|
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 ... |
1004-1075 |
1.60e-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: 154.78 E-value: 1.60e-44
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907075644 1004 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1075
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 ... |
795-865 |
4.20e-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: 4.20e-44
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907075644 795 FAQWDGPTVVAWLELWLGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 865
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 ... |
919-984 |
1.13e-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: 1.13e-43
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907075644 919 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 984
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 ... |
923-982 |
2.06e-31 |
|
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and in adheren junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188894 Cd Length: 60 Bit Score: 117.25 E-value: 2.06e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 923 WIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 982
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 ... |
802-860 |
2.89e-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: 2.89e-27
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907075644 802 TVVAWLELWLGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 860
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 ... |
1012-1073 |
5.25e-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: 5.25e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907075644 1012 RVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNN 1073
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 ... |
1004-1075 |
1.24e-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: 1.24e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907075644 1004 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1075
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 ... |
796-860 |
3.40e-17 |
|
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrin contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved into interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188963 Cd Length: 70 Bit Score: 77.11 E-value: 3.40e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907075644 796 AQWDGPTVVAWLELWLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 860
Cdd:cd09564 2 SRWKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
|
|
| SAM_liprin-beta1,2_repeat2 |
cd09566 |
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ... |
918-982 |
1.40e-16 |
|
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta potentially is able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.
Pssm-ID: 188965 Cd Length: 63 Bit Score: 75.04 E-value: 1.40e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907075644 918 DMNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLrVHLKMVDSFHRTSLQYGIMCLK 982
Cdd:cd09566 1 KLDTHWV-LRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDL-LHLKVTSALHHASIRRGIQVLR 63
|
|
| SAM_kazrin_repeat2 |
cd09567 |
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ... |
918-982 |
1.48e-16 |
|
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188966 Cd Length: 65 Bit Score: 75.14 E-value: 1.48e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907075644 918 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 982
Cdd:cd09567 1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
184-432 |
2.34e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.60 E-value: 2.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 184 EMAQMKERLTALSSRVGEVEQ-------EAETARK-DLIKTEEMntkyQRDIREAMAQKEDMEERITTLEKRYLSAQRES 255
Cdd:COG1196 180 KLEATEENLERLEDILGELERqleplerQAEKAERyRELKEELK----ELEAELLLLKLRELEAELEELEAELEELEAEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 256 TSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQT----MRKAETLPEVEAELAQRIAALTKAEERHGNI 331
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLeqdiARLEERRRELEERLEELEEELAELEEELEEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 332 EERMRHLEGQLEEKNQELQRARQREkmnEEHNKRLSDTVDRLLTESNERLQLhLKERMAALEEKNVLIQESENFRKNLEE 411
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAEL---AEAEEALLEAEAELAEAEEELEEL-AEELLEALRAAAELAAQLEELEEAEEA 411
|
250 260
....*....|....*....|.
gi 1907075644 412 SLHDKERLAEEIEKLRSELDQ 432
Cdd:COG1196 412 LLERLERLEEELEELEEALAE 432
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
27-382 |
4.00e-16 |
|
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: 83.95 E-value: 4.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 27 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERS---LRMTVVKRQAQSPSGVSSEVEVLKAL 103
Cdd:TIGR02168 691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEveqLEERIAQLSKELTELEAEIEELEERL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 104 KSLFEHHKALDEKIVALREQnvhIQRkmVSSEGSTESEHLEGMEAGQKVHEKRLSNGSIDSTDDTSQIVELQELLEKQNY 183
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQ---IEQ--LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 184 EMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMND 263
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 264 KLENELAnkeailrQMEEKNRQLQERL-ELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNI----------- 331
Cdd:TIGR02168 926 QLELRLE-------GLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVnlaaieeyeel 998
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907075644 332 EERMRHLEGQLEeknqELQRARQR-----EKMNEEHNKRLSDTVDRLltesNERLQ 382
Cdd:TIGR02168 999 KERYDFLTAQKE----DLTEAKETleeaiEEIDREARERFKDTFDQV----NENFQ 1046
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
140-433 |
1.05e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 82.68 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 140 SEHLEGMEAGQKVHEKRLSNGSIDSTDDtsQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEM 219
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEA--ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 220 NTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQ 299
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 300 TMRkaetlpEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKnQELQRARQREKMNEEHNKRLSDTVDRLLTESNE 379
Cdd:COG1196 377 AEE------ELEELAEELLEALRAAAELAAQLEELEEAEEALLERL-ERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1907075644 380 RLQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQM 433
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| SAM_liprin-beta1,2_repeat3 |
cd09569 |
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ... |
1004-1075 |
1.87e-15 |
|
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.
Pssm-ID: 188968 Cd Length: 72 Bit Score: 72.10 E-value: 1.87e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907075644 1004 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1075
Cdd:cd09569 1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
148-436 |
2.63e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 81.26 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 148 AGQKVHEKRLSNGSIDSTDdtSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDI 227
Cdd:TIGR02168 651 DGDLVRPGGVITGGSAKTN--SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 228 REAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTmrkAETL 307
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL---REAL 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 308 PEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRAR-QREKMNEEHNKrlsdtVDRLLTESNERLQLHLK 386
Cdd:TIGR02168 806 DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSeDIESLAAEIEE-----LEELIEELESELEALLN 880
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1907075644 387 ERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQMKMR 436
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELR 930
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
195-442 |
3.60e-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: 80.87 E-value: 3.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 195 LSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEA 274
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 275 ILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpevEAELAQRIAALTKAEERH-------GNIEERMRHLEGQLEEKNQ 347
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQL---KEELKALREALDELRAELtllneeaANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 348 ELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLHLKER-------MAALEEKNVLIQESENFRKNLEESLHDKE 417
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEIEELeelIEELESELEALLNERasleealALLRSELEELSEELRELESKRSELRRELE 918
|
250 260
....*....|....*....|....*
gi 1907075644 418 RLAEEIEKLRSELDQMKMRTGSLIE 442
Cdd:TIGR02168 919 ELREKLAQLELRLEGLEVRIDNLQE 943
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
34-433 |
2.03e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 78.56 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 34 KELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSrherslrmTVVKRQAQSPSGVSSEVEVLKALKslfehhkal 113
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELE--------QLRKELEELSRQISALRKDLARLE--------- 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 114 dEKIVALREQNVHIQRKMVSSEGSTESEHLEGMEAGQKVHEKRlsngsidstddtSQIVELQELLEKQNYEMAQMKERLT 193
Cdd:TIGR02168 740 -AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE------------AEIEELEAQIEQLKEELKALREALD 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 194 ALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQREStsihdmnDKLENELANKE 273
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI-------EELESELEALL 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 274 AILRQMEEKNRQLQERLELAEQKLQqtmrkaetlpEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKnqeLQRAR 353
Cdd:TIGR02168 880 NERASLEEALALLRSELEELSEELR----------ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL---QERLS 946
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 354 QREKMNEEHNKRLSDTVDRLLTESNERLQLhLKERMAALEEKNVL-IQESENFRKNLEESLHDKERLAEEIEKLRSELDQ 432
Cdd:TIGR02168 947 EEYSLTLEEAEALENKIEDDEEEARRRLKR-LENKIKELGPVNLAaIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEE 1025
|
.
gi 1907075644 433 M 433
Cdd:TIGR02168 1026 I 1026
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
918-982 |
5.31e-14 |
|
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.
Pssm-ID: 425739 Cd Length: 64 Bit Score: 67.68 E-value: 5.31e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907075644 918 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 982
Cdd:pfam00536 1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
40-395 |
3.78e-13 |
|
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: 74.33 E-value: 3.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 40 REQLLEKEEEISELKAERNNTRLLLEHLECLVsrHERSLRMTVVKRQAqspsgvsseVEVLKALKSLFEHHKALDEKIVA 119
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRL--DELSQELSDASRKI---------GEIEKEIEQLEQEEEKLKERLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 120 LREQNVHIQRKM--VSSEGSTESEHLEGMEAgqKVHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSS 197
Cdd:TIGR02169 742 LEEDLSSLEQEIenVKSELKELEARIEELEE--DLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 198 RVGEVEQEAETARKdlikteEMNTKyQRDIREAMAQKEDMEERITTLEKRYLSAQRE----STSIHDMNDKLEN---ELA 270
Cdd:TIGR02169 820 KLNRLTLEKEYLEK------EIQEL-QEQRIDLKEQIKSIEKEIENLNGKKEELEEEleelEAALRDLESRLGDlkkERD 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 271 NKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAA----------LTKAEERHGNIEERMRHLEG 340
Cdd:TIGR02169 893 ELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeeelsLEDVQAELQRVEEEIRALEP 972
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1907075644 341 QLEEKNQELqrarqrekmnEEHNKRLSDTVDRLLTESNERLQlhLKERMAALEEK 395
Cdd:TIGR02169 973 VNMLAIQEY----------EEVLKRLDELKEKRAKLEEERKA--ILERIEEYEKK 1015
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
170-440 |
4.13e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 74.32 E-value: 4.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 170 QIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYL 249
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 250 SAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQqtmrkaetlpEVEAELAQRIAALTKAEERHG 329
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE----------ELEAELEELESRLEELEEQLE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 330 NIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALE-EKNVLIQESENFRKN 408
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEeELEELQEELERLEEA 462
|
250 260 270
....*....|....*....|....*....|..
gi 1907075644 409 LEESLHDKERLAEEIEKLRSELDQMKMRTGSL 440
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQARLDSL 494
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
221-432 |
4.53e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.82 E-value: 4.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 221 TKYQRDIREAMAQKEDMEERIT-------TLEKRY--LSAQRESTSIHdmnDKLENELANKEAILRQMEEknRQLQERLE 291
Cdd:COG1196 168 SKYKERKEEAERKLEATEENLErledilgELERQLepLERQAEKAERY---RELKEELKELEAELLLLKL--RELEAELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 292 LAEQKLQQTMRKAETLpevEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVD 371
Cdd:COG1196 243 ELEAELEELEAELEEL---EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907075644 372 RLLTEsNERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQ 432
Cdd:COG1196 320 ELEEE-LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
103-384 |
6.58e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.55 E-value: 6.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 103 LKSLFEHHKALDEKIVALREQNVHIQRKMVSSEGS---TESEHLEgMEAGQKVHEKRLSNGSIDSTDDTSQIVELQE--- 176
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKleeLRLEVSE-LEEEIEELQKELYALANEISRLEQQKQILRErla 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 177 ----LLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQ 252
Cdd:TIGR02168 313 nlerQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 253 RESTSIhdmndklENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKA--ETLPEVEAELAQRIAALTKAEERHGN 330
Cdd:TIGR02168 393 LQIASL-------NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqAELEELEEELEELQEELERLEEALEE 465
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1907075644 331 IEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLH 384
Cdd:TIGR02168 466 LREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
154-433 |
1.01e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 72.79 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 154 EKRLSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQ 233
Cdd:TIGR02169 701 ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEA 780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 234 KEDMEERIttlekrylsAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAE 313
Cdd:TIGR02169 781 LNDLEARL---------SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKS 851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 314 LAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARqrekmnEEHNKRLSDTVDRL--LTESNERLQLHLKERMAA 391
Cdd:TIGR02169 852 IEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER------DELEAQLRELERKIeeLEAQIEKKRKRLSELKAK 925
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1907075644 392 LEEKNVLIQESENFRKNLEES---LHDKERLAEEIEKLRSELDQM 433
Cdd:TIGR02169 926 LEALEEELSEIEDPKGEDEEIpeeELSLEDVQAELQRVEEEIRAL 970
|
|
| SAM_liprin-beta1,2_repeat1 |
cd09563 |
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
795-859 |
1.17e-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: 1.17e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907075644 795 FAQWDGPTVVAWL-ELWLGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQ 859
Cdd:cd09563 1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
156-440 |
1.47e-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: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 156 RLSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKdliKTEEMntkyQRDIREAMAQKE 235
Cdd:TIGR02169 661 APRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASR---KIGEI----EKEIEQLEQEEE 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 236 DMEERITTLEKRYLSAQRESTSIHDMNDKLENELAnkeailrQMEEKNRQLQERLELAEQKLQQtmrkaETLPEVEAEla 315
Cdd:TIGR02169 734 KLKERLEELEEDLSSLEQEIENVKSELKELEARIE-------ELEEDLHKLEEALNDLEARLSH-----SRIPEIQAE-- 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 316 qriaaLTKAEERHGNIEERMRHLEGQLEEKNQELQRArqREKMNEEHNKRlsdtvdRLLTESNERLQLHLKERMAALEEK 395
Cdd:TIGR02169 800 -----LSKLEEEVSRIEARLREIEQKLNRLTLEKEYL--EKEIQELQEQR------IDLKEQIKSIEKEIENLNGKKEEL 866
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1907075644 396 NVLIQESENFRKNLEESLHDkerLAEEIEKLRSELDQMKMRTGSL 440
Cdd:TIGR02169 867 EEELEELEAALRDLESRLGD---LKKERDELEAQLRELERKIEEL 908
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
28-440 |
1.60e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.99 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 28 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLrmtvvkrqaqspsgvsSEVEVLKALKSLF 107
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERR----------------EELETLEAEIEDL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 108 EHHKALDEKIVALREQNVHIQRKMVSSEGSTESEHLEGMEagqkvhekrLSNGSIDSTDD-----TSQIVELQELLEKQN 182
Cdd:PRK02224 264 RETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG---------LDDADAEAVEArreelEDRDEELRDRLEECR 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 183 YEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMN 262
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 263 DKLENELANKEAILRQMEEKNRQLQERLELAEQklqqtMRKAETLPEVEAEL--AQRIAALTKAEERHGNIEERMRHLEG 340
Cdd:PRK02224 415 EELREERDELREREAELEATLRTARERVEEAEA-----LLEAGKCPECGQPVegSPHVETIEEDRERVEELEAELEDLEE 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 341 QLEEKNQELQRARQREKMNEEHNKRLS--DTVDRLLTESNERLQlHLKERMAAL-EEKNVLIQESENFRKNLEESLHDKE 417
Cdd:PRK02224 490 EVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIE-EKRERAEELrERAAELEAEAEEKREAAAEAEEEAE 568
|
410 420
....*....|....*....|...
gi 1907075644 418 RLAEEIEKLRSELDQMKMRTGSL 440
Cdd:PRK02224 569 EAREEVAELNSKLAELKERIESL 591
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
25-440 |
6.08e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.07 E-value: 6.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 25 TFQEFAALTKELNACREQLLEKEEEISELKAERNNTRL----LLEHLECLVSRHERSLRMTVVKRQAQSpsgvssevEVL 100
Cdd:PRK02224 270 TEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDAdaeaVEARREELEDRDEELRDRLEECRVAAQ--------AHN 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 101 KALKSLFEHHKALDEKIVALREQNVHIQRKMVSSEG--STESEHLEGMEAGQKVHEKRLSNGSIDstddtsqivelqelL 178
Cdd:PRK02224 342 EEAESLREDADDLEERAEELREEAAELESELEEAREavEDRREEIEELEEEIEELRERFGDAPVD--------------L 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 179 EKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQ-----RDIREA--MAQKEDMEERITTLEKRYLSA 251
Cdd:PRK02224 408 GNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgQPVEGSphVETIEEDRERVEELEAELEDL 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 252 QRESTSIHDMNDKLEnELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETL----PEVEAELAQRIAALTKAEER 327
Cdd:PRK02224 488 EEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELreraAELEAEAEEKREAAAEAEEE 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 328 HGNIEERMRHLEGQLEEKNQELQR-ARQREKMNEEHNKRlsDTVDRLL----------TESNERLQlHLKERMAALEEK- 395
Cdd:PRK02224 567 AEEAREEVAELNSKLAELKERIESlERIRTLLAAIADAE--DEIERLRekrealaelnDERRERLA-EKRERKRELEAEf 643
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1907075644 396 -NVLIQESENFRKNLEESLhdkERLAEEIEKLRSELDQMKMRTGSL 440
Cdd:PRK02224 644 dEARIEEAREDKERAEEYL---EQVEEKLDELREERDDLQAEIGAV 686
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
168-426 |
9.04e-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: 69.70 E-value: 9.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 168 TSQIVELQELLEKQNYEMAQMKERLT-------ALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEER 240
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEelqkelyALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 241 ITTLEKRYLSAQRESTSihdmndkLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpevEAELAQRIAA 320
Cdd:TIGR02168 339 LAELEEKLEELKEELES-------LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL---NNEIERLEAR 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 321 LTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNkrlsdtvdrlLTESNERLQLHLKERMAALEEKNVLIQ 400
Cdd:TIGR02168 409 LERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEE----------LQEELERLEEALEELREELEEAEQALD 478
|
250 260
....*....|....*....|....*.
gi 1907075644 401 ESENFRKNLEESLHDKERLAEEIEKL 426
Cdd:TIGR02168 479 AAERELAQLQARLDSLERLQENLEGF 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
25-328 |
2.44e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.54 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 25 TFQEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLEclvsrherslrmtvvkrqaqspsgvsSEVEVLKALK 104
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ--------------------------KELYALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 105 SLFEHHKaldeKIVALREQNVHIQRKMVSSEGSTESEHLEgmEAGQKVHEKRlsngsidstddtSQIVELQELLEKQNYE 184
Cdd:TIGR02168 298 SRLEQQK----QILRERLANLERQLEELEAQLEELESKLD--ELAEELAELE------------EKLEELKEELESLEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 185 MAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRyLSAQRESTSIHDMnDK 264
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE-IEELLKKLEEAEL-KE 437
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907075644 265 LENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERH 328
Cdd:TIGR02168 438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENL 501
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
35-361 |
6.53e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 6.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 35 ELNACREQLLEKEEEISELKAERNNTRLLLEHLEclvsrherslrmtvvkrqaqspsgvsSEVEVLKalkslfEHHKALD 114
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELE--------------------------AELEELR------LELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 115 EKIVALREQNVHIQRKmvssegstesehLEGMEAGQKVHEKRLSngsidstDDTSQIVELQELLEKQNYEMAQMKERLTA 194
Cdd:COG1196 281 LELEEAQAEEYELLAE------------LARLEQDIARLEERRR-------ELEERLEELEEELAELEEELEELEEELEE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 195 LSSRVGEVEQEAETARKDLIKTEEmntkyqrdirEAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEA 274
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEE----------ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 275 ILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQ 354
Cdd:COG1196 412 LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491
|
....*..
gi 1907075644 355 REKMNEE 361
Cdd:COG1196 492 RLLLLLE 498
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
169-431 |
3.12e-10 |
|
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: 63.55 E-value: 3.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 169 SQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRY 248
Cdd:pfam19220 48 SRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 249 LSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERH 328
Cdd:pfam19220 128 AAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDAT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 329 gniEERMRHLEGQLEEKNQELQRA-RQREKMNEEHNKRLSDTVDRLLTESNerlqlhlkeRMAALEeknVLIQESENFRK 407
Cdd:pfam19220 208 ---RARLRALEGQLAAEQAERERAeAQLEEAVEAHRAERASLRMKLEALTA---------RAAATE---QLLAEARNQLR 272
|
250 260
....*....|....*....|....
gi 1907075644 408 NLEESLHDKERLAEEIEKLRSELD 431
Cdd:pfam19220 273 DRDEAIRAAERRLKEASIERDTLE 296
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
25-432 |
4.18e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.31 E-value: 4.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 25 TFQEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLEclvsrhERSLRMTVVKRQAQspsgvssEVEVLKALK 104
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE------EKVKELKELKEKAE-------EYIKLSEFY 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 105 SLFEHHKALDEKIVA-LREQNVHIQRKMvsSEGSTESEHLEGMEAGQKVHEKRLSNGSIDSTddtsqivELQELLEKQNy 183
Cdd:PRK03918 303 EEYLDELREIEKRLSrLEEEINGIEERI--KELEEKEERLEELKKKLKELEKRLEELEERHE-------LYEEAKAKKE- 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 184 EMAQMKERLTALSsrVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEK---RYLSAQRESTSIHD 260
Cdd:PRK03918 373 ELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgKCPVCGRELTEEHR 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 261 MN--DKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQ-----TMRK-AETLPEVEAELAQ-RIAALTKAEERHGNI 331
Cdd:PRK03918 451 KEllEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKeseliKLKElAEQLKELEEKLKKyNLEELEKKAEEYEKL 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 332 EERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLsDTVDRLLTESNERLQLHLKERMAALEEKnvlIQESENFRK---N 408
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKL-DELEEELAELLKELEELGFESVEELEER---LKELEPFYNeylE 606
|
410 420
....*....|....*....|....
