|
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 ... |
1013-1084 |
3.75e-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: 154.01 E-value: 3.75e-44
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535318 1013 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1084
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 ... |
804-874 |
7.58e-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: 153.10 E-value: 7.58e-44
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462535318 804 FAQWDGPTVVAWLELWLGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 874
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 ... |
928-993 |
1.14e-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: 1.14e-43
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462535318 928 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 993
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 ... |
932-991 |
2.01e-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: 2.01e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 932 WIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 991
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 ... |
811-869 |
4.33e-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: 104.61 E-value: 4.33e-27
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462535318 811 TVVAWLELWLGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 869
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 ... |
1021-1082 |
7.44e-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: 98.38 E-value: 7.44e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535318 1021 RVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNN 1082
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 ... |
1013-1084 |
1.33e-18 |
|
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188969 Cd Length: 72 Bit Score: 80.95 E-value: 1.33e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535318 1013 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1084
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 ... |
805-869 |
5.91e-17 |
|
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrin contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved into interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188963 Cd Length: 70 Bit Score: 76.34 E-value: 5.91e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462535318 805 AQWDGPTVVAWLELWLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 869
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 ... |
927-991 |
1.41e-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: 1.41e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462535318 927 DMNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLrVHLKMVDSFHRTSLQYGIMCLK 991
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 ... |
927-991 |
1.78e-16 |
|
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188966 Cd Length: 65 Bit Score: 74.75 E-value: 1.78e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462535318 927 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 991
Cdd:cd09567 1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
175-447 |
2.46e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.14 E-value: 2.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 175 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLikteemntkyqrdiREAMAQKEDMEERITTLEKRYL 254
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE--------------YELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 255 SAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQtmrKAETLPEVEAELAQRIAALTKAEERHG 334
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE---AEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 335 NIEERMRHLEGQLEEKNQELQRARQREkmnEEHNKRLSDTVDRLLTESNERLQLHLKERmAALEEKNVLIQESETFRKNL 414
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERL---ERLEEELEELEEALAELEEEEEEEEEALE-EAAEEEAELEEEEEALLELL 465
|
250 260 270
....*....|....*....|....*....|...
gi 2462535318 415 EESLHDKERLAEEIEKLRSELDQLKMRTGSLIE 447
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| SAM_liprin-beta1,2_repeat3 |
cd09569 |
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ... |
1013-1084 |
2.48e-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: 71.72 E-value: 2.48e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535318 1013 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1084
Cdd:cd09569 1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
173-440 |
3.05e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 81.26 E-value: 3.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 173 TSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKR 252
Cdd:TIGR02168 711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 253 YLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEER 332
Cdd:TIGR02168 791 IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 333 hgnIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERL-QLHLKERMAALEEKNVLIQESE 408
Cdd:TIGR02168 871 ---LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELrreLEELREKLaQLELRLEGLEVRIDNLQERLSE 947
|
250 260 270
....*....|....*....|....*....|..
gi 2462535318 409 TFRKNLEESLHDKERLAEEIEKLRSELDQLKM 440
Cdd:TIGR02168 948 EYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7-387 |
3.26e-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: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 7 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRmtvvkrqaqspsgvssevevlkALKSL 86
Cdd:TIGR02168 691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE----------------------QLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 87 FEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQnvhIQRkmASSEGSTESEHLEGMEPGQKVHEKRLSNGS 166
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ---IEQ--LKEELKALREALDELRAELTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 167 IDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERI 246
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 247 TTLEKRYLSAQRESTSIHDMNDKLENELAnkeailrQMEEKNRQLQERL-ELAEQKLQQTMRKAETLPEVEAELAQRIAA 325
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLE-------GLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462535318 326 LTKAEERHGNI-----------EERMRHLEGQLEeknqELQRARQR-----EKMNEEHNKRLSDTVDRLltesNERLQ 387
Cdd:TIGR02168 977 LENKIKELGPVnlaaieeyeelKERYDFLTAQKE----DLTEAKETleeaiEEIDREARERFKDTFDQV----NENFQ 1046
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
194-447 |
4.66e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 80.49 E-value: 4.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 194 KERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENE 273
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 274 LANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpevEAELAQRIAALTKAEERH-------GNIEERMRHLEGQ 346
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL---KEELKALREALDELRAELtllneeaANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 347 LEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLHLKER-------MAALEEKNVLIQESETFRKNLEE 416
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELeelIEELESELEALLNERasleealALLRSELEELSEELRELESKRSE 912
|
250 260 270
....*....|....*....|....*....|.
