EHHKA--------LDEKIVALREQNVHIQRKMVSSEGSTE--SEHLEGMEAGQKVHEKRLSNGSIDSTDDTSQIVELQEl 251
Cdd:PRK02224 271 EREREelaeevrdLRERLEELEEERDDLLAEAGLDDADAEavEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRE- 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 252 lekqnyEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEmntkyqrdirecylqamaQKEDMEERITTLEKRYLSAQR 331
Cdd:PRK02224 350 ------DADDLEERAEELREEAAELESELEEAREAVEDRRE------------------EIEELEEEIEELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 332 ESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQklqqtMRKAETLPEVEAEL--AQRIAALTKAEERHGNI 409
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA-----LLEAGKCPECGQPVegSPHVETIEEDRERVEEL 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 410 EERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLS--DTVDRLLTESNERLQlHLKERMAAL-EEKNVLIQESENFRKN 486
Cdd:PRK02224 481 EAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIE-EKRERAEELrERAAELEAEAEEKREA 559
|
410 420 430
....*....|....*....|....*....|..
gi 1907075611 487 LEESLHDKERLAEEIEKLRSELDQMKMRTGSL 518
Cdd:PRK02224 560 AAEAEEEAEEAREEVAELNSKLAELKERIESL 591
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
49-439 |
9.21e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 9.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 49 LRETQESLslaqQRLQDVIYD----RDSLQRQLNSALpqdiesltggltgskgadppEFAALTKELNACREQLL-----E 119
Cdd:COG1196 181 LEATEENL----ERLEDILGElerqLEPLERQAEKAE--------------------RYRELKEELKELEAELLllklrE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 120 KEEEISELKAERNNTRLLLEHLEclvsrherslrmtvvKRQAQspsgVSSEVEVLKalkslfEHHKALDEKIVALREQNV 199
Cdd:COG1196 237 LEAELEELEAELEELEAELEELE---------------AELAE----LEAELEELR------LELEELELELEEAQAEEY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 200 HIQRKmvssegstesehLEGMEAGQKVHEKRLSngsidstDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQE 279
Cdd:COG1196 292 ELLAE------------LARLEQDIARLEERRR-------ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 280 AETARKDLIKTEEmntkyqrdirecylQAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEE 359
Cdd:COG1196 353 LEEAEAELAEAEE--------------ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 360 KNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEE 439
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
41-401 |
4.54e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 64.32 E-value: 4.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 41 ERDRLLDTLRETQESLSLaQQRLQDVIYDRDSLQRQLNSaLPQDIESLTGGL---TGSKGADPPEFAALTKELNACREQL 117
Cdd:TIGR02169 662 PRGGILFSRSEPAELQRL-RERLEGLKRELSSLQSELRR-IENRLDELSQELsdaSRKIGEIEKEIEQLEQEEEKLKERL 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 118 LEKEEEISELKAERNNTRLLLEHLECLVSRHERSLrmtvvkrqaqspsgvSSEVEVLKALKSLFEHH--KALDEKIVALR 195
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDL---------------HKLEEALNDLEARLSHSriPEIQAELSKLE 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 196 EQNVHIQRKMVSSEGSTESEHLEGMEAGQKVHEKRLSNGSIDSTDDT--SQIVELQELLEKQNYEMAQMKERLTALSSRV 273
Cdd:TIGR02169 805 EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSieKEIENLNGKKEELEEELEELEAALRDLESRL 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 274 GEVEQEAETARKDL----IKTEEMNTKYQRdIRECYLQAMAQKEDMEERITTLEKRYLSAQRESTSIHDMnDKLENELAN 349
Cdd:TIGR02169 885 GDLKKERDELEAQLreleRKIEELEAQIEK-KRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL-EDVQAELQR 962
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1907075611 350 KEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTK 401
Cdd:TIGR02169 963 VEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
39-518 |
1.90e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.98 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 39 LDERDRLLDTLRETQESLSLAQQRLQDVIyDRDSLQRQLNSALPQDIEsltgGLTGSKGADPPEFAALTKELNACREQLL 118
Cdd:PRK02224 215 LAELDEEIERYEEQREQARETRDEADEVL-EEHEERREELETLEAEIE----DLRETIAETEREREELAEEVRDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 119 EKEEEISELKAERNNTRL----LLEHLECLVSRHERSLRMTVVKRQAQSpsgvssevEVLKALKSLFEHHKALDEKIVAL 194
Cdd:PRK02224 290 ELEEERDDLLAEAGLDDAdaeaVEARREELEDRDEELRDRLEECRVAAQ--------AHNEEAESLREDADDLEERAEEL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 195 REQNVHIQRKMVSSEG--STESEHLEGMEAGQKVHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSR 272
Cdd:PRK02224 362 REEAAELESELEEAREavEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARER 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 273 VGEVEQ--------EAETARKDLIKTEEMNTKYQR--DIRECYLQAMAQKEDMEERITTLEKrYLSAQRESTSIHDMNDK 342
Cdd:PRK02224 442 VEEAEAlleagkcpECGQPVEGSPHVETIEEDRERveELEAELEDLEEEVEEVEERLERAED-LVEAEDRIERLEERRED 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 343 LENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQL-- 420
Cdd:PRK02224 521 LEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLaa 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 421 -EEKNQELQRARQREK----MNEEHNKRLSDTVDRL-----------LTESNERLQlHLKERMAALEEKnvlIQESENFR 484
Cdd:PRK02224 601 iADAEDEIERLREKREalaeLNDERRERLAEKRERKreleaefdearIEEAREDKE-RAEEYLEQVEEK---LDELREER 676
|
490 500 510
....*....|....*....|....*....|....
gi 1907075611 485 KNLEESLHDKERLAEEIEKLRSELDQMKMRTGSL 518
Cdd:PRK02224 677 DDLQAEIGAVENELEELEELRERREALENRVEAL 710
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
247-518 |
2.23e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 247 ELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMntkyqrdirecylqamaqkedmEERITTLEKRy 326
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL----------------------KEEIEELEKE- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 327 lsaqrestsihdmNDKLENELANKEAILRQMEEKNRQLQERLELAEQK---LQQTMRKAETLPEVEAELAQRIAALTKAE 403
Cdd:PRK03918 247 -------------LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkeLKELKEKAEEYIKLSEFYEEYLDELREIE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 404 ERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDtvdrlLTESNERLQ--LHLKERMAALEEKnVLIQESE 481
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEE-----LEERHELYEeaKAKKEELERLKKR-LTGLTPE 387
|
250 260 270
....*....|....*....|....*....|....*..
gi 1907075611 482 NFRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSL 518
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL 424
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
310-518 |
2.73e-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: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 310 AQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAET----L 385
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENvkseL 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 386 PEVEAELAQRIAALTKAEERHGNIEERMRHleGQLEEKNQELqrarqrEKMNEEHnKRLSDTVDRLLTESNERLQL--HL 463
Cdd:TIGR02169 761 KELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAEL------SKLEEEV-SRIEARLREIEQKLNRLTLEkeYL 831
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907075611 464 KERMAALEEKNVLIQESEN-FRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSL 518
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKsIEKEIENLNGKKEELEEELEELEAALRDLESRLGDL 887
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
307-517 |
3.51e-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: 60.16 E-value: 3.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 307 QAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLp 386
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 387 evEAELAQRIAALTK------------------AEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTV 448
Cdd:COG4942 103 --KEELAELLRALYRlgrqpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907075611 449 DRLLTEsNERLQLHLKERMAALEEKNvliQESENFRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGS 517
Cdd:COG4942 181 AELEEE-RAALEALKAERQKLLARLE---KELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
230-518 |
3.52e-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: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 230 RLSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLikteemntkyqRDIRECYLQAM 309
Cdd:TIGR02169 661 APRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKI-----------GEIEKEIEQLE 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 310 AQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLelAEQKLQQTMRKAETLPEVE 389
Cdd:TIGR02169 730 QEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEV 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 390 AELAQRIAALTKAEERhgnieermRHLEGQ-LEEKNQELQrarqrEKMNEEHNKRlsdtvdrlltESNERLQLHLKERMA 468
Cdd:TIGR02169 808 SRIEARLREIEQKLNR--------LTLEKEyLEKEIQELQ-----EQRIDLKEQI----------KSIEKEIENLNGKKE 864
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1907075611 469 ALEEKnvlIQESENFRKNLEESLHDkerLAEEIEKLRSELDQMKMRTGSL 518
Cdd:TIGR02169 865 ELEEE---LEELEAALRDLESRLGD---LKKERDELEAQLRELERKIEEL 908
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
275-512 |
4.67e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.84 E-value: 4.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 275 EVEQEAETARKDLIKTEEMNTKYQRDIRECYLQA-MAQK-EDMEERITTLEKRYLSAQREStsihdmndkLENELANKEA 352
Cdd:TIGR02168 176 ETERKLERTRENLDRLEDILNELERQLKSLERQAeKAERyKELKAELRELELALLVLRLEE---------LREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 353 ILRQMEEKNRQLQERLELAEQKLQQTMRKaetlpevEAELAQRIAALTKAEERHGNIEERmrhLEGQLEEKNQELQRARQ 432
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLE-------VSELEEEIEELQKELYALANEISR---LEQQKQILRERLANLER 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 433 REKMNE---EHNKRLSDTVDRLLTESNERLQLhLKERMAALEEKnvlIQESENFRKNLEESLHDKErlaEEIEKLRSELD 509
Cdd:TIGR02168 317 QLEELEaqlEELESKLDELAEELAELEEKLEE-LKEELESLEAE---LEELEAELEELESRLEELE---EQLETLRSKVA 389
|
...
gi 1907075611 510 QMK 512
Cdd:TIGR02168 390 QLE 392
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
243-439 |
4.68e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.84 E-value: 4.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 243 SQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIrecylqaMAQKEDMEERITTL 322
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI-------AEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 323 EKRYLSAQR------------ESTSIHDMNDKLEN----ELANKEAILRQMEEKNR--QLQERLELAEQKLQQTMRKAET 384
Cdd:COG3883 89 GERARALYRsggsvsyldvllGSESFSDFLDRLSAlskiADADADLLEELKADKAEleAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907075611 385 -LPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEE 439
Cdd:COG3883 169 aKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
240-664 |
4.98e-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: 60.85 E-value: 4.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 240 DDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEmntkyqrdirecYLQAMAQKEDMEERI 319
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAER------------YQALLKEKREYEGYE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 320 TTLEKRYLSAQREstsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAelaqrIAAL 399
Cdd:TIGR02169 228 LLKEKEALERQKE---------AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ-----LRVK 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 400 TKAEERHGNIEErmrhLEGQLEEKNQELQRA-RQREKMNEEHNKRLSdtvdrlltesnerlqlhlkermaaleeknvliq 478
Cdd:TIGR02169 294 EKIGELEAEIAS----LERSIAEKERELEDAeERLAKLEAEIDKLLA--------------------------------- 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 479 ESENFRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSLieptisrthidtSTELRYSVGSLVDSQSDYRTTKVIRRPR 558
Cdd:TIGR02169 337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEV------------DKEFAETRDELKDYREKLEKLKREINEL 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 559 RGRMGVRRDEPKVKS--LGDHEwnrtQQIGVLGSHPFESDTEMSDIDDDDRETIFSSMDLLSPSGHSDAQTLAmmLQEQL 636
Cdd:TIGR02169 405 KRELDRLQEELQRLSeeLADLN----AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD--LKEEY 478
|
410 420
....*....|....*....|....*...
gi 1907075611 637 DAINKEIRLIQEEKESTELRAEEIENRV 664
Cdd:TIGR02169 479 DRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
877-943 |
5.01e-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: 5.01e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907075611 877 FAQWDGPTVVAWLELwLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 943
Cdd:smart00454 1 VSQWSPESVADWLES-IGLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
40-511 |
7.16e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 7.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 40 DERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALpQDIESLTGgltgskgadppEFAALTKELNACREQLLE 119
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE-ERLEELEE-----------ELAELEEELEELEEELEE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 120 KEEEISELKAERNNTRLLLEHLECLVSRHERSL---RMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKIVALRE 196
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELaeaEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 197 QNVHIQRKMVSSEGS--TESEHLEGMEAGQKVHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVG 274
Cdd:COG1196 422 ELEELEEALAELEEEeeEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 275 EVEQEAETARKDLIKTE------------EMNTKYQRDIRECYLQAMAQK-----EDMEERITTLEKRYLS--------- 328
Cdd:COG1196 502 DYEGFLEGVKAALLLAGlrglagavavliGVEAAYEAALEAALAAALQNIvveddEVAAAAIEYLKAAKAGratflpldk 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 329 -AQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHG 407
Cdd:COG1196 582 iRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGS 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 408 NIEERMRHLEGQLEEKNQELQRARQRE-KMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESENFRKN 486
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAERLaEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
|
490 500 510
....*....|....*....|....*....|....*...
gi 1907075611 487 LEESLHDKERLAE-------------EIEKLRSELDQM 511
Cdd:COG1196 742 LEEEELLEEEALEelpeppdleelerELERLEREIEAL 779
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
115-510 |
9.54e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 9.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 115 EQLLEKEEEISELKAERNNTRLLLEHLECLVSR-HERSLRMTVVKRQAQSPSGvssEVEVLKA-LKSLFEHHKALDEKIV 192
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVKElEELKEEIEELEKELESLEG---SKRKLEEkIRELEERIEELKKEIE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 193 ALREqnvhiQRKMVSSEGSTESEHLEgMEAGQKVHEKRLSNGSIDSTDDTSQIVELQEL---LEKQNYEMAQMKERLTAL 269
Cdd:PRK03918 277 ELEE-----KVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERikeLEEKEERLEELKKKLKEL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 270 SSRVGEVEQEAETARKDLIKTEEMNTKYQR-------DIRECYLQAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDK 342
Cdd:PRK03918 351 EKRLEELEERHELYEEAKAKKEELERLKKRltgltpeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 343 LEN--------------------------ELANKEAILRQMEEKNRQLQERLELAEQKLQQ-----TMRK-AETLPEVEA 390
Cdd:PRK03918 431 LKKakgkcpvcgrelteehrkelleeytaELKRIEKELKEIEEKERKLRKELRELEKVLKKeseliKLKElAEQLKELEE 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 391 ELAQ-RIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLsDTVDRLLTESNERLQLHLKERMAA 469
Cdd:PRK03918 511 KLKKyNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKL-DELEEELAELLKELEELGFESVEE 589
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1907075611 470 LEEKnvlIQESENFRK---NLEESLHDKERLAEEIEKLRSELDQ 510
Cdd:PRK03918 590 LEER---LKELEPFYNeylELKDAEKELEREEKELKKLEEELDK 630
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
208-493 |
1.09e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.15 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 208 SEGSTESEHLEGMEAGQKVHEKRLSNgSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARkdl 287
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKADEAKKAE-EKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR--- 1593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 288 ikTEEMNTKYQRdirECYLQAMAQKEDMEERITTLEKRylSAQRESTSIHDMNDKLENEL--------ANKEAILRQMEE 359
Cdd:PTZ00121 1594 --IEEVMKLYEE---EKKMKAEEAKKAEEAKIKAEELK--KAEEEKKKVEQLKKKEAEEKkkaeelkkAEEENKIKAAEE 1666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 360 KNRQLQERLELAE-QKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNE 438
Cdd:PTZ00121 1667 AKKAEEDKKKAEEaKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA 1746
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907075611 439 EHNKR---LSDTVDRLLTESNERLQLHLKERMAALEEKnvLIQESENFRKNLEESLHD 493
Cdd:PTZ00121 1747 EEAKKdeeEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE--LDEEDEKRRMEVDKKIKD 1802
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
114-439 |
1.12e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.70 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 114 REQLLEKEE-EISELKAERNNTRLLLEHLECLVSRHERSLRmtvvKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEkiv 192
Cdd:TIGR02169 214 QALLKEKREyEGYELLKEKEALERQKEAIERQLASLEEELE----KLTEEISELEKRLEEIEQLLEELNKKIKDLGE--- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 193 alrEQNVHIQRKMVSSEGSTESehlegMEAGQKVHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSR 272
Cdd:TIGR02169 287 ---EEQLRVKEKIGELEAEIAS-----LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 273 VGEVEQEAETARKDLiktEEMNTKYQRDIREcylqamaqKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEA 352
Cdd:TIGR02169 359 YAELKEELEDLRAEL---EEVDKEFAETRDE--------LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 353 ILRQMEEKNRQLQERLElaeqklqqtmRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQ 432
Cdd:TIGR02169 428 AIAGIEAKINELEEEKE----------DKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEA 497
|
....*..