gi 1907075644 409 LEESLHDKERLAEEIEKLRSELDQ 432
Cdd:PRK03918 607 LKDAEKELEREEKELKKLEEELDK 630
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
169-361 |
5.51e-10 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 62.54 E-value: 5.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 169 SQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAmaqKEDMEERITTLEKRY 248
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA---EAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 249 LSAQR------------ESTSIHDMNDKLEN----ELANKEAILRQMEEKNR--QLQERLELAEQKLQQTMRKAET-LPE 309
Cdd:COG3883 93 RALYRsggsvsyldvllGSESFSDFLDRLSAlskiADADADLLEELKADKAEleAKKAELEAKLAELEALKAELEAaKAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1907075644 310 VEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEE 361
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
224-439 |
7.46e-10 |
|
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: 62.09 E-value: 7.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 224 QRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK 303
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 304 AETLpevEAELAQRIAALTK------------------AEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKR 365
Cdd:COG4942 99 LEAQ---KEELAELLRALYRlgrqpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907075644 366 LSDTVDRLLTEsNERLQLHLKERMAALEEKNvliQESENFRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGS 439
Cdd:COG4942 176 LEALLAELEEE-RAALEALKAERQKLLARLE---KELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
27-430 |
1.21e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.77 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 27 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERS-LRMTVVKRQAQSPSGVSSEVEVLKALKS 105
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKeLQAELEELEEELEELQEELERLEEALEE 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 106 LFEHHKALDEKIVALREQNVHIQRKMVSSEgsTESEHLEGMEAGQK--VHEKRLSNGSIDS------------------- 164
Cdd:TIGR02168 466 LREELEEAEQALDAAERELAQLQARLDSLE--RLQENLEGFSEGVKalLKNQSGLSGILGVlselisvdegyeaaieaal 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 165 --------TDDTSQIVELQELLEKQNYEMAQMKE----RLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQR------- 225
Cdd:TIGR02168 544 ggrlqavvVENLNAAKKAIAFLKQNELGRVTFLPldsiKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKalsyllg 623
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 226 ------DIREAMAQ--KEDMEERITTLE-----KRYLSAQRESTSIHDMNDKlENELANKEAILRQMEEKNRQLQERLEL 292
Cdd:TIGR02168 624 gvlvvdDLDNALELakKLRPGYRIVTLDgdlvrPGGVITGGSAKTNSSILER-RREIEELEEKIEELEEKIAELEKALAE 702
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 293 AEQKLQQTMRKAETLPEVEAELAQRIAA----LTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSD 368
Cdd:TIGR02168 703 LRKELEELEEELEQLRKELEELSRQISAlrkdLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA 782
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907075644 369 ---TVDRLLTESNERLQLhLKERMAALEEK----NVLIQESENFRKNLEESLHDKERLAEEIEKLRSEL 430
Cdd:TIGR02168 783 eieELEAQIEQLKEELKA-LREALDELRAEltllNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
40-361 |
1.98e-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: 62.01 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 40 REQLLEKEE-EISELKAERNNTRLLLEHLECLVSRHERSLRmtvvKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEkiv 118
Cdd:TIGR02169 214 QALLKEKREyEGYELLKEKEALERQKEAIERQLASLEEELE----KLTEEISELEKRLEEIEQLLEELNKKIKDLGE--- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 119 alrEQNVHIQRKMVSSEGSTESehlegMEAGQKVHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSR 198
Cdd:TIGR02169 287 ---EEQLRVKEKIGELEAEIAS-----LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 199 VGEVEQEAETARKDLiktEEMNTKYQRDIREAMAQKEDME---ERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAI 275
Cdd:TIGR02169 359 YAELKEELEDLRAEL---EEVDKEFAETRDELKDYREKLEklkREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 276 LRQMEEKNRQLQERLELAEQKLQQTmrkaetlpeveaelaqrIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQR 355
Cdd:TIGR02169 436 INELEEEKEDKALEIKKQEWKLEQL-----------------AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ 498
|
....*.
gi 1907075644 356 EKMNEE 361
Cdd:TIGR02169 499 ARASEE 504
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
192-433 |
2.49e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 192 LTALSSRVGEVEQ--EAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKrYLSAQREstsIHDMNDKLENEL 269
Cdd:PRK03918 127 LNAIYIRQGEIDAilESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEK-FIKRTEN---IEELIKEKEKEL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 270 ANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQ---LEEKN 346
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEieeLEEKV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 347 QELQRARQREKMNEEHNKRLSDTVDRL-----LTESNERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAE 421
Cdd:PRK03918 283 KELKELKEKAEEYIKLSEFYEEYLDELreiekRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHE 362
|
250
....*....|..
gi 1907075644 422 EIEKLRSELDQM 433
Cdd:PRK03918 363 LYEEAKAKKEEL 374
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
166-586 |
2.68e-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: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 166 DDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEemntKYQrdirEAMAQKEDMEERITTLE 245
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE----RYQ----ALLKEKREYEGYELLKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 246 KRYLSAQREstsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAelaqrIAALTKAE 325
Cdd:TIGR02169 232 KEALERQKE---------AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ-----LRVKEKIG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 326 ERHGNIEErmrhLEGQLEEKNQELQRA-RQREKMNEEHNKRLSdtvdrlltesnerlqlhlkermaaleeknvliqESEN 404
Cdd:TIGR02169 298 ELEAEIAS----LERSIAEKERELEDAeERLAKLEAEIDKLLA---------------------------------EIEE 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 405 FRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSLieptisrthidtSTELRYSVGSLVDSQSDYRTTKVIRRPRRGRM 484
Cdd:TIGR02169 341 LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEV------------DKEFAETRDELKDYREKLEKLKREINELKREL 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 485 GVRRDEPKVKS--LGDHEwnrtQQIGVLGSHPFESDTEMSDIDDDDRETIFSSMDLLSPSGHSDAQTLAmmLQEQLDAIN 562
Cdd:TIGR02169 409 DRLQEELQRLSeeLADLN----AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD--LKEEYDRVE 482
|
410 420
....*....|....*....|....
gi 1907075644 563 KEIRLIQEEKESTELRAEEIENRV 586
Cdd:TIGR02169 483 KELSKLQRELAEAEAQARASEERV 506
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
173-411 |
3.32e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 3.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 173 ELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARK---DLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRyl 249
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKevkELEELKEEIEELEKELESLEGSKRKLEEKIRELEER-- 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 250 saqrestsIHDMNDKLEnELANKEAILRQMEEKN---RQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEE 326
Cdd:PRK03918 268 --------IEELKKEIE-ELEEKVKELKELKEKAeeyIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 327 RHGNIEERMRHLE---GQLEEKNQELQRARQREKMNEEHNKRLS----DTVDRLLTESNERLQLHLKERMAALEEKNVLI 399
Cdd:PRK03918 339 RLEELKKKLKELEkrlEELEERHELYEEAKAKKEELERLKKRLTgltpEKLEKELEELEKAKEEIEEEISKITARIGELK 418
|
250
....*....|..
gi 1907075644 400 QESENFRKNLEE 411
Cdd:PRK03918 419 KEIKELKKAIEE 430
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
795-861 |
3.96e-09 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 53.84 E-value: 3.96e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907075644 795 FAQWDGPTVVAWLELwLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 861
Cdd:smart00454 1 VSQWSPESVADWLES-IGLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
45-445 |
5.09e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.93 E-value: 5.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 45 EKEEEISELKAERNNTRLllehlECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKIVALREQN 124
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKA-----DAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAK 1437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 125 VHIQRKMVSSEGSTESEHLEGME-AGQKVHEKRLSNGSIDSTDDTSQIVELQELLE----------------KQNYEMAQ 187
Cdd:PTZ00121 1438 KKAEEAKKADEAKKKAEEAKKAEeAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEeakkkadeakkaaeakKKADEAKK 1517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 188 MKERLTALSSRVGEVEQEAETARK--------DLIKTEEMntKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIH 259
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKADEAKKaeekkkadELKKAEEL--KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIE 1595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 260 DMNDKLENELANKEAILRQMEE---------KNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGN 330
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKAEEakikaeelkKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK 1675
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 331 IEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLltesnERLQLHLKERMAALEEknvLIQESENFRKNLE 410
Cdd:PTZ00121 1676 KAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA-----EELKKAEEENKIKAEE---AKKEAEEDKKKAE 1747
|
410 420 430
....*....|....*....|....*....|....*
gi 1907075644 411 ESLHDKERlAEEIEKLRSELDQMKMRTGSLIEPTI 445
Cdd:PTZ00121 1748 EAKKDEEE-KKKIAHLKKEEEKKAEEIRKEKEAVI 1781
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
32-441 |
6.08e-09 |
|
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: 60.42 E-value: 6.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 32 LTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHeRSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHK 111
Cdd:TIGR04523 171 LENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKN-KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEIS 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 112 ALDEKIVALREQNVHIQRKMV--SSEGSTESEHLEGMEAGQKVHEKRLSNGSIDSTDDTSQivELQELLEKQNYEMAQMK 189
Cdd:TIGR04523 250 NTQTQLNQLKDEQNKIKKQLSekQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNK--ELKSELKNQEKKLEEIQ 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 190 ERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREamaqKEDMEERIttlekrylsaQRESTSIHDMNDKLENEL 269
Cdd:TIGR04523 328 NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE----KQNEIEKL----------KKENQSYKQEIKNLESQI 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 270 ANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKA----EERHGNIEERMRHLEGQ---- 341
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvkELIIKNLDNTRESLETQlkvl 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 342 ----------LEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNErlqlhLKERMAALE----EKNVLIQESENFRK 407
Cdd:TIGR04523 474 srsinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS-----LKEKIEKLEsekkEKESKISDLEDELN 548
|
410 420 430
....*....|....*....|....*....|....
gi 1907075644 408 NLEESLhDKERLAEEIEKLRSELDQMKMRTGSLI 441
Cdd:TIGR04523 549 KDDFEL-KKENLEKEIDEKNKEIEELKQTQKSLK 581
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
134-415 |
7.02e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.54 E-value: 7.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 134 SEGSTESEHLEGMEAGQKVHEKRLSNgSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDl 213
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKADEAKKAE-EKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIE- 1595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 214 iktEEMNTKYQRDIREAMAQKEDMEERITTLEKRylSAQRESTSIHDMNDKLENEL--------ANKEAILRQMEEKNRQ 285
Cdd:PTZ00121 1596 ---EVMKLYEEEKKMKAEEAKKAEEAKIKAEELK--KAEEEKKKVEQLKKKEAEEKkkaeelkkAEEENKIKAAEEAKKA 1670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 286 LQERLELAE-QKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNK 364
Cdd:PTZ00121 1671 EEDKKKAEEaKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK 1750
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1907075644 365 R---LSDTVDRLLTESNERLQLHLKERMAALEEKnvLIQESENFRKNLEESLHD 415
Cdd:PTZ00121 1751 KdeeEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE--LDEEDEKRRMEVDKKIKD 1802
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
176-457 |
7.24e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.46 E-value: 7.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 176 ELLEKQnyemAQMKERLTALSSRVGEVE-----QEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLS 250
Cdd:TIGR02168 203 KSLERQ----AEKAERYKELKAELRELElallvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 251 AQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALtkaeerhgn 330
Cdd:TIGR02168 279 LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL--------- 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 331 iEERMRHLEGQLEEKNQELQRARQREKMNEEHnkrlsdtvdrLLTESNERLQLhlkermaaLEEKNVLIQESENFRKNLE 410
Cdd:TIGR02168 350 -KEELESLEAELEELEAELEELESRLEELEEQ----------LETLRSKVAQL--------ELQIASLNNEIERLEARLE 410
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1907075644 411 ESLHDKERLAEEIEKLRSELDQMKMRTGSLIEPTISRTHIDTSTELR 457
Cdd:TIGR02168 411 RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE 457
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
28-323 |
8.00e-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: 60.08 E-value: 8.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 28 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLrmtvvkrqaqspsgvSSEVEVLKALKSLF 107
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL---------------HKLEEALNDLEARL 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 108 EHH--KALDEKIVALREQNVHIQRKMVSSEGSTESEHLEGMEAGQKVHEKRLSNGSIDSTDDT--SQIVELQELLEKQNY 183
Cdd:TIGR02169 789 SHSriPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSieKEIENLNGKKEELEE 868
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 184 EMAQMKERLTALSSRVGEVEQEAETARKDL----IKTEEMNTKYQRD---IREAMAQKEDMEERITTLEKRYLSAQREST 256
Cdd:TIGR02169 869 ELEELEAALRDLESRLGDLKKERDELEAQLreleRKIEELEAQIEKKrkrLSELKAKLEALEEELSEIEDPKGEDEEIPE 948
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907075644 257 SIHDMnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTK 323
Cdd:TIGR02169 949 EELSL-EDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
28-434 |
8.40e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.08 E-value: 8.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 28 EFAALTKELNACREQLLE---KEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALK 104
Cdd:PRK03918 315 RLSRLEEEINGIEERIKEleeKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELE 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 105 SLFEHHKALDEKIvalreqnvhiqRKMVSSEGSTESEHLEGMEAGQKVHEKR----LSNGSIDSTDDTSQIVELQELLEK 180
Cdd:PRK03918 395 ELEKAKEEIEEEI-----------SKITARIGELKKEIKELKKAIEELKKAKgkcpVCGRELTEEHRKELLEEYTAELKR 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 181 QNYEMAQMKERLTALSSRVGEVEQEAETARK--------DLIKT--EEMNTKYQRDIREAMAQKEDMEERITTLEKRYLS 250
Cdd:PRK03918 464 IEKELKEIEEKERKLRKELRELEKVLKKESEliklkelaEQLKEleEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKS 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 251 AQRESTSIHDMNDK---LENELANKEA----ILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTK 323
Cdd:PRK03918 544 LKKELEKLEELKKKlaeLEKKLDELEEelaeLLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKK 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 324 AEERHGNIEERMRHLEGQLEEKNQELQRARQreKMNEEHNKRLSDTVDRLltesnERLQLHLKERMAALEEknvLIQESE 403
Cdd:PRK03918 624 LEEELDKAFEELAETEKRLEELRKELEELEK--KYSEEEYEELREEYLEL-----SRELAGLRAELEELEK---RREEIK 693
|
410 420 430
....*....|....*....|....*....|.
gi 1907075644 404 NFRKNLEESLHDKERLAEEIEKLRSELDQMK 434
Cdd:PRK03918 694 KTLEKLKEELEEREKAKKELEKLEKALERVE 724
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
169-380 |
8.52e-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: 59.01 E-value: 8.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 169 SQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRY 248
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 249 ----LSAQREST--------SIHDMNDkLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQ 316
Cdd:COG4942 107 aellRALYRLGRqpplalllSPEDFLD-AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907075644 317 RIAALTKAEERHgniEERMRHLEGQLEEKNQELQRARQREkmneehnKRLSDTVDRLLTESNER 380
Cdd:COG4942 186 ERAALEALKAER---QKLLARLEKELAELAAELAELQQEA-------EELEALIARLEAEAAAA 239
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
41-436 |
1.36e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 41 EQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRmtVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKIVAL 120
Cdd:PRK03918 286 KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN--GIEERIKELEEKEERLEELKKKLKELEKRLEELEERHEL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 121 REQnvhIQRKMVSSEGstesehlegmeagqkvHEKRLSNGSIDstddtsQIVELQELLEKQNYEMaqmKERLTALSSRVG 200
Cdd:PRK03918 364 YEE---AKAKKEELER----------------LKKRLTGLTPE------KLEKELEELEKAKEEI---EEEISKITARIG 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 201 EVEQEAETARKDLIKTEEMNTK------------YQRDIREAMAQKEDMEERITTLEKRYLSAQRESTsihdmndKLENE 268
Cdd:PRK03918 416 ELKKEIKELKKAIEELKKAKGKcpvcgrelteehRKELLEEYTAELKRIEKELKEIEEKERKLRKELR-------ELEKV 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 269 LANKEAI--LRQMEEKNRQLQERLE-LAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEK 345
Cdd:PRK03918 489 LKKESELikLKELAEQLKELEEKLKkYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDEL 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 346 NQELQRA-RQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESEnfrknLEESLHDKERLAEEIE 424
Cdd:PRK03918 569 EEELAELlKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEE-----LDKAFEELAETEKRLE 643
|
410
....*....|..
gi 1907075644 425 KLRSELDQMKMR 436
Cdd:PRK03918 644 ELRKELEELEKK 655
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
33-427 |
1.53e-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: 59.29 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 33 TKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMtvVKRQAQSPSGVS------------------ 94
Cdd:TIGR00606 411 AQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKF--VIKELQQLEGSSdrileldqelrkaerels 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 95 -----SEVEVLKA-LKSLFEHHKALDEKIVALREQNVHIQRKmVSSEGSTESEHLEGMEAGQKVHE--KRLSNGSIDSTD 166
Cdd:TIGR00606 489 kaeknSLTETLKKeVKSLQNEKADLDRKLRKLDQEMEQLNHH-TTTRTQMEMLTKDKMDKDEQIRKikSRHSDELTSLLG 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 167 DTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQkEDMEERITTLEK 246
Cdd:TIGR00606 568 YFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS-QDEESDLERLKE 646
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 247 RYLSAQRESTSIH---DMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAET-LPEVEAELA----QRI 318
Cdd:TIGR00606 647 EIEKSSKQRAMLAgatAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDkLKSTESELKkkekRRD 726
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 319 AALTKAEERHGNIEERMRHLEgQLEEKNQELQRARQREKMNEEHNKRLSDTV-------DRLLTESN--ERLQLHLKERM 389
Cdd:TIGR00606 727 EMLGLAPGRQSIIDLKEKEIP-ELRNKLQKVNRDIQRLKNDIEEQETLLGTImpeeesaKVCLTDVTimERFQMELKDVE 805
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1907075644 390 AALEEKNVLIQESE------NFRKNLEESLHDKERLAEEIEKLR 427
Cdd:TIGR00606 806 RKIAQQAAKLQGSDldrtvqQVNQEKQEKQHELDTVVSKIELNR 849
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
27-329 |
1.53e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 27 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEhleclvsrherslrmtvvKRQAQSPSGVSSEVEVLKALKSL 106
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELE------------------EAQAEEYELLAELARLEQDIARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 107 FEHHKALDEKIVALREQNVHIQRKMVSSEGSTESEHLEGMEAGQKVHEKRLsngsidstddtsQIVELQELLEKQNYEMA 186
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA------------ELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 187 QMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLE 266
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907075644 267 NELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHG 329
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
221-434 |
1.63e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 221 TKYQRDIREAMAQKEDMEERITTLE---------KRYLSAQRESTSI-HDMNDKLENelANKEAILRQMEEKNRQLqERL 290
Cdd:TIGR02168 168 SKYKERRKETERKLERTRENLDRLEdilnelerqLKSLERQAEKAERyKELKAELRE--LELALLVLRLEELREEL-EEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 291 ELAEQKLQQTMRKAET-LPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDT 369
Cdd:TIGR02168 245 QEELKEAEEELEELTAeLQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ 324
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907075644 370 VDRL----------LTESNERLQLhLKERMAALEEKnvlIQESENFRKNLEESLHDKErlaEEIEKLRSELDQMK 434
Cdd:TIGR02168 325 LEELeskldelaeeLAELEEKLEE-LKEELESLEAE---LEELEAELEELESRLEELE---EQLETLRSKVAQLE 392
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
263-429 |
1.72e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 263 DKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtLPEVEAELA---QRIAALTKAEERHGNIEERMRHLE 339
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID-VASAEREIAeleAELERLDASSDDLAALEEQLEELE 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 340 GQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLT-------ESNERLQLHLKERMAALEEKNVLIQESENFRKNLEES 412
Cdd:COG4913 699 AELEELEEELDELKGEIGRLEKELEQAEEELDELQDrleaaedLARLELRALLEERFAAALGDAVERELRENLEERIDAL 778
|
170
....*....|....*..