gi 2462535318 417 SLHDKERLAEEIEKLRSELDQLKMRTGSLIE 447
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEGLEVRIDNLQE 943
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
169-441 |
6.59e-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: 80.10 E-value: 6.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 169 STDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITT 248
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 249 LEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTmrkAETLPEVEAELAQRIAALTK 328
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL---REALDELRAELTLLNEEAAN 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 329 AEERHGNIEERMRHLEGQLEEKNQELQRAR-QREKMNEEHNKrlsdtVDRLLTESNERLQLHLKERMAALEEKNVLIQES 407
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSeDIESLAAEIEE-----LEELIEELESELEALLNERASLEEALALLRSEL 896
|
250 260 270
....*....|....*....|....*....|....
gi 2462535318 408 ETFRKNLEESLHDKERLAEEIEKLRSELDQLKMR 441
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKLAQLELR 930
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
8-495 |
1.04e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 79.31 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 8 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLrmtvvkrqaqspsgvsSEVEVLKALKSLF 87
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERR----------------EELETLEAEIEDL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 88 EHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREqnvhiqrkMASSEGSTESEHLEGMEPGQKVHEKRLSNGSI 167
Cdd:PRK02224 264 RETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG--------LDDADAEAVEARREELEDRDEELRDRLEECRV 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 168 DSTDETSQIVELqellekqnyemaqmKERLAALSSRVGEVEQEAETARKDLIKTEEmntkyqrDIREAMAQKEDMEERIT 247
Cdd:PRK02224 336 AAQAHNEEAESL--------------REDADDLEERAEELREEAAELESELEEARE-------AVEDRREEIEELEEEIE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 248 TLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQklqqtMRKAETLPEVEAEL--AQRIAA 325
Cdd:PRK02224 395 ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA-----LLEAGKCPECGQPVegSPHVET 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 326 LTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLS--DTVDRLLTESNERLQlHLKERMAAL-EEKNV 402
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIE-EKRERAEELrERAAE 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 403 LIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLiePTIpRTHLDTSAELRYSVGSLVDSQSDYRTTKVIR 482
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL--ERI-RTLLAAIADAEDEIERLREKREALAELNDER 625
|
490
....*....|...
gi 2462535318 483 RPRRGRMGVRRDE 495
Cdd:PRK02224 626 RERLAEKRERKRE 638
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
80-433 |
1.17e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 79.33 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 80 LKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHE 159
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 160 KRlsngsidstdetSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQK 239
Cdd:TIGR02168 780 AE------------AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 240 EDMEERITTLEKRYLSAQREStsihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQqtmrkaetlpEVEAEL 319
Cdd:TIGR02168 848 EELSEDIESLAAEIEELEELI-------EELESELEALLNERASLEEALALLRSELEELSEELR----------ELESKR 910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 320 AQRIAALTKAEERHGNIEERMRHLEGQLEEKnqeLQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLhLKERMAALEE 399
Cdd:TIGR02168 911 SELRRELEELREKLAQLELRLEGLEVRIDNL---QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR-LENKIKELGP 986
|
330 340 350
....*....|....*....|....*....|....*
gi 2462535318 400 KNVL-IQESETFRKNLEESLHDKERLAEEIEKLRS 433
Cdd:TIGR02168 987 VNLAaIEEYEELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
20-439 |
2.36e-14 |
|
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: 78.19 E-value: 2.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 20 REQLLEKEEEISELKAERNNTRLLLEHLECLVsrHERSLRMTVVKRQAqspSGVSSEVEVLKAlkslfEHhkaldEKVRE 99
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRL--DELSQELSDASRKI---GEIEKEIEQLEQ-----EE-----EKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 100 RLRVSLERVSALEEELAAANQEIVALREQnvhIQRKMAssegstesehlegmepgqKVHEKRLSNGSIDSTDETSQIVEL 179
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELEAR---IEELEE------------------DLHKLEEALNDLEARLSHSRIPEI 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 180 QELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARkdliktEEMNTKyQRDIREAMAQKEDMEERITTLEKRYlsaqre 259
Cdd:TIGR02169 797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE------KEIQEL-QEQRIDLKEQIKSIEKEIENLNGKK------ 863
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 260 stsihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpEVEAELAQRIAALTKAeeRHGNIEER 339
Cdd:TIGR02169 864 --------EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL-EAQIEKKRKRLSELKA--KLEALEEE 932
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 340 MRHLE---GQLEEKNQELQRARQREKMNEEhnkrlsdtvdrlltesnerlqlhLKERMAALEEKNVL-IQESETFRKNLE 415
Cdd:TIGR02169 933 LSEIEdpkGEDEEIPEEELSLEDVQAELQR-----------------------VEEEIRALEPVNMLaIQEYEEVLKRLD 989
|
410 420
....*....|....*....|....*..