gi 1907075611 433 REKMNEE 439
Cdd:TIGR02169 498 QARASEE 504
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
30-523 |
1.17e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 30 HFEQLMVNMLDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQDiESLTGGLTGSKGADP----PEFAA 105
Cdd:PTZ00121 1264 HFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAEEAKKKADAakkkAEEAK 1342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 106 LTKELNACREQLLEKEEEISELKAERNNTRLLLEH--LECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEH 183
Cdd:PTZ00121 1343 KAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKkkADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADE 1422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 184 HKALDEKIVALREQNVHIQRKMVSSEGSTESEHLEGME-AGQKVHEKRLSNGSIDSTDDTSQIVELQELLE--------- 253
Cdd:PTZ00121 1423 AKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEeAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEeakkkadea 1502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 254 -------KQNYEMAQMKERLTALSSRVGEVEQEAETARK--DLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITTLEK 324
Cdd:PTZ00121 1503 kkaaeakKKADEAKKAEEAKKADEAKKAEEAKKADEAKKaeEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRK 1582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 325 RYLSAQRESTSIHDMNDKLENELANKEAILRQMEE---------KNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQR 395
Cdd:PTZ00121 1583 AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikaeelkKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK 1662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 396 IAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLltesnERLQLHLKERMAALEEknv 475
Cdd:PTZ00121 1663 AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA-----EELKKAEEENKIKAEE--- 1734
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1907075611 476 LIQESENFRKNLEESLHDKERlAEEIEKLRSELDQMKMRTGSLIEPTI 523
Cdd:PTZ00121 1735 AKKEAEEDKKKAEEAKKDEEE-KKKIAHLKKEEEKKAEEIRKEKEAVI 1781
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
115-508 |
1.28e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 115 EQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRmtVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKIVAL 194
Cdd:PRK03918 286 KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN--GIEERIKELEEKEERLEELKKKLKELEKRLEELEERHEL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 195 REQnvhIQRKMVSSEGstesehlegmeagqkvHEKRLSNGSIDstddtsQIVELQELLEKQNYEmaqMKERLTALSSRVG 274
Cdd:PRK03918 364 YEE---AKAKKEELER----------------LKKRLTGLTPE------KLEKELEELEKAKEE---IEEEISKITARIG 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 275 EVEQEAETARKDLIKTE-------------------EMNTKYQR---DIRECYLQAMAQKEDMEERITTLEKrYLSAQRE 332
Cdd:PRK03918 416 ELKKEIKELKKAIEELKkakgkcpvcgrelteehrkELLEEYTAelkRIEKELKEIEEKERKLRKELRELEK-VLKKESE 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 333 STSIHDMNDKLEN-ELANKEAILRQMEEKNRQ---LQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGN 408
Cdd:PRK03918 495 LIKLKELAEQLKElEEKLKKYNLEELEKKAEEyekLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAE 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 409 IEERMRHL----EGQLEEKNQELqrarqrEKMNEEHNkRLSDTVDRL--LTESNERLQLHLKERMAALEEKNVLIQESEN 482
Cdd:PRK03918 575 LLKELEELgfesVEELEERLKEL------EPFYNEYL-ELKDAEKELerEEKELKKLEEELDKAFEELAETEKRLEELRK 647
|
410 420
....*....|....*....|....*...
gi 1907075611 483 FRKNLEESLHDKE--RLAEEIEKLRSEL 508
Cdd:PRK03918 648 ELEELEKKYSEEEyeELREEYLELSREL 675
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
312-511 |
1.47e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 312 KEDMEERITTLEKrYLSAQREstsIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAE 391
Cdd:PRK03918 171 IKEIKRRIERLEK-FIKRTEN---IEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 392 LAQRIAALTKAEERHGNIEERMRHLEGQ---LEEKNQELQRARQREKMNEEHNKRLSDTVDRL-----LTESNERLQLHL 463
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEieeLEEKVKELKELKEKAEEYIKLSEFYEEYLDELreiekRLSRLEEEINGI 326
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907075611 464 KERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQM 511
Cdd:PRK03918 327 EERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEL 374
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
106-519 |
1.58e-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: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 106 LTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHeRSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHK 185
Cdd:TIGR04523 171 LENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKN-KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEIS 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 186 ALDEKIVALREQNVHIQRKMV--SSEGSTESEHLEGMEAGQKVHEKRLSNGSIDSTDDTSQivELQELLEKQNYEMAQMK 263
Cdd:TIGR04523 250 NTQTQLNQLKDEQNKIKKQLSekQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNK--ELKSELKNQEKKLEEIQ 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 264 ERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREcylqamaqKEDMEERIttlekrylsaQRESTSIHDMNDKL 343
Cdd:TIGR04523 328 NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE--------KQNEIEKL----------KKENQSYKQEIKNL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 344 ENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKA----EERHGNIEERMRHLEGQ 419
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvkELIIKNLDNTRESLETQ 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 420 --------------LEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNErlqlhLKERMAALE----EKNVLIQESE 481
Cdd:TIGR04523 470 lkvlsrsinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS-----LKEKIEKLEsekkEKESKISDLE 544
|
410 420 430
....*....|....*....|....*....|....*...
gi 1907075611 482 NFRKNLEESLhDKERLAEEIEKLRSELDQMKMRTGSLI 519
Cdd:TIGR04523 545 DELNKDDFEL-KKENLEKEIDEKNKEIEELKQTQKSLK 581
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
341-507 |
2.02e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 341 DKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtLPEVEAELA---QRIAALTKAEERHGNIEERMRHLE 417
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID-VASAEREIAeleAELERLDASSDDLAALEEQLEELE 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 418 GQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLT-------ESNERLQLHLKERMAALEEKNVLIQESENFRKNLEES 490
Cdd:COG4913 699 AELEELEEELDELKGEIGRLEKELEQAEEELDELQDrleaaedLARLELRALLEERFAAALGDAVERELRENLEERIDAL 778
|
170
....*....|....*..
gi 1907075611 491 LHDKERLAEEIEKLRSE 507
Cdd:COG4913 779 RARLNRAEEELERAMRA 795
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
243-509 |
2.02e-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: 58.16 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 243 SQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEemntkyqRDIRECYLQAMAQKEDMEER---I 319
Cdd:pfam19220 48 SRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLE-------AALREAEAAKEELRIELRDKtaqA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 320 TTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAAL 399
Cdd:pfam19220 121 EALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAEL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 400 TKAEERHgniEERMRHLEGQLEEKNQELQRA-RQREKMNEEHNKRLSDTVDRLLTESNerlqlhlkeRMAALEeknVLIQ 478
Cdd:pfam19220 201 ETQLDAT---RARLRALEGQLAAEQAERERAeAQLEEAVEAHRAERASLRMKLEALTA---------RAAATE---QLLA 265
|
250 260 270
....*....|....*....|....*....|.
gi 1907075611 479 ESENFRKNLEESLHDKERLAEEIEKLRSELD 509
Cdd:pfam19220 266 EARNQLRDRDEAIRAAERRLKEASIERDTLE 296
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
108-511 |
2.05e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 58.83 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 108 KELNACREQLLEKEEEISELKAERNNtrlLLEHLECLVSRHERSLRMTVVkrQAQSPSGVSSEVE-VLKALKSLFEHHKA 186
Cdd:TIGR00618 472 EQQLQTKEQIHLQETRKKAVVLARLL---ELQEEPCPLCGSCIHPNPARQ--DIDNPGPLTRRMQrGEQTYAQLETSEED 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 187 LDEKIVALREQNVHIQRKMVSSEGSTE------SEHLEGMEAGQKVHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEMA 260
Cdd:TIGR00618 547 VYHQLTSERKQRASLKEQMQEIQQSFSiltqcdNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQD 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 261 QMKERLTalssrvgEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITTLEKRYLSAQRESTSIHDM- 339
Cdd:TIGR00618 627 LQDVRLH-------LQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMl 699
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 340 ---NDKLENELANKEAILRQMEE-------KNRQLQERLELAEQKLQQTMRKAET-LPEVEAELAQRIAALTKAEERhgn 408
Cdd:TIGR00618 700 aqcQTLLRELETHIEEYDREFNEienasssLGSDLAAREDALNQSLKELMHQARTvLKARTEAHFNNNEEVTAALQT--- 776
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 409 iEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESENFRKNLE 488
Cdd:TIGR00618 777 -GAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYE 855
|
410 420
....*....|....*....|...
gi 1907075611 489 ESLHDKERLAEEIEKLRSELDQM 511
Cdd:TIGR00618 856 ECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
237-515 |
3.70e-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: 57.88 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 237 DSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDI---RECYLQAMAQKE 313
Cdd:pfam01576 216 ESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLeseRAARNKAEKQRR 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 314 DMEERI------------TTLEKRYLSAQREsTSIHDMNDKLENELANKEAILRQMEEKNRQ----LQERLELAEQKLQQ 377
Cdd:pfam01576 296 DLGEELealkteledtldTTAAQQELRSKRE-QEVTELKKALEEETRSHEAQLQEMRQKHTQaleeLTEQLEQAKRNKAN 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 378 TMRKAETLPEVEAELAQRIAALTKAEerhGNIEERMRHLEGQLEEKNQELQRA-RQREKMNEEHNK-------------- 442
Cdd:pfam01576 375 LEKAKQALESENAELQAELRTLQQAK---QDSEHKRKKLEGQLQELQARLSESeRQRAELAEKLSKlqselesvssllne 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 443 ------RLSDTVDRL---LTESNERLQ------LHLKERMAALEEknvliqESENFRKNLEESLHDKERLAEEIEKLRSE 507
Cdd:pfam01576 452 aegkniKLSKDVSSLesqLQDTQELLQeetrqkLNLSTRLRQLED------ERNSLQEQLEEEEEAKRNVERQLSTLQAQ 525
|
....*...
gi 1907075611 508 LDQMKMRT 515
Cdd:pfam01576 526 LSDMKKKL 533
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
102-512 |
4.75e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 4.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 102 EFAALTKELNACREQLLE---KEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALK 178
Cdd:PRK03918 315 RLSRLEEEINGIEERIKEleeKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELE 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 179 SLFEHHKALDEKIvalreqnvhiqRKMVSSEGSTESEHLEGMEAGQKVHEKR----LSNGSIDSTDDTSQIVELQELLEK 254
Cdd:PRK03918 395 ELEKAKEEIEEEI-----------SKITARIGELKKEIKELKKAIEELKKAKgkcpVCGRELTEEHRKELLEEYTAELKR 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 255 QNYEMAQMKERLTALSSRVGEVEQEAETARK---------DLIKTEEMNTKYQRDIREcylQAMAQKEDMEERITTLEKR 325
Cdd:PRK03918 464 IEKELKEIEEKERKLRKELRELEKVLKKESEliklkelaeQLKELEEKLKKYNLEELE---KKAEEYEKLKEKLIKLKGE 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 326 YLSAQRESTSIHDMNDK---LENELANKEA----ILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAA 398
Cdd:PRK03918 541 IKSLKKELEKLEELKKKlaeLEKKLDELEEelaeLLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKE 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 399 LTKAEERHGNIEERMRHLEGQLEEKNQELQRARQreKMNEEHNKRLSDTVDRLltesnERLQLHLKERMAALEEknvLIQ 478
Cdd:PRK03918 621 LKKLEEELDKAFEELAETEKRLEELRKELEELEK--KYSEEEYEELREEYLEL-----SRELAGLRAELEELEK---RRE 690
|
410 420 430
....*....|....*....|....*....|....
gi 1907075611 479 ESENFRKNLEESLHDKERLAEEIEKLRSELDQMK 512
Cdd:PRK03918 691 EIKKTLEKLKEELEEREKAKKELEKLEKALERVE 724
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
53-505 |
6.96e-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: 57.36 E-value: 6.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 53 QESLSLAQQRLQDVIYDRDSLQRQLNSALPQDI--------ESLTGGLTGSKGADPPEFAALTKELNACREQLLEKEEEI 124
Cdd:TIGR00606 349 QGRLQLQADRHQEHIRARDSLIQSLATRLELDGfergpfseRQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 125 SELKAERNNTRLLLEHLECLVSRHERSLRMtvVKRQAQSPSGVS-----------------------SEVEVLKA-LKSL 180
Cdd:TIGR00606 429 DEIRDEKKGLGRTIELKKEILEKKQEELKF--VIKELQQLEGSSdrileldqelrkaerelskaeknSLTETLKKeVKSL 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 181 FEHHKALDEKIVALREQNVHIQRKmVSSEGSTESEHLEGMEAGQKVHE--KRLSNGSIDSTDDTSQIVELQELLEKQNYE 258
Cdd:TIGR00606 507 QNEKADLDRKLRKLDQEMEQLNHH-TTTRTQMEMLTKDKMDKDEQIRKikSRHSDELTSLLGYFPNKKQLEDWLHSKSKE 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 259 MAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREcylqaMAQKEDMEERITTLEKRYLSAQRESTSIH- 337
Cdd:TIGR00606 586 INQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFD-----VCGSQDEESDLERLKEEIEKSSKQRAMLAg 660
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 338 --DMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAET-LPEVEAELA----QRIAALTKAEERHGNIE 410
Cdd:TIGR00606 661 atAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDkLKSTESELKkkekRRDEMLGLAPGRQSIID 740
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 411 ERMRHLEgQLEEKNQELQRARQREKMNEEHNKRLSDTV-------DRLLTESN--ERLQLHLKERMAALEEKNVLIQESE 481
Cdd:TIGR00606 741 LKEKEIP-ELRNKLQKVNRDIQRLKNDIEEQETLLGTImpeeesaKVCLTDVTimERFQMELKDVERKIAQQAAKLQGSD 819
|
490 500 510
....*....|....*....|....*....|
gi 1907075611 482 ------NFRKNLEESLHDKERLAEEIEKLR 505
Cdd:TIGR00606 820 ldrtvqQVNQEKQEKQHELDTVVSKIELNR 849
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
104-509 |
7.77e-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: 57.27 E-value: 7.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 104 AALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRH---------ERSLRmtvVKRQAQSpsgvssevEVL 174
Cdd:COG3096 781 AAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVGGHlavafapdpEAELA---ALRQRRS--------ELE 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 175 KALKSLFEHHKALDEKIVALREQnVHIQRKMVSSEGSTESEHLEgmeagQKVHEKRlsngsidstddtsqiVELQELLEK 254
Cdd:COG3096 850 RELAQHRAQEQQLRQQLDQLKEQ-LQLLNKLLPQANLLADETLA-----DRLEELR---------------EELDAAQEA 908
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 255 QNYeMAQMKERLTalssrvgEVEQEAETARKDLIKTEEMntkyQRDirecYLQAMAQKEDMEERITTLEkrYLSAQREST 334
Cdd:COG3096 909 QAF-IQQHGKALA-------QLEPLVAVLQSDPEQFEQL----QAD----YLQAKEQQRRLKQQIFALS--EVVQRRPHF 970
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 335 SIHD----------MNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAAL----- 399
Cdd:COG3096 971 SYEDavgllgensdLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELgvqad 1050
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 400 TKAEERhgnIEERMRHLEGQL----EEKNQ-ELQRARQREKMnEEHNKRLSDtVDRLLTESNERLQLHLKERMAALEekn 474
Cdd:COG3096 1051 AEAEER---ARIRRDELHEELsqnrSRRSQlEKQLTRCEAEM-DSLQKRLRK-AERDYKQEREQVVQAKAGWCAVLR--- 1122
|
410 420 430
....*....|....*....|....*....|....*
gi 1907075611 475 vLIQESenfrkNLEESLHDKERLAEEIEKLRSELD 509
Cdd:COG3096 1123 -LARDN-----DVERRLHRRELAYLSADELRSMSD 1151
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
244-458 |
9.26e-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: 55.93 E-value: 9.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 244 QIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITTLe 323
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 324 krYLSAQRESTSI----HDMNDkLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAAL 399
Cdd:COG4942 114 --YRLGRQPPLALllspEDFLD-AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907075611 400 TKAEERHgniEERMRHLEGQLEEKNQELQRARQREkmneehnKRLSDTVDRLLTESNER 458
Cdd:COG4942 191 EALKAER---QKLLARLEKELAELAAELAELQQEA-------EELEALIARLEAEAAAA 239
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
40-512 |
9.73e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 56.67 E-value: 9.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 40 DERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNS--ALPQDIESLTGGLTGSKGADPPEFAALTK--------- 108
Cdd:pfam15921 142 DLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSheGVLQEIRSILVDFEEASGKKIYEHDSMSTmhfrslgsa 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 109 ----------ELNACREQLLEKEEEISELKAE-RNNTRLLLEH----LECLVSRHERSL-------------------RM 154
Cdd:pfam15921 222 iskilreldtEISYLKGRIFPVEDQLEALKSEsQNKIELLLQQhqdrIEQLISEHEVEItgltekassarsqansiqsQL 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 155 TVVKRQAQSPSGVS----SEVE-VLKALKS-LFEHHKALDEKIVALREQNV---------HIQRKMVSSEGSTESEHLEG 219
Cdd:pfam15921 302 EIIQEQARNQNSMYmrqlSDLEsTVSQLRSeLREAKRMYEDKIEELEKQLVlanselteaRTERDQFSQESGNLDDQLQK 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 220 MEAGQKVHEKRLS-----NGSIDSTDDTSQIV--ELQELLEKQNYEMAQMKERLTALSSRV-GEVEQEAETARKdliKTE 291
Cdd:pfam15921 382 LLADLHKREKELSlekeqNKRLWDRDTGNSITidHLRRELDDRNMEVQRLEALLKAMKSECqGQMERQMAAIQG---KNE 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 292 EMntkyqRDIRECYLQAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENelanKEAILRQMEEKNRQLQERLELA 371
Cdd:pfam15921 459 SL-----EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQE----KERAIEATNAEITKLRSRVDLK 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 372 EQKLQQTMRKAETLPEVEAE-----------------LAQRIAALTKAEERHGNIEERMR----HLEGQLEEKNQELQRA 430
Cdd:pfam15921 530 LQELQHLKNEGDHLRNVQTEcealklqmaekdkvieiLRQQIENMTQLVGQHGRTAGAMQvekaQLEKEINDRRLELQEF 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 431 R----QREKMNEEHNKRLSD---TVDRLLTESNERL-----------QLhLKERMAALEEKNVLIQESE----NFRKNLE 488
Cdd:pfam15921 610 KilkdKKDAKIRELEARVSDlelEKVKLVNAGSERLravkdikqerdQL-LNEVKTSRNELNSLSEDYEvlkrNFRNKSE 688
|
570 580
....*....|....*....|....