gi 1907075644 413 LHDKERLAEEIEKLRSE 429
Cdd:COG4913 779 RARLNRAEEELERAMRA 795
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
121-431 |
2.26e-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: 58.65 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 121 REQNVHIQRKMVSSEGSTESEHLEGMEAG-QKVH-EKRLSNGSIDSTDDTSQIVELQEllEKQNYEMAQMKERLTALSSR 198
Cdd:pfam01576 90 RSQQLQNEKKKMQQHIQDLEEQLDEEEAArQKLQlEKVTTEAKIKKLEEDILLLEDQN--SKLSKERKLLEERISEFTSN 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 199 VGEVEQEAETARKDLIKTEEMNTkyqrDIREAMAQKEDMEERittLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQ 278
Cdd:pfam01576 168 LAEEEEKAKSLSKLKNKHEAMIS----DLEERLKKEEKGRQE---LEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 279 MEEKNRQLQERLE---LAEQKLQQTMRKAET-LPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEK------NQE 348
Cdd:pfam01576 241 KEEELQAALARLEeetAQKNNALKKIRELEAqISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTldttaaQQE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 349 LQRARQRE--------------------KMNEEHNKRLSDTVDRLltESNERLQLHLKERMAALEEKNVLI--------- 399
Cdd:pfam01576 321 LRSKREQEvtelkkaleeetrsheaqlqEMRQKHTQALEELTEQL--EQAKRNKANLEKAKQALESENAELqaelrtlqq 398
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1907075644 400 --QESENFRKNLEESLHD-----------KERLAEEIEKLRSELD 431
Cdd:pfam01576 399 akQDSEHKRKKLEGQLQElqarlseserqRAELAEKLSKLQSELE 443
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
30-441 |
2.43e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 30 AALTKELNACREQL---LEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVvkrqaqspSGVSSEVEVLKALKSL 106
Cdd:PRK03918 168 GEVIKEIKRRIERLekfIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL--------EKLEKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 107 FE-----------HHKALDEKIVALREQNVHIQRKM-VSSEGSTESEHLEG-------MEAGQKVHEKRLSNGSIDSTDD 167
Cdd:PRK03918 240 IEelekeleslegSKRKLEEKIRELEERIEELKKEIeELEEKVKELKELKEkaeeyikLSEFYEEYLDELREIEKRLSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 168 TSQIVELQELLEKqnyemaqmkerLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRdIREAMAQKEDMEERIT----- 242
Cdd:PRK03918 320 EEEINGIEERIKE-----------LEEKEERLEELKKKLKELEKRLEELEERHELYEE-AKAKKEELERLKKRLTgltpe 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 243 TLEKRYLSAQRESTSIHDMNDKLENELANkeaiLRQMEEKNRQLQERLELAEQKLQQTMR------KAETLPEVEAELAQ 316
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEISKITARIGE----LKKEIKELKKAIEELKKAKGKCPVCGRelteehRKELLEEYTAELKR 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 317 RIAALTKAEERHGNIEERMRHLEGQLEeKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLhLKERMAALEEKn 396
Cdd:PRK03918 464 IEKELKEIEEKERKLRKELRELEKVLK-KESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEK-LKEKLIKLKGE- 540
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1907075644 397 vliqesenfRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSLI 441
Cdd:PRK03918 541 ---------IKSLKKELEKLEELKKKLAELEKKLDELEEELAELL 576
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
30-431 |
2.61e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 58.43 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 30 AALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRH---------ERSLRmtvVKRQAQSpsgvssevEVL 100
Cdd:COG3096 781 AAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVGGHlavafapdpEAELA---ALRQRRS--------ELE 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 101 KALKSLFEHHKALDEKIVALREQnVHIQRKMVSSEGSTESEHLEgmeagQKVHEKRlsngsidstddtsqiVELQELLEK 180
Cdd:COG3096 850 RELAQHRAQEQQLRQQLDQLKEQ-LQLLNKLLPQANLLADETLA-----DRLEELR---------------EELDAAQEA 908
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 181 QNYeMAQMKERLTalssrvgEVEQEAETARKDLIKTEEMNTKYQRdireAMAQKEDMEERITTLEkrYLSAQRESTSIHD 260
Cdd:COG3096 909 QAF-IQQHGKALA-------QLEPLVAVLQSDPEQFEQLQADYLQ----AKEQQRRLKQQIFALS--EVVQRRPHFSYED 974
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 261 ----------MNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAAL-----TKAE 325
Cdd:COG3096 975 avgllgensdLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELgvqadAEAE 1054
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 326 ERhgnIEERMRHLEGQL----EEKNQ-ELQRARQREKMnEEHNKRLSDtVDRLLTESNERLQLHLKERMAALEeknvLIQ 400
Cdd:COG3096 1055 ER---ARIRRDELHEELsqnrSRRSQlEKQLTRCEAEM-DSLQKRLRK-AERDYKQEREQVVQAKAGWCAVLR----LAR 1125
|
410 420 430
....*....|....*....|....*....|.
gi 1907075644 401 ESenfrkNLEESLHDKERLAEEIEKLRSELD 431
Cdd:COG3096 1126 DN-----DVERRLHRRELAYLSADELRSMSD 1151
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
34-433 |
2.73e-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: 58.44 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 34 KELNACREQLLEKEEEISELKAERNNtrlLLEHLECLVSRHERSLRMTVVkrQAQSPSGVSSEVE-VLKALKSLFEHHKA 112
Cdd:TIGR00618 472 EQQLQTKEQIHLQETRKKAVVLARLL---ELQEEPCPLCGSCIHPNPARQ--DIDNPGPLTRRMQrGEQTYAQLETSEED 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 113 LDEKIVALREQNVHIQRKMVSSEGSTE------SEHLEGMEAGQKVHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEMA 186
Cdd:TIGR00618 547 VYHQLTSERKQRASLKEQMQEIQQSFSiltqcdNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQD 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 187 QMKERLTalssrvgEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERitTLEKRYLSAQRESTSIHDMNDKLE 266
Cdd:TIGR00618 627 LQDVRLH-------LQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKE--LLASRQLALQKMQSEKEQLTYWKE 697
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 267 nELANKEAILRQMEE---KNRQLQERLELAEQKLQQTMR-KAETLPEVEAEL-AQRIAALTKAEERHGNIEER------- 334
Cdd:TIGR00618 698 -MLAQCQTLLRELEThieEYDREFNEIENASSSLGSDLAaREDALNQSLKELmHQARTVLKARTEAHFNNNEEvtaalqt 776
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 335 ---MRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESENFRKNLEE 411
Cdd:TIGR00618 777 gaeLSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEE 856
|
410 420
....*....|....*....|..
gi 1907075644 412 SLHDKERLAEEIEKLRSELDQM 433
Cdd:TIGR00618 857 CSKQLAQLTQEQAKIIQLSDKL 878
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
170-344 |
3.88e-08 |
|
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: 55.32 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 170 QIVELQELLEkqnyEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKR-- 247
Cdd:COG1579 8 ALLDLQELDS----ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 248 -------YLSAQRESTSIHDMNDKLEnelankEAILRQMEEKNrQLQERLELAEQKLQQtmrKAETLPEVEAELAQRIAA 320
Cdd:COG1579 84 nvrnnkeYEALQKEIESLKRRISDLE------DEILELMERIE-ELEEELAELEAELAE---LEAELEEKKAELDEELAE 153
|
170 180
....*....|....*....|....
gi 1907075644 321 LTKAEERhgnIEERMRHLEGQLEE 344
Cdd:COG1579 154 LEAELEE---LEAEREELAAKIPP 174
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
169-448 |
4.28e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.83 E-value: 4.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 169 SQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRY 248
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 249 LSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMrkaetlpevEAELAQRIAALTKAEERH 328
Cdd:COG4372 125 QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS---------EAEAEQALDELLKEANRN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 329 GNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESENFRKN 408
Cdd:COG4372 196 AEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEE 275
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1907075644 409 LEESLHDKERLAEEIEKLRSELDQMKMRTGSLIEPTISRT 448
Cdd:COG4372 276 EELEIAALELEALEEAALELKLLALLLNLAALSLIGALED 315
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
927-982 |
9.06e-08 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 49.99 E-value: 9.06e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907075644 927 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 982
Cdd:smart00454 11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
244-436 |
1.26e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 244 LEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTK 323
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 324 AEERHgNIEERMRHLEGQLEE---KNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKErmaaleeknvLIQ 400
Cdd:COG4717 131 YQELE-ALEAELAELPERLEEleeRLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD----------LAE 199
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907075644 401 ESENFRKNLEESLHDKERLAEEIEKLRSELDQMKMR 436
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
251-431 |
1.26e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.20 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 251 AQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGN 330
Cdd:PRK02224 197 EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 331 IEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNErlqlhLKERmaaLEEKNVLIQESENFRKNLE 410
Cdd:PRK02224 277 LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEE-----LRDR---LEECRVAAQAHNEEAESLR 348
|
170 180
....*....|....*....|.
gi 1907075644 411 ESLHDKERLAEEIEKLRSELD 431
Cdd:PRK02224 349 EDADDLEERAEELREEAAELE 369
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
210-433 |
1.29e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 56.13 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 210 RKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRY----LSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQ 285
Cdd:TIGR00618 165 KKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSqlltLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAY 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 286 LQERLELAEQK------LQQTMRKAETLPEVEAELAQRIAALTKAE--ERHGNIEERMRHLEGQLEEKNQELQ-RARQRE 356
Cdd:TIGR00618 245 LTQKREAQEEQlkkqqlLKQLRARIEELRAQEAVLEETQERINRARkaAPLAAHIKAVTQIEQQAQRIHTELQsKMRSRA 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 357 KMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESENFRKNLEESLH----DKERLAEEIEKLRSELDQ 432
Cdd:TIGR00618 325 KLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHtlqqQKTTLTQKLQSLCKELDI 404
|
.
gi 1907075644 433 M 433
Cdd:TIGR00618 405 L 405
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
185-393 |
1.74e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 185 MAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQREStsihdmnDK 264
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREEL-------EK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 265 LENELANKEAI--LRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGN-IEERMRHLEGQ 341
Cdd:COG4717 121 LEKLLQLLPLYqeLEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLaTEEELQDLAEE 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1907075644 342 LEEKNQELQRARQREKMNEEHNKRLSDTVDRLlteSNERLQLHLKERMAALE 393
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQL---ENELEAAALEERLKEAR 249
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
163-437 |
1.92e-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: 55.57 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 163 DSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIR-------EAMAQKE 235
Cdd:pfam01576 216 ESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLEseraarnKAEKQRR 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 236 DMEERI------------TTLEKRYLSAQREsTSIHDMNDKLENELANKEAILRQMEEKNRQ----LQERLELAEQKLQQ 299
Cdd:pfam01576 296 DLGEELealkteledtldTTAAQQELRSKRE-QEVTELKKALEEETRSHEAQLQEMRQKHTQaleeLTEQLEQAKRNKAN 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 300 TMRKAETLPEVEAELAQRIAALTKAEerhGNIEERMRHLEGQLEEKNQELQRA-RQREKMNEEHNK-------------- 364
Cdd:pfam01576 375 LEKAKQALESENAELQAELRTLQQAK---QDSEHKRKKLEGQLQELQARLSESeRQRAELAEKLSKlqselesvssllne 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 365 ------RLSDTVDRL---LTESNERLQ------LHLKERMAALEEknvliqESENFRKNLEESLHDKERLAEEIEKLRSE 429
Cdd:pfam01576 452 aegkniKLSKDVSSLesqLQDTQELLQeetrqkLNLSTRLRQLED------ERNSLQEQLEEEEEAKRNVERQLSTLQAQ 525
|
....*...
gi 1907075644 430 LDQMKMRT 437
Cdd:pfam01576 526 LSDMKKKL 533
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
168-457 |
2.34e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 168 TSQIVELQELLEKQNYEMAQMKERLTALS--SRVGEVEQEAETARKDLIKTEEMntkyQRDIREAMAQKEDMEERITTLE 245
Cdd:COG4913 623 EEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAE----LERLDASSDDLAALEEQLEELE 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 246 KRYlsaqrestsihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlPEVEAELAQRIAALtKAE 325
Cdd:COG4913 699 AEL--------------EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR--LELRALLEERFAAA-LGD 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 326 ERHGNIEERmrhLEGQLEEKNQELQRARQR-EKMNEEHNKRLSDTVDRLLT--ESNERLQLHLK----ERMAALEEK--N 396
Cdd:COG4913 762 AVERELREN---LEERIDALRARLNRAEEElERAMRAFNREWPAETADLDAdlESLPEYLALLDrleeDGLPEYEERfkE 838
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907075644 397 VLIQESENFRKNLEESLHDKERLAEE-IEKLRSELDQMKMRTGSLIEPTISRTHIDTSTELR 457
Cdd:COG4913 839 LLNENSIEFVADLLSKLRRAIREIKErIDPLNDSLKRIPFGPGRYLRLEARPRPDPEVREFR 900
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
32-425 |
2.41e-07 |
|
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: 55.03 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 32 LTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTvvKRQAQSpsgVSSEVEVLKALKSLfEHHK 111
Cdd:TIGR04523 237 KQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKEL--EKQLNQ---LKSEISDLNNQKEQ-DWNK 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 112 ALDEKIVALREQNVHIQRKMVSSEGSTES--EHLEGMEagQKVHEKRLSNGSIDStddtsQIVELQELLEKQNYEMAQMK 189
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQlnEQISQLK--KELTNSESENSEKQR-----ELEEKQNEIEKLKKENQSYK 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 190 ERLTALSSRVGEVEQEAEtarkdliKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQREstsIHDmndkLENEL 269
Cdd:TIGR04523 384 QEIKNLESQINDLESKIQ-------NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE---IKD----LTNQD 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 270 ANKEAILRQMEEKNRQLQERLEL-------AEQKLQQTMR-------KAETLPEVEAELAQRIAALTKaeeRHGNIEERM 335
Cdd:TIGR04523 450 SVKELIIKNLDNTRESLETQLKVlsrsinkIKQNLEQKQKelkskekELKKLNEEKKELEEKVKDLTK---KISSLKEKI 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 336 RHLEGQLEEKNQEL-QRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESENFRKNLEESLH 414
Cdd:TIGR04523 527 EKLESEKKEKESKIsDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIE 606
|
410
....*....|.
gi 1907075644 415 DKERLAEEIEK 425
Cdd:TIGR04523 607 EKEKKISSLEK 617
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
145-434 |
2.80e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.14 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 145 GMEAGQKVHEKRLS------NGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEE 218
Cdd:COG4372 1 GDRLGEKVGKARLSlfglrpKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 219 MNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQREstsihdmNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQ 298
Cdd:COG4372 81 ELEELNEQLQAAQAELAQAQEELESLQEEAEELQEE-------LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 299 QTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESN 378
Cdd:COG4372 154 ELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907075644 379 ERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQMK 434
Cdd:COG4372 234 ALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALE 289
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
170-354 |
3.37e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 170 QIVELQELLEKQNyEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEmnTKYQRDIREAMAQKEDMEERITTLEKRYL 249
Cdd:COG4913 250 QIELLEPIRELAE-RYAAARERLAELEYLRAALRLWFAQRRLELLEAEL--EELRAELARLEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 250 SAQREstsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQkLQQTMRKAE-TLPEVEAELAQRI----AALTKA 324
Cdd:COG4913 327 ELEAQ---------IRGNGGDRLEQLEREIERLERELEERERRRAR-LEALLAALGlPLPASAEEFAALRaeaaALLEAL 396
|
170 180 190
....*....|....*....|....*....|
gi 1907075644 325 EERHGNIEERMRHLEGQLEEKNQELQRARQ 354
Cdd:COG4913 397 EEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
27-436 |
3.45e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 27 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSL---RMTVVKRQAQSPSGVSSEVEVLKAL 103
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELaeaEEELEELAEELLEALRAAAELAAQL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 104 KSLFEHHKALDEKIVALREQNVHIQRKMVSSEGS--TESEHLEGMEAGQKVHEKRLSNGSIDSTDDTSQIVELQELLEKQ 181
Cdd:COG1196 403 EELEEAEEALLERLERLEEELEELEEALAELEEEeeEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 182 NYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTE------------EMNTKYQRDIREAMA---------QKEDMEER 240
Cdd:COG1196 483 LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGlrglagavavliGVEAAYEAALEAALAaalqnivveDDEVAAAA 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 241 ITTLEKRYLS----------AQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEV 310
Cdd:COG1196 563 IEYLKAAKAGratflpldkiRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTL 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 311 EAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQRE-KMNEEHNKRLSDTVDRLLTESNERLQLHLKERM 389
Cdd:COG1196 643 AGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLaEEELELEEALLAEEEEERELAEAEEERLEEELE 722
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1907075644 390 AALEEKNVLIQESENFRKNLEESLHDKERLAEE------IEKLRSELDQMKMR 436
Cdd:COG1196 723 EEALEEQLEAEREELLEELLEEEELLEEEALEElpeppdLEELERELERLERE 775
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
27-426 |
3.89e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 3.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 27 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQaqspsgVSSEVEVLKALKSL 106
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAE------LAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 107 FEHHKALDEKIVALREQNVHIQRKMVSSEGSTESEHLEGMEagqkvhekrlsngsidstDDTSQIVELQELLEKQNYEMA 186
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ------------------DLAEELEELQQRLAELEEELE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 187 QMKERLTALSSRVGEVEQEAETARK-------------------------DLIKTEEMNTK------------YQRDIRE 229
Cdd:COG4717 217 EAQEELEELEEELEQLENELEAAALeerlkearlllliaaallallglggSLLSLILTIAGvlflvlgllallFLLLARE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 230 AMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQT--MRKAETL 307
Cdd:COG4717 297 KASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEEleQEIAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 308 PEVEAE-LAQRIAALTKAEERHgNIEERMRHLEGQLEEKNQELQRARQREKmNEEHNKRLSDTVDRLLTESNERLQLHlk 386
Cdd:COG4717 377 AEAGVEdEEELRAALEQAEEYQ-ELKEELEELEEQLEELLGELEELLEALD-EEELEEELEELEEELEELEEELEELR-- 452
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1907075644 387 ERMAALEEKnvlIQESENfRKNLEESLHDKERLAEEIEKL 426
Cdd:COG4717 453 EELAELEAE---LEQLEE-DGELAELLQELEELKAELREL 488
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
27-453 |
4.40e-07 |
|
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: 54.67 E-value: 4.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 27 QEFAA-LTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQ------AQSPSGVSSEVEV 99
Cdd:TIGR00606 694 QEFISdLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQkvnrdiQRLKNDIEEQETL 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 100 LKALKSLFEHHKALDEKIVALreQNVHIQRKMVSSEGSTESEHLEGMEAGQKVHEKRLSNGSIDSTDDT--SQIVELQEL 177
Cdd:TIGR00606 774 LGTIMPEEESAKVCLTDVTIM--ERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTvvSKIELNRKL 851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 178 LEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKrylSAQRESTS 257
Cdd:TIGR00606 852 IQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEK---DQQEKEEL 928
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 258 IHDMNDklENELANKEaiLRQMEEKNRQLQERLELAEQKLQQTmrKAETLPEVEAELAQRIAALTKAEERHGNIEERMRH 337
Cdd:TIGR00606 929 ISSKET--SNKKAQDK--VNDIKEKVKNIHGYMKDIENKIQDG--KDDYLKQKETELNTVNAQLEECEKHQEKINEDMRL 1002
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 338 LEGQLEEKNQE---LQRARQREKMNEEHnKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESENF-----RKNL 409
Cdd:TIGR00606 1003 MRQDIDTQKIQerwLQDNLTLRKRENEL-KEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLalgrqKGYE 1081
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1907075644 410 EESLHDKERLAEEI-----EKLRSELDQMKMRTGSLIEPTISRTHIDTS 453
Cdd:TIGR00606 1082 KEIKHFKKELREPQfrdaeEKYREMMIVMRTTELVNKDLDIYYKTLDQA 1130
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
75-596 |
4.70e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 54.35 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 75 ERSLRMTVVKRQAQSPSGVSSE----VEVLKALKSLFEHhkaldekivALREQNVHIQ---RKMVSSEGSTE---SEHLE 144
Cdd:pfam15921 125 ERDAMADIRRRESQSQEDLRNQlqntVHELEAAKCLKED---------MLEDSNTQIEqlrKMMLSHEGVLQeirSILVD 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 145 GMEA-GQKVHEKrlsngsidstdDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKY 223
Cdd:pfam15921 196 FEEAsGKKIYEH-----------DSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQ 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 224 QRDIREAMAQKEDMEerITTLEKRYLSAQRESTSIhdmndklenelankeailrqmeeknrqlQERLEL-AEQKLQQTMR 302
Cdd:pfam15921 265 HQDRIEQLISEHEVE--ITGLTEKASSARSQANSI----------------------------QSQLEIiQEQARNQNSM 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 303 KAETLPEVEAELAQRIAALTKAEERHgniEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLT------- 375
Cdd:pfam15921 315 YMRQLSDLESTVSQLRSELREAKRMY---EDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLAdlhkrek 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 376 ------ESNERL-------QLHLKERMAALEEKNVLIQESENFRKNLEE-----------SLHDKERLAEEIEKLRSELD 431
Cdd:pfam15921 392 elslekEQNKRLwdrdtgnSITIDHLRRELDDRNMEVQRLEALLKAMKSecqgqmerqmaAIQGKNESLEKVSSLTAQLE 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 432 QMKMRTGSLIEPTISRTHIDTSTELRYS--VGSLVDSQSDYRTTKVIRRPRRGRMGVRRDEPK-VKSLGDHEWNRTQQIG 508
Cdd:pfam15921 472 STKEMLRKVVEELTAKKMTLESSERTVSdlTASLQEKERAIEATNAEITKLRSRVDLKLQELQhLKNEGDHLRNVQTECE 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 509 VLGSHPFESDTEMSDIddddRETIFSSMDLLSPSGHSDA--QTLAMMLQEQLDAINKEIRLIQEEKESTELRAEEIENRV 586
Cdd:pfam15921 552 ALKLQMAEKDKVIEIL----RQQIENMTQLVGQHGRTAGamQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARV 627
|
570
....*....|
gi 1907075644 587 ASVSLEGLNL 596
Cdd:pfam15921 628 SDLELEKVKL 637
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
1005-1076 |
5.18e-07 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 48.06 E-value: 5.18e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907075644 1005 VLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDEnfdysSLALLLQIPTQNTQARQILEREYNNLLA 1076
Cdd:smart00454 1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLT-----SEEDLKELGITKLGHRKKILKAIQKLKE 67
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
168-442 |
5.73e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.20 E-value: 5.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 168 TSQIVELQELLEKQNYemAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEkr 247
Cdd:TIGR00618 273 RAQEAVLEETQERINR--ARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQ-- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 248 ylSAQRESTSIHDMNDKlenELANKEAILRQMEEKN--RQLQERLELAEQKLQQTMRKAETLPE----VEAELAQRIAAL 321
Cdd:TIGR00618 349 --TLHSQEIHIRDAHEV---ATSIREISCQQHTLTQhiHTLQQQKTTLTQKLQSLCKELDILQReqatIDTRTSAFRDLQ 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 322 TKAEERHGNIEERMRHLEGQ----------LEEKNQELQRARQR---EKMNEEHNKRLSDTVDRLLTESNERLQLH---- 384
Cdd:TIGR00618 424 GQLAHAKKQQELQQRYAELCaaaitctaqcEKLEKIHLQESAQSlkeREQQLQTKEQIHLQETRKKAVVLARLLELqeep 503
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 385 --LKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSLIE 442
Cdd:TIGR00618 504 cpLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKE 563
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
95-434 |
7.34e-07 |
|
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: 53.59 E-value: 7.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 95 SEVEVLKALKSLFEHHKALDEKIVALREQNVHIQR-KMVSSEGSTESEHLEGMEAGQKVHEKRLSNGSIDSTDDTSQIVE 173
Cdd:pfam17380 266 TENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERlRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 174 LQELLEK-----QNYEMAQMKERLTALssrvgEVEQEAETARKDLiKTEEMNTKYQRDIREAMAQKEDMEERittlEKRY 248
Cdd:pfam17380 346 RERELERirqeeRKRELERIRQEEIAM-----EISRMRELERLQM-ERQQKNERVRQELEAARKVKILEEER----QRKI 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 249 LSAQRESTSIhdmndKLENELANKEAILRQMEEKNRQLqERLELAEQKLQQTMrkaETLPEVEAELAQRIAALTKAEERH 328
Cdd:pfam17380 416 QQQKVEMEQI-----RAEQEEARQREVRRLEEERAREM-ERVRLEEQERQQQV---ERLRQQEEERKRKKLELEKEKRDR 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 329 GNIEERMRH-LEGQLEEKnqelqrarqREKMNEEHNKRlsdtvdrlltesnERLQLHLKERMAALEEKNVLIQESENFRK 407
Cdd:pfam17380 487 KRAEEQRRKiLEKELEER---------KQAMIEEERKR-------------KLLEKEMEERQKAIYEEERRREAEEERRK 544
|
330 340 350
....*....|....*....|....*....|
gi 1907075644 408 NLEesLHDKERLAEEIEKL---RSELDQMK 434
Cdd:pfam17380 545 QQE--MEERRRIQEQMRKAteeRSRLEAME 572
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
268-425 |
8.04e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 53.24 E-value: 8.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 268 ELANKEAIlRQMEEKNRQLQERLELAEQKLQQTMRKAETlpEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ 347
Cdd:PRK12704 34 KEAEEEAK-RILEEAKKEAEAIKKEALLEAKEEIHKLRN--EFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 348 ELQRARQREKMNEEHNKRLSDTVDRLLTESNERLqlhlkERMAAL---EEKNVLIQESEnfrknlEESLHDKERLAEEIE 424
Cdd:PRK12704 111 ELEKKEKELEQKQQELEKKEEELEELIEEQLQEL-----ERISGLtaeEAKEILLEKVE------EEARHEAAVLIKEIE 179
|
.