gi 2462535318 416 ESLHDKERLAEE---IEKLRSELDQLK 439
Cdd:TIGR02169 990 ELKEKRAKLEEErkaILERIEEYEKKK 1016
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
927-991 |
5.46e-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: 5.46e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462535318 927 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 991
Cdd:pfam00536 1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
88-447 |
1.48e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 75.36 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 88 EHHKALDEKVRER-LRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEgstesehlegmepgqkvhekrlsngs 166
Cdd:COG1196 213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELE-------------------------- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 167 idstdetSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERI 246
Cdd:COG1196 267 -------AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 247 TTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAAL 326
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 327 TKAEERhgnIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNvliqe 406
Cdd:COG1196 420 EEELEE---LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA----- 491
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2462535318 407 setfRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIE 447
Cdd:COG1196 492 ----RLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV 528
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
196-439 |
2.21e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.09 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 196 RLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELA 275
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 276 NKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRI----AALTKAEERHGNIEERMRHLEGQLEEKN 351
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELesleAELEELEAELEELESRLEELEEQLETLR 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 352 QELQRARQREKMNEEHNKRLSDTVDRlLTESNERLQLHLKERMAALEEKNV--LIQESETFRKNLEESLHDKERLAEEIE 429
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEARLER-LEDRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQEELERLEEALE 464
|
250
....*....|
gi 2462535318 430 KLRSELDQLK 439
Cdd:TIGR02168 465 ELREELEEAE 474
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
175-445 |
3.21e-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: 74.71 E-value: 3.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 175 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYL 254
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 255 SAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQqtmrkaetlpEVEAELAQRIAALTKAEERHG 334
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE----------ELEAELEELESRLEELEEQLE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 335 NIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALE-EKNVLIQESETFRKN 413
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEeELEELQEELERLEEA 462
|
250 260 270
....*....|....*....|....*....|..
gi 2462535318 414 LEESLHDKERLAEEIEKLRSELDQLKMRTGSL 445
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQARLDSL 494
|
|
| SAM_liprin-beta1,2_repeat1 |
cd09563 |
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
804-868 |
1.65e-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: 63.40 E-value: 1.65e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462535318 804 FAQWDGPTVVAWL-ELWLGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQ 868
Cdd:cd09563 1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7-435 |
2.09e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.01 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 7 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEvevLKALKSL 86
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE---LKELQAE 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 87 FEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEgsTESEHLEGMEPGQK--VHEKRLSN 164
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE--RLQENLEGFSEGVKalLKNQSGLS 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 165 G---------SIDSTDET------------------SQIVELQELLEKQNYEMAQMKE----RLAALSSRVGEVEQEAET 213
Cdd:TIGR02168 520 GilgvlseliSVDEGYEAaieaalggrlqavvvenlNAAKKAIAFLKQNELGRVTFLPldsiKGTEIQGNDREILKNIEG 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 214 ARKDLIKTEEMNTKYQR-------------DIREAMAQ--KEDMEERITTLE-----KRYLSAQRESTSIHDMNDKlENE 273
Cdd:TIGR02168 600 FLGVAKDLVKFDPKLRKalsyllggvlvvdDLDNALELakKLRPGYRIVTLDgdlvrPGGVITGGSAKTNSSILER-RRE 678
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 274 LANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAA----LTKAEERHGNIEERMRHLEGQLEE 349
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAlrkdLARLEAEVEQLEERIAQLSKELTE 758
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 350 KNQELQRARQREKMNEEHNKRLSD---TVDRLLTESNERLQLhLKERMAALEEK----NVLIQESETFRKNLEESLHDKE 422
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAeieELEAQIEQLKEELKA-LREALDELRAEltllNEEAANLRERLESLERRIAATE 837
|
490
....*....|...