gi 1907075611 489 ESLHDKERLAEEIEKLRSELDQMK 512
Cdd:pfam15921 689 EMETTTNKLKMQLKSAQSELEQTR 712
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
1009-1064 |
1.09e-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: 49.99 E-value: 1.09e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907075611 1009 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1064
Cdd:smart00454 11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
195-509 |
1.45e-07 |
|
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: 55.95 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 195 REQNVHIQRKMVSSEGSTESEHLEGMEAG-QKVH-EKRLSNGSIDSTDDTSQIVELQEllEKQNYEMAQMKERLTALSSR 272
Cdd:pfam01576 90 RSQQLQNEKKKMQQHIQDLEEQLDEEEAArQKLQlEKVTTEAKIKKLEEDILLLEDQN--SKLSKERKLLEERISEFTSN 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 273 VGEVEQEAETARKDLIKTEEMNTKYQRDIRECylqamaqkedmEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEA 352
Cdd:pfam01576 168 LAEEEEKAKSLSKLKNKHEAMISDLEERLKKE-----------EKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 353 ILRQMEEKNRQLQERLE---LAEQKLQQTMRKAET-LPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEK----- 423
Cdd:pfam01576 237 QLAKKEEELQAALARLEeetAQKNNALKKIRELEAqISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTldtta 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 424 -NQELQRARQRE--------------------KMNEEHNKRLSDTVDRLltESNERLQLHLKERMAALEEKNVLI----- 477
Cdd:pfam01576 317 aQQELRSKREQEvtelkkaleeetrsheaqlqEMRQKHTQALEELTEQL--EQAKRNKANLEKAKQALESENAELqaelr 394
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1907075611 478 ------QESENFRKNLEESLHD-----------KERLAEEIEKLRSELD 509
Cdd:pfam01576 395 tlqqakQDSEHKRKKLEGQLQElqarlseserqRAELAEKLSKLQSELE 443
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
329-509 |
1.52e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.82 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 329 AQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGN 408
Cdd:PRK02224 197 EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 409 IEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNErlqlhLKERmaaLEEKNVLIQESENFRKNLE 488
Cdd:PRK02224 277 LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEE-----LRDR---LEECRVAAQAHNEEAESLR 348
|
170 180
....*....|....*....|.
gi 1907075611 489 ESLHDKERLAEEIEKLRSELD 509
Cdd:PRK02224 349 EDADDLEERAEELREEAAELE 369
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
322-514 |
1.75e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 322 LEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTK 401
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 402 AEERHgNIEERMRHLEGQLEE---KNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKErmaaleeknvLIQ 478
Cdd:COG4717 131 YQELE-ALEAELAELPERLEEleeRLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD----------LAE 199
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907075611 479 ESENFRKNLEESLHDKERLAEEIEKLRSELDQMKMR 514
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 ... |
240-508 |
2.25e-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: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 240 DDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVE-QEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEER 318
Cdd:pfam02463 159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKlQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 319 ITTLEKRYLSAQRESTSihdMNDKLENELANKEAILRQMEEKNR--QLQERLELAEQKLQQTMRKAETLPEVEAELAQRI 396
Cdd:pfam02463 239 IDLLQELLRDEQEEIES---SKQEIEKEEEKLAQVLKENKEEEKekKLQEEELKLLAKEEEELKSELLKLERRKVDDEEK 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 397 AA-----LTKAEERHGNIEERMRHLEGQLEEKN---QELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMA 468
Cdd:pfam02463 316 LKesekeKKKAEKELKKEKEEIEELEKELKELEikrEAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE 395
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1907075611 469 ALEEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSEL 508
Cdd:pfam02463 396 ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEE 435
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
30-471 |
2.51e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 55.51 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 30 HFEQLMVNMLDERDRLLDTLRETQESLSLAQQRlQDVIYDRDS--------LQRQLN--SALPQDIESLTGGLTGS---- 95
Cdd:pfam15921 367 QFSQESGNLDDQLQKLLADLHKREKELSLEKEQ-NKRLWDRDTgnsitidhLRRELDdrNMEVQRLEALLKAMKSEcqgq 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 96 ----------KGADPPEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKrQAQSPS 165
Cdd:pfam15921 446 merqmaaiqgKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAE-ITKLRS 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 166 GVSSEVEVLKALKSLFEH-------------HKALDEKIVALREQNVHIQRKMVSSEGSTESE-HLEGMEAGQKVHEKRL 231
Cdd:pfam15921 525 RVDLKLQELQHLKNEGDHlrnvqtecealklQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAmQVEKAQLEKEINDRRL 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 232 SNGSIDSTDDT--SQIVELQELLEKQNYEMAQM----KERLTALSSRVGEVEQ---EAETARKDLIKTEEMNTKYQRDIR 302
Cdd:pfam15921 605 ELQEFKILKDKkdAKIRELEARVSDLELEKVKLvnagSERLRAVKDIKQERDQllnEVKTSRNELNSLSEDYEVLKRNFR 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 303 EcylqamaQKEDMEERITTLEKRYLSAQRE----STSIHDMNDKLENELANKEAILRQMEEKNRQ---LQERLELAEQKL 375
Cdd:pfam15921 685 N-------KSEEMETTTNKLKMQLKSAQSEleqtRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQidaLQSKIQFLEEAM 757
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 376 QQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMneehnkRLSDTVDRLLTES 455
Cdd:pfam15921 758 TNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASL------QFAECQDIIQRQE 831
|
490
....*....|....*.
gi 1907075611 456 NERLQLHLKERMAALE 471
Cdd:pfam15921 832 QESVRLKLQHTLDVKE 847
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
39-436 |
3.62e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 39 LDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLnSALPQDIESLTGGLtgskgadppEFAALTKELNACREQLL 118
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAEL-EELREELEKLEKLL---------QLLPLYQELEALEAELA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 119 EKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKIVALREQN 198
Cdd:COG4717 143 ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 199 VHIQRKMVSSEGSTESEHLEgmeagQKVHEKRLSN----------GSIDSTDDTSQIVE------------LQELLEKQN 256
Cdd:COG4717 223 EELEEELEQLENELEAAALE-----ERLKEARLLLliaaallallGLGGSLLSLILTIAgvlflvlgllalLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 257 YEMAQMKERLTALSSRvgevEQEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITTLEKRYLSAQRESTSI 336
Cdd:COG4717 298 ASLGKEAEELQALPAL----EELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 337 HDMNDKLENELANKEAILRQMEEKnRQLQERLELAEQKLQQ------TMRKAETLPEVEAELAQRIAALTKAEERHGNIE 410
Cdd:COG4717 374 ALLAEAGVEDEEELRAALEQAEEY-QELKEELEELEEQLEEllgeleELLEALDEEELEEELEELEEELEELEEELEELR 452
|
410 420
....*....|....*....|....*...
gi 1907075611 411 ERMRHLEGQLE--EKNQELQRARQREKM 436
Cdd:COG4717 453 EELAELEAELEqlEEDGELAELLQELEE 480
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
354-512 |
4.89e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 354 LRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKaeeRHGNIEERMRHLEGQLEEKNQELQRARQR 433
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR---RIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 434 EKMNEEHNKRLSDTVDRL--------------LTESNERLQLH---LKERMAALEEKNVLIQESENFRKNLEESLHDKER 496
Cdd:COG4942 99 LEAQKEELAELLRALYRLgrqpplalllspedFLDAVRRLQYLkylAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170
....*....|....*.
gi 1907075611 497 LAEEIEKLRSELDQMK 512
Cdd:COG4942 179 LLAELEEERAALEALK 194
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
1087-1158 |
6.37e-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: 47.68 E-value: 6.37e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907075611 1087 VLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDEnfdysSLALLLQIPTQNTQARQILEREYNNLLA 1158
Cdd:smart00454 1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLT-----SEEDLKELGITKLGHRKKILKAIQKLKE 67
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
346-503 |
7.68e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 53.24 E-value: 7.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 346 ELANKEAIlRQMEEKNRQLQERLELAEQKLQQTMRKAETlpEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ 425
Cdd:PRK12704 34 KEAEEEAK-RILEEAKKEAEAIKKEALLEAKEEIHKLRN--EFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 426 ELQRARQREKMNEEHNKRLSDTVDRLLTESNERLqlhlkERMAAL---EEKNVLIQESEnfrknlEESLHDKERLAEEIE 502
Cdd:PRK12704 111 ELEKKEKELEQKQQELEKKEEELEELIEEQLQEL-----ERISGLtaeEAKEILLEKVE------EEARHEAAVLIKEIE 179
|
.
gi 1907075611 503 K 503
Cdd:PRK12704 180 E 180
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
306-511 |
1.21e-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: 53.05 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 306 LQAMAQKEDMEERITTLEKRY----LSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQK------L 375
Cdd:TIGR00618 183 LMEFAKKKSLHGKAELLTLRSqlltLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQlkkqqlL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 376 QQTMRKAETLPEVEAELAQRIAALTKA--EERHGNIEERMRHLEGQLEEKNQELQ-RARQREKMNEEHNKRLSDTVDRLL 452
Cdd:TIGR00618 263 KQLRARIEELRAQEAVLEETQERINRArkAAPLAAHIKAVTQIEQQAQRIHTELQsKMRSRAKLLMKRAAHVKQQSSIEE 342
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907075611 453 TESNERLQLHLKERMAALEEKNVLIQESENFRKNLEESLH----DKERLAEEIEKLRSELDQM 511
Cdd:TIGR00618 343 QRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHtlqqQKTTLTQKLQSLCKELDIL 405
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
244-514 |
1.49e-06 |
|
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: 51.84 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 244 QIVELQELLEKQNYEMAQMKERLTALssrvgeVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITTLE 323
Cdd:pfam13868 81 QIEEREQKRQEEYEEKLQEREQMDEI------VERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREED 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 324 KRYLSAQREstsihdMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAE 403
Cdd:pfam13868 155 ERILEYLKE------KAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 404 ERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEknvLIQESE-N 482
Cdd:pfam13868 229 KKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEK---QIEEREeQ 305
|
250 260 270
....*....|....*....|....*....|..
gi 1907075611 483 FRKNLEESLHDKERLAEEIEKLRSELDQMKMR 514
Cdd:pfam13868 306 RAAEREEELEEGERLREEEAERRERIEEERQK 337
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
258-488 |
1.51e-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: 52.43 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 258 EMAQMKE--RLTALSSRVGE-VEQEAETARKDLIKTEEMNTKYQRDIRECYL----QAMAQKEDM----EERITTLEKRY 326
Cdd:pfam17380 373 EISRMREleRLQMERQQKNErVRQELEAARKVKILEEERQRKIQQQKVEMEQiraeQEEARQREVrrleEERAREMERVR 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 327 LSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQtmRKAETLPE------VEAELAQRIAALT 400
Cdd:pfam17380 453 LEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEE--RKQAMIEEerkrklLEKEMEERQKAIY 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 401 KAEERHGNIEERMRHLEgqLEEknqelqRARQREKMneehnkrlsdtvdRLLTESNERLQLHLKERmaaleEKNVLIQES 480
Cdd:pfam17380 531 EEERRREAEEERRKQQE--MEE------RRRIQEQM-------------RKATEERSRLEAMERER-----EMMRQIVES 584
|
....*...
gi 1907075611 481 ENFRKNLE 488
Cdd:pfam17380 585 EKARAEYE 592
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
35-460 |
1.58e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.60 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 35 MVNMLDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSA-------------LPQDIESLTGGLTGSKGADPP 101
Cdd:PRK01156 244 LSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPvyknrnyindyfkYKNDIENKKQILSNIDAEINK 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 102 EFAALTK--ELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHErSLRM-----------------TVVKRQAQ 162
Cdd:PRK01156 324 YHAIIKKlsVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIE-SLKKkieeyskniermsafisEILKIQEI 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 163 SPSGVSSEV-EVLKALKSLFEHHKALDEKIVALREQNVHIQRKMVSSEGSTESEhLEGMEAGQKVHEKRLSNGSIDSTDD 241
Cdd:PRK01156 403 DPDAIKKELnEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCP-VCGTTLGEEKSNHIINHYNEKKSRL 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 242 TSQIVELQELLEKQNYEMAQMKERLTALSSrvGEVEQ------EAETARKDL--------------IKTEEMNTKYQ--- 298
Cdd:PRK01156 482 EEKIREIEIEVKDIDEKIVDLKKRKEYLES--EEINKsineynKIESARADLedikikinelkdkhDKYEEIKNRYKslk 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 299 ----RDIRECYLQAMAQKEDMEerITTLEKRYLSAQRESTSIHDMNDKLENELANKEA----ILRQMEEKNRQLQERLEL 370
Cdd:PRK01156 560 ledlDSKRTSWLNALAVISLID--IETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSyidkSIREIENEANNLNNKYNE 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 371 AEQK--LQQTMR-KAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDT 447
Cdd:PRK01156 638 IQENkiLIEKLRgKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDR 717
|
490
....*....|...
gi 1907075611 448 VdrllTESNERLQ 460
Cdd:PRK01156 718 I----NDINETLE 726
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
102-504 |
2.16e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 102 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQaqspsgVSSEVEVLKALKSLF 181
Cdd:COG4717 82 EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAE------LAELPERLEELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 182 EHHKALDEKIVALREQNVHIQRKMVSSEGSTESEHLEGMEagqkvhekrlsngsidstDDTSQIVELQELLEKQNYEMAQ 261
Cdd:COG4717 156 EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ------------------DLAEELEELQQRLAELEEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 262 MKERLTALSSRVGEVEQEAETARKDLIKTEEMNT--------------------------------------KYQRDIRE 303
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALEERLKEARLLlliaaallallglggsllsliltiagvlflvlgllallFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 304 CYLQAMAQKEDMEERITTLEKRYLSAQRESTSI-HDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKA 382
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEELEELLAALGLpPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 383 ETLPEVEAELAQRIAALTKAEErhgnIEERMRHLEGQLEEKNQELQRARQREKmNEEHNKRLSDTVDRLLTESNERLQLH 462
Cdd:COG4717 378 EAGVEDEEELRAALEQAEEYQE----LKEELEELEEQLEELLGELEELLEALD-EEELEEELEELEEELEELEEELEELR 452
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1907075611 463 lkERMAALEEKnvlIQESENfRKNLEESLHDKERLAEEIEKL 504
Cdd:COG4717 453 --EELAELEAE---LEQLEE-DGELAELLQELEELKAELREL 488
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
307-481 |
2.29e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 307 QAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAilrQMEEKNRQLQERLELAEQKLQQTMRKAETLP 386
Cdd:COG3883 27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA---EIAEAEAEIEERREELGERARALYRSGGSVS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 387 EVEA--------ELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNER 458
Cdd:COG3883 104 YLDVllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL 183
|
170 180
....*....|....*....|...