gi 1907075644 425 K 425
Cdd:PRK12704 180 E 180
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
27-505 |
1.21e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 52.92 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 27 QEFAALTKELNacrEQLLEKEEEISELKAERNNTRLLL--------EHLECLVSRHERSLRMTVVKR---QAQSPSgVSS 95
Cdd:pfam12128 279 EERQETSAELN---QLLRTLDDQWKEKRDELNGELSAAdaavakdrSELEALEDQHGAFLDADIETAaadQEQLPS-WQS 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 96 EVEVL-KALKSLFEHHKALDEKIVALR----EQNVHI----------QRKMVSSEGSTESEHLEGMEAG-QKVHEKRLSN 159
Cdd:pfam12128 355 ELENLeERLKALTGKHQDVTAKYNRRRskikEQNNRDiagikdklakIREARDRQLAVAEDDLQALESElREQLEAGKLE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 160 GSIDSTDDTSQIVELQELLEKQNYEmAQMKERLTALSSRVGEVEQEAETARKDLikteemnTKYQRDIREAMAQKEDMEE 239
Cdd:pfam12128 435 FNEEEYRLKSRLGELKLRLNQATAT-PELLLQLENFDERIERAREEQEAANAEV-------ERLQSELRQARKRRDQASE 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 240 RITTLEKRYLSAQRESTSIHDMND----KLENELANKEAILRQMEEK--NRQLQERLELAEQKLQQTMRKAETL------ 307
Cdd:pfam12128 507 ALRQASRRLEERQSALDELELQLFpqagTLLHFLRKEAPDWEQSIGKviSPELLHRTDLDPEVWDGSVGGELNLygvkld 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 308 -------------PEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL- 373
Cdd:pfam12128 587 lkridvpewaaseEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEk 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 374 --LTESNERLQLHLKERMAALE-EKNVLIQESENF-----RKNLEESLHDKERLAEEIEKLRSELDQMKmrTGSLIEPTI 445
Cdd:pfam12128 667 dkKNKALAERKDSANERLNSLEaQLKQLDKKHQAWleeqkEQKREARTEKQAYWQVVEGALDAQLALLK--AAIAARRSG 744
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907075644 446 SRTHIDT-STELRYSVGSL-VDSQSDYRTTKVIRRPRRGRMGVRRDEPKVKSLgdHEWNRTQ 505
Cdd:pfam12128 745 AKAELKAlETWYKRDLASLgVDPDVIAKLKREIRTLERKIERIAVRRQEVLRY--FDWYQET 804
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
225-436 |
1.24e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 225 RDIREAMaqkEDMEERITTLE------KRYLSAQRESTSIHDMNDKLEnelankeaiLRQMEEKNRQLQERLELAEQKLQ 298
Cdd:COG4913 238 ERAHEAL---EDAREQIELLEpirelaERYAAARERLAELEYLRAALR---------LWFAQRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 299 QTMRKAETLPEVEAELAQRIAALTKAEERHGNIEErmrhleGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESN 378
Cdd:COG4913 306 RLEAELERLEARLDALREELDELEAQIRGNGGDRL------EQLEREIERLERELEERERRRARLEALLAALGLPLPASA 379
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907075644 379 ERLQLHLKERMAALEEknvLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQMKMR 436
Cdd:COG4913 380 EEFAALRAEAAALLEA---LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
96-425 |
1.47e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 96 EVEVLKALKSLFEHHKALDEKIVALREQNVHIQRKMVSSEGSteseHLEGMEAGQKVHEKRLSNgSIDSTDDTSQIVELQ 175
Cdd:PTZ00121 1222 DAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMA----HFARRQAAIKAEEARKAD-ELKKAEEKKKADEAK 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 176 ELLEKQNYE----MAQMKERLTALSSRVGEVEQEAETARKdliKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSA 251
Cdd:PTZ00121 1297 KAEEKKKADeakkKAEEAKKADEAKKKAEEAKKKADAAKK---KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK 1373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 252 QRESTSIHDMNDKLEnELANKEAILRQMEEKNRQLQE--RLELAEQKLQQTMRKAETLPEVEaELAQRIAALTKAEERHG 329
Cdd:PTZ00121 1374 EEAKKKADAAKKKAE-EKKKADEAKKKAEEDKKKADElkKAAAAKKKADEAKKKAEEKKKAD-EAKKKAEEAKKADEAKK 1451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 330 NIEERMRHLEgqLEEKNQELQRARQREKMNEEhnKRLSDTVDRLLTESNERLQlhlkERMAALEEKnvliQESENFRKNL 409
Cdd:PTZ00121 1452 KAEEAKKAEE--AKKKAEEAKKADEAKKKAEE--AKKADEAKKKAEEAKKKAD----EAKKAAEAK----KKADEAKKAE 1519
|
330
....*....|....*.
gi 1907075644 410 EESLHDKERLAEEIEK 425
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKK 1535
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
147-336 |
1.51e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 147 EAGQKVHEKRLSNGSIDSTDDT----SQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDlikteEMNTK 222
Cdd:COG3206 193 EAEAALEEFRQKNGLVDLSEEAklllQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQS-----PVIQQ 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 223 YQRDIREAMAQKEDMEERITTLEKRYLSAQREstsIHDMNDKLENELankEAILRQMEEKNRQLQERLELAEQKLQQTMR 302
Cdd:COG3206 268 LRAQLAELEAELAELSARYTPNHPDVIALRAQ---IAALRAQLQQEA---QRILASLEAELEALQAREASLQAQLAQLEA 341
|
170 180 190
....*....|....*....|....*....|....
gi 1907075644 303 KAETLPEVEAELAQRIAALTKAEERHGNIEERMR 336
Cdd:COG3206 342 RLAELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
25-393 |
1.69e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.43 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 25 TFQEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKrQAQSPSGVSSEVEVLKALK 104
Cdd:pfam15921 459 SLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAE-ITKLRSRVDLKLQELQHLK 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 105 SLFEH-------------HKALDEKIVALREQNVHIQRKMVSSEGSTESE-HLEGMEAGQKVHEKRLSNGSIDSTDDT-- 168
Cdd:pfam15921 538 NEGDHlrnvqtecealklQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAmQVEKAQLEKEINDRRLELQEFKILKDKkd 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 169 SQIVELQELLEKQNYEMAQM----KERLTALSSRVGEVEQ---EAETARKDLIKTEEMNTKYQRDIREamaQKEDMEERI 241
Cdd:pfam15921 618 AKIRELEARVSDLELEKVKLvnagSERLRAVKDIKQERDQllnEVKTSRNELNSLSEDYEVLKRNFRN---KSEEMETTT 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 242 TTLEKRYLSAQRE----STSIHDMNDKLENELANKEAILRQMEEKNRQ---LQERLELAEQKLQQTMRKAETLPEVEAEL 314
Cdd:pfam15921 695 NKLKMQLKSAQSEleqtRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQidaLQSKIQFLEEAMTNANKEKHFLKEEKNKL 774
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907075644 315 AQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMneehnkRLSDTVDRLLTESNERLQLHLKERMAALE 393
Cdd:pfam15921 775 SQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASL------QFAECQDIIQRQEQESVRLKLQHTLDVKE 847
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
227-394 |
1.74e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.31 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 227 IREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAeqklqQTMRKAET 306
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-----RNNKEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 307 LpevEAELAQriaaltkAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLK 386
Cdd:COG1579 94 L---QKEIES-------LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
....*...
gi 1907075644 387 ERMAALEE 394
Cdd:COG1579 164 EREELAAK 171
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
226-403 |
1.86e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 226 DIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKA- 304
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALy 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 305 ---ETLPEVEA--------ELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL 373
Cdd:COG3883 97 rsgGSVSYLDVllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190
....*....|....*....|....*....|
gi 1907075644 374 LTESNERLQLHLKERMAALEEKNVLIQESE 403
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
27-440 |
1.87e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.43 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 27 QEFAALTKELNA-CREQLlekEEEISELKAERNNtrllLEHLECLVSRHERS---LRMTVVKRQAQSPSGVSSEVEVLKA 102
Cdd:pfam15921 429 QRLEALLKAMKSeCQGQM---ERQMAAIQGKNES----LEKVSSLTAQLESTkemLRKVVEELTAKKMTLESSERTVSDL 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 103 LKSLFEHHKALDEKIVALREQNVHIQRKMVSSEG-STESEHLEGMEAGQKVHEKRLSngsidstdDTSQIVE-LQELLEK 180
Cdd:pfam15921 502 TASLQEKERAIEATNAEITKLRSRVDLKLQELQHlKNEGDHLRNVQTECEALKLQMA--------EKDKVIEiLRQQIEN 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 181 QNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHD 260
Cdd:pfam15921 574 MTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQ 653
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 261 MNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAET-LPEVEAELAQRIAALTKAEERHGNIEERMRHLE 339
Cdd:pfam15921 654 ERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMqLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQ 733
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 340 GQLEEKNQELQRARQREKMNEEhnkrlsdtvdrLLTESNerlqlhlKERMAALEEKNVLIQEsenfrknLEESLHDKERL 419
Cdd:pfam15921 734 KQITAKRGQIDALQSKIQFLEE-----------AMTNAN-------KEKHFLKEEKNKLSQE-------LSTVATEKNKM 788
|
410 420
....*....|....*....|.
gi 1907075644 420 AEEIEKLRSELDQMKMRTGSL 440
Cdd:pfam15921 789 AGELEVLRSQERRLKEKVANM 809
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
181-425 |
2.00e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 181 QNYEMAQMKErltalsSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMeerittlekRYLSAQRESTSIHD 260
Cdd:PTZ00121 1077 KDFDFDAKED------NRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDA---------RKAEEARKAEDARK 1141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 261 MNDKLENELANKEAILRQMEEKnRQLQERLELAEQKLQQTMRKAETLPEVE----AELAQRIAALTKAEERHgNIEERMR 336
Cdd:PTZ00121 1142 AEEARKAEDAKRVEIARKAEDA-RKAEEARKAEDAKKAEAARKAEEVRKAEelrkAEDARKAEAARKAEEER-KAEEARK 1219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 337 HLEgqlEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAAL--EEKnvliQESENFRKNLEESLH 414
Cdd:PTZ00121 1220 AED---AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIkaEEA----RKADELKKAEEKKKA 1292
|
250
....*....|.
gi 1907075644 415 DKERLAEEIEK 425
Cdd:PTZ00121 1293 DEAKKAEEKKK 1303
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
170-436 |
2.28e-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: 51.07 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 170 QIVELQELLEKQNYEMAQMKERLTALssrvgeVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEErittleKRYL 249
Cdd:pfam13868 81 QIEEREQKRQEEYEEKLQEREQMDEI------VERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKE------LEKE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 250 SAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLElaeQKLQQTMRKAETLPEVEAELAQ-------RIAALT 322
Cdd:pfam13868 149 EEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLR---AQQEKAQDEKAERDELRAKLYQeeqerkeRQKERE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 323 KAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEknvLIQES 402
Cdd:pfam13868 226 EAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEK---QIEER 302
|
250 260 270
....*....|....*....|....*....|....*
gi 1907075644 403 E-NFRKNLEESLHDKERLAEEIEKLRSELDQMKMR 436
Cdd:pfam13868 303 EeQRAAEREEELEEGERLREEEAERRERIEEERQK 337
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
27-358 |
2.36e-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: 51.22 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 27 QEFAALTKELNA-------CREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQA--QSPSGVSSEV 97
Cdd:pfam19220 69 RELAGLTRRLSAaegeleeLVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRAleEENKALREEA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 98 EVLKALKSLFEHHKALDEKIVALREQNVHIQRKMVSSEGSTESEHlegmEAGQKVHEKRLSNGSIDSTDDTSQIVELQEL 177
Cdd:pfam19220 149 QAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAEL----TRRLAELETQLDATRARLRALEGQLAAEQAE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 178 LEK----QNYEMAQMKERLTALSSRVgeveqEAETARkdLIKTEEMNTkyqrdirEAMAQKEDMEERITTLEKRYLSAQR 253
Cdd:pfam19220 225 RERaeaqLEEAVEAHRAERASLRMKL-----EALTAR--AAATEQLLA-------EARNQLRDRDEAIRAAERRLKEASI 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 254 ESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLElaeqklqqTMRKAetlpeveaeLAQRIAALTKAEERHGNIEE 333
Cdd:pfam19220 291 ERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAE--------MLTKA---------LAAKDAALERAEERIASLSD 353
|
330 340 350
....*....|....*....|....*....|..
gi 1907075644 334 RMRHLEGQ-------LEEKNQELQRARQREKM 358
Cdd:pfam19220 354 RIAELTKRfeveraaLEQANRRLKEELQRERA 385
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
42-395 |
2.44e-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: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 42 QLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSL-RMTVVKRQAQSPSGvsSEVEVLKALKSLFEHHKALDEKIVAL 120
Cdd:pfam05483 385 ELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLdEKKQFEKIAEELKG--KEQELIFLLQAREKEIHDLEIQLTAI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 121 REQNVHIQRKMVSSEGSTESEHLEGMEAGQKVHEKRLSNGSI--DSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSR 198
Cdd:pfam05483 463 KTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELtqEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEK 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 199 VGEVEQEAETARKDLI-----------KTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMN----- 262
Cdd:pfam05483 543 EMNLRDELESVREEFIqkgdevkckldKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENkalkk 622
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 263 ----------------DKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETL--------PEVEAELAQRI 318
Cdd:pfam05483 623 kgsaenkqlnayeikvNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIadeavklqKEIDKRCQHKI 702
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 319 AALTKAEERHGN-----IEERMRHLeGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLL---TESNERLQLHLKERMA 390
Cdd:pfam05483 703 AEMVALMEKHKHqydkiIEERDSEL-GLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLeieKEEKEKLKMEAKENTA 781
|
....*
gi 1907075644 391 ALEEK 395
Cdd:pfam05483 782 ILKDK 786
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
185-372 |
2.74e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 185 MAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTS----IHD 260
Cdd:COG1196 632 LEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEeereLAE 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 261 MNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNI--------- 331
Cdd:COG1196 712 AEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPVnllaieeye 791
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907075644 332 --EERMRHLEGQLEeknqELQRARQR-----EKMNEEHNKRLSDTVDR 372
Cdd:COG1196 792 elEERYDFLSEQRE----DLEEARETleeaiEEIDRETRERFLETFDA 835
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
24-430 |
3.03e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 24 YTFQEFAALTKELNACREQLLEKEEE----ISELKAERNNTRLLLEHLEclvsrhERSLRMTVVKRQAQSPSGVSSEVEV 99
Cdd:PRK03918 384 LTPEKLEKELEELEKAKEEIEEEISKitarIGELKKEIKELKKAIEELK------KAKGKCPVCGRELTEEHRKELLEEY 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 100 LKALKSLFEHHKALDEKIVALREQNVHIQRKMV-SSEGSTESEHLEgmeagqkvhekrlsngsidstddtsQIVELQELL 178
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKkESELIKLKELAE-------------------------QLKELEEKL 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 179 EKQNYEMAQMKER-LTALSSRVGEVEQEAETARKDLIKTEEMNTKyqrdIREAMAQKEDMEERITTLEKRYLSAQREstS 257
Cdd:PRK03918 513 KKYNLEELEKKAEeYEKLKEKLIKLKGEIKSLKKELEKLEELKKK----LAELEKKLDELEEELAELLKELEELGFE--S 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 258 IHDMNDKLE---------NELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlpeveaELAQRIAALTK--AEE 326
Cdd:PRK03918 587 VEELEERLKelepfyneyLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE-------ELRKELEELEKkySEE 659
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 327 RHGNIEERMRHLEGQLEEKNQELqrarqrekmneEHNKRLSDTVDRLLTEsnerlqlhLKERMAALEEKnvlIQESENFR 406
Cdd:PRK03918 660 EYEELREEYLELSRELAGLRAEL-----------EELEKRREEIKKTLEK--------LKEELEEREKA---KKELEKLE 717
|
410 420
....*....|....*....|....
gi 1907075644 407 KNLEeslhDKERLAEEIEKLRSEL 430
Cdd:PRK03918 718 KALE----RVEELREKVKKYKALL 737
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
152-428 |
5.31e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.11 E-value: 5.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 152 VHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDL------IKTEEMNTKYQR 225
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLnlvqtaLRQQEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 226 DIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELA----------------------------------- 270
Cdd:PRK04863 356 DLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLAdyqqaldvqqtraiqyqqavqalerakqlcglpdl 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 271 ---NKEAILRQMEEKNRQLQERLELAEQKLQ-------------QTMRKAetLPEVEAELAQRIA--ALTKAEErHGNIE 332
Cdd:PRK04863 436 tadNAEDWLEEFQAKEQEATEELLSLEQKLSvaqaahsqfeqayQLVRKI--AGEVSRSEAWDVAreLLRRLRE-QRHLA 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 333 ERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDrllteSNERLQLHLKERMAALEEknvLIQESENFRKNLEES 412
Cdd:PRK04863 513 EQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLD-----DEDELEQLQEELEARLES---LSESVSEARERRMAL 584
|
330
....*....|....*.
gi 1907075644 413 LHDKERLAEEIEKLRS 428
Cdd:PRK04863 585 RQQLEQLQARIQRLAA 600
|
|
| SAM_superfamily |
cd09487 |
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
927-978 |
6.08e-06 |
|
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.