gi 2462535318 423 RLAEEIEKLRSEL 435
Cdd:TIGR02168 838 RRLEDLEEQIEEL 850
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
226-437 |
2.15e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.89 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 226 TKYQRDIREAMAQKEDMEERIT-------TLEKRY--LSAQRESTSIHdmnDKLENELANKEAILRQMEEknRQLQERLE 296
Cdd:COG1196 168 SKYKERKEEAERKLEATEENLErledilgELERQLepLERQAEKAERY---RELKEELKELEAELLLLKL--RELEAELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 297 LAEQKLQQTMRKAETLpevEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVD 376
Cdd:COG1196 243 ELEAELEELEAELEEL---EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462535318 377 RLLTEsNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQ 437
Cdd:COG1196 320 ELEEE-LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
10-437 |
3.60e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.86 E-value: 3.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 10 AALTKELNACREQL---LEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVvkrqaqspSGVSSEVEVLKALKSL 86
Cdd:PRK03918 168 GEVIKEIKRRIERLekfIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL--------EKLEKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 87 FEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQnvhIQRKMASSEGSTESEHLEGMEPGQKVHEKRLSNGS 166
Cdd:PRK03918 240 IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK---VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 167 IDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNT-----------KYQRDIREA 235
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERlkkrltgltpeKLEKELEEL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 236 MAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLEN--------------------------ELANKEAILRQMEEKNR 289
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelteehrkelleeytaELKRIEKELKEIEEKER 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 290 QLQERLELAEQKLQQ-----TMRK-AETLPEVEAELAQ-RIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREK 362
Cdd:PRK03918 477 KLRKELRELEKVLKKeseliKLKElAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKK 556
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462535318 363 MNEEHNKRLsDTVDRLLTESNERLQLHLKERMAALEEKnvlIQESETFRK---NLEESLHDKERLAEEIEKLRSELDQ 437
Cdd:PRK03918 557 KLAELEKKL-DELEEELAELLKELEELGFESVEELEER---LKELEPFYNeylELKDAEKELEREEKELKKLEEELDK 630
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
161-445 |
4.70e-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: 70.87 E-value: 4.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 161 RLSNGSIDSTDETSQIVELQELLEKqnyemaqMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKE 240
Cdd:TIGR02169 661 APRGGILFSRSEPAELQRLRERLEG-------LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 241 DMEERITTLEKRYLSAQRESTSIHDMNDKLENELAnkeailrQMEEKNRQLQERLELAEQKLQQtmrkaETLPEVEAEla 320
Cdd:TIGR02169 734 KLKERLEELEEDLSSLEQEIENVKSELKELEARIE-------ELEEDLHKLEEALNDLEARLSH-----SRIPEIQAE-- 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 321 qriaaLTKAEERHGNIEERMRHLEGQLEEKNQELQRArqREKMNEEHNKRlsdtvdRLLTESNERLQLHLKERMAALEEK 400
Cdd:TIGR02169 800 -----LSKLEEEVSRIEARLREIEQKLNRLTLEKEYL--EKEIQELQEQR------IDLKEQIKSIEKEIENLNGKKEEL 866
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2462535318 401 NVLIQESETFRKNLEESLHDkerLAEEIEKLRSELDQLKMRTGSL 445
Cdd:TIGR02169 867 EEELEELEAALRDLESRLGD---LKKERDELEAQLRELERKIEEL 908
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
75-366 |
8.08e-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: 70.10 E-value: 8.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 75 SEVEVLKALKSLFEHHKALDEKVRERLrvslERVSALEEELAAANQEIVAL-REQNVHIQRKMASSEGSTES--EHLEGM 151
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELE----KRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASleRSIAEK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 152 EPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRD 231
Cdd:TIGR02169 314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 232 IREAmaqKEDMEERITTLEKRYLSAQRESTSIHDMNdkleNELANKEAILRQMEEKNRQLQERLELAEQKLQQTmrkaet 311
Cdd:TIGR02169 394 LEKL---KREINELKRELDRLQEELQRLSEELADLN----AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL------ 460
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2462535318 312 lpeveaelaqrIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEE 366
Cdd:TIGR02169 461 -----------AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
171-447 |
8.39e-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: 70.09 E-value: 8.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 171 DETSQIVELQELLEKQNYEMAQMKERLA-------ALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDME 243