gi 1907075611 459 LQLHLKERMAALEEKNVLIQESE 481
Cdd:COG3883 184 LAQLSAEEAAAEAQLAELEAELA 206
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
44-473 |
2.48e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.03 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 44 RLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSA------LPQDIESLTGGLTGSKGADPPEFAALTKELNACREQL 117
Cdd:pfam05483 307 RSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAkaahsfVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMEL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 118 LEKEEEISELKAERNNTRLLLEHLECLVSRHERSL-RMTVVKRQAQSPSGvsSEVEVLKALKSLFEHHKALDEKIVALRE 196
Cdd:pfam05483 387 QKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLdEKKQFEKIAEELKG--KEQELIFLLQAREKEIHDLEIQLTAIKT 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 197 QNVHIQRKMVSSEGSTESEHLEGMEAGQKVHEKRLSNGSI--DSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVG 274
Cdd:pfam05483 465 SEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELtqEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEM 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 275 EVEQEAETARKDLI-KTEEMNTKY------QRDIRECYLQAMAQKEDMEERITTLEKRYLSAQRESTSIHDMN------- 340
Cdd:pfam05483 545 NLRDELESVREEFIqKGDEVKCKLdkseenARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENkalkkkg 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 341 --------------DKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETL--------PEVEAELAQRIAA 398
Cdd:pfam05483 625 saenkqlnayeikvNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIadeavklqKEIDKRCQHKIAE 704
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 399 LTKAEERHGN-----IEERMRHLeGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLL---TESNERLQLHLKERMAAL 470
Cdd:pfam05483 705 MVALMEKHKHqydkiIEERDSEL-GLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLeieKEEKEKLKMEAKENTAIL 783
|
...
gi 1907075611 471 EEK 473
Cdd:pfam05483 784 KDK 786
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
244-422 |
2.83e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.92 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 244 QIVELQELLEkqnyEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAmaqkEDMEERITTLE 323
Cdd:COG1579 8 ALLDLQELDS----ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI----EEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 324 KR---------YLSAQRESTSIHDMNDKLEnelankEAILRQMEEKNrQLQERLELAEQKLQQtmrKAETLPEVEAELAQ 394
Cdd:COG1579 80 EQlgnvrnnkeYEALQKEIESLKRRISDLE------DEILELMERIE-ELEEELAELEAELAE---LEAELEEKKAELDE 149
|
170 180
....*....|....*....|....*...
gi 1907075611 395 RIAALTKAEERhgnIEERMRHLEGQLEE 422
Cdd:COG1579 150 ELAELEAELEE---LEAEREELAAKIPP 174
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
102-430 |
3.23e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 102 EFAALTKELNACREQLLEKEEEISELKAERnntRLLLEHLEclvsRHERSLRMTVVKRQAQSpsgvSSEVEVLKALKSLF 181
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEE---YELLAELA----RLEQDIARLEERRRELE----ERLEELEEELAELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 182 EHHKALDEKIVALREQNVHIQRKMVSSEG--STESEHLEGMEAGQKVHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEM 259
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAelAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 260 AQMKERLTALSSRVGEVEQEAETARKDLIKTEEMntkyQRDIRECYLQAMAQKEDMEERITTLEKRYLSAQRESTSIHDM 339
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEA----LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 340 NDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQtmRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQ 419
Cdd:COG1196 486 LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA--GAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAI 563
|
330
....*....|.
gi 1907075611 420 LEEKNQELQRA 430
Cdd:COG1196 564 EYLKAAKAGRA 574
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
243-526 |
3.56e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.67 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 243 SQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRecylQAMAQKEDMEERITTL 322
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE----SLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 323 EKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMrkaetlpevEAELAQRIAALTKA 402
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS---------EAEAEQALDELLKE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 403 EERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESEN 482
Cdd:COG4372 192 ANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEK 271
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1907075611 483 FRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSLIEPTISRT 526
Cdd:COG4372 272 DTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALED 315
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
38-509 |
3.97e-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: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 38 MLDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSlQRQLNSALPQDIESltggltgskgadppefaaltkELNACREQL 117
Cdd:pfam15921 122 MQMERDAMADIRRRESQSQEDLRNQLQNTVHELEA-AKCLKEDMLEDSNT---------------------QIEQLRKMM 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 118 LEKEEEISELKA-----ERNNTRLLLEHlECLVSRHERSLRMTVVKRQAQspsgVSSEVEVLKA----LKSLFEHHKALD 188
Cdd:pfam15921 180 LSHEGVLQEIRSilvdfEEASGKKIYEH-DSMSTMHFRSLGSAISKILRE----LDTEISYLKGrifpVEDQLEALKSES 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 189 EKIVALREQNVHIQRKMVSSEGSTESEHLEgmeagQKVHEKRLSNGSIDstddtSQIVELQELLEKQNyemAQMKERLTA 268
Cdd:pfam15921 255 QNKIELLLQQHQDRIEQLISEHEVEITGLT-----EKASSARSQANSIQ-----SQLEIIQEQARNQN---SMYMRQLSD 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 269 LSSRVGEVEQEAETARKdlikteemntKYQRDIRECYLQAMAQKEDMEERITtlEKRYLSaqRESTSIHDMNDKLENELA 348
Cdd:pfam15921 322 LESTVSQLRSELREAKR----------MYEDKIEELEKQLVLANSELTEART--ERDQFS--QESGNLDDQLQKLLADLH 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 349 NKEAILRQMEEKNRQLQERlelaeqklqqTMRKAETLPEVEAEL------AQRIAALTKA--EERHGNIEERMRHLEGql 420
Cdd:pfam15921 388 KREKELSLEKEQNKRLWDR----------DTGNSITIDHLRRELddrnmeVQRLEALLKAmkSECQGQMERQMAAIQG-- 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 421 eeKNQELQRARQrekmneehnkrlsdtvdrlLTESNERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAE- 499
Cdd:pfam15921 456 --KNESLEKVSS-------------------LTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEa 514
|
490
....*....|...
gi 1907075611 500 ---EIEKLRSELD 509
Cdd:pfam15921 515 tnaEITKLRSRVD 527
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
171-517 |
4.39e-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: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 171 VEVLKALKSLFEHHKALDEKIVALREQNVHIQRKMVSSEGSTESEHLEGMEAGQKVHEKRLSNGSIDST-DDTSQIVEL- 248
Cdd:COG5185 183 GLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTsDKLEKLVEQn 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 249 QELLEKQNYEMAQMKERLTALSS-----------RVGEVEQEAETAR-----KDLIKTEEMNTKYQRDIRECYLQAMAQK 312
Cdd:COG5185 263 TDLRLEKLGENAESSKRLNENANnlikqfentkeKIAEYTKSIDIKKateslEEQLAAAEAEQELEESKRETETGIQNLT 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 313 EDMEERITTLEKRYLSAQRESTSIHDMND------KLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLP 386
Cdd:COG5185 343 AEIEQGQESLTENLEAIKEEIENIVGEVElsksseELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQI 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 387 E--------VEAELAQRIAALTKAEERhgnIEERMRHLEGQLEEKNQELQRARQRE--KMNEEHNKRLSDTVDRLLT--E 454
Cdd:COG5185 423 EelqrqieqATSSNEEVSKLLNELISE---LNKVMREADEESQSRLEEAYDEINRSvrSKKEDLNEELTQIESRVSTlkA 499
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907075611 455 SNERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKERlaEEIEKLRSELDQMKMRTGS 517
Cdd:COG5185 500 TLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILAL--ENLIPASELIQASNAKTDG 560
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
106-503 |
4.65e-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: 51.17 E-value: 4.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 106 LTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTvvKRQAQSpsgVSSEVEVLKALKSLfEHHK 185
Cdd:TIGR04523 237 KQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKEL--EKQLNQ---LKSEISDLNNQKEQ-DWNK 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 186 ALDEKIVALREQNVHIQRKMVSSEGSTES--EHLEGMEagQKVHEKRLSNGSIDStddtsQIVELQELLEKQNYEMAQMK 263
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQlnEQISQLK--KELTNSESENSEKQR-----ELEEKQNEIEKLKKENQSYK 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 264 ERLTALSSRVGEVE-----QEAETARKDL-IKTEEMN----TKYQRDIRECYLQAMAQKEDMEERITTLEKRY--LSAQR 331
Cdd:TIGR04523 384 QEIKNLESQINDLEskiqnQEKLNQQKDEqIKKLQQEkellEKEIERLKETIIKNNSEIKDLTNQDSVKELIIknLDNTR 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 332 ES--TSIHDMNDKLENELANKEAILRQMEEKNRQLqerLELAEQKLQqtmrkaetLPEVEAELAQRIAALTKAEErhgNI 409
Cdd:TIGR04523 464 ESleTQLKVLSRSINKIKQNLEQKQKELKSKEKEL---KKLNEEKKE--------LEEKVKDLTKKISSLKEKIE---KL 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 410 EERMRHLEGQLEEKNQELqrarqrEKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESENFRKNLEE 489
Cdd:TIGR04523 530 ESEKKEKESKISDLEDEL------NKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIK 603
|
410
....*....|....
gi 1907075611 490 SLHDKERLAEEIEK 503
Cdd:TIGR04523 604 EIEEKEKKISSLEK 617
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
226-506 |
5.12e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.11 E-value: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 226 VHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDL------IKTEEMNTKYQR 299
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLnlvqtaLRQQEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 300 DIRECYLQAMAQKE-------------------------------DMEERITTLEKR---YLSAQRESTSIHDMNDKLEN 345
Cdd:PRK04863 356 DLEELEERLEEQNEvveeadeqqeenearaeaaeeevdelksqlaDYQQALDVQQTRaiqYQQAVQALERAKQLCGLPDL 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 346 ELANKEAILRQMEEKNRQLQERLELAEQKLQ-------------QTMRKAetLPEVEAELAQRIA--ALTKAEErHGNIE 410
Cdd:PRK04863 436 TADNAEDWLEEFQAKEQEATEELLSLEQKLSvaqaahsqfeqayQLVRKI--AGEVSRSEAWDVAreLLRRLRE-QRHLA 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 411 ERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDrllteSNERLQLHLKERMAALEEknvLIQESENFRKNLEES 490
Cdd:PRK04863 513 EQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLD-----DEDELEQLQEELEARLES---LSESVSEARERRMAL 584
|
330
....*....|....*.
gi 1907075611 491 LHDKERLAEEIEKLRS 506
Cdd:PRK04863 585 RQQLEQLQARIQRLAA 600
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
91-436 |
5.83e-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: 50.07 E-value: 5.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 91 GLTGSKGADPPEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLE---CLVSRHERSLRmtvvkrqaQSPSGV 167
Cdd:pfam19220 73 GLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALErqlAAETEQNRALE--------EENKAL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 168 SSEVEVLKALKSLFEHHKALDEKIVALREQNVHIQRKMVSSEGSTESEHlegmEAGQKVHEKRLSNGSIDSTDDTSQIVE 247
Cdd:pfam19220 145 REEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAEL----TRRLAELETQLDATRARLRALEGQLAA 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 248 LQELLEK----QNYEMAQMKERLTALSSRVgeveqEAETARkdLIKTEEMNTkyqrdirecylQAMAQKEDMEERITTLE 323
Cdd:pfam19220 221 EQAERERaeaqLEEAVEAHRAERASLRMKL-----EALTAR--AAATEQLLA-----------EARNQLRDRDEAIRAAE 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 324 KRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLElaeqklqqTMRKAetlpeveaeLAQRIAALTKAE 403
Cdd:pfam19220 283 RRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAE--------MLTKA---------LAAKDAALERAE 345
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1907075611 404 ERHGNIEERMRHLEGQ-------LEEKNQELQRARQREKM 436
Cdd:pfam19220 346 ERIASLSDRIAELTKRfeveraaLEQANRRLKEELQRERA 385
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
115-531 |
7.28e-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: 50.43 E-value: 7.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 115 EQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQ------AQSPSGVSSEVEVLKALKSLFEHHKALD 188
Cdd:TIGR00606 709 DKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQkvnrdiQRLKNDIEEQETLLGTIMPEEESAKVCL 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 189 EKIVALreQNVHIQRKMVSSEGSTESEHLEGMEAGQKVHEKRLSNGSIDSTDDT--SQIVELQELLEKQNYEMAQMKERL 266
Cdd:TIGR00606 789 TDVTIM--ERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTvvSKIELNRKLIQDQQEQIQHLKSKT 866
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 267 TALSSRVGEVEQEAETARKDLIKTEEMNTkyqrDIRECYLQAMAQKEDMEERITTLEKrylSAQRESTSIHDMNDklENE 346
Cdd:TIGR00606 867 NELKSEKLQIGTNLQRRQQFEEQLVELST----EVQSLIREIKDAKEQDSPLETFLEK---DQQEKEELISSKET--SNK 937
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 347 LANKEaiLRQMEEKNRQLQERLELAEQKLQQTmrKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQE 426
Cdd:TIGR00606 938 KAQDK--VNDIKEKVKNIHGYMKDIENKIQDG--KDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQ 1013
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 427 ---LQRARQREKMNEEHnKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESENF-----RKNLEESLHDKERLA 498
Cdd:TIGR00606 1014 erwLQDNLTLRKRENEL-KEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLalgrqKGYEKEIKHFKKELR 1092
|
410 420 430
....*....|....*....|....*....|....*...
gi 1907075611 499 EEI-----EKLRSELDQMKMRTGSLIEPTISRTHIDTS 531
Cdd:TIGR00606 1093 EPQfrdaeEKYREMMIVMRTTELVNKDLDIYYKTLDQA 1130
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
357-510 |
7.42e-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: 7.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 357 MEEKNRQLqERLELAEQKLQQTMRKAETLP----EVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQ 432
Cdd:COG1579 2 MPEDLRAL-LDLQELDSELDRLEHRLKELPaelaELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 433 R--------------------EKMNEEHNKRLSDTVDRLltESNERLQLHLKERMAALEEKnvLIQESENFRKNLEESLH 492
Cdd:COG1579 81 QlgnvrnnkeyealqkeieslKRRISDLEDEILELMERI--EELEEELAELEAELAELEAE--LEEKKAELDEELAELEA 156
|
170
....*....|....*...
gi 1907075611 493 DKERLAEEIEKLRSELDQ 510
Cdd:COG1579 157 ELEELEAEREELAAKIPP 174
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
221-414 |
7.51e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 7.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 221 EAGQKVHEKRLSNGSIDSTDDT----SQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAetarkdlikTEEMNTK 296
Cdd:COG3206 193 EAEAALEEFRQKNGLVDLSEEAklllQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDAL---------PELLQSP 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 297 YQRDIRECYLQAMAQKEDMEERITTLEKRYLSAQREstsIHDMNDKLENELankEAILRQMEEKNRQLQERLELAEQKLQ 376
Cdd:COG3206 264 VIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ---IAALRAQLQQEA---QRILASLEAELEALQAREASLQAQLA 337
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907075611 377 QTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMR 414
Cdd:COG3206 338 QLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
102-583 |
7.92e-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: 50.61 E-value: 7.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 102 EFAALTKELNacrEQLLEKEEEISELKAERNNTRLLL--------EHLECLVSRHERSLRMTVVKR---QAQSPSgVSSE 170
Cdd:pfam12128 280 ERQETSAELN---QLLRTLDDQWKEKRDELNGELSAAdaavakdrSELEALEDQHGAFLDADIETAaadQEQLPS-WQSE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 171 VEVL-KALKSLFEHHKALDEKIVALREQnvhiqrkmVSSEGSTESEHLEGMEAGQKvhEKRLSNGSIDSTDDTSQIVELQ 249
Cdd:pfam12128 356 LENLeERLKALTGKHQDVTAKYNRRRSK--------IKEQNNRDIAGIKDKLAKIR--EARDRQLAVAEDDLQALESELR 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 250 ELLEKQNYEMAQMKERLtalSSRVGE--VEQEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITTLEKRYL 327
Cdd:pfam12128 426 EQLEAGKLEFNEEEYRL---KSRLGElkLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRD 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 328 SAQRESTSIHDMNDKLENELA-----------------NKEAIL-RQMEEK--NRQLQERLELAEQKLQQTMRKAETL-- 385
Cdd:pfam12128 503 QASEALRQASRRLEERQSALDelelqlfpqagtllhflRKEAPDwEQSIGKviSPELLHRTDLDPEVWDGSVGGELNLyg 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 386 -----------------PEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTV 448
Cdd:pfam12128 583 vkldlkridvpewaaseEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEK 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 449 DRL---LTESNERLQLHLKERMAALE-EKNVLIQESENF-----RKNLEESLHDKERLAEEIEKLRSELDQMKmrTGSLI 519
Cdd:pfam12128 663 QSEkdkKNKALAERKDSANERLNSLEaQLKQLDKKHQAWleeqkEQKREARTEKQAYWQVVEGALDAQLALLK--AAIAA 740
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907075611 520 EPTISRTHIDT-STELRYSVGSL-VDSQSDYRTTKVIRRPRRGRMGVRRDEPKVKSLgdHEWNRTQ 583
Cdd:pfam12128 741 RRSGAKAELKAlETWYKRDLASLgVDPDVIAKLKREIRTLERKIERIAVRRQEVLRY--FDWYQET 804
|
|
| SAM_superfamily |
cd09487 |
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
1009-1060 |
7.93e-06 |
|
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.