Pssm-ID: 188886 [Multi-domain] Cd Length: 56 Bit Score: 44.54 E-value: 6.08e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1907075644 927 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGI 978
Cdd:cd09487 4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
166-430 |
6.23e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 50.74 E-value: 6.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 166 DDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVE----QEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERI 241
Cdd:pfam02463 159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKlqelKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 242 TTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAA- 320
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKe 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 321 ----LTKAEERHGNIEERMRHLEGQLEEKN---QELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALE 393
Cdd:pfam02463 319 sekeKKKAEKELKKEKEEIEELEKELKELEikrEAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
|
250 260 270
....*....|....*....|....*....|....*..
gi 1907075644 394 EKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSEL 430
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEE 435
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
279-432 |
6.27e-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: 6.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 279 MEEKNRQLqERLELAEQKLQQTMRKAETLP----EVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQ 354
Cdd:COG1579 2 MPEDLRAL-LDLQELDSELDRLEHRLKELPaelaELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 355 R--------------------EKMNEEHNKRLSDTVDRLltESNERLQLHLKERMAALEEKnvLIQESENFRKNLEESLH 414
Cdd:COG1579 81 QlgnvrnnkeyealqkeieslKRRISDLEDEILELMERI--EELEEELAELEAELAELEAE--LEEKKAELDEELAELEA 156
|
170
....*....|....*...
gi 1907075644 415 DKERLAEEIEKLRSELDQ 432
Cdd:COG1579 157 ELEELEAEREELAAKIPP 174
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
170-327 |
6.93e-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: 6.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 170 QIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEE--MNTKYQRDIREAMAQKEDMEERITTLEKR 247
Cdd:COG1579 32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlGNVRNNKEYEALQKEIESLKRRISDLEDE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 248 YLsaqrestsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQtmRKAETLPEVEAELAQRIAALTKAEER 327
Cdd:COG1579 112 IL--------------ELMERIEELEEELAELEAELAELEAELEEKKAELDE--ELAELEAELEELEAEREELAAKIPPE 175
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
201-433 |
9.21e-06 |
|
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: 49.74 E-value: 9.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 201 EVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRylsaqrestsihdmndkleneLANKEAILRQME 280
Cdd:pfam05557 17 EKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKR---------------------EAEAEEALREQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 281 EKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHgnieermrhlEGQLEEKNQELQRARQR----- 355
Cdd:pfam05557 76 ELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRA----------ELELQSTNSELEELQERldllk 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 356 ------EKMNEEHNKRLSdtvdrLLTESNERLQ----------------LHLKERMAALEEKNVLIQESENFRKNLEESL 413
Cdd:pfam05557 146 akaseaEQLRQNLEKQQS-----SLAEAEQRIKelefeiqsqeqdseivKNSKSELARIPELEKELERLREHNKHLNENI 220
|
250 260
....*....|....*....|
gi 1907075644 414 HDKERLAEEIEKLRSELDQM 433
Cdd:pfam05557 221 ENKLLLKEEVEDLKRKLERE 240
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
253-430 |
1.05e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 253 RESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQ--QTMRKAETLPEVEAELAQRIAALTKAEERHGN 330
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 331 IEERMRHLEGQLEEKNQELQRARQRekMNEEHNKRLSDTVDRLltesnERLQlhlkERMAALEEKNVLIQESENFRKNLE 410
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQ--LSLATEEELQDLAEEL-----EELQ----QRLAELEEELEEAQEELEELEEEL 229
|
170 180
....*....|....*....|
gi 1907075644 411 ESLHDKERLAEEIEKLRSEL 430
Cdd:COG4717 230 EQLENELEAAALEERLKEAR 249
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
266-432 |
1.31e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 266 ENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlpEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEK 345
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN---ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 346 NQELQRARQREKMNEE--HNKRLSDTVDRL-----LTESNERLQLHLKERMAALEEKnvliqesenfRKNLEESLHDKER 418
Cdd:COG3883 92 ARALYRSGGSVSYLDVllGSESFSDFLDRLsalskIADADADLLEELKADKAELEAK----------KAELEAKLAELEA 161
|
170
....*....|....
gi 1907075644 419 LAEEIEKLRSELDQ 432
Cdd:COG3883 162 LKAELEAAKAELEA 175
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
47-439 |
1.73e-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: 49.05 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 47 EEEISELKAERNNTRLLLEHLECLVsrHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEhhkALDEKIVALrEQNVH 126
Cdd:pfam10174 177 GEEDWERTRRIAEAEMQLGHLEVLL--DQKEKENIHLREELHRRNQLQPDPAKTKALQTVIE---MKDTKISSL-ERNIR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 127 ---IQRKMVSSEGSTES----EHLEGMEAgQKVHEKRLSNgSIDSTDD-----TSQIVELQ---ELLEKQNYEMAQ---- 187
Cdd:pfam10174 251 dleDEVQMLKTNGLLHTedreEEIKQMEV-YKSHSKFMKN-KIDQLKQelskkESELLALQtklETLTNQNSDCKQhiev 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 188 MKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQ-----------------RDIREAMAQKE--------------- 235
Cdd:pfam10174 329 LKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTkqlqdlteekstlageiRDLKDMLDVKErkinvlqkkienlqe 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 236 ---DMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAIL-RQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVE 311
Cdd:pfam10174 409 qlrDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIeRLKEQREREDRERLEELESLKKENKDLKEKVSALQ 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 312 AELAQRIAALTKAEERHGN-------IEERMRHLEGQLEEKNQE-------LQRARQRE---KMNEEHNKRLS---DTVD 371
Cdd:pfam10174 489 PELTEKESSLIDLKEHASSlassglkKDSKLKSLEIAVEQKKEEcsklenqLKKAHNAEeavRTNPEINDRIRlleQEVA 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 372 RLLTESN------ERLQLHLKE----------RMAALEE-------------KNVLIQESENFRKN---LEESLHDK--- 416
Cdd:pfam10174 569 RYKEESGkaqaevERLLGILREvenekndkdkKIAELESltlrqmkeqnkkvANIKHGQQEMKKKGaqlLEEARRREdnl 648
|
490 500 510
....*....|....*....|....*....|..
gi 1907075644 417 ---------ERLAEEIEKLRSELDQMKMRTGS 439
Cdd:pfam10174 649 adnsqqlqlEELMGALEKTRQELDATKARLSS 680
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
27-434 |
1.77e-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: 49.20 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 27 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAqspsgVSSEVEVLKALK-S 105
Cdd:TIGR00618 386 QQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAA-----ITCTAQCEKLEKiH 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 106 LFEHHKALDEKIVALRE-QNVHIQRKMVSSEGSTESEHLEGME---AGQKVHEKRLSNGSIDSTDDTSQIVELQELLEKQ 181
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTkEQIHLQETRKKAVVLARLLELQEEPcplCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQL 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 182 NYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQREStsiHDM 261
Cdd:TIGR00618 541 ETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQ---HAL 617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 262 NDKLENELANKEAIL--RQMEEKNRQL-----QERLELAEQKLQQTMRKAETLPEveAELAQRIAALTKAEERHGN---- 330
Cdd:TIGR00618 618 LRKLQPEQDLQDVRLhlQQCSQELALKltalhALQLTLTQERVREHALSIRVLPK--ELLASRQLALQKMQSEKEQltyw 695
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 331 ------IEERMRHLEGQLEEKNQELQR------------ARQREKMNEEHNK--RLSDTVDRLLTESNERLQLHLKERMA 390
Cdd:TIGR00618 696 kemlaqCQTLLRELETHIEEYDREFNEienassslgsdlAAREDALNQSLKElmHQARTVLKARTEAHFNNNEEVTAALQ 775
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1907075644 391 ALEEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQMK 434
Cdd:TIGR00618 776 TGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDIL 819
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
116-303 |
2.03e-05 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 46.82 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 116 KIVALREQNVHIQRKMvsSEGSTESEHLEGMeagQKVHEKRLSNgsIDSTDDtsqivELQELLEKQNYEMAQMKERLTAL 195
Cdd:pfam15619 12 KIKELQNELAELQSKL--EELRKENRLLKRL---QKRQEKALGK--YEGTES-----ELPQLIARHNEEVRVLRERLRRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 196 SSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREA-MAQKEDMEERITTLEKRYLSAQREstsIHDMNDKLEN------- 267
Cdd:pfam15619 80 QEKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKnLAEREELQKKLEQLEAKLEDKDEK---IQDLERKLELenksfrr 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907075644 268 ELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK 303
Cdd:pfam15619 157 QLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKERE 192
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
262-366 |
2.23e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.67 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 262 NDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAEL---AQRIA--ALTKAEERHGNIEERMR 336
Cdd:PRK00409 515 KEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLleeAEKEAqqAIKEAKKEADEIIKELR 594
|
90 100 110
....*....|....*....|....*....|...
gi 1907075644 337 HLE--GQLEEKNQELQRARQR-EKMNEEHNKRL 366
Cdd:PRK00409 595 QLQkgGYASVKAHELIEARKRlNKANEKKEKKK 627
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
30-436 |
2.25e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 30 AALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMtvvkrqaqspsgvssevevlkalkslfeh 109
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV----------------------------- 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 110 hKALDEKIVALREQnvhiqrkmvssegstesehLEGMEAGQkvhekrlsngsidstddtSQIVELQELLEKQNYEMAQMK 189
Cdd:COG4913 664 -ASAEREIAELEAE-------------------LERLDASS------------------DDLAALEEQLEELEAELEELE 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 190 ERLTALSSRVGEVEQEAETArkdlikteemntkyQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIhdmnDKLENEL 269
Cdd:COG4913 706 EELDELKGEIGRLEKELEQA--------------EEELDELQDRLEAAEDLARLELRALLEERFAAALG----DAVEREL 767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 270 AnkeailRQMEEKNRQLQERLELAEQKLQQTMRKA-ETLPEVEAELAQRIAALTKAEERHGNIEERmrhlegQLEEKNQE 348
Cdd:COG4913 768 R------ENLEERIDALRARLNRAEEELERAMRAFnREWPAETADLDADLESLPEYLALLDRLEED------GLPEYEER 835
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 349 LQRARQR----------EKMNEEHN---KRLsDTVDRLLTESN----ERLQLHLKERM--AALEEKNVLIQESEN-FRKN 408
Cdd:COG4913 836 FKELLNEnsiefvadllSKLRRAIReikERI-DPLNDSLKRIPfgpgRYLRLEARPRPdpEVREFRQELRAVTSGaSLFD 914
|
410 420
....*....|....*....|....*...
gi 1907075644 409 LEESLHDKERLAEEIEKLRSELDQMKMR 436
Cdd:COG4913 915 EELSEARFAALKRLIERLRSEEEESDRR 942
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
173-355 |
3.15e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 48.15 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 173 ELQELLEKQNyEMAQMKERLT-------ALSSRVGEVEQ-EAEtaRKDLIKTEEMNTKYQRdIREAMAQKED-MEERITT 243
Cdd:COG0497 173 ELEELRADEA-ERARELDLLRfqleeleAAALQPGEEEElEEE--RRRLSNAEKLREALQE-ALEALSGGEGgALDLLGQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 244 LEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQ---ERLELAEQKLQ---QTMRK----AETLPEVEAE 313
Cdd:COG0497 249 ALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEfdpERLEEVEERLAllrRLARKygvtVEELLAYAEE 328
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907075644 314 LAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQR 355
Cdd:COG0497 329 LRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKK 370
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
97-439 |
3.87e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 47.64 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 97 VEVLKALKSLFEHHKALDEKIVALREQNVHIQRKMVSSEGSTESEHLEGMEAGQKVHEKRLSNGSIDST-DDTSQIVEL- 174
Cdd:COG5185 183 GLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTsDKLEKLVEQn 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 175 QELLEKQNYEMAQMKERLTALSS-----------RVGEVEQEAETAR-----KDLIKTEEMNTKYQRDIREA----MAQK 234
Cdd:COG5185 263 TDLRLEKLGENAESSKRLNENANnlikqfentkeKIAEYTKSIDIKKateslEEQLAAAEAEQELEESKRETetgiQNLT 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 235 EDMEERITTLEKRYLSAQRESTSIHDMND------KLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLP 308
Cdd:COG5185 343 AEIEQGQESLTENLEAIKEEIENIVGEVElsksseELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQI 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 309 E--------VEAELAQRIAALTKAEERhgnIEERMRHLEGQLEEKNQELQRARQRE--KMNEEHNKRLSDTVDRLLT--E 376
Cdd:COG5185 423 EelqrqieqATSSNEEVSKLLNELISE---LNKVMREADEESQSRLEEAYDEINRSvrSKKEDLNEELTQIESRVSTlkA 499
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907075644 377 SNERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKERlaEEIEKLRSELDQMKMRTGS 439
Cdd:COG5185 500 TLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILAL--ENLIPASELIQASNAKTDG 560
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
115-434 |
3.95e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 47.54 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 115 EKIVALREQNVHIQRK----MVSSE--GSTESEHLEGM--EAGQKVHEKRLSNG-SIDSTDDT-----SQIVELQELLEK 180
Cdd:pfam06160 92 EELLDDIEEDIKQILEeldeLLESEekNREEVEELKDKyrELRKTLLANRFSYGpAIDELEKQlaeieEEFSQFEELTES 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 181 QNYEMA-----QMKERLTALSSRVGEVEQEAETARKDLikTEEMNtkyqrDIREAMAQkedMEERITTLEkrYLSAQRES 255
Cdd:pfam06160 172 GDYLEArevleKLEEETDALEELMEDIPPLYEELKTEL--PDQLE-----ELKEGYRE---MEEEGYALE--HLNVDKEI 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 256 TSIHDMNDKLENELANKEaiLRQMEEKNRQLQERLElaeqKLQQTMRKaetlpEVEAELaqriaaltKAEERHGNIEERM 335
Cdd:pfam06160 240 QQLEEQLEENLALLENLE--LDEAEEALEEIEERID----QLYDLLEK-----EVDAKK--------YVEKNLPEIEDYL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 336 RHLEGQLEEKNQELQRARQREKMNEEH-------NKRLsDTVDRLLTESNERLQLH------LKERMAALEEKNVLIQES 402
Cdd:pfam06160 301 EHAEEQNKELKEELERVQQSYTLNENElervrglEKQL-EELEKRYDEIVERLEEKevayseLQEELEEILEQLEEIEEE 379
|
330 340 350
....*....|....*....|....*....|....
gi 1907075644 403 -ENFRKNLeESLHDKERLA-EEIEKLRSELDQMK 434
Cdd:pfam06160 380 qEEFKESL-QSLRKDELEArEKLDEFKLELREIK 412
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
30-435 |
3.95e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.86 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 30 AALTKELNACREQLLEKEEEIS-------ELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRqAQSPSGVSSEVEVLKA 102
Cdd:pfam01576 225 AELQAQIAELRAQLAKKEEELQaalarleEETAQKNNALKKIRELEAQISELQEDLESERAAR-NKAEKQRRDLGEELEA 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 103 LKSLFEH---HKALDEKIVALREQNVHIQRKMVSSEGstesehlegmeagqKVHEKRLSNGSIDSTddtSQIVELQELLE 179
Cdd:pfam01576 304 LKTELEDtldTTAAQQELRSKREQEVTELKKALEEET--------------RSHEAQLQEMRQKHT---QALEELTEQLE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 180 KQNYEMAQMKERLTALSSRVGEVEQEAETarkdlIKTEEMNTKYQRDIREAMAQKedmeerittLEKRYLSAQRESTSIH 259
Cdd:pfam01576 367 QAKRNKANLEKAKQALESENAELQAELRT-----LQQAKQDSEHKRKKLEGQLQE---------LQARLSESERQRAELA 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 260 DMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMrkaETLPEveaELAQRIAALTKAEErhgnIEERMRHLE 339
Cdd:pfam01576 433 EKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQ---ELLQE---ETRQKLNLSTRLRQ----LEDERNSLQ 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 340 GQLEEknqELQRARQREKMNEEHNKRLSDTVDRLLTESnerlqlhlkERMAALEE-KNVLIQESENFRKNLEESLHDKER 418
Cdd:pfam01576 503 EQLEE---EEEAKRNVERQLSTLQAQLSDMKKKLEEDA---------GTLEALEEgKKRLQRELEALTQQLEEKAAAYDK 570
|
410
....*....|....*..
gi 1907075644 419 LAEEIEKLRSELDQMKM 435
Cdd:pfam01576 571 LEKTKNRLQQELDDLLV 587
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
174-436 |
4.25e-05 |
|
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: 47.58 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 174 LQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLiktEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQR 253
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQW---ERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 254 ESTSIHdmndklenelANKEAILRQMEEKNRQLQErLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEE-RHGNIE 332
Cdd:pfam07888 109 SSEELS----------EEKDALLAQRAAHEARIRE-LEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEaERKQLQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 333 ERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLH--LKERMAALEEK-NVLIQESENFR 406
Cdd:pfam07888 178 AKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLtqkLTTAHRKEAENeaLLEELRSLQERlNASERKVEGLG 257
|
250 260 270
....*....|....*....|....*....|
gi 1907075644 407 KNLEESLHDKERLAEEIEKLRSELDQMKMR 436
Cdd:pfam07888 258 EELSSMAAQRDRTQAELHQARLQAAQLTLQ 287
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
319-434 |
4.64e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.55 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 319 AALTKAEERHGNIEER-----MRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLlTESNERLQLHLK-----ER 388
Cdd:COG2433 380 EALEELIEKELPEEEPeaereKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEK-DERIERLERELSearseER 458
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1907075644 389 MAALEEKNVLIQESENfrKNLEESLHDKErlaEEIEKLRSELDQMK 434
Cdd:COG2433 459 REIRKDREISRLDREI--ERLERELEEER---ERIEELKRKLERLK 499
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
28-284 |
5.12e-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: 5.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 28 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRhERSLRMTVVKRQAQSpsgVSSEVEVLK-ALKSL 106
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKD-LGEEEQLRVKEKIGE---LEAEIASLErSIAEK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 107 FEHHKALDEKIVALREQNVHIQRKMVSSEGSTESEHL-------EGMEAGQKVHEKRLSNGSIDSTDDTS--QIVELQEL 177
Cdd:TIGR02169 314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKrrdklteEYAELKEELEDLRAELEEVDKEFAETrdELKDYREK 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 178 LEKQNYEMAQMK-------ERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLS 250
Cdd:TIGR02169 394 LEKLKREINELKreldrlqEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD 473
|
250 260 270
....*....|....*....|....*....|....