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEelqkelyALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 244 ERITTLEKRYLSAQRESTSihdmndkLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpevEAELAQRI 323
Cdd:TIGR02168 337 EELAELEEKLEELKEELES-------LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL---NNEIERLE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 324 AALTKAEERHGNIEERMRHLEGQLEEKNQELQRAR--QREKMNEEHNKRLSDTVDRLLTESNERLQlhLKERMAALEEKN 401
Cdd:TIGR02168 407 ARLERLEDRRERLQQEIEELLKKLEEAELKELQAEleELEEELEELQEELERLEEALEELREELEE--AEQALDAAEREL 484
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2462535318 402 VLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIE 447
Cdd:TIGR02168 485 AQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIS 530
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
6-441 |
3.23e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.78 E-value: 3.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 6 LQEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLEclvsRHERSLRMTVvkRQAQSPSGVSSEVEVLKALKS 85
Cdd:PRK03918 230 VKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK----KEIEELEEKV--KELKELKEKAEEYIKLSEFYE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 86 LFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTES-EHLEGMEPGQKVHEKRLSN 164
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyEEAKAKKEELERLKKRLTG 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 165 GSIDSTDETSQIV-----ELQELLEKQNYEMAQMKERLAALSSRVGEVEQE-----------AETARKDLIK--TEEMNt 226
Cdd:PRK03918 384 LTPEKLEKELEELekakeEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgrelTEEHRKELLEeyTAELK- 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 227 KYQRDIREAMAQKEDMEERITTLEKrYLSAQRESTSIHDMNDKLEN-ELANKEAILRQMEEKNRQ---LQERLELAEQKL 302
Cdd:PRK03918 463 RIEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQLKElEEKLKKYNLEELEKKAEEyekLKEKLIKLKGEI 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 303 QQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHL----EGQLEEKNQELqrarqrEKMNEEHNkRLSDTVDRL 378
Cdd:PRK03918 542 KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesVEELEERLKEL------EPFYNEYL-ELKDAEKEL 614
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462535318 379 --LTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKE---------RLAEEIEKLRSELDQLKMR 441
Cdd:PRK03918 615 erEEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyeelreeylELSRELAGLRAELEELEKR 688
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
6-363 |
8.39e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 66.33 E-value: 8.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 6 LQEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHE------------RSLRMTVVKRQAQSPSGV 73
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAleaelaelperlEELEERLEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 74 SSEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEgmep 153
Cdd:COG4717 167 ELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE---- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 154 gQKVHEKRLS-------------NGSIDSTDETSQ---------IVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEA 211
Cdd:COG4717 243 -ERLKEARLLlliaaallallglGGSLLSLILTIAgvlflvlglLALLFLLLAREKASLGKEAEELQALPALEELEEEEL 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 212 ETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKnRQL 291
Cdd:COG4717 322 EELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEY-QEL 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 292 QERLELAEQKLQQ------TMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLE--EKNQELQRARQREKM 363
Cdd:COG4717 401 KEELEELEEQLEEllgeleELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEqlEEDGELAELLQELEE 480
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
4-360 |
1.89e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.34 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 4 LFLQEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLEclvSRHERslrmtvvkrqaqspsgvsSEVEVLKAL 83
Cdd:COG1196 229 LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR---LELEE------------------LELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 84 KSLFEHHKALdEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEgstesehlegmepgqkvhekrls 163
Cdd:COG1196 288 AEEYELLAEL-ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE----------------------- 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 164 ngsidstdetSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDME 243
Cdd:COG1196 344 ----------EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 244 ERITTLEKRYLSAQREstsihdmndkLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRI 323
Cdd:COG1196 414 ERLERLEEELEELEEA----------LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
330 340 350
....*....|....*....|....*....|....*..