Pssm-ID: 188886 [Multi-domain] Cd Length: 56 Bit Score: 44.15 E-value: 7.93e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1907075611 1009 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGI 1060
Cdd:cd09487 4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
313-514 |
8.05e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 8.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 313 EDMEERITTLE------KRYLSAQRESTSIHDMNDKLEnelankeaiLRQMEEKNRQLQERLELAEQKLQQTMRKAETLP 386
Cdd:COG4913 245 EDAREQIELLEpirelaERYAAARERLAELEYLRAALR---------LWFAQRRLELLEAELEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 387 EVEAELAQRIAALTKAEERHGNIEErmrhleGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKER 466
Cdd:COG4913 316 ARLDALREELDELEAQIRGNGGDRL------EQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEA 389
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907075611 467 MAALEEknvLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQMKMR 514
Cdd:COG4913 390 AALLEA---LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
316-472 |
8.13e-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: 48.38 E-value: 8.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 316 EERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLElaeqKLQQTMRKAETLPEVEAeLAQR 395
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK----KYEEQLGNVRNNKEYEA-LQKE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907075611 396 IAALtkaEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEE 472
Cdd:COG1579 98 IESL---KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
178-674 |
8.94e-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: 50.12 E-value: 8.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 178 KSLFEHHKALDEKIVALREQNVHIQRKMvsSEGSTESEHLEGMEAGQKVHEKRLSNGSIDSTDDTSQIVELQE-LLEKQN 256
Cdd:pfam15921 92 RRLNESNELHEKQKFYLRQSVIDLQTKL--QEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEdMLEDSN 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 257 YEMAQMKERLTALSSRVGEVEQE----AETARKDLIKTEEMNTKYQRDIRECyLQAMAQKEDME-----ERITTLEKRYL 327
Cdd:pfam15921 170 TQIEQLRKMMLSHEGVLQEIRSIlvdfEEASGKKIYEHDSMSTMHFRSLGSA-ISKILRELDTEisylkGRIFPVEDQLE 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 328 SAQRESTS-----IHDMNDKLENELANKEAILRQMEEKN-------RQLQERLEL-AEQKLQQTMRKAETLPEVEAELAQ 394
Cdd:pfam15921 249 ALKSESQNkiellLQQHQDRIEQLISEHEVEITGLTEKAssarsqaNSIQSQLEIiQEQARNQNSMYMRQLSDLESTVSQ 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 395 RIAALTKAEERHgniEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLT-------------ESNERL-- 459
Cdd:pfam15921 329 LRSELREAKRMY---EDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLAdlhkrekelslekEQNKRLwd 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 460 -----QLHLKERMAALEEKNVLIQESENFRKNLEE-----------SLHDKERLAEEIEKLRSELDQMKMRTGSLIEPTI 523
Cdd:pfam15921 406 rdtgnSITIDHLRRELDDRNMEVQRLEALLKAMKSecqgqmerqmaAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELT 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 524 SRTHIDTSTELRYS--VGSLVDSQSDYRTTKVIRRPRRGRMGVRRDEPK-VKSLGDHEWNRTQQIGVLGSHPFESDTEMS 600
Cdd:pfam15921 486 AKKMTLESSERTVSdlTASLQEKERAIEATNAEITKLRSRVDLKLQELQhLKNEGDHLRNVQTECEALKLQMAEKDKVIE 565
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907075611 601 DIddddRETIFSSMDLLSPSGHSDA--QTLAMMLQEQLDAINKEIRLIQEEKESTELRAEEIENRVASVSLEGLNL 674
Cdd:pfam15921 566 IL----RQQIENMTQLVGQHGRTAGamQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKL 637
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
244-432 |
8.99e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 8.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 244 QIVELQELLEKQNyEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEemntkyQRDIRECYLQAMAQKEDMEERITTLE 323
Cdd:COG4913 250 QIELLEPIRELAE-RYAAARERLAELEYLRAALRLWFAQRRLELLEAE------LEELRAELARLEAELERLEARLDALR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 324 KRYLSAQREstsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQkLQQTMRKAE-TLPEVEAELAQRI----AA 398
Cdd:COG4913 323 EELDELEAQ---------IRGNGGDRLEQLEREIERLERELEERERRRAR-LEALLAALGlPLPASAEEFAALRaeaaAL 392
|
170 180 190
....*....|....*....|....*....|....
gi 1907075611 399 LTKAEERHGNIEERMRHLEGQLEEKNQELQRARQ 432
Cdd:COG4913 393 LEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
242-535 |
9.78e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 9.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 242 TSQIVELQELLEKQNYEMAQMKERLTALS--SRVGEVEQEAETARKDLIKTEEMntkyqrdiRECYLQAMAQKEDMEERI 319
Cdd:COG4913 623 EEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAE--------LERLDASSDDLAALEEQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 320 TTLEKRYlsaqrestsihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlPEVEAELAQRIAAL 399
Cdd:COG4913 695 EELEAEL--------------EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR--LELRALLEERFAAA 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 400 tKAEERHGNIEERmrhLEGQLEEKNQELQRARQR-EKMNEEHNKRLSDTVDRLLT--ESNERLQLHLK----ERMAALEE 472
Cdd:COG4913 759 -LGDAVERELREN---LEERIDALRARLNRAEEElERAMRAFNREWPAETADLDAdlESLPEYLALLDrleeDGLPEYEE 834
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907075611 473 K--NVLIQESENFRKNLEESLHDKERLAEE-IEKLRSELDQMKMRTGSLIEPTISRTHIDTSTELR 535
Cdd:COG4913 835 RfkELLNENSIEFVADLLSKLRRAIREIKErIDPLNDSLKRIPFGPGRYLRLEARPRPDPEVREFR 900
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
259-450 |
1.18e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 259 MAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITTLEKRYLSAQRESTSIHD 338
Cdd:COG1196 632 LEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 339 MNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNI--------- 409
Cdd:COG1196 712 AEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPVnllaieeye 791
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907075611 410 --EERMRHLEGQLEeknqELQRARQR-----EKMNEEHNKRLSDTVDR 450
Cdd:COG1196 792 elEERYDFLSEQRE----DLEEARETleeaiEEIDRETRERFLETFDA 835
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
331-508 |
1.36e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 331 RESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQ--QTMRKAETLPEVEAELAQRIAALTKAEERHGN 408
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 409 IEERMRHLEGQLEEKNQELQRARQRekMNEEHNKRLSDTVDRLltesnERLQlhlkERMAALEEKNVLIQESENFRKNLE 488
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQ--LSLATEEELQDLAEEL-----EELQ----QRLAELEEELEEAQEELEELEEEL 229
|
170 180
....*....|....*....|
gi 1907075611 489 ESLHDKERLAEEIEKLRSEL 508
Cdd:COG4717 230 EQLENELEAAALEERLKEAR 249
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
343-520 |
1.89e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 343 LENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEE 422
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 423 KNQELQRARQREKMNEEHNKRLSDtvdrlLTESNERLQlHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIE 502
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEE-----LEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIE 327
|
170
....*....|....*...
gi 1907075611 503 KLRSELDQMKMRTGSLIE 520
Cdd:PRK03918 328 ERIKELEEKEERLEELKK 345
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
344-510 |
1.94e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 344 ENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlpEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEK 423
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN---ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 424 NQELQRARQREKMNEE--HNKRLSDTVDRL-----LTESNERLQLHLKERMAALEEKnvliqesenfRKNLEESLHDKER 496
Cdd:COG3883 92 ARALYRSGGSVSYLDVllGSESFSDFLDRLsalskIADADADLLEELKADKAELEAK----------KAELEAKLAELEA 161
|
170
....*....|....
gi 1907075611 497 LAEEIEKLRSELDQ 510
Cdd:COG3883 162 LKAELEAAKAELEA 175
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
334-444 |
2.20e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.67 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 334 TSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAEL---AQRIA--ALTKAEERHGN 408
Cdd:PRK00409 509 KLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLleeAEKEAqqAIKEAKKEADE 588
|
90 100 110
....*....|....*....|....*....|....*....
gi 1907075611 409 IEERMRHLE--GQLEEKNQELQRARQR-EKMNEEHNKRL 444
Cdd:PRK00409 589 IIKELRQLQkgGYASVKAHELIEARKRlNKANEKKEKKK 627
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
39-512 |
2.42e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.81 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 39 LDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQDIE--SLTGGLTGSKGADPPEFAALTKELNACREQ 116
Cdd:TIGR00618 371 SCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAfrDLQGQLAHAKKQQELQQRYAELCAAAITCT 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 117 LLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQaqspsgvssEVEVLKALKSLFEhhkaldekivalrE 196
Cdd:TIGR00618 451 AQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLA---------RLLELQEEPCPLC-------------G 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 197 QNVHIQRKMVSS-EGSTESEHLEGMEAGQKVHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGE 275
Cdd:TIGR00618 509 SCIHPNPARQDIdNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPN 588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 276 VEQEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILR 355
Cdd:TIGR00618 589 LQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIR 668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 356 QMEEKNRQLQERLELAEQ-KLQQTMRKAETLPEVEaELAQRIAALTKAEERHGNIEERMRH-----LEGQLEEKNQELQR 429
Cdd:TIGR00618 669 VLPKELLASRQLALQKMQsEKEQLTYWKEMLAQCQ-TLLRELETHIEEYDREFNEIENASSslgsdLAAREDALNQSLKE 747
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 430 ARqrekmneehnkRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELD 509
Cdd:TIGR00618 748 LM-----------HQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDE 816
|
...
gi 1907075611 510 QMK 512
Cdd:TIGR00618 817 DIL 819
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
190-381 |
3.00e-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: 46.05 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 190 KIVALREQNVHIQRKMvsSEGSTESEHLEGMeagQKVHEKRLSNgsIDSTDDtsqivELQELLEKQNYEMAQMKERLTAL 269
Cdd:pfam15619 12 KIKELQNELAELQSKL--EELRKENRLLKRL---QKRQEKALGK--YEGTES-----ELPQLIARHNEEVRVLRERLRRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 270 SSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREcylQAMAQKEDMEERITTLEKRYLSAQREstsIHDMNDKLEN---- 345
Cdd:pfam15619 80 QEKERDLERKLKEKEAELLRLRDQLKRLEKLSED---KNLAEREELQKKLEQLEAKLEDKDEK---IQDLERKLELenks 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907075611 346 ---ELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK 381
Cdd:pfam15619 154 frrQLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKERE 192
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
219-512 |
3.88e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 219 GMEAGQKVHEKRLSNGSIdSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQ 298
Cdd:COG4372 1 GDRLGEKVGKARLSLFGL-RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 299 RDIRecylQAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQT 378
Cdd:COG4372 80 EELE----ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 379 MRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNER 458
Cdd:COG4372 156 EEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1907075611 459 LQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQMK 512
Cdd:COG4372 236 SALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALE 289
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
243-405 |
3.91e-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: 46.46 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 243 SQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARK-------DLIKTEEMNTKYQ------RDIREcYLQAM 309
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKeikrlelEIEEVEARIKKYEeqlgnvRNNKE-YEALQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 310 AQKEDMEERITTLEKRYLsaqrestsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQtmRKAETLPEVE 389
Cdd:COG1579 96 KEIESLKRRISDLEDEIL--------------ELMERIEELEEELAELEAELAELEAELEEKKAELDE--ELAELEAELE 159
|
170
....*....|....*.
gi 1907075611 390 AELAQRIAALTKAEER 405
Cdd:COG1579 160 ELEAEREELAAKIPPE 175
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
397-512 |
4.21e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.93 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 397 AALTKAEERHGNIEER-----MRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLlTESNERLQLHLK-----ER 466
Cdd:COG2433 380 EALEELIEKELPEEEPeaereKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEK-DERIERLERELSearseER 458
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1907075611 467 MAALEEKNVLIQESENfrKNLEESLHDKErlaEEIEKLRSELDQMK 512
Cdd:COG2433 459 REIRKDREISRLDREI--ERLERELEEER---ERIEELKRKLERLK 499
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
45-517 |
4.43e-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: 47.89 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 45 LLDTLRETQES---LSLAQQRLQDVIydrdSLQRQLNSALPQDIESltgglTGSKGADPPEFAALT-------------- 107
Cdd:pfam10174 58 LKEQYRVTQEEnqhLQLTIQALQDEL----RAQRDLNQLLQQDFTT-----SPVDGEDKFSTPELTeenfrrlqseherq 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 108 -KELNACREQLLEKEEEISE----LKAERNNTRLLLEHLEC-------LVSRHERSLRMTVVKRQAQSPSG--------- 166
Cdd:pfam10174 129 aKELFLLRKTLEEMELRIETqkqtLGARDESIKKLLEMLQSkglpkksGEEDWERTRRIAEAEMQLGHLEVlldqkeken 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 167 ------------VSSEVEVLKALKSLFEhhkALDEKIVALrEQNVH---IQRKMVSSEGSTES----EHLEGMEAgQKVH 227
Cdd:pfam10174 209 ihlreelhrrnqLQPDPAKTKALQTVIE---MKDTKISSL-ERNIRdleDEVQMLKTNGLLHTedreEEIKQMEV-YKSH 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 228 EKRLSNgSIDSTDD-----TSQIVELQ---ELLEKQNYEMAQ----MKERLTALSSRVGEVEQEAETARKDLIKTEEMNT 295
Cdd:pfam10174 284 SKFMKN-KIDQLKQelskkESELLALQtklETLTNQNSDCKQhievLKESLTAKEQRAAILQTEVDALRLRLEEKESFLN 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 296 KYQRDIREC------------YLQAM-------------------AQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLE 344
Cdd:pfam10174 363 KKTKQLQDLteekstlageirDLKDMldvkerkinvlqkkienlqEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLE 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 345 NELANKEAIL-RQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGN-------IEERMRHL 416
Cdd:pfam10174 443 EALSEKERIIeRLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSlassglkKDSKLKSL 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 417 EGQLEEKNQE-------LQRARQRE---KMNEEHNKRLS---DTVDRLLTESN------ERLQLHLKE----------RM 467
Cdd:pfam10174 523 EIAVEQKKEEcsklenqLKKAHNAEeavRTNPEINDRIRlleQEVARYKEESGkaqaevERLLGILREvenekndkdkKI 602
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907075611 468 AALEE-------------KNVLIQESENFRKN---LEESLHDK------------ERLAEEIEKLRSELDQMKMRTGS 517
Cdd:pfam10174 603 AELESltlrqmkeqnkkvANIKHGQQEMKKKGaqlLEEARRREdnladnsqqlqlEELMGALEKTRQELDATKARLSS 680
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
284-507 |
4.68e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 48.15 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 284 RKDLIKTEEMNTKYQRDI-RECYLQAMAQKEDMEERITTLEKRYLSAQREstsihdmndklenelanKEAILRQMEEKNR 362
Cdd:COG5022 809 RKEYRSYLACIIKLQKTIkREKKLRETEEVEFSLKAEVLIQKFGRSLKAK-----------------KRFSLLKKETIYL 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 363 QLQERLELAEQK---LQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIE-----ERMRHLEGQLEEKNQELQRARQRE 434
Cdd:COG5022 872 QSAQRVELAERQlqeLKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENlefktELIARLKKLLNNIDLEEGPSIEYV 951
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907075611 435 KmNEEHNKRLsdTVDRLLTESNERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSE 507
Cdd:COG5022 952 K-LPELNKLH--EVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKEL 1021
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
41-362 |
5.55e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.76 E-value: 5.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 41 ERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQDIESLTGG------LTGSKGADPPEFAALTKELNACR 114
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKReyegyeLLKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 115 EQLLEKEEEISELKAERNNTRLLLEHLECLVSRhERSLRMTVVKRQAQSpsgVSSEVEVLK-ALKSLFEHHKALDEKIVA 193
Cdd:TIGR02169 251 EELEKLTEEISELEKRLEEIEQLLEELNKKIKD-LGEEEQLRVKEKIGE---LEAEIASLErSIAEKERELEDAEERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 194 LREQNVHIQRKMVSSEGSTESEHL-------EGMEAGQKVHEKRLSNGSIDSTDDTS--QIVELQELLEKQNYEMAQMK- 263
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKrrdklteEYAELKEELEDLRAELEEVDKEFAETrdELKDYREKLEKLKREINELKr 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 264 ------ERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEeritTLEKRYLSAQRESTSIH 337
Cdd:TIGR02169 407 eldrlqEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS----KYEQELYDLKEEYDRVE 482
|
330 340
....*....|....*....|....*
gi 1907075611 338 DMNDKLENELANKEAILRQMEEKNR 362
Cdd:TIGR02169 483 KELSKLQRELAEAEAQARASEERVR 507
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
189-512 |
5.63e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 47.16 E-value: 5.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 189 EKIVALREQNVHIQRK----MVSSE--GSTESEHLEGM--EAGQKVHEKRLSNG-SIDSTDDT-----SQIVELQELLEK 254
Cdd:pfam06160 92 EELLDDIEEDIKQILEeldeLLESEekNREEVEELKDKyrELRKTLLANRFSYGpAIDELEKQlaeieEEFSQFEELTES 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 255 QNYEMA-----QMKERLTALSSRVGEVEQEAETARKDLikTEEMNtkyqrDIRECYLQAMAQKEDMEErittlekryLSA 329
Cdd:pfam06160 172 GDYLEArevleKLEEETDALEELMEDIPPLYEELKTEL--PDQLE-----ELKEGYREMEEEGYALEH---------LNV 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 330 QRESTSIHDMNDKLENELANKEaiLRQMEEKNRQLQERLElaeqKLQQTMRKaetlpEVEAELaqriaaltKAEERHGNI 409
Cdd:pfam06160 236 DKEIQQLEEQLEENLALLENLE--LDEAEEALEEIEERID----QLYDLLEK-----EVDAKK--------YVEKNLPEI 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 410 EERMRHLEGQLEEKNQELQRARQREKMNEEH-------NKRLsDTVDRLLTESNERLQLH------LKERMAALEEKNVL 476
Cdd:pfam06160 297 EDYLEHAEEQNKELKEELERVQQSYTLNENElervrglEKQL-EELEKRYDEIVERLEEKevayseLQEELEEILEQLEE 375
|
330 340 350
....*....|....*....|....*....|....*...