gi 1907075644 251 AQRESTSIHDMNDKLENELANKEAILRQMEEKNR 284
Cdd:TIGR02169 474 LKEEYDRVEKELSKLQRELAEAEAQARASEERVR 507
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
234-440 |
5.70e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.60 E-value: 5.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 234 KEDMEERITTLEKRYLSAQRESTSIHDmndkLENELANKEAILRQmEEKNRQLQERLELAEQKLQQTMRKAETLPEVEA- 312
Cdd:PRK11281 38 EADVQAQLDALNKQKLLEAEDKLVQQD----LEQTLALLDKIDRQ-KEETEQLKQQLAQAPAKLRQAQAELEALKDDNDe 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 313 ELAQRIAALTkaeerhgnieerMRHLEGQLEEKNQELQRARqrekmneehnKRLSDTVDRLLTESN--ERLQlhlkermA 390
Cdd:PRK11281 113 ETRETLSTLS------------LRQLESRLAQTLDQLQNAQ----------NDLAEYNSQLVSLQTqpERAQ-------A 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1907075644 391 ALEEKNVLIQESENFRKNLEESlhDKERLAEEIEKLRSELD----QMKMRTGSL 440
Cdd:PRK11281 164 ALYANSQRLQQIRNLLKGGKVG--GKALRPSQRVLLQAEQAllnaQNDLQRKSL 215
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
173-401 |
6.33e-05 |
|
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: 45.87 E-value: 6.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 173 ELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKryLSAQ 252
Cdd:pfam06008 27 QLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKE--INEK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 253 RESTSIHDM---NDKLENELANKEAILRQMeeKNRQLQERLELAEQKLqqtmRKAETLPEVEAELAQRIAALTKAeerhg 329
Cdd:pfam06008 105 VATLGENDFalpSSDLSRMLAEAQRMLGEI--RSRDFGTQLQNAEAEL----KAAQDLLSRIQTWFQSPQEENKA----- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 330 nIEERMRHLEGQLEEKNQELQ--------RARQREKMNEEHNKRLSDTVDRLLT--ESNERLQLHLKERMAALEEKNVLI 399
Cdd:pfam06008 174 -LANALRDSLAEYEAKLSDLRellreaaaKTRDANRLNLANQANLREFQRKKEEvsEQKNQLEETLKTARDSLDAANLLL 252
|
..
gi 1907075644 400 QE 401
Cdd:pfam06008 253 QE 254
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
245-426 |
9.88e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 9.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 245 EKRYLSAQREStsihdmndkLENELANkeaiLRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKA 324
Cdd:PRK04863 507 EQRHLAEQLQQ---------LRMRLSE----LEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSES 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 325 EERHGNIEERMRHLEGQLEEKNQELQRARQrekmnEEHNkrLSDTVDRLLTESNERLqlhlkERMAALEE--KNVLIQES 402
Cdd:PRK04863 574 VSEARERRMALRQQLEQLQARIQRLAARAP-----AWLA--AQDALARLREQSGEEF-----EDSQDVTEymQQLLERER 641
|
170 180
....*....|....*....|....
gi 1907075644 403 EnFRKNLEESLHDKERLAEEIEKL 426
Cdd:PRK04863 642 E-LTVERDELAARKQALDEEIERL 664
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
797-861 |
1.04e-04 |
|
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.
Pssm-ID: 425739 Cd Length: 64 Bit Score: 41.49 E-value: 1.04e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907075644 797 QWDGPTVVAWLElWLGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQEM 861
Cdd:pfam00536 2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
173-428 |
1.12e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.48 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 173 ELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLikteemnTKYQRDIREAMAQKEDMEERITTLEKrylsaQ 252
Cdd:COG3096 358 ELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQL-------ADYQQALDVQQTRAIQYQQAVQALEK-----A 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 253 RESTSIHDMN-DKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETL----PEVEAELA-QRIAALTKAEE 326
Cdd:COG3096 426 RALCGLPDLTpENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVckiaGEVERSQAwQTARELLRRYR 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 327 RHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDrllteSNERLQLHLKERMAALEEknvLIQESENFR 406
Cdd:COG3096 506 SQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLD-----AAEELEELLAELEAQLEE---LEEQAAEAV 577
|
250 260
....*....|....*....|..
gi 1907075644 407 KNLEESLHDKERLAEEIEKLRS 428
Cdd:COG3096 578 EQRSELRQQLEQLRARIKELAA 599
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
284-481 |
1.13e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 46.24 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 284 RQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERmrhlegqlEEKNQELQRARQREKMNEEHN 363
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRER--------EELQREEERLVQKEEQLDARA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 364 KRLSDTVDRLLTESN----ERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHD--KERLAEEIEKLRSELD-QMKMR 436
Cdd:PRK12705 98 EKLDNLENQLEEREKalsaRELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAelEEEKAQRVKKIEEEADlEAERK 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907075644 437 TGSLIEPTISRTHIDTSTELRYSVgslVDSQSDYRTTKVIRRPRR 481
Cdd:PRK12705 178 AQNILAQAMQRIASETASDLSVSV---VPIPSDAMKGRIIGREGR 219
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
1005-1075 |
1.18e-04 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 41.10 E-value: 1.18e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907075644 1005 VLVWSNDRVIRWIQAIGLREYANNILESGVHG--SLIALDENFdysslalLLQIPTQNTQARQILEREYNNLL 1075
Cdd:pfam07647 1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGaeLLLRLTLED-------LKRLGITSVGHRRKILKKIQELK 66
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
27-382 |
1.20e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 27 QEFAALTKELNACREQLLEKEEEISElkaernNTRLLLEHLECLVSR----HERSLRmtVVKRQAQSPSGVSSEVEVLKa 102
Cdd:PRK01156 419 QDISSKVSSLNQRIRALRENLDELSR------NMEMLNGQSVCPVCGttlgEEKSNH--IINHYNEKKSRLEEKIREIE- 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 103 lkslfEHHKALDEKIVALREQNVHIQRKMVSsEGSTESEHLEGMEAgqkvhekrlsngsiDSTDDTSQIVELQELLEKQN 182
Cdd:PRK01156 490 -----IEVKDIDEKIVDLKKRKEYLESEEIN-KSINEYNKIESARA--------------DLEDIKIKINELKDKHDKYE 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 183 yemaQMKERLTALssRVGEVEQEaetarkdliKTEEMNTKYQR---DIREAMAQKEDMEERITTLEKRylsAQRESTSIH 259
Cdd:PRK01156 550 ----EIKNRYKSL--KLEDLDSK---------RTSWLNALAVIsliDIETNRSRSNEIKKQLNDLESR---LQEIEIGFP 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 260 DMNDKLENELANKEAILRQMEEKNRQLQErLELAEQKLQQTMrkaETLPEVEAELAQRIAALTKAEERHGNIEERMRHLE 339
Cdd:PRK01156 612 DDKSYIDKSIREIENEANNLNNKYNEIQE-NKILIEKLRGKI---DNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSR 687
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1907075644 340 GQLEEKNQELQRARQREKMNEEHNKRLSDTVdrllTESNERLQ 382
Cdd:PRK01156 688 KALDDAKANRARLESTIEILRTRINELSDRI----NDINETLE 726
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
27-442 |
1.30e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 27 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTvvKRQAQSpsgVSSEVEVLKA-LKS 105
Cdd:TIGR02168 337 EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL--ELQIAS---LNNEIERLEArLER 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 106 LFEHHKALDEKIVALREQNVHIQRKMVSSEGSTESEHLEGMEAGQKVHEKRLSNGSidstddtSQIVELQELLEKQNYEM 185
Cdd:TIGR02168 412 LEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELR-------EELEEAEQALDAAEREL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 186 AQMKERLTALSSRVGEVEQEAETARK----------------DLIKTEEmntKYQRDIREAMAqkedmeERITTLEKRYL 249
Cdd:TIGR02168 485 AQLQARLDSLERLQENLEGFSEGVKAllknqsglsgilgvlsELISVDE---GYEAAIEAALG------GRLQAVVVENL 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 250 SAQRESTSIhdmndkLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAEL--------------- 314
Cdd:TIGR02168 556 NAAKKAIAF------LKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLrkalsyllggvlvvd 629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 315 ----AQRIAALTKAEER-----------HG---------------------NIEERMRHLEGQLEEKNQELQRAR-QREK 357
Cdd:TIGR02168 630 dldnALELAKKLRPGYRivtldgdlvrpGGvitggsaktnssilerrreieELEEKIEELEEKIAELEKALAELRkELEE 709
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 358 MNEEHNK--RLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESENF-------RKNLEESLHDKERLAEEIEKLRS 428
Cdd:TIGR02168 710 LEEELEQlrKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELeaeieelEERLEEAEEELAEAEAEIEELEA 789
|
490
....*....|....
gi 1907075644 429 ELDQMKMRTGSLIE 442
Cdd:TIGR02168 790 QIEQLKEELKALRE 803
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
264-434 |
1.36e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 264 KLENELANKEAILRQMEEKNRQLQERLELAEQKLQqtmrkaetlpEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLE 343
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLE----------AAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 344 E-KNQELQRARQREKmnEEHNKRLSDTVDRLLtesnerlqlhlkERMAALEEKNVLIQESENFRKNLEESL-HDKERLAE 421
Cdd:COG1579 84 NvRNNKEYEALQKEI--ESLKRRISDLEDEIL------------ELMERIEELEEELAELEAELAELEAELeEKKAELDE 149
|
170
....*....|...
gi 1907075644 422 EIEKLRSELDQMK 434
Cdd:COG1579 150 ELAELEAELEELE 162
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
201-427 |
2.39e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.21 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 201 EVEQEAET-----ARKDLIKTEEMNTKYQRD---IREAMA----QKEDMEERITTLEKRYLSAQRE----STSIHDMNDK 264
Cdd:PRK04778 90 EAEELNDKfrfrkAKHEINEIESLLDLIEEDieqILEELQelleSEEKNREEVEQLKDLYRELRKSllanRFSFGPALDE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 265 LENELANKEAILRQMEEKN-----RQLQERLELAEQKLQQTMRKAETLPEVEAELAQRI-AALTKAEE------------ 326
Cdd:PRK04778 170 LEKQLENLEEEFSQFVELTesgdyVEAREILDQLEEELAALEQIMEEIPELLKELQTELpDQLQELKAgyrelveegyhl 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 327 RHGNIEERMRHLEGQLEEKNQELQR---ARQREKmNEEHNKRLSDTVDRLLTEsnerlqlhlkerMAAleeKNVLIQESE 403
Cdd:PRK04778 250 DHLDIEKEIQDLKEQIDENLALLEEldlDEAEEK-NEEIQERIDQLYDILERE------------VKA---RKYVEKNSD 313
|
250 260
....*....|....*....|....
gi 1907075644 404 NFRKNLEESLHDKERLAEEIEKLR 427
Cdd:PRK04778 314 TLPDFLEHAKEQNKELKEEIDRVK 337
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
227-434 |
2.45e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 227 IREAMAQKEDMEERITTLEKRYlsaqresTSIHDMNDKLEnELANKEAILRQMEEKNRQLQE-RLELAEQKLQQTMRKAE 305
Cdd:COG4913 213 VREYMLEEPDTFEAADALVEHF-------DDLERAHEALE-DAREQIELLEPIRELAERYAAaRERLAELEYLRAALRLW 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 306 TLpEVEAELAQriAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQRekmneehnkRLSDTVDRL--LTESNERLQL 383
Cdd:COG4913 285 FA-QRRLELLE--AELEELRAELARLEAELERLEARLDALREELDELEAQ---------IRGNGGDRLeqLEREIERLER 352
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907075644 384 HLKERMAALEEKNVLIQ--------ESENFRKNLEESLHDKERLAEEIEKLRSELDQMK 434
Cdd:COG4913 353 ELEERERRRARLEALLAalglplpaSAEEFAALRAEAAALLEALEEELEALEEALAEAE 411
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
32-433 |
2.73e-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: 45.17 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 32 LTKELNACREQL---LEKEEEISELKAERNNTRLLLEH-LECLVSRHERSLRmTVVKRQAQSPSGVSSEVEVLKALKSLF 107
Cdd:pfam01576 297 LGEELEALKTELedtLDTTAAQQELRSKREQEVTELKKaLEEETRSHEAQLQ-EMRQKHTQALEELTEQLEQAKRNKANL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 108 EHHKAldekivALREQNVHIQRKMVS-SEGSTESEHlegmeaGQKVHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEma 186
Cdd:pfam01576 376 EKAKQ------ALESENAELQAELRTlQQAKQDSEH------KRKKLEGQLQELQARLSESERQRAELAEKLSKLQSE-- 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 187 qmkerLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKrylsaqrESTSIHDMndkLE 266
Cdd:pfam01576 442 -----LESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLED-------ERNSLQEQ---LE 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 267 NELANKEAILRQMEEKNRQLQErlelAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERM----RHLEGQL 342
Cdd:pfam01576 507 EEEEAKRNVERQLSTLQAQLSD----MKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLektkNRLQQEL 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 343 EEKNQELQRARQREKMNEEHNKRLsdtvDRLLTESNERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEE 422
Cdd:pfam01576 583 DDLLVDLDHQRQLVSNLEKKQKKF----DQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERT 658
|
410
....*....|.
gi 1907075644 423 IEKLRSELDQM 433
Cdd:pfam01576 659 NKQLRAEMEDL 669
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
287-425 |
2.81e-04 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 42.29 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 287 QERLELAEQKLQQtmrkaetLPEVEAELAQRIAALTKaeeRHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRL 366
Cdd:pfam12718 13 QERAEELEEKVKE-------LEQENLEKEQEIKSLTH---KNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNENLTRKI 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907075644 367 sdtvdRLLTESNERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIEK 425
Cdd:pfam12718 83 -----QLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEE 136
|
|
| pepcterm_ChnLen |
TIGR03007 |
polysaccharide chain length determinant protein, PEP-CTERM locus subfamily; Members of this ... |
147-316 |
3.17e-04 |
|
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: 44.66 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 147 EAGQKVHEKRLSNG---SIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLI-----KTEE 218
Cdd:TIGR03007 179 AAENRLKAFKQENGgilPDQEGDYYSEISEAQEELEAARLELNEAIAQRDALKRQLGGEEPVLLAGSSVANseldgRIEA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 219 MNTKYQR----------DIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQE 288
Cdd:TIGR03007 259 LEKQLDAlrlrytdkhpDVIATKREIAQLEEQKEEEGSAKNGGPERGEIANPVYQQLQIELAEAEAEIASLEARVAELTA 338
|
170 180
....*....|....*....|....*...
gi 1907075644 289 RLElaeqklqQTMRKAETLPEVEAELAQ 316
Cdd:TIGR03007 339 RIE-------RLESLLRTIPEVEAELTQ 359
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
169-321 |
3.32e-04 |
|
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: 42.97 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 169 SQIVELQELLEKQNYEMA-------QMKERLTALSSRVGEVEQEAETARKD---LIKTEEMNTKYQRDIREAMAQKEDME 238
Cdd:pfam13851 33 EEIAELKKKEERNEKLMSeiqqenkRLTEPLQKAQEEVEELRKQLENYEKDkqsLKNLKARLKVLEKELKDLKWEHEVLE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 239 ERITTLEKRY--LSAQREStSIHDMNDKLENE---LANK-EAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEA 312
Cdd:pfam13851 113 QRFEKVERERdeLYDKFEA-AIQDVQQKTGLKnllLEKKlQALGETLEKKEAQLNEVLAAANLDPDALQAVTEKLEDVLE 191
|
....*....
gi 1907075644 313 ELAQRIAAL 321
Cdd:pfam13851 192 SKNQLIKDL 200
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
181-411 |
3.89e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 181 QNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQR--DIREAMAQKEDMEERITTLEKRYLSAQREstsi 258
Cdd:COG3206 159 EAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQknGLVDLSEEAKLLLQQLSELESQLAEARAE---- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 259 hdmndklenelankeaiLRQMEEKNRQLQERLELAEQKLQQTMRkAETLPEVEAELAQRIAALTKAEERHGNIEERMRHL 338
Cdd:COG3206 235 -----------------LAEAEARLAALRAQLGSGPDALPELLQ-SPVIQQLRAQLAELEAELAELSARYTPNHPDVIAL 296
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907075644 339 EGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESENFRKNLEE 411
Cdd:COG3206 297 RAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES 369
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
200-451 |
4.19e-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: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 200 GEVEQEAETARKDLIKTEE--MNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIhDMNDKLENELANKEAILR 277
Cdd:pfam02463 142 GKIEIIAMMKPERRLEIEEeaAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKL-KEQAKKALEYYQLKEKLE 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 278 QMEEKNRQLQERLELAEQK---------LQQTMRKAETLPEVEAELAQRIAALTKAEER-HGNIEERMRHLEGQLEEKNQ 347
Cdd:pfam02463 221 LEEEYLLYLDYLKLNEERIdllqellrdEQEEIESSKQEIEKEEEKLAQVLKENKEEEKeKKLQEEELKLLAKEEEELKS 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 348 ELQRARQREKMNEEhNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIEKLR 427
Cdd:pfam02463 301 ELLKLERRKVDDEE-KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKK 379
|
250 260
....*....|....*....|....
gi 1907075644 428 SELDQMKMRTGSLIEPTISRTHID 451
Cdd:pfam02463 380 KLESERLSSAAKLKEEELELKSEE 403
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
135-429 |
4.62e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 135 EGSTESEHLEGMEAGQKVHEKRLSNGSiDSTDDTSQIVELQELLE-KQNYEMAQMKERLTALSSRVGEVEQEAETARK-- 211
Cdd:PTZ00121 1143 EEARKAEDAKRVEIARKAEDARKAEEA-RKAEDAKKAEAARKAEEvRKAEELRKAEDARKAEAARKAEEERKAEEARKae 1221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 212 DLIKTEEMNTKYQRDIREAMAQKEDmEERITTLEKRYLSAQRESTSIHDMNDKLENelANKEAILRQMEEKNRQLQERLE 291
Cdd:PTZ00121 1222 DAKKAEAVKKAEEAKKDAEEAKKAE-EERNNEEIRKFEEARMAHFARRQAAIKAEE--ARKADELKKAEEKKKADEAKKA 1298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 292 LAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLE---GQLEEKNQELQRARQREKMNEEHNKRLSD 368
Cdd:PTZ00121 1299 EEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEaakAEAEAAADEAEAAEEKAEAAEKKKEEAKK 1378
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907075644 369 TVDRLLTESNE-RLQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKE--RLAEEIEKLRSE 429
Cdd:PTZ00121 1379 KADAAKKKAEEkKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEekKKADEAKKKAEE 1442
|
|
| SAM_STIM-1,2-like |
cd09504 |
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ... |
798-856 |
4.98e-04 |
|
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like (Stromal interaction molecule) proteins is a putative protein-protein interaction domain. STIM1 and STIM2 human proteins are type I transmembrane proteins. The N-terminal part of them includes "hidden" EF-hand and SAM domains. This region is responsible for sensing changes in store-operated and basal cytoplasmic Ca2+ levels and initiates oligomerization. "Hidden" EF hand and SAM domains have a stable intramolecular association, and the SAM domain is a component that regulates stability within STIM proteins. Destabilization of the EF-SAM association during Ca2+ depletion leads to partial unfolding and aggregation (homooligomerization), thus activating the store-operated Ca2+ entry. Immunoprecipitation analysis indicates that STIM1 and STIM2 can form co-precipitable oligomeric associations in vivo. It was suggested that STIM1 and STIM2 are involved in opposite regulation of store operated channels in plasma membrane.