gi 1907075611 477 IQES-ENFRKNLeESLHDKERLA-EEIEKLRSELDQMK 512
Cdd:pfam06160 376 IEEEqEEFKESL-QSLRKDELEArEKLDEFKLELREIK 412
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
255-503 |
6.08e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 255 QNYEMAQMKErltalsSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREcylqAMAQKEDMeerittlekRYLSAQREST 334
Cdd:PTZ00121 1077 KDFDFDAKED------NRADEATEEAFGKAEEAKKTETGKAEEARKAEE----AKKKAEDA---------RKAEEARKAE 1137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 335 SIHDMNDKLENELANKEAILRQMEEKnRQLQERLELAEQKLQQTMRKAETLPEVE----AELAQRIAALTKAEERHgNIE 410
Cdd:PTZ00121 1138 DARKAEEARKAEDAKRVEIARKAEDA-RKAEEARKAEDAKKAEAARKAEEVRKAEelrkAEDARKAEAARKAEEER-KAE 1215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 411 ERMRHLEgqlEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAAL--EEKnvliQESENFRKNLE 488
Cdd:PTZ00121 1216 EARKAED---AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIkaEEA----RKADELKKAEE 1288
|
250
....*....|....*
gi 1907075611 489 ESLHDKERLAEEIEK 503
Cdd:PTZ00121 1289 KKKADEAKKAEEKKK 1303
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
247-506 |
7.66e-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: 47.25 E-value: 7.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 247 ELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLikteemnTKYQRDIRE------CYLQAMAQKEDMEERit 320
Cdd:COG3096 358 ELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQL-------ADYQQALDVqqtraiQYQQAVQALEKARAL-- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 321 tLEKRYLSAqrestsihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETL----PEVEAELA-QR 395
Cdd:COG3096 429 -CGLPDLTP-----------ENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVckiaGEVERSQAwQT 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 396 IAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDrllteSNERLQLHLKERMAALEEknv 475
Cdd:COG3096 497 ARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLD-----AAEELEELLAELEAQLEE--- 568
|
250 260 270
....*....|....*....|....*....|.
gi 1907075611 476 LIQESENFRKNLEESLHDKERLAEEIEKLRS 506
Cdd:COG3096 569 LEEQAAEAVEQRSELRQQLEQLRARIKELAA 599
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
312-518 |
8.60e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.21 E-value: 8.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 312 KEDMEERITTLEKRYLSAQRESTSIHDmndkLENELANKEAILRQmEEKNRQLQERLELAEQKLQQTMRKAETLPEVEA- 390
Cdd:PRK11281 38 EADVQAQLDALNKQKLLEAEDKLVQQD----LEQTLALLDKIDRQ-KEETEQLKQQLAQAPAKLRQAQAELEALKDDNDe 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 391 ELAQRIAALTkaeerhgnieerMRHLEGQLEEKNQELQRARqrekmneehnKRLSDTVDRLLTESN--ERLQlhlkermA 468
Cdd:PRK11281 113 ETRETLSTLS------------LRQLESRLAQTLDQLQNAQ----------NDLAEYNSQLVSLQTqpERAQ-------A 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1907075611 469 ALEEKNVLIQESENFRKNLEESlhDKERLAEEIEKLRSELD----QMKMRTGSL 518
Cdd:PRK11281 164 ALYANSQRLQQIRNLLKGGKVG--GKALRPSQRVLLQAEQAllnaQNDLQRKSL 215
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
362-559 |
1.10e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 46.24 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 362 RQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERmrhlegqlEEKNQELQRARQREKMNEEHN 441
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRER--------EELQREEERLVQKEEQLDARA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 442 KRLSDTVDRLLTESN----ERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHD--KERLAEEIEKLRSELD-QMKMR 514
Cdd:PRK12705 98 EKLDNLENQLEEREKalsaRELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAelEEEKAQRVKKIEEEADlEAERK 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907075611 515 TGSLIEPTISRTHIDTSTELRYSVgslVDSQSDYRTTKVIRRPRR 559
Cdd:PRK12705 178 AQNILAQAMQRIASETASDLSVSV---VPIPSDAMKGRIIGREGR 219
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
879-943 |
1.26e-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: 41.10 E-value: 1.26e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907075611 879 QWDGPTVVAWLElWLGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQEM 943
Cdd:pfam00536 2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
83-513 |
1.29e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 46.32 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 83 QDIESLTGGLTGSKGADPPEFAALTKELNACREQLLEKEEEIS-------ELKAERNNTRLLLEHLECLVSRHERSLRMT 155
Cdd:pfam01576 204 QELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQaalarleEETAQKNNALKKIRELEAQISELQEDLESE 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 156 VVKRqAQSPSGVSSEVEVLKALKSLFEH---HKALDEKIVALREQNVHIQRKMVSSEGstesehlegmeagqKVHEKRLS 232
Cdd:pfam01576 284 RAAR-NKAEKQRRDLGEELEALKTELEDtldTTAAQQELRSKREQEVTELKKALEEET--------------RSHEAQLQ 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 233 NGSIDSTddtSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETarkdlIKTEEMNTKYQRDIRECYLQamaqk 312
Cdd:pfam01576 349 EMRQKHT---QALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRT-----LQQAKQDSEHKRKKLEGQLQ----- 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 313 edmeeritTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMrkaETLPEveaEL 392
Cdd:pfam01576 416 --------ELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQ---ELLQE---ET 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 393 AQRIAALTKAEErhgnIEERMRHLEGQLEEknqELQRARQREKMNEEHNKRLSDTVDRLLTESnerlqlhlkERMAALEE 472
Cdd:pfam01576 482 RQKLNLSTRLRQ----LEDERNSLQEQLEE---EEEAKRNVERQLSTLQAQLSDMKKKLEEDA---------GTLEALEE 545
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1907075611 473 -KNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQMKM 513
Cdd:pfam01576 546 gKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLV 587
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
1087-1157 |
1.37e-04 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 41.10 E-value: 1.37e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907075611 1087 VLVWSNDRVIRWIQAIGLREYANNILESGVHG--SLIALDENFdysslalLLQIPTQNTQARQILEREYNNLL 1157
Cdd:pfam07647 1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGaeLLLRLTLED-------LKRLGITSVGHRRKILKKIQELK 66
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
323-504 |
1.49e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 323 EKRYLSAQREStsihdmndkLENELANkeaiLRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKA 402
Cdd:PRK04863 507 EQRHLAEQLQQ---------LRMRLSE----LEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSES 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 403 EERHGNIEERMRHLEGQLEEKNQELQRARQrekmnEEHNkrLSDTVDRLLTESNERLqlhlkERMAALEE--KNVLIQES 480
Cdd:PRK04863 574 VSEARERRMALRQQLEQLQARIQRLAARAP-----AWLA--AQDALARLREQSGEEF-----EDSQDVTEymQQLLERER 641
|
170 180
....*....|....*....|....
gi 1907075611 481 EnFRKNLEESLHDKERLAEEIEKL 504
Cdd:PRK04863 642 E-LTVERDELAARKQALDEEIERL 664
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
342-512 |
1.66e-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: 44.53 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 342 KLENELANKEAILRQMEEKNRQLQERLELAEQKLQqtmrkaetlpEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLE 421
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLE----------AAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 422 E-KNQELQRARQREKmnEEHNKRLSDTVDRLLtesnerlqlhlkERMAALEEKNVLIQESENFRKNLEESL-HDKERLAE 499
Cdd:COG1579 84 NvRNNKEYEALQKEI--ESLKRRISDLEDEIL------------ELMERIEELEEELAELEAELAELEAELeEKKAELDE 149
|
170
....*....|...
gi 1907075611 500 EIEKLRSELDQMK 512
Cdd:COG1579 150 ELAELEAELEELE 162
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
273-471 |
1.97e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 273 VGEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITTLEKryLSAQREstsihdmndKLENELANKEA 352
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEE--LEEELE---------ELEAELEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 353 ILRQME--EKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHL--------EGQLEE 422
Cdd:COG4717 117 ELEKLEklLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELleqlslatEEELQD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907075611 423 KNQELQRARQREKMNEEHNKRLSDTVDRLLTE----SNERLQLHLKERMAALE 471
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEEEleqlENELEAAALEERLKEAR 249
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
247-433 |
2.28e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 45.45 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 247 ELQELLEKQNyEMAQMKERLT-------ALSSRVGEVEQ-EAEtaRKDLIKTEEMntkyQRDIRECYlQAMAQKED-MEE 317
Cdd:COG0497 173 ELEELRADEA-ERARELDLLRfqleeleAAALQPGEEEElEEE--RRRLSNAEKL----REALQEAL-EALSGGEGgALD 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 318 RITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQ---ERLELAEQKLQ---QTMRK----AETLPE 387
Cdd:COG0497 245 LLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEfdpERLEEVEERLAllrRLARKygvtVEELLA 324
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907075611 388 VEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQR 433
Cdd:COG0497 325 YAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKK 370
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
284-511 |
2.80e-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: 45.12 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 284 RKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITTLEKRYlsaQRESTSIHDMND---KLENELANKEAILRQMEEK 360
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQL---DRESDRNQELQKrirLLEKREAEAEEALREQAEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 361 NRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHgnieermrhlEGQLEEKNQELQRARQR------- 433
Cdd:pfam05557 78 NRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRA----------ELELQSTNSELEELQERldllkak 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 434 ----EKMNEEHNKRLSdtvdrLLTESNERLQ----------------LHLKERMAALEEKNVLIQESENFRKNLEESLHD 493
Cdd:pfam05557 148 aseaEQLRQNLEKQQS-----SLAEAEQRIKelefeiqsqeqdseivKNSKSELARIPELEKELERLREHNKHLNENIEN 222
|
250
....*....|....*...
gi 1907075611 494 KERLAEEIEKLRSELDQM 511
Cdd:pfam05557 223 KLLLKEEVEDLKRKLERE 240
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
365-503 |
3.36e-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: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 365 QERLELAEQKLQQtmrkaetLPEVEAELAQRIAALTKaeeRHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRL 444
Cdd:pfam12718 13 QERAEELEEKVKE-------LEQENLEKEQEIKSLTH---KNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNENLTRKI 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907075611 445 sdtvdRLLTESNERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIEK 503
Cdd:pfam12718 83 -----QLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEE 136
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
104-514 |
3.37e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 104 AALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMtvvkrqaqspsgvssevevlkalkslfeh 183
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV----------------------------- 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 184 hKALDEKIVALREQnvhiqrkmvssegstesehLEGMEAGQkvhekrlsngsidstddtSQIVELQELLEKQNYEMAQMK 263
Cdd:COG4913 664 -ASAEREIAELEAE-------------------LERLDASS------------------DDLAALEEQLEELEAELEELE 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 264 ERLTALSSRVGEVEQEAETARKDLIKTEEMntkyqrdirecyLQAMAQKEDMEERiTTLEKRYLSAQRestsihdmnDKL 343
Cdd:COG4913 706 EELDELKGEIGRLEKELEQAEEELDELQDR------------LEAAEDLARLELR-ALLEERFAAALG---------DAV 763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 344 ENELAnkeailRQMEEKNRQLQERLELAEQKLQQTMRKA-ETLPEVEAELAQRIAALTKAEERHGNIEERmrhlegQLEE 422
Cdd:COG4913 764 ERELR------ENLEERIDALRARLNRAEEELERAMRAFnREWPAETADLDADLESLPEYLALLDRLEED------GLPE 831
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 423 KNQELQRARQR----------EKMNEEHN---KRLsDTVDRLLTESN----ERLQLHLKERM--AALEEKNVLIQESEN- 482
Cdd:COG4913 832 YEERFKELLNEnsiefvadllSKLRRAIReikERI-DPLNDSLKRIPfgpgRYLRLEARPRPdpEVREFRQELRAVTSGa 910
|
410 420 430
....*....|....*....|....*....|..
gi 1907075611 483 FRKNLEESLHDKERLAEEIEKLRSELDQMKMR 514
Cdd:COG4913 911 SLFDEELSEARFAALKRLIERLRSEEEESDRR 942
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
247-479 |
3.61e-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: 43.94 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 247 ELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYlQAMAQKEDMEERITTLEKR- 325
Cdd:pfam06008 27 QLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAK-ELAEAIKNLIDNIKEINEKv 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 326 -YLSAQRESTSihdmNDKLENELANKEAILRQMeeKNRQLQERLELAEQKLqqtmRKAETLPEVEAELAQRIAALTKAee 404
Cdd:pfam06008 106 aTLGENDFALP----SSDLSRMLAEAQRMLGEI--RSRDFGTQLQNAEAEL----KAAQDLLSRIQTWFQSPQEENKA-- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 405 rhgnIEERMRHLEGQLEEKNQELQ--------RARQREKMNEEHNKRLSDTVDRLLT--ESNERLQLHLKERMAALEEKN 474
Cdd:pfam06008 174 ----LANALRDSLAEYEAKLSDLRellreaaaKTRDANRLNLANQANLREFQRKKEEvsEQKNQLEETLKTARDSLDAAN 249
|
....*
gi 1907075611 475 VLIQE 479
Cdd:pfam06008 250 LLLQE 254
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
274-529 |
4.46e-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: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 274 GEVEQEAETARKDLIKTEE--MNTKYQRDIRECYLQAMAQKEDMEERITTLEKRYLSAQREstsihDMNDKLENELANKE 351
Cdd:pfam02463 142 GKIEIIAMMKPERRLEIEEeaAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKL-----KEQAKKALEYYQLK 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 352 AILRQMEEKNRQLQERLELAEQK---------LQQTMRKAETLPEVEAELAQRIAALTKAEER-HGNIEERMRHLEGQLE 421
Cdd:pfam02463 217 EKLELEEEYLLYLDYLKLNEERIdllqellrdEQEEIESSKQEIEKEEEKLAQVLKENKEEEKeKKLQEEELKLLAKEEE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 422 EKNQELQRARQREKMNEEhNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEI 501
Cdd:pfam02463 297 ELKSELLKLERRKVDDEE-KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEEL 375
|
250 260
....*....|....*....|....*...
gi 1907075611 502 EKLRSELDQMKMRTGSLIEPTISRTHID 529
Cdd:pfam02463 376 LAKKKLESERLSSAAKLKEEELELKSEE 403
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
40-425 |
4.70e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.56 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 40 DERDRLLDTLRETQEsLSLAQQRL-QDVIYDRDSLQRQLNsALPQ---------DIESLTGGLTGSKGAdppeFAALTKE 109
Cdd:COG3096 303 EEQYRLVEMARELEE-LSARESDLeQDYQAASDHLNLVQT-ALRQqekieryqeDLEELTERLEEQEEV----VEEAAEQ 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 110 LNACREQLLEKEEEISELKAErnntrlLLEHLECLVSRHERSLRMtvvkRQAQSPSGVSSEVEVLKAL--KSLFEHHKAL 187
Cdd:COG3096 377 LAEAEARLEAAEEEVDSLKSQ------LADYQQALDVQQTRAIQY----QQAVQALEKARALCGLPDLtpENAEDYLAAF 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 188 DEKIVALREQNVHIQRKMVSSEgSTESEHLEGMEAGQKVhekrlsNGSIDSTDDTSQIvelQELLEKQNYEMAQMkERLT 267
Cdd:COG3096 447 RAKEQQATEEVLELEQKLSVAD-AARRQFEKAYELVCKI------AGEVERSQAWQTA---RELLRRYRSQQALA-QRLQ 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 268 ALSSRVGEVEQ------EAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITTLEKRYLSAQREstsihdmnd 341
Cdd:COG3096 516 QLRAQLAELEQrlrqqqNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQ--------- 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 342 klENELANKEAILRQMEEKNRQLQERLE-LAEQKLQQTmrkaETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQL 420
Cdd:COG3096 587 --LEQLRARIKELAARAPAWLAAQDALErLREQSGEAL----ADSQEVTAAMQQLLEREREATVERDELAARKQALESQI 660
|
....*
gi 1907075611 421 EEKNQ 425
Cdd:COG3096 661 ERLSQ 665
|
|
| SAM_STIM-1,2-like |
cd09504 |
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ... |
880-938 |
4.94e-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: 40.01 E-value: 4.94e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907075611 880 WDGPTVVAWLELWLGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNPLHRLKLRL 938
Cdd:cd09504 5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
275-505 |
6.73e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.67 E-value: 6.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 275 EVEQEAET-----ARKDLIKTEEMNTKYQRDIRECyLQAMA----QKEDMEERITTLEKRYLSAQRE----STSIHDMND 341
Cdd:PRK04778 90 EAEELNDKfrfrkAKHEINEIESLLDLIEEDIEQI-LEELQelleSEEKNREEVEQLKDLYRELRKSllanRFSFGPALD 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 342 KLENELANKEAILRQMEEKN-----RQLQERLELAEQKLQQTMRKAETLPEVEAELAQRI-AALTKAEE----------- 404
Cdd:PRK04778 169 ELEKQLENLEEEFSQFVELTesgdyVEAREILDQLEEELAALEQIMEEIPELLKELQTELpDQLQELKAgyrelveegyh 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 405 -RHGNIEERMRHLEGQLEEKNQELQR---ARQREKmNEEHNKRLSDTVDRLLTEsnerlqlhlkerMAAleeKNVLIQES 480
Cdd:PRK04778 249 lDHLDIEKEIQDLKEQIDENLALLEEldlDEAEEK-NEEIQERIDQLYDILERE------------VKA---RKYVEKNS 312
|
250 260
....*....|....*....|....*
gi 1907075611 481 ENFRKNLEESLHDKERLAEEIEKLR 505
Cdd:PRK04778 313 DTLPDFLEHAKEQNKELKEEIDRVK 337
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
341-508 |
8.95e-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: 41.97 E-value: 8.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 341 DKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlPEVEAELAQRIAALTKAEERHG-----------NI 409
Cdd:pfam04012 39 VKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGN--EELAREALAEKKSLEKQAEALEtqlaqqrsaveQL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 410 EERMRHLEGQLEEKNQE-------LQRARQREKMNEehnkrlsdTVDRLLTESNERLQLHLKERMAALEEKNVLIQESEn 482
Cdd:pfam04012 117 RKQLAALETKIQQLKAKknllkarLKAAKAQEAVQT--------SLGSLSTSSATDSFERIEEKIEEREARADAAAELA- 187
|
170 180
....*....|....*....|....*.
gi 1907075611 483 FRKNLEESLHDKERLAEEIEKLRSEL 508
Cdd:pfam04012 188 SAVDLDAKLEQAGIQMEVSEDVLARL 213
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
242-531 |
9.07e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.80 E-value: 9.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 242 TSQIVELQELLEKQNYemAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKyqrdIRECYLQAMAQKEDMEERITT 321
Cdd:TIGR00618 273 RAQEAVLEETQERINR--ARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAK----LLMKRAAHVKQQSSIEEQRRL 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 322 LEkrylSAQRESTSIHDMNDKlenELANKEAILRQMEEKN--RQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAal 399
Cdd:TIGR00618 347 LQ----TLHSQEIHIRDAHEV---ATSIREISCQQHTLTQhiHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTS-- 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 400 tkaeerhgnieeRMRHLEGQLeeknqelQRARQREKMNEEHNkrlsdtvdrlltesnERLQLHLKERMAALEEKNVLIQE 479
Cdd:TIGR00618 418 ------------AFRDLQGQL-------AHAKKQQELQQRYA---------------ELCAAAITCTAQCEKLEKIHLQE 463
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 480 SENFRKNLEESLHDKERLAEEIEKLRSELDQMKMR--------TGSLIEPTISRTHIDTS 531
Cdd:TIGR00618 464 SAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLElqeepcplCGSCIHPNPARQDIDNP 523
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
341-515 |
9.15e-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: 42.05 E-value: 9.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 341 DKLENELANKEAILRQME------------EKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIaaltkaEERHGN 408
Cdd:cd00176 10 DELEAWLSEKEELLSSTDygddlesveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI------QERLEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 409 IEERMRHLEGQLEEKNQELQRARQREKMNEEH---NKRLSDTVDRLLTESN-------ERLQLHLKERMAALEEKNVLIQ 478
Cdd:cd00176 84 LNQRWEELRELAEERRQRLEEALDLQQFFRDAddlEQWLEEKEAALASEDLgkdlesvEELLKKHKELEEELEAHEPRLK 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907075611 479 ESENFRKNLEESLH--DKERLAEEIEKLRSELDQMKMRT 515
Cdd:cd00176 164 SLNELAEELLEEGHpdADEEIEEKLEELNERWEELLELA 202
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
179-512 |
1.09e-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: 43.17 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 179 SLFEHHKALDEKIVALREQNVHIQRKMVSSEG------STESEHLEGMEAGQK-VHEKRLSNGSIdSTDDTSQIVELQEL 251
Cdd:pfam05483 68 SDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAelkqkeNKLQENRKIIEAQRKaIQELQFENEKV-SLKLEEEIQENKDL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 252 LEKQN---YEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDME-------ERITT 321
Cdd:pfam05483 147 IKENNatrHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHfklkedhEKIQH 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 322 LEKRYL----SAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK----AETLPEVEAELA 393
Cdd:pfam05483 227 LEEEYKkeinDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKkdhlTKELEDIKMSLQ 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 394 QRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLH---LKERMAAL 470
Cdd:pfam05483 307 RSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNedqLKIITMEL 386
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1907075611 471 EEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQMK 512
Cdd:pfam05483 387 QKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFE 428
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
248-514 |
1.15e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.96 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 248 LQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLiktEEMNTKYQRDIRECYLQAMAQKEDMEErittLEKRYL 327
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQW---ERQRRELESRVAELKEELRQSREKHEE----LEEKYK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 328 SAQRESTSIHdmndklenelANKEAILRQMEEKNRQLQErLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEE-RH 406
Cdd:pfam07888 105 ELSASSEELS----------EEKDALLAQRAAHEARIRE-LEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEaER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 407 GNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLH--LKERMAALEEK-NVLIQES 480
Cdd:pfam07888 174 KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLtqkLTTAHRKEAENeaLLEELRSLQERlNASERKV 253
|
250 260 270
....*....|....*....|....*....|....
gi 1907075611 481 ENFRKNLEESLHDKERLAEEIEKLRSELDQMKMR 514
Cdd:pfam07888 254 EGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQ 287
|
|
| PRK03992 |
PRK03992 |
proteasome-activating nucleotidase; Provisional |
465-523 |
1.26e-03 |
|
proteasome-activating nucleotidase; Provisional
Pssm-ID: 179699 [Multi-domain] Cd Length: 389 Bit Score: 42.51 E-value: 1.26e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 465 ERMAALEEKNV-LIQESENFRKNLEESLHDKERLAEEIEKLRSELDqmKMRTGSLIEPTI 523
Cdd:PRK03992 1 ERLEALEERNSeLEEQIRQLELKLRDLEAENEKLERELERLKSELE--KLKSPPLIVATV 58
|
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
223-587 |
1.38e-03 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 43.19 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 223 GQKVHEK--RLSNGSID----STDDTSQIVELQELLEKQNYEMAQMKERLTALS-SRVGEVEQE---AETARKDLIKTEe 292
Cdd:COG5192 415 GKAIAEEtsREDELSFDdsdvSTSDENEDVDFTGKKGAINNEDESDNEEVAFDSdSQFDESEGNlrwKEGLASKLAYSQ- 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 293 mNTKYQRDIREC-YLQAMAQKEDMEERittlekrylsaQRESTSIHDMNDKLENElanKEAILRQMEEKNRQLQERLE-L 370
Cdd:COG5192 494 -SGKRGRNIQKIfYDESLSPEECIEEY-----------KGESAKSSESDLVVQDE---PEDFFDVSKVANESISSNHEkL 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 371 AEQKLQQTMRKAETLPEVEAELAQriAALTKAEERHgniEErmrhLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDR 450
Cdd:COG5192 559 MESEFEELKKKWSSLAQLKSRFQK--DATLDSIEGE---EE----LIQDDEKGNFEDLEDEENSSDNEMEESRGSSVTAE 629
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 451 LLTESNERLQLHLKERMAALEEK---NVLIQESENFRKN-LEESLHDKERLAEEIEKLRSELDQM---------KMRTGS 517
Cdd:COG5192 630 NEESADEVDYETEREENARKKEElrgNFELEERGDPEKKdVDWYTEEKRKIEEQLKINRSEFETMvpesrvvieGYRAGR 709
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907075611 518 LIEPTISRTHIDTSTELRYS----VGSLVDSQSDYRTTKV-IRRPRRGRMGVRRDEPKVKSLGdheWNRTQQIGV 587
Cdd:COG5192 710 YVRIVLSHVPLEFVDEFNSRypivLGGLLPAEKEMGIVQGrIKRHRWHKKILKTNDPLIFSVG---WRRFQSIPV 781
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
248-433 |
1.70e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 248 LQELLEKQNyemAQMKERLTALSSRVGEVEQEAETARKDLIK----------TEEMNTKYQR--DIRECYLQAMAQKEDM 315
Cdd:COG3206 162 LEQNLELRR---EEARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdlSEEAKLLLQQlsELESQLAEARAELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 316 EERITTLEKRYLSAQRESTSI--HDMNDKLENELANKEAILRQMEEKN-------RQLQERLELAEQKLQQTMRK----- 381
Cdd:COG3206 239 EARLAALRAQLGSGPDALPELlqSPVIQQLRAQLAELEAELAELSARYtpnhpdvIALRAQIAALRAQLQQEAQRilasl 318
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907075611 382 ---AETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQR 433
Cdd:COG3206 319 eaeLEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQR 373
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
351-504 |
1.80e-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: 42.63 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 351 EAILRQMEEKNRQLQERLELAE---QKLQQTMRKAETLPEVEAELAQRIAALtkaEERHGNIEERMRHLEGQLEEKNQEL 427
Cdd:COG3096 518 RAQLAELEQRLRQQQNAERLLEefcQRIGQQLDAAEELEELLAELEAQLEEL---EEQAAEAVEQRSELRQQLEQLRARI 594
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907075611 428 QRARQREKMNEEHNKRLSdtvdRLLTESNERLQlHLKERMAALEekNVLIQESEnFRKNLEESLHDKERLAEEIEKL 504
Cdd:COG3096 595 KELAARAPAWLAAQDALE----RLREQSGEALA-DSQEVTAAMQ--QLLERERE-ATVERDELAARKQALESQIERL 663
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
152-670 |
2.26e-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: 42.34 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 152 LRMTVVKRQAQSPSG------VSSEVEVLKALKSLFEHHKA----LDEKIVALREQNVHIQRKMVSSEGSTESEHLEGME 221
Cdd:TIGR00606 222 IRDQITSKEAQLESSreivksYENELDPLKNRLKEIEHNLSkimkLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 222 AGQKVHEKRLSNGSidstDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVG------EVEQEAETARKDLIKTEEMNT 295
Cdd:TIGR00606 302 QLNDLYHNHQRTVR----EKERELVDCQRELEKLNKERRLLNQEKTELLVEQGrlqlqaDRHQEHIRARDSLIQSLATRL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 296 K---YQRDI---RECYLQAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLE 369
Cdd:TIGR00606 378 EldgFERGPfseRQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELK 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 370 LAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEErHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNkRLSDTVD 449
Cdd:TIGR00606 458 FVIKELQQLEGSSDRILELDQELRKAERELSKAEK-NSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLN-HHTTTRT 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 450 RLLTESNERLQLHLKERMAALEEKNVLIQESENF--RKNLEESLH----DKERLAEEIEKLRSELDQMKMRTGSLIEPTI 523
Cdd:TIGR00606 536 QMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFpnKKQLEDWLHskskEINQTRDRLAKLNKELASLEQNKNHINNELE 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 524 SRTHIDTSTELR-YSVGSLVDSQSDY-RTTKVIRRPRRGRMGVRRDEPKVKSLGDHEWNRTQQIGVLGSHPFESDTEMSD 601
Cdd:TIGR00606 616 SKEEQLSSYEDKlFDVCGSQDEESDLeRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQE 695
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907075611 602 IDDDdretiFSSMDLLSPSGHSDAQTLAMMLQEQLDAINKEIRLIQEEKESTELRAEEIENRVASVSLE 670
Cdd:TIGR00606 696 FISD-----LQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRD 759
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
1009-1064 |
2.49e-03 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 37.63 E-value: 2.49e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907075611 1009 EWLPSLGLPQYRSYFMECLVD-ARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1064
Cdd:pfam07647 11 DWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLK-RLGITSVGHRRKILKKIQELK 66
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
354-467 |
2.51e-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: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 354 LRQMEEKNRQLQ-ERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQ 432
Cdd:COG0542 413 LDELERRLEQLEiEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEK 492
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907075611 433 R----EKMNEEHNKRLSDTVD-----------------RLLTESNERLqLHLKERM 467
Cdd:COG0542 493 ElaelEEELAELAPLLREEVTeediaevvsrwtgipvgKLLEGEREKL-LNLEEEL 547
|
|
| pepcterm_ChnLen |
TIGR03007 |
polysaccharide chain length determinant protein, PEP-CTERM locus subfamily; Members of this ... |
221-394 |
2.53e-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: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 221 EAGQKVHEKRLSNG---SIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLI-----KTEE 292
Cdd:TIGR03007 179 AAENRLKAFKQENGgilPDQEGDYYSEISEAQEELEAARLELNEAIAQRDALKRQLGGEEPVLLAGSSVANseldgRIEA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 293 MNTKYQrDIRECYLQAMAQKEDMEERITTLEKRYLSA-------QRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQ 365
Cdd:TIGR03007 259 LEKQLD-ALRLRYTDKHPDVIATKREIAQLEEQKEEEgsaknggPERGEIANPVYQQLQIELAEAEAEIASLEARVAELT 337
|
170 180
....*....|....*....|....*....
gi 1907075611 366 ERLElaeqklqQTMRKAETLPEVEAELAQ 394
Cdd:TIGR03007 338 ARIE-------RLESLLRTIPEVEAELTQ 359
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
249-431 |
2.59e-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: 40.89 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 249 QELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLikteEMNTKYQRDIRECylqamaqkEDMEERITTLEKRYLS 328
Cdd:cd00176 64 EQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRL----EEALDLQQFFRDA--------DDLEQWLEEKEAALAS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 329 aqrestsihdmnDKLENELANKEAILRQMEEknrqLQERLELAEQKLQQTMRKAETLPEveaelAQRIAALTKAEERHGN 408
Cdd:cd00176 132 ------------EDLGKDLESVEELLKKHKE----LEEELEAHEPRLKSLNELAEELLE-----EGHPDADEEIEEKLEE 190
|
170 180
....*....|....*....|...