Pssm-ID: 188903 Cd Length: 74 Bit Score: 39.62 E-value: 4.98e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907075644 798 WDGPTVVAWLELWLGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNPLHRLKLRL 856
Cdd:cd09504 5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
44-434 |
5.04e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.33 E-value: 5.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 44 LEKEEEISElkaernNTRLLLEHLeclVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALksLFEHHKALDEKIVALRE- 122
Cdd:pfam05483 134 LKLEEEIQE------NKDLIKENN---ATRHLCNLLKETCARSAEKTKKYEYEREETRQV--YMDLNNNIEKMILAFEEl 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 123 ----QNVHIQRKMVSSEGSTESEHLEgMEAGQKVH--EKRLSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALS 196
Cdd:pfam05483 203 rvqaENARLEMHFKLKEDHEKIQHLE-EEYKKEINdkEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQD 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 197 SRVGEVEQEAETARKDLiktEEMNTKYQRDIREAMAQKEDM-----------EERITTLEK--------RYLSAQRESTS 257
Cdd:pfam05483 282 ENLKELIEKKDHLTKEL---EDIKMSLQRSMSTQKALEEDLqiatkticqltEEKEAQMEElnkakaahSFVVTEFEATT 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 258 ------IHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNI 331
Cdd:pfam05483 359 csleelLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKE 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 332 EERMRHLEGQlEEKNQELQRARQREKMNEEH-NKRLSDTVDRLLTESNERLQLHLKERMAALEEKNvLIQESENFRKNLE 410
Cdd:pfam05483 439 QELIFLLQAR-EKEIHDLEIQLTAIKTSEEHyLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKE-LTQEASDMTLELK 516
|
410 420 430
....*....|....*....|....*....|.
gi 1907075644 411 ESLHD-------KERLAEEIEKLRSELDQMK 434
Cdd:pfam05483 517 KHQEDiinckkqEERMLKQIENLEEKEMNLR 547
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
263-437 |
5.51e-04 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 42.82 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 263 DKLENELANKEAILRQME------------EKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIaaltkaEERHGN 330
Cdd:cd00176 10 DELEAWLSEKEELLSSTDygddlesveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI------QERLEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 331 IEERMRHLEGQLEEKNQELQRARQREKMNEEH---NKRLSDTVDRLLTESN-------ERLQLHLKERMAALEEKNVLIQ 400
Cdd:cd00176 84 LNQRWEELRELAEERRQRLEEALDLQQFFRDAddlEQWLEEKEAALASEDLgkdlesvEELLKKHKELEEELEAHEPRLK 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907075644 401 ESENFRKNLEESLH--DKERLAEEIEKLRSELDQMKMRT 437
Cdd:cd00176 164 SLNELAEELLEEGHpdADEEIEEKLEELNERWEELLELA 202
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
257-434 |
6.08e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.50 E-value: 6.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 257 SIHDMND---KLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK---------AETLPEVEAELAQRIAALTKA 324
Cdd:COG1842 31 AIRDMEEdlvEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKgredlareaLERKAELEAQAEALEAQLAQL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 325 EERHGNIEERMRHLEGQLEEKNQELQRARQREKMNeEHNKRLSDTVDRLLTESNErlqlhlkERMAALEEKnvliQESEN 404
Cdd:COG1842 111 EEQVEKLKEALRQLESKLEELKAKKDTLKARAKAA-KAQEKVNEALSGIDSDDAT-------SALERMEEK----IEEME 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907075644 405 FRKNLEESLHDKERLAEEIEKLRS------ELDQMK 434
Cdd:COG1842 179 ARAEAAAELAAGDSLDDELAELEAdsevedELAALK 214
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
175-353 |
7.26e-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: 42.43 E-value: 7.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 175 QELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLikteEMNTKYQRDIREAmaqkEDMEERITTLEKRYLSaqre 254
Cdd:cd00176 64 EQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRL----EEALDLQQFFRDA----DDLEQWLEEKEAALAS---- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 255 stsihdmnDKLENELANKEAILRQMEEknrqLQERLELAEQKLQQTMRKAETLPEveaelAQRIAALTKAEERHGNIEER 334
Cdd:cd00176 132 --------EDLGKDLESVEELLKKHKE----LEEELEAHEPRLKSLNELAEELLE-----EGHPDADEEIEEKLEELNER 194
|
170
....*....|....*....
gi 1907075644 335 MRHLEGQLEEKNQELQRAR 353
Cdd:cd00176 195 WEELLELAEERQKKLEEAL 213
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
78-592 |
7.26e-04 |
|
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: 43.88 E-value: 7.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 78 LRMTVVKRQAQSPSG------VSSEVEVLKALKSLFEHHKA----LDEKIVALREQNVHIQRKMVSSEGSTESEHLEGME 147
Cdd:TIGR00606 222 IRDQITSKEAQLESSreivksYENELDPLKNRLKEIEHNLSkimkLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 148 AGQKVHEKRLSNGSidstDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVG------EVEQEAETARKDLIKTEEMNT 221
Cdd:TIGR00606 302 QLNDLYHNHQRTVR----EKERELVDCQRELEKLNKERRLLNQEKTELLVEQGrlqlqaDRHQEHIRARDSLIQSLATRL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 222 KY---------QRDIREAMA-QKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLE 291
Cdd:TIGR00606 378 ELdgfergpfsERQIKNFHTlVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELK 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 292 LAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEErHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNkRLSDTVD 371
Cdd:TIGR00606 458 FVIKELQQLEGSSDRILELDQELRKAERELSKAEK-NSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLN-HHTTTRT 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 372 RLLTESNERLQLHLKERMAALEEKNVLIQESENF--RKNLEESLH----DKERLAEEIEKLRSELDQMKMRTGSLIEPTI 445
Cdd:TIGR00606 536 QMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFpnKKQLEDWLHskskEINQTRDRLAKLNKELASLEQNKNHINNELE 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 446 SRTHIDTSTELR-YSVGSLVDSQSDY-RTTKVIRRPRRGRMGVRRDEPKVKSLGDHEWNRTQQIGVLGSHPFESDTEMSD 523
Cdd:TIGR00606 616 SKEEQLSSYEDKlFDVCGSQDEESDLeRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQE 695
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907075644 524 IDDDdretiFSSMDLLSPSGHSDAQTLAMMLQEQLDAINKEIRLIQEEKESTELRAEEIENRVASVSLE 592
Cdd:TIGR00606 696 FISD-----LQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRD 759
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
111-457 |
7.54e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 7.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 111 KALDEKIVALREQNVHIQRKmvSSEGSTESEHLEGMEAGQKVHEKRLsngsidstDDTSQIVELQELLEkqnyEMAQMKE 190
Cdd:COG4717 74 KELEEELKEAEEKEEEYAEL--QEELEELEEELEELEAELEELREEL--------EKLEKLLQLLPLYQ----ELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 191 RLTALSSRVGEVEQEAET---ARKDLIKTEEMNTKYQRDIREAMAQK-EDMEERITTLEKRYLSAQRESTSIHDMNDKLE 266
Cdd:COG4717 140 ELAELPERLEELEERLEElreLEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 267 NELANKEAILRQMEEKNRQLQERLELAEQK-----------LQQTMRKAETLPEVEAELAQRIAAL--------TKAEER 327
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEERLKEARlllliaaallaLLGLGGSLLSLILTIAGVLFLVLGLlallflllAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 328 HGNIEERMRHLEGQLEEKNQELQRARQREKMNEEhnkrLSDTVDRLLTESNERLQLHLKERMAALEEknVLIQESENFRK 407
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPD----LSPEELLELLDRIEELQELLREAEELEEE--LQLEELEQEIA 373
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907075644 408 NL--------EESLHDKERLAEEIEKLRSELDQMKMRTGSLIEPTISRTHIDTSTELR 457
Cdd:COG4717 374 ALlaeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE 431
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
263-430 |
7.71e-04 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 42.36 E-value: 7.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 263 DKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlPEVEAELAQRIAALTKAEERHG-----------NI 331
Cdd:pfam04012 39 VKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGN--EELAREALAEKKSLEKQAEALEtqlaqqrsaveQL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 332 EERMRHLEGQLEEKNQE-------LQRARQREKMNEehnkrlsdTVDRLLTESNERLQLHLKERMAALEEKNVLIQESEn 404
Cdd:pfam04012 117 RKQLAALETKIQQLKAKknllkarLKAAKAQEAVQT--------SLGSLSTSSATDSFERIEEKIEEREARADAAAELA- 187
|
170 180
....*....|....*....|....*.
gi 1907075644 405 FRKNLEESLHDKERLAEEIEKLRSEL 430
Cdd:pfam04012 188 SAVDLDAKLEQAGIQMEVSEDVLARL 213
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
162-332 |
8.11e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 8.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 162 IDSTDDtsQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIK-------------------------- 215
Cdd:COG3883 39 LDALQA--ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraralyrsggsvsyldvllgsesfsd 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 216 -------TEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQE 288
Cdd:COG3883 117 fldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEA 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907075644 289 RLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIE 332
Cdd:COG3883 197 QLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
219-434 |
8.87e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.14 E-value: 8.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 219 MNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQREstsihdmndkLENELANKEAILRQMEEKNRQLQErleLAEQKLQ 298
Cdd:COG0497 138 LDPDAQRELLDAFAGLEELLEEYREAYRAWRALKKE----------LEELRADEAERARELDLLRFQLEE---LEAAALQ 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 299 qtmrkaetlPEVEAELAQRIAALTKAEERHGNIEERMRHLEGqlEEKN--QELQRARQR-EKMnEEHNKRLSDTVDRL-- 373
Cdd:COG0497 205 ---------PGEEEELEEERRRLSNAEKLREALQEALEALSG--GEGGalDLLGQALRAlERL-AEYDPSLAELAERLes 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 374 ----LTESNERLQLHLK------ERMAALEEK-----------NVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQ 432
Cdd:COG0497 273 alieLEEAASELRRYLDslefdpERLEEVEERlallrrlarkyGVTVEELLAYAEELRAELAELENSDERLEELEAELAE 352
|
..
gi 1907075644 433 MK 434
Cdd:COG0497 353 AE 354
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
27-349 |
1.06e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.27 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 27 QEFAALTKELNACREQLLEKEEEISELKAERNNtrlLLEHLEclvsrhERSLRMTVVKRQAQSPSGVSSEVEVlkALKSL 106
Cdd:pfam10174 373 EEKSTLAGEIRDLKDMLDVKERKINVLQKKIEN---LQEQLR------DKDKQLAGLKERVKSLQTDSSNTDT--ALTTL 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 107 FEhhkALDEK---IVALREQNvhiqrkmvSSEGSTESEHLEGMEAGQKVHEKRLSNGSIDSTDDTSQIVELQE------- 176
Cdd:pfam10174 442 EE---ALSEKeriIERLKEQR--------EREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEhasslas 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 177 -------LLEKQNYEMAQMKERLTALSSRVGEVEQEAETARK-----DLIKTEEMNTKYQRD---------------IRE 229
Cdd:pfam10174 511 sglkkdsKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTnpeinDRIRLLEQEVARYKEesgkaqaeverllgiLRE 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 230 AMAQKEDMEERITTLEKRYLSaQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPE 309
Cdd:pfam10174 591 VENEKNDKDKKIAELESLTLR-QMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQ 669
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1907075644 310 VEAELAQRIAALTKA-EERHGNIE----ERMRHLEGQLEEKNQEL 349
Cdd:pfam10174 670 ELDATKARLSSTQQSlAEKDGHLTnlraERRKQLEEILEMKQEAL 714
|
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
149-509 |
1.11e-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: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 149 GQKVHEK--RLSNGSID----STDDTSQIVELQELLEKQNYEMAQMKERLtALSSRVGEVEQEAETARKDLIKTEEMNTk 222
Cdd:COG5192 415 GKAIAEEtsREDELSFDdsdvSTSDENEDVDFTGKKGAINNEDESDNEEV-AFDSDSQFDESEGNLRWKEGLASKLAYS- 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 223 yQRDIREAMAQKEDMEERITTlEKRYLSAQRESTSIHDMNDKLENElanKEAILRQMEEKNRQLQERLE-LAEQKLQQTM 301
Cdd:COG5192 493 -QSGKRGRNIQKIFYDESLSP-EECIEEYKGESAKSSESDLVVQDE---PEDFFDVSKVANESISSNHEkLMESEFEELK 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 302 RKAETLPEVEAELAQriAALTKAEERHgniEErmrhLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERL 381
Cdd:COG5192 568 KKWSSLAQLKSRFQK--DATLDSIEGE---EE----LIQDDEKGNFEDLEDEENSSDNEMEESRGSSVTAENEESADEVD 638
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 382 QLHLKERMAALEEK---NVLIQESENFRKN-LEESLHDKERLAEEIEKLRSELDQM---------KMRTGSLIEPTISRT 448
Cdd:COG5192 639 YETEREENARKKEElrgNFELEERGDPEKKdVDWYTEEKRKIEEQLKINRSEFETMvpesrvvieGYRAGRYVRIVLSHV 718
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907075644 449 HIDTSTELRYS----VGSLVDSQSDYRTTKV-IRRPRRGRMGVRRDEPKVKSLGdheWNRTQQIGV 509
Cdd:COG5192 719 PLEFVDEFNSRypivLGGLLPAEKEMGIVQGrIKRHRWHKKILKTNDPLIFSVG---WRRFQSIPV 781
|
|
| PRK03992 |
PRK03992 |
proteasome-activating nucleotidase; Provisional |
387-445 |
1.16e-03 |
|
proteasome-activating nucleotidase; Provisional
Pssm-ID: 179699 [Multi-domain] Cd Length: 389 Bit Score: 42.51 E-value: 1.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 387 ERMAALEEKNV-LIQESENFRKNLEESLHDKERLAEEIEKLRSELDqmKMRTGSLIEPTI 445
Cdd:PRK03992 1 ERLEALEERNSeLEEQIRQLELKLRDLEAENEKLERELERLKSELE--KLKSPPLIVATV 58
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
160-343 |
1.17e-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: 42.36 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 160 GSIDSTDDTSQIVELQELLEKQNYEMAQM---------KERLTALSSRVGEVEQEAETARKDLikteemnTKYQRDIrea 230
Cdd:cd22656 82 AQNAGGTIDSYYAEILELIDDLADATDDEeleeakktiKALLDDLLKEAKKYQDKAAKVVDKL-------TDFENQT--- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 231 MAQKEDMEERITTLEKRYlsaQRESTSIHDMN-DKLENELAN-KEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLP 308
Cdd:cd22656 152 EKDQTALETLEKALKDLL---TDEGGAIARKEiKDLQKELEKlNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLT 228
|
170 180 190
....*....|....*....|....*....|....*
gi 1907075644 309 EVEAELAQRIAALTKAEERHGNIEERMRHLEGQLE 343
Cdd:cd22656 229 AADTDLDNLLALIGPAIPALEKLQGAWQAIATDLD 263
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
273-426 |
1.21e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.40 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 273 EAILRQMEEKNRQLQERLELAE---QKLQQTMRKAETLPEVEAELAQRIAALtkaEERHGNIEERMRHLEGQLEEKNQEL 349
Cdd:COG3096 518 RAQLAELEQRLRQQQNAERLLEefcQRIGQQLDAAEELEELLAELEAQLEEL---EEQAAEAVEQRSELRQQLEQLRARI 594
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907075644 350 QRARQREKMNEEHNKRLSdtvdRLLTESNERLQlHLKERMAALEEknVLIQESEnFRKNLEESLHDKERLAEEIEKL 426
Cdd:COG3096 595 KELAARAPAWLAAQDALE----RLREQSGEALA-DSQEVTAAMQQ--LLERERE-ATVERDELAARKQALESQIERL 663
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
170-381 |
1.32e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 170 QIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTlekryl 249
Cdd:pfam01576 890 RIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKS------ 963
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 250 saqrestsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK-AETLPEVEAElaQRIAALTKAEERH 328
Cdd:pfam01576 964 --------------KFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKlKEVLLQVEDE--RRHADQYKDQAEK 1027
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1907075644 329 GNIeeRMRHLEGQLEEKNQELQRAR-QREKMNEEhnkrLSDTvdrllTESNERL 381
Cdd:pfam01576 1028 GNS--RMKQLKRQLEEAEEEASRANaARRKLQRE----LDDA-----TESNESM 1070
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
30-366 |
1.69e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 30 AALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHerslrmtvvkrqaqspSGVSSEVEVLKALKSLFEH 109
Cdd:PRK04863 782 AAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSH----------------LAVAFEADPEAELRQLNRR 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 110 HKALDEKIVALREQNVHIQRKMVSSEgstesehlEGMEAGQKVhekrlsNGSIDSTDDTSQIVELQELLEkQNYEMAQMK 189
Cdd:PRK04863 846 RVELERALADHESQEQQQRSQLEQAK--------EGLSALNRL------LPRLNLLADETLADRVEEIRE-QLDEAEEAK 910
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 190 ERLTALSSRVGEVEQEAETARKDliktEEMNTKYQRDIREAMAQKEDMEERITTL----EKR----YLSAQRESTSIHDM 261
Cdd:PRK04863 911 RFVQQHGNALAQLEPIVSVLQSD----PEQFEQLKQDYQQAQQTQRDAKQQAFALtevvQRRahfsYEDAAEMLAKNSDL 986
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 262 NDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALT-----KAEERhgnIEERMR 336
Cdd:PRK04863 987 NEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGvpadsGAEER---ARARRD 1063
|
330 340 350
....*....|....*....|....*....|....*
gi 1907075644 337 HLEGQL----EEKNQ-ELQRARQREKMNEEhNKRL 366
Cdd:PRK04863 1064 ELHARLsanrSRRNQlEKQLTFCEAEMDNL-TKKL 1097
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
26-288 |
1.81e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.58 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 26 FQEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLEclvsrherSLRMTVVKRQAQSPSGVSSEVEVLKALKs 105
Cdd:PLN02939 162 LTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLE--------KLRNELLIRGATEGLCVHSLSKELDVLK- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 106 lfEHHKALDEKIVALREQNVHIQrKMVSSEGSTESEHlEGMEAGQKVHEKRLsngsIDSTDDTSQIVELQ-ELLEKQNYE 184
Cdd:PLN02939 233 --EENMLLKDDIQFLKAELIEVA-ETEERVFKLEKER-SLLDASLRELESKF----IVAQEDVSKLSPLQyDCWWEKVEN 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 185 MAQMKERLTALSSRVGEVEQEAETARKDLIKTEEmntkyqrDIREAMAQK------EDMEERITTLEKRYlsaQRESTSI 258
Cdd:PLN02939 305 LQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEA-------SLKEANVSKfssykvELLQQKLKLLEERL---QASDHEI 374
|
250 260 270
....*....|....*....|....*....|..
gi 1907075644 259 HDMNDKLENELANKEAILRQM--EEKNRQLQE 288
Cdd:PLN02939 375 HSYIQLYQESIKEFQDTLSKLkeESKKRSLEH 406
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
927-982 |
2.15e-03 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 37.63 E-value: 2.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907075644 927 EWLPSLGLPQYRSYFMECLVD-ARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 982
Cdd:pfam07647 11 DWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLK-RLGITSVGHRRKILKKIQELK 66
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
55-349 |
2.15e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.52 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 55 AERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPsgvssevEVLKALKSLFEH-HKALDEKIVALReQNVHIQRKMVS 133
Cdd:pfam12128 247 QQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQ-------ETSAELNQLLRTlDDQWKEKRDELN-GELSAADAAVA 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 134 SEgsteSEHLEGMEAGQKVHEKrlsngsidstDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETaRKDL 213
Cdd:pfam12128 319 KD----RSELEALEDQHGAFLD----------ADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNR-RRSK 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 214 IKtEEMNTKYQRDIREAMAQKEDMEERITTLEKRYlsAQRESTSIHDMN-DKLENELANKEAILRQMEEKNR-------- 284
Cdd:pfam12128 384 IK-EQNNRDIAGIKDKLAKIREARDRQLAVAEDDL--QALESELREQLEaGKLEFNEEEYRLKSRLGELKLRlnqatatp 460
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907075644 285 -------QLQERLELAEQKLQQTMRKAETLpevEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQEL 349
Cdd:pfam12128 461 elllqleNFDERIERAREEQEAANAEVERL---QSELRQARKRRDQASEALRQASRRLEERQSALDELELQL 529
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
189-434 |
2.19e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 189 KERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENE 268
Cdd:TIGR04523 67 EEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 269 LANKEAILRQMEEKNRQLQERLELAEQKL----QQTMRKAETLPEVEAELAQ---RIAALTKAEERHGNIEERMRHLEGQ 341
Cdd:TIGR04523 147 IKKKEKELEKLNNKYNDLKKQKEELENELnlleKEKLNIQKNIDKIKNKLLKlelLLSNLKKKIQKNKSLESQISELKKQ 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 342 -------LEEKNQELQrarqrekmneEHNKRLSDTVDRL--LTESNERLQLHLKERMAALEEKNVLIQESENFRKNLEES 412
Cdd:TIGR04523 227 nnqlkdnIEKKQQEIN----------EKTTEISNTQTQLnqLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSE 296
|
250 260
....*....|....*....|....