gi 1907075611 409 IEERMRHLEGQLEEKNQELQRAR 431
Cdd:cd00176 191 LNERWEELLELAEERQKKLEEAL 213
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
362-502 |
2.67e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 40.64 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 362 RQLQERLELAEQKLQQTMRKAETLP----------------EVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ 425
Cdd:pfam12072 27 AKIGSAEELAKRIIEEAKKEAETKKkealleakeeihklraEAERELKERRNELQRQERRLLQKEETLDRKDESLEKKEE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 426 ELQRARQREKMNEEHNKRLSDTVDRLLTESNERLqlhlkERMAAL---EEKNVLIQESEnfrknlEESLHDKERLAEEIE 502
Cdd:pfam12072 107 SLEKKEKELEAQQQQLEEKEEELEELIEEQRQEL-----ERISGLtseEAKEILLDEVE------EELRHEAAVMIKEIE 175
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
346-658 |
2.70e-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: 42.03 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 346 ELANKEAILRQMEEKNRQLQERLELAEQklqQTMRKAETlpeveaelaQRIAALTKAEERHGniEERMRHLEG-QLEEKN 424
Cdd:pfam17380 294 EKMEQERLRQEKEEKAREVERRRKLEEA---EKARQAEM---------DRQAAIYAEQERMA--MERERELERiRQEERK 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 425 QELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHL----------KERMAALEEKNVLIQ----ESENFRKNL--- 487
Cdd:pfam17380 360 RELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELeaarkvkileEERQRKIQQQKVEMEqiraEQEEARQREvrr 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 488 --EESLHDKERLAEE-------IEKLRSELDQMKMRTGSLIEPTISRTHIDtstELRYSVgslVDSQSDYRTTKVIRRPR 558
Cdd:pfam17380 440 leEERAREMERVRLEeqerqqqVERLRQQEEERKRKKLELEKEKRDRKRAE---EQRRKI---LEKELEERKQAMIEEER 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 559 RGRMGVRRDEPKVKSLGDHEWNRTQQigvlgshpfesDTEMSDIDDDDRETIFSSMDLLSPSghsdaqtlammlQEQLDA 638
Cdd:pfam17380 514 KRKLLEKEMEERQKAIYEEERRREAE-----------EERRKQQEMEERRRIQEQMRKATEE------------RSRLEA 570
|
330 340
....*....|....*....|
gi 1907075611 639 INKEIRLIQEEKESTELRAE 658
Cdd:pfam17380 571 MEREREMMRQIVESEKARAE 590
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
293-512 |
2.84e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.98 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 293 MNTKYQRDIrecyLQAMAQKEDMEERITTLEKRYLSAQREstsihdmndkLENELANKEAILRQMEEKNRQLQErleLAE 372
Cdd:COG0497 138 LDPDAQREL----LDAFAGLEELLEEYREAYRAWRALKKE----------LEELRADEAERARELDLLRFQLEE---LEA 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 373 QKLQqtmrkaetlPEVEAELAQRIAALTKAEERHGNIEERMRHLEGqlEEKN--QELQRARQR-EKMnEEHNKRLSDTVD 449
Cdd:COG0497 201 AALQ---------PGEEEELEEERRRLSNAEKLREALQEALEALSG--GEGGalDLLGQALRAlERL-AEYDPSLAELAE 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 450 RL------LTESNERLQLHLK------ERMAALEEK-----------NVLIQESENFRKNLEESLHDKERLAEEIEKLRS 506
Cdd:COG0497 269 RLesalieLEEAASELRRYLDslefdpERLEEVEERlallrrlarkyGVTVEELLAYAEELRAELAELENSDERLEELEA 348
|
....*.
gi 1907075611 507 ELDQMK 512
Cdd:COG0497 349 ELAEAE 354
|
|
| BAR_SNX7 |
cd07666 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 7; BAR domains are dimerization, lipid ... |
252-447 |
2.88e-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: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 252 LEKQNYEMAQMKERLTALSSRVGE-VEQEAETARKDLIKTEEMNtkyqrDIREcYLQAMAQK----EDMEERITTLEKRY 326
Cdd:cd07666 14 LTAQAWELSSHKKQGPGLLSRMGQtVKAVASSVRGVKNRPEEFT-----EMNE-YVEAFSQKinvlDKISQRIYKEQREY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 327 LSAQRESTSIHDMNDKLENELANK--------EAILRQMEEKNRQLQERLE-------LAEQKLQQTMRKAEtlpEVEAE 391
Cdd:cd07666 88 FEELKEYGPIYTLWSASEEELADSlkgmasciDRCCKATDKRMKGLSEQLLpviheyvLYSETLMGVIKRRD---QIQAE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907075611 392 LAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDT 447
Cdd:cd07666 165 LDSKVEALANKKADRDLLKEEIEKLEDKVECANNALKADWERWKQNMQTDLRSAFT 220
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
208-505 |
3.09e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 208 SEGSTESEHLEGMEAGqKVHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKErltalSSRVGEVEQEAETARKDL 287
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETG-KAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAE-----DAKRVEIARKAEDARKAE 1167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 288 IKTEEMNTKYQRDIRecylQAMAQKEDMEERITTlEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQER 367
Cdd:PTZ00121 1168 EARKAEDAKKAEAAR----KAEEVRKAEELRKAE-DARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEA 1242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 368 LELAEQKLQQTMRKAETL---------PEVEAELAQRIAALTKAEERHGNIE----ERMRHLEgQLEEKNQELQRARQRE 434
Cdd:PTZ00121 1243 KKAEEERNNEEIRKFEEArmahfarrqAAIKAEEARKADELKKAEEKKKADEakkaEEKKKAD-EAKKKAEEAKKADEAK 1321
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907075611 435 KMNEEHNKRlSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIEKLR 505
Cdd:PTZ00121 1322 KKAEEAKKK-ADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK 1391
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
45-511 |
3.80e-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: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 45 LLDTLRETQESLSLAQQRLQDVIYDRDSLQRQL------NSALPQDIESLTGgltgSKGADPPEFAALTKELNACREQL- 117
Cdd:pfam01576 234 LRAQLAKKEEELQAALARLEEETAQKNNALKKIreleaqISELQEDLESERA----ARNKAEKQRRDLGEELEALKTELe 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 118 --LEKEEEISELKAERNNTRLLLEH-LECLVSRHERSLRmTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKAldekivAL 194
Cdd:pfam01576 310 dtLDTTAAQQELRSKREQEVTELKKaLEEETRSHEAQLQ-EMRQKHTQALEELTEQLEQAKRNKANLEKAKQ------AL 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 195 REQNVHIQRKMVS-SEGSTESEHlegmeaGQKVHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEmaqmkerLTALSSRV 273
Cdd:pfam01576 383 ESENAELQAELRTlQQAKQDSEH------KRKKLEGQLQELQARLSESERQRAELAEKLSKLQSE-------LESVSSLL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 274 GEVEQEAETARKDLIKTEEmntkYQRDIRECYLQAMAQKEDMEERITTLEKrylsaqrESTSIHDMndkLENELANKEAI 353
Cdd:pfam01576 450 NEAEGKNIKLSKDVSSLES----QLQDTQELLQEETRQKLNLSTRLRQLED-------ERNSLQEQ---LEEEEEAKRNV 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 354 LRQMEEKNRQLQErlelAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERM----RHLEGQLEEKNQELQR 429
Cdd:pfam01576 516 ERQLSTLQAQLSD----MKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLektkNRLQQELDDLLVDLDH 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 430 ARQREKMNEEHNKRLsdtvDRLLTESNERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELD 509
Cdd:pfam01576 592 QRQLVSNLEKKQKKF----DQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEME 667
|
..
gi 1907075611 510 QM 511
Cdd:pfam01576 668 DL 669
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
185-535 |
3.88e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 185 KALDEKIVALREQNVHIQRKmvSSEGSTESEHLEGMEAGQKVHEKRLsngsidstDDTSQIVELQELLEkqnyEMAQMKE 264
Cdd:COG4717 74 KELEEELKEAEEKEEEYAEL--QEELEELEEELEELEAELEELREEL--------EKLEKLLQLLPLYQ----ELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 265 RLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLE 344
Cdd:COG4717 140 ELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 345 NELANKEAILRQMEEKNRQLQERLELAEQK-----------LQQTMRKAETLPEVEAELAQRIAAL--------TKAEER 405
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEERLKEARlllliaaallaLLGLGGSLLSLILTIAGVLFLVLGLlallflllAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 406 HGNIEERMRHLEGQLEEKNQELQRARQREKMNEEhnkrLSDTVDRLLTESNERLQLHLKERMAALEEknVLIQESENFRK 485
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPD----LSPEELLELLDRIEELQELLREAEELEEE--LQLEELEQEIA 373
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907075611 486 NL--------EESLHDKERLAEEIEKLRSELDQMKMRTGSLIEPTISRTHIDTSTELR 535
Cdd:COG4717 374 ALlaeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE 431
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
247-444 |
3.89e-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: 41.18 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 247 ELQELLEKQNYEMAQMKERLTALSSRvgEVEQEAETARKDLIKTEEmntKYQRDIREcylQAMAQKEDMEERITTLEKRY 326
Cdd:pfam15558 35 EELRRRDQKRQETLERERRLLLQQSQ--EQWQAEKEQRKARLGREE---RRRADRRE---KQVIEKESRWREQAEDQENQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 327 LSAQRESTSIHDMNDKLENE--LANKEAILRQMEEKNR-QLQERLELAEQKLQQ--------------------TMRKAE 383
Cdd:pfam15558 107 RQEKLERARQEAEQRKQCQEqrLKEKEEELQALREQNSlQLQERLEEACHKRQLkereeqkkvqennlsellnhQARKVL 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907075611 384 TLPEVEAELAQRIAAL----TKAEERH-GNIEERMRHLEGQLEEKNQELQRARQR-EKMNEEHNKRL 444
Cdd:pfam15558 187 VDCQAKAEELLRRLSLeqslQRSQENYeQLVEERHRELREKAQKEEEQFQRAKWRaEEKEEERQEHK 253
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
329-506 |
4.70e-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: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 329 AQRESTSIHDMNDKLENELAnkEAILRQMEEKNRQLQERLELAEQKLQQTMRKaetlpEVEAELAQRIAALTKaeerhgn 408
Cdd:pfam09731 314 IERALEKQKEELDKLAEELS--ARLEEVRAADEAQLRLEFEREREEIRESYEE-----KLRTELERQAEAHEE------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 409 ieermrHLEGQLEEKNQELQRARQR---EKMNEEHNKRLSDtVDRLLTESNERLQLhLKERMAALEEKN---VLIQESEN 482
Cdd:pfam09731 380 ------HLKDVLVEQEIELQREFLQdikEKVEEERAGRLLK-LNELLANLKGLEKA-TSSHSEVEDENRkaqQLWLAVEA 451
|
170 180
....*....|....*....|....*.
gi 1907075611 483 FRKNLEESLHDKER--LAEEIEKLRS 506
Cdd:pfam09731 452 LRSTLEDGSADSRPrpLVRELKALKE 477
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
234-421 |
4.71e-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: 40.43 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 234 GSIDSTDDTSQIVELQELLEKQNYEMAQM---------KERLTALSSRVGEVEQEAETARKDLikteemnTKYQRDIrec 304
Cdd:cd22656 82 AQNAGGTIDSYYAEILELIDDLADATDDEeleeakktiKALLDDLLKEAKKYQDKAAKVVDKL-------TDFENQT--- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 305 ylqaMAQKEDMEERITTLEKRYlsaQRESTSIHDMN-DKLENELAN-KEAILRQMEEKNRQLQERLELAEQKLQQTMRKA 382
Cdd:cd22656 152 ----EKDQTALETLEKALKDLL---TDEGGAIARKEiKDLQKELEKlNEEYAAKLKAKIDELKALIADDEAKLAAALRLI 224
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907075611 383 ETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLE 421
Cdd:cd22656 225 ADLTAADTDLDNLLALIGPAIPALEKLQGAWQAIATDLD 263
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
104-444 |
5.08e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 104 AALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHerslrmtvvkrqaqspSGVSSEVEVLKALKSLFEH 183
Cdd:PRK04863 782 AAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSH----------------LAVAFEADPEAELRQLNRR 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 184 HKALDEKIVALREQNVHIQRKMVSSEgstesehlEGMEAGQKVhekrlsNGSIDSTDDTSQIVELQELLEkQNYEMAQMK 263
Cdd:PRK04863 846 RVELERALADHESQEQQQRSQLEQAK--------EGLSALNRL------LPRLNLLADETLADRVEEIRE-QLDEAEEAK 910
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 264 ERLTALSSRVGEVEQEAETARKDliktEEMNTKYQRDirecYLQAMAQKEDMEERITTL----EKR----YLSAQRESTS 335
Cdd:PRK04863 911 RFVQQHGNALAQLEPIVSVLQSD----PEQFEQLKQD----YQQAQQTQRDAKQQAFALtevvQRRahfsYEDAAEMLAK 982
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 336 IHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALT---------KAEERH 406
Cdd:PRK04863 983 NSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGvpadsgaeeRARARR 1062
|
330 340 350
....*....|....*....|....*....|....*....
gi 1907075611 407 GNIEERMRHLEGQleeKNQ-ELQRARQREKMNEEhNKRL 444
Cdd:PRK04863 1063 DELHARLSANRSR---RNQlEKQLTFCEAEMDNL-TKKL 1097
|
|
| SAM_superfamily |
cd09487 |
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
885-942 |
5.38e-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: 5.38e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907075611 885 VVAWLElWLGMPaWYVAACRANVKSGAIMSALSDTEIQrEIGISNPLHRLKLRLAIQE 942
Cdd:cd09487 2 VAEWLE-SLGLE-QYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAIQR 56
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
346-514 |
7.34e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.46 E-value: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 346 ELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ 425
Cdd:PRK12705 40 QEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSAREL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 426 EL--QRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESENfRKNLEESLhdkERLAEEIEK 503
Cdd:PRK12705 120 ELeeLEKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKA-QNILAQAM---QRIASETAS 195
|
170
....*....|....*..
gi 1907075611 504 LRS------ELDQMKMR 514
Cdd:PRK12705 196 DLSvsvvpiPSDAMKGR 212
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
310-431 |
7.35e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.95 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 310 AQKEDMEERITTLEKRYLSAQREstsihdmNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVE 389
Cdd:PRK09039 74 QGNQDLQDSVANLRASLSAAEAE-------RSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQI 146
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1907075611 390 AELAQRIAAL--------TKAEERHGNIEERMRHLEGQLEEKNQELQRAR 431
Cdd:PRK09039 147 AALRRQLAALeaaldaseKRDRESQAKIADLGRRLNVALAQRVQELNRYR 196
|
|
| SAM_SARM1-like_repeat1 |
cd09501 |
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
1009-1053 |
8.07e-03 |
|
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of SARM1-like adaptor proteins is a protein-protein interaction domain. SARM1-like proteins contain two tandem SAM domains. SARM1-like proteins are involved in TLR (Toll-like receptor) signaling. They are responsible for targeted localization of the whole protein to post-synaptic regions of axons. In humans SARM1 expression is detected in kidney and liver.
Pssm-ID: 188900 [Multi-domain] Cd Length: 69 Bit Score: 36.13 E-value: 8.07e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1907075611 1009 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHR 1053
Cdd:cd09501 11 TWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLR 55
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
243-399 |
8.28e-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: 8.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 243 SQIVELQELLEKQNYEMA-------QMKERLTALSSRVGEVEQEAETARKDliKTEEMNTKYQRDIRECYLQAMA-QKED 314
Cdd:pfam13851 33 EEIAELKKKEERNEKLMSeiqqenkRLTEPLQKAQEEVEELRKQLENYEKD--KQSLKNLKARLKVLEKELKDLKwEHEV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 315 MEERITTLEKRY--LSAQREStSIHDMNDKLENE---LANK-EAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEV 388
Cdd:pfam13851 111 LEQRFEKVERERdeLYDKFEA-AIQDVQQKTGLKnllLEKKlQALGETLEKKEAQLNEVLAAANLDPDALQAVTEKLEDV 189
|
170
....*....|.
gi 1907075611 389 EAELAQRIAAL 399
Cdd:pfam13851 190 LESKNQLIKDL 200
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
221-410 |
9.73e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 9.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 221 EAGQKVHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEE-----MNT 295
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREelgerARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075611 296 KYQRDIRECYL-------------------------------QAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLE 344
Cdd:COG3883 95 LYRSGGSVSYLdvllgsesfsdfldrlsalskiadadadlleELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907075611 345 NELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIE 410
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| |