gi 1907075644 413 LHD--KERLAEEIEKLRSELDQMK 434
Cdd:TIGR04523 297 ISDlnNQKEQDWNKELKSELKNQE 320
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
204-361 |
2.32e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 204 QEAETARKDLIKTEEmntkyqrdiREAMAQKEDMEerittlekryLSAQREstsIHDMNDKLENELANKEAILRQMEEKN 283
Cdd:PRK12704 34 KEAEEEAKRILEEAK---------KEAEAIKKEAL----------LEAKEE---IHKLRNEFEKELRERRNELQKLEKRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 284 RQLQERLElaeqklqqtmRKAETLPEVEAELAQRIAALTKAEErhgNIEERmrhlEGQLEEK----NQELQR-------- 351
Cdd:PRK12704 92 LQKEENLD----------RKLELLEKREEELEKKEKELEQKQQ---ELEKK----EEELEELieeqLQELERisgltaee 154
|
170
....*....|..
gi 1907075644 352 ARQR--EKMNEE 361
Cdd:PRK12704 155 AKEIllEKVEEE 166
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
276-389 |
2.38e-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: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 276 LRQMEEKNRQLQ-ERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQ 354
Cdd:COG0542 413 LDELERRLEQLEiEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEK 492
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907075644 355 R----EKMNEEHNKRLSDTVD-----------------RLLTESNERLqLHLKERM 389
Cdd:COG0542 493 ElaelEEELAELAPLLREEVTeediaevvsrwtgipvgKLLEGEREKL-LNLEEEL 547
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
284-424 |
2.89e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 40.25 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 284 RQLQERLELAEQKLQQTMRKAETLP----------------EVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ 347
Cdd:pfam12072 27 AKIGSAEELAKRIIEEAKKEAETKKkealleakeeihklraEAERELKERRNELQRQERRLLQKEETLDRKDESLEKKEE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 348 ELQRARQREKMNEEHNKRLSDTVDRLLTESNERLqlhlkERMAAL---EEKNVLIQESEnfrknlEESLHDKERLAEEIE 424
Cdd:pfam12072 107 SLEKKEKELEAQQQQLEEKEEELEELIEEQRQEL-----ERISGLtseEAKEILLDEVE------EELRHEAAVMIKEIE 175
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
268-580 |
3.24e-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: 41.65 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 268 ELANKEAILRQMEEKNRQLQERLELAEQklqQTMRKAETlpeveaelaQRIAALTKAEERHGniEERMRHLEG-QLEEKN 346
Cdd:pfam17380 294 EKMEQERLRQEKEEKAREVERRRKLEEA---EKARQAEM---------DRQAAIYAEQERMA--MERERELERiRQEERK 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 347 QELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHL----------KERMAALEEKNVLIQ----ESENFRKNL--- 409
Cdd:pfam17380 360 RELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELeaarkvkileEERQRKIQQQKVEMEqiraEQEEARQREvrr 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 410 --EESLHDKERLAEE-------IEKLRSELDQMKMRTGSLIEPTISRTHIDtstELRYSVgslVDSQSDYRTTKVIRRPR 480
Cdd:pfam17380 440 leEERAREMERVRLEeqerqqqVERLRQQEEERKRKKLELEKEKRDRKRAE---EQRRKI---LEKELEERKQAMIEEER 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 481 RGRMGVRRDEPKVKSLGDHEWNRTQQigvlgshpfesDTEMSDIDDDDRETIFSSMDLLSPSghsdaqtlammlQEQLDA 560
Cdd:pfam17380 514 KRKLLEKEMEERQKAIYEEERRREAE-----------EERRKQQEMEERRRIQEQMRKATEE------------RSRLEA 570
|
330 340
....*....|....*....|
gi 1907075644 561 INKEIRLIQEEKESTELRAE 580
Cdd:pfam17380 571 MEREREMMRQIVESEKARAE 590
|
|
| BAR_SNX7 |
cd07666 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 7; BAR domains are dimerization, lipid ... |
178-369 |
3.40e-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: 40.66 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 178 LEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQrDIREAMAQK----EDMEERITTLEKRYLSAQR 253
Cdd:cd07666 14 LTAQAWELSSHKKQGPGLLSRMGQTVKAVASSVRGVKNRPEEFTEMN-EYVEAFSQKinvlDKISQRIYKEQREYFEELK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 254 ESTSIHDMNDKLENELANK--------EAILRQMEEKNRQLQERLE-------LAEQKLQQTMRKAEtlpEVEAELAQRI 318
Cdd:cd07666 93 EYGPIYTLWSASEEELADSlkgmasciDRCCKATDKRMKGLSEQLLpviheyvLYSETLMGVIKRRD---QIQAELDSKV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1907075644 319 AALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDT 369
Cdd:cd07666 170 EALANKKADRDLLKEEIEKLEDKVECANNALKADWERWKQNMQTDLRSAFT 220
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
173-366 |
3.86e-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: 40.79 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 173 ELQELLEKQNYEMAQMKERLTALSSRvgEVEQEAETARKDLIKTEEmntKYQRDIRE-AMAQKEDMEERITTLEKRYLSA 251
Cdd:pfam15558 35 EELRRRDQKRQETLERERRLLLQQSQ--EQWQAEKEQRKARLGREE---RRRADRREkQVIEKESRWREQAEDQENQRQE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 252 QRESTSIHDMNDKLENE--LANKEAILRQMEEKNR-QLQERLELAEQKLQQ--------------------TMRKAETLP 308
Cdd:pfam15558 110 KLERARQEAEQRKQCQEqrLKEKEEELQALREQNSlQLQERLEEACHKRQLkereeqkkvqennlsellnhQARKVLVDC 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907075644 309 EVEAELAQRIAAL----TKAEERH-GNIEERMRHLEGQLEEKNQELQRARQR-EKMNEEHNKRL 366
Cdd:pfam15558 190 QAKAEELLRRLSLeqslQRSQENYeQLVEERHRELREKAQKEEEQFQRAKWRaEEKEEERQEHK 253
|
|
| SAM_superfamily |
cd09487 |
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
803-860 |
4.17e-03 |
|
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.
Pssm-ID: 188886 [Multi-domain] Cd Length: 56 Bit Score: 36.45 E-value: 4.17e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907075644 803 VVAWLElWLGMPaWYVAACRANVKSGAIMSALSDTEIQrEIGISNPLHRLKLRLAIQE 860
Cdd:cd09487 2 VAEWLE-SLGLE-QYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAIQR 56
|
|
| PLC-beta_C |
pfam08703 |
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ... |
173-316 |
4.45e-03 |
|
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of phospholipase C beta.
Pssm-ID: 462571 [Multi-domain] Cd Length: 176 Bit Score: 39.28 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 173 ELQELLEKQNYEMAQMKER-LTALSSRVGEVEQEAETARKDLIKteEMNTKYQRDIREAMAQKEDmeERITTLEKRYLSA 251
Cdd:pfam08703 13 ELLELREEQYEQEKKRKEQhLTEQIQKLKELAREKQAAELKALK--ESSESEKKEMKKKLERKRL--ESIQEAKKRTSDK 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907075644 252 QRESTSIHDMNDKLENELANkeaILRQMEEKNRQLQERLELAEQKLQQTMRkaETLPEVEAELAQ 316
Cdd:pfam08703 89 AAQERLKKEINNSHIQEVVQ---SIKQLEEKQKRRQEKLEEKQAECLQQIK--EEEPQLQAELNA 148
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
251-428 |
4.81e-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: 40.90 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 251 AQRESTSIHDMNDKLENELAnkEAILRQMEEKNRQLQERLELAEQKLQQTMRKaetlpEVEAELAQRIAALTKaeerhgn 330
Cdd:pfam09731 314 IERALEKQKEELDKLAEELS--ARLEEVRAADEAQLRLEFEREREEIRESYEE-----KLRTELERQAEAHEE------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 331 ieermrHLEGQLEEKNQELQRARQR---EKMNEEHNKRLSDtVDRLLTESNERLQLhLKERMAALEEKN---VLIQESEN 404
Cdd:pfam09731 380 ------HLKDVLVEQEIELQREFLQdikEKVEEERAGRLLK-LNELLANLKGLEKA-TSSHSEVEDENRkaqQLWLAVEA 451
|
170 180
....*....|....*....|....*.
gi 1907075644 405 FRKNLEESLHDKER--LAEEIEKLRS 428
Cdd:pfam09731 452 LRSTLEDGSADSRPrpLVRELKALKE 477
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
30-274 |
5.49e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 30 AALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLrmtvvkrqaqspsgvsseVEVLKALKSLFEH 109
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI------------------AALARRIRALEQE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 110 HKALDEKIVALREQNVHIQRKMvssegSTESEHLEGMEAGQKVHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEMAQMK 189
Cdd:COG4942 78 LAALEAELAELEKEIAELRAEL-----EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 190 ERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDM----EERITTLEKRYLSAQRESTSIHDMNDKL 265
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLlarlEKELAELAAELAELQQEAEELEALIARL 232
|
....*....
gi 1907075644 266 ENELANKEA 274
Cdd:COG4942 233 EAEAAAAAE 241
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
232-353 |
5.67e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.33 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 232 AQKEDMEERITTLEKRYLSAQREstsihdmNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVE 311
Cdd:PRK09039 74 QGNQDLQDSVANLRASLSAAEAE-------RSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQI 146
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1907075644 312 AELAQRIAAL--------TKAEERHGNIEERMRHLEGQLEEKNQELQRAR 353
Cdd:PRK09039 147 AALRRQLAALeaaldaseKRDRESQAKIADLGRRLNVALAQRVQELNRYR 196
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
163-434 |
5.89e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.88 E-value: 5.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 163 DSTDDTSQIVELQEL-LEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEE-- 239
Cdd:pfam05557 111 NELSELRRQIQRAELeLQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIvk 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 240 -------RITTLEKRyLSAQRE-----STSIHDmNDKLENELANKEAILRQME---EKNRQLQERLELAEQKLQQ----- 299
Cdd:pfam05557 191 nskselaRIPELEKE-LERLREhnkhlNENIEN-KLLLKEEVEDLKRKLEREEkyrEEAATLELEKEKLEQELQSwvkla 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 300 -----TMRKAETLPEVEAELAQRIAALTkaeERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLl 374
Cdd:pfam05557 269 qdtglNLRSPEDLSRRIEQLQQREIVLK---EENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRL- 344
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 375 tesNERLQLHLKERmaaleekNVLIQESENFRKNLEESLHDkERLAEEIEKLRSELDQMK 434
Cdd:pfam05557 345 ---QRRVLLLTKER-------DGYRAILESYDKELTMSNYS-PQLLERIEEAEDMTQKMQ 393
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
157-432 |
6.49e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.81 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 157 LSNGSIDSTD-DTSQIVelQELLEKQNYEMAQMKERLTALssrvgeveQEAETARKDLIKTEEMNTKYQRDIREAMAQKE 235
Cdd:PRK10929 13 LSWGAYAATApDEKQIT--QELEQAKAAKTPAQAEIVEAL--------QSALNWLEERKGSLERAKQYQQVIDNFPKLSA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 236 DMEERITTLEKRYLSAqRESTSIHDMNDKL---ENELANKEAILRQMEEKNRQLQERLELAEQK-------LQQTMRKAE 305
Cdd:PRK10929 83 ELRQQLNNERDEPRSV-PPNMSTDALEQEIlqvSSQLLEKSRQAQQEQDRAREISDSLSQLPQQqtearrqLNEIERRLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 306 TLPEVEAELAQRIAALTKAEE--RHGNIEErmrhLE-GQLEEKN-QELQRARqrekmNEEHNKRlSDTVDRLLTESNERL 381
Cdd:PRK10929 162 TLGTPNTPLAQAQLTALQAESaaLKALVDE----LElAQLSANNrQELARLR-----SELAKKR-SQQLDAYLQALRNQL 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1907075644 382 Q-LHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQ 432
Cdd:PRK10929 232 NsQRQREAERALESTELLAEQSGDLPKSIVAQFKINRELSQALNQQAQRMDL 283
|
|
| SAM_SARM1-like_repeat1 |
cd09501 |
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
927-971 |
6.89e-03 |
|
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of SARM1-like adaptor proteins is a protein-protein interaction domain. SARM1-like proteins contain two tandem SAM domains. SARM1-like proteins are involved in TLR (Toll-like receptor) signaling. They are responsible for targeted localization of the whole protein to post-synaptic regions of axons. In humans SARM1 expression is detected in kidney and liver.
Pssm-ID: 188900 [Multi-domain] Cd Length: 69 Bit Score: 36.51 E-value: 6.89e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1907075644 927 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHR 971
Cdd:cd09501 11 TWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLR 55
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
27-271 |
6.96e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.39 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 27 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRmtVVKRQAQSpsgVSSEVEVL-KALKS 105
Cdd:TIGR04523 419 QEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLK--VLSRSINK---IKQNLEQKqKELKS 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 106 LFEHHKALDEKIVALREQNVHIQRKMVSSEGSTESEHLEGMEAGQKVHEKrlsNGSIDSTDDTSQIVELQELLEKQNYEM 185
Cdd:TIGR04523 494 KEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL---EDELNKDDFELKKENLEKEIDEKNKEI 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 186 AQMKERLTALSSRVGEVEQEA---ETARKDLIKTEEMNTKYQ----RDIREAMAQKEDMEERITTLEKRYLSAQRESTSI 258
Cdd:TIGR04523 571 EELKQTQKSLKKKQEEKQELIdqkEKEKKDLIKEIEEKEKKIssleKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQI 650
|
250
....*....|...
gi 1907075644 259 HDMNDKLENELAN 271
Cdd:TIGR04523 651 KETIKEIRNKWPE 663
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
268-436 |
7.40e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.46 E-value: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 268 ELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ 347
Cdd:PRK12705 40 QEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSAREL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 348 EL--QRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESENfRKNLEESLhdkERLAEEIEK 425
Cdd:PRK12705 120 ELeeLEKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKA-QNILAQAM---QRIASETAS 195
|
170
....*....|....*..
gi 1907075644 426 LRS------ELDQMKMR 436
Cdd:PRK12705 196 DLSvsvvpiPSDAMKGR 212
|
|
| DUF4472 |
pfam14739 |
Domain of unknown function (DUF4472); This family is specific to the Chordates. Some members ... |
174-269 |
8.10e-03 |
|
Domain of unknown function (DUF4472); This family is specific to the Chordates. Some members also carry Kinesin-motor domains at their N-terminus, Kinesin, pfam00225.
Pssm-ID: 464291 [Multi-domain] Cd Length: 107 Bit Score: 37.28 E-value: 8.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 174 LQELLEKQNYEMaqmKERLTALSSRVGEVEQEAETARKDLIKTEEmntkyqrDIREAMAQKEDMEERITTLEKRYLSAQR 253
Cdd:pfam14739 22 LREQYEAEKFEL---KNKLLNLENRVLELELRLEKAAEEIQDLRE-------RLRELEDDRRELAEEFVALKKNYQALSK 91
|
90
....*....|....*.
gi 1907075644 254 ESTSIHDMNDKLENEL 269
Cdd:pfam14739 92 ELEAEVAKNQELSLEL 107
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
164-434 |
8.25e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.51 E-value: 8.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 164 STDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKdliKTEEMNTKyqrdIREAMAQKEDMEERITT 243
Cdd:COG1340 3 TDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNA---QVKELREE----AQELREKRDELNEKVKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 244 LEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLqERLElaeqKLQQTMrkaETLPEVEAELAQRIAALTK 323
Cdd:COG1340 76 LKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEI-ERLE----WRQQTE---VLSPEEEKELVEKIKELEK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 324 -AEERhgnieERMRHLEGQLEEKNQELQRARqrEKMNEEHNKrlsdtvdrlLTESNERLQlHLKERMAALeeknvlIQES 402
Cdd:COG1340 148 eLEKA-----KKALEKNEKLKELRAELKELR--KEAEEIHKK---------IKELAEEAQ-ELHEEMIEL------YKEA 204
|
250 260 270
....*....|....*....|....*....|..
gi 1907075644 403 ENFRKNLEESLHDKERLAEEIEKLRSELDQMK 434
Cdd:COG1340 205 DELRKEADELHKEIVEAQEKADELHEEIIELQ 236
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
265-432 |
9.59e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 39.21 E-value: 9.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 265 LENELANKEAILRQmEEKNRQLQERLELAEQKLQQTMRKAETL-----------------PEVEAELAQRIAALTKAEER 327
Cdd:pfam12795 22 LQQALSLLDKIDAS-KQRAAAYQKALDDAPAELRELRQELAALqakaeaapkeilaslslEELEQRLLQTSAQLQELQNQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 328 HGNIEERMRHLEGQLEEKNQELQRARQREkmnEEHNKRLSDTVDRLLTESNERlQLHLKERMAALEEKNVLI---QESEN 404
Cdd:pfam12795 101 LAQLNSQLIELQTRPERAQQQLSEARQRL---QQIRNRLNGPAPPGEPLSEAQ-RWALQAELAALKAQIDMLeqeLLSNN 176
|
170 180 190
....*....|....*....|....*....|...
gi 1907075644 405 FRKNLEESLHD-----KERLAEEIEKLRSELDQ 432
Cdd:pfam12795 177 NRQDLLKARRDlltlrIQRLEQQLQALQELLNE 209
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
258-448 |
9.64e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 9.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 258 IHDMndkLENELANK-EAILRQMEEKNRQLQERLELAEQKLQQtmrkaetLPEVEAELAQRIAALTKAEERHGNIEERMR 336
Cdd:COG4717 43 IRAM---LLERLEKEaDELFKPQGRKPELNLKELKELEEELKE-------AEEKEEEYAELQEELEELEEELEELEAELE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 337 HLEGQLEEKNQELQRARQREKMnEEHNKRLSDtvdrlltesnerlqlhLKERMAALEEKnvliqesenfRKNLEESLHDK 416
Cdd:COG4717 113 ELREELEKLEKLLQLLPLYQEL-EALEAELAE----------------LPERLEELEER----------LEELRELEEEL 165
|
170 180 190
....*....|....*....|....*....|..
gi 1907075644 417 ERLAEEIEKLRSELDQMKMRTGSLIEPTISRT 448
Cdd:COG4717 166 EELEAELAELQEELEELLEQLSLATEEELQDL 197
|
|
| MAP65_ASE1 |
pfam03999 |
Microtubule associated protein (MAP65/ASE1 family); |
173-433 |
9.68e-03 |
|
Microtubule associated protein (MAP65/ASE1 family);
Pssm-ID: 427641 [Multi-domain] Cd Length: 477 Bit Score: 39.99 E-value: 9.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 173 ELQELLEKQNYEMAQMKERLTALSSRVGEVE----QEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRY 248
Cdd:pfam03999 6 HLHVIWQEIGFSEDKRLQILSRLKDHIKEFYtdalSEENDKEQRILQSIADLRAEAAILCLYMRNRLLHEERDPFEPKKG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 249 LSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQErlELAEQKLQQTmrkAETLPEVE--AELAQRIAALTKAEE 326
Cdd:pfam03999 86 MSLLQKEKKLDTQLEHLRKEKAPRLAEIKELLEQLQQLCE--ELGEEPLPLL---IDPLPSLEelESFRKHLENLRNEKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 327 RH--------GNIEERMRHLEGQL-----------EEKNQELQR------ARQREKMNEEHNKRlSDTVDRLLTESNE-- 379
Cdd:pfam03999 161 RRleevnelkKQIKLLMEELDLVPgtdfeedllceSEDNFCLSRenidklRKLIKQLEEQKAER-EEKIDDLREKILElw 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075644 380 -RLQLHLKERMAALEEKNVLIQESenfRKNLEESLH-----DKERLAEEIEKLRSELDQM 433
Cdd:pfam03999 240 nRLQVPQEEQESFVRENNSLSQDT---IDALREELQrleelKKKNIKKLIEDLRVEIEEL 296
|
|
| |