gi 2462535318 324 AALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQR 360
Cdd:COG1196 484 EELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
5-333 |
2.21e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.08 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 5 FLQEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLEclvsrherslrmtvvkrqaqspsgvsSEVEVLKALK 84
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ--------------------------KELYALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 85 SLFEHHKaldekvrERLRVSLERvsaLEEELAAANQEIVALREQNVHIQRKMASSEgstesehlegmepgqkvhekrlsn 164
Cdd:TIGR02168 298 SRLEQQK-------QILRERLAN---LERQLEELEAQLEELESKLDELAEELAELE------------------------ 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 165 gsidstdetSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEE 244
Cdd:TIGR02168 344 ---------EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 245 RITTLEKRyLSAQRESTSIHDMnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIA 324
Cdd:TIGR02168 415 RRERLQQE-IEELLKKLEEAEL-KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
|
....*....
gi 2462535318 325 ALTKAEERH 333
Cdd:TIGR02168 493 SLERLQENL 501
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
171-436 |
2.66e-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: 63.93 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 171 DETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLE 250
Cdd:pfam19220 45 QAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 251 KRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAE 330
Cdd:pfam19220 125 RQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 331 ERHgniEERMRHLEGQLEEKNQELQRA-RQREKMNEEHNKRLSD-------------TVDRLLTESNERLQlHLKERMAA 396
Cdd:pfam19220 205 DAT---RARLRALEGQLAAEQAERERAeAQLEEAVEAHRAERASlrmklealtaraaATEQLLAEARNQLR-DRDEAIRA 280
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2462535318 397 LEEKNV-LIQESETFRKNLEESLHDKERLAE---EIEKLRSELD 436
Cdd:pfam19220 281 AERRLKeASIERDTLERRLAGLEADLERRTQqfqEMQRARAELE 324
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
194-445 |
2.78e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.70 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 194 KERLAALSSRVGEVEQEAETARKDLIKTEemntkyqRDIREAMAQKEDMEERITTLEKRYlsaqRESTSIHDMNDKLENE 273
Cdd:PRK03918 178 IERLEKFIKRTENIEELIKEKEKELEEVL-------REINEISSELPELREELEKLEKEV----KELEELKEEIEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 274 LANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVE--AELAQRIAAL-TKAEERHGNIEERMRHLEGQLEEK 350
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKekAEEYIKLSEFyEEYLDELREIEKRLSRLEEEINGI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 351 NQELQRARQREKMNEEHNKRLSDTVDRL--LTESNERLQ--LHLKERMAALEEKnVLIQESETFRKNLEESLHDKERLAE 426
Cdd:PRK03918 327 EERIKELEEKEERLEELKKKLKELEKRLeeLEERHELYEeaKAKKEELERLKKR-LTGLTPEKLEKELEELEKAKEEIEE 405
|
250
....*....|....*....
gi 2462535318 427 EIEKLRSELDQLKMRTGSL 445
Cdd:PRK03918 406 EISKITARIGELKKEIKEL 424
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
98-445 |
3.80e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 64.59 E-value: 3.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 98 RERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMA---SSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDEts 174
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAelnEAESDLEQDYQAASDHLNLVQTALRQQEKIERYQA-- 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 175 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLikteemntkyqrdireamaqkEDMEERITTLEKR-- 252
Cdd:PRK04863 356 DLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQL---------------------ADYQQALDVQQTRai 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 253 -YLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTmRKAETLPEVEAELAQRIAALTKAEE 331
Cdd:PRK04863 415 qYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVA-QAAHSQFEQAYQLVRKIAGEVSRSE 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 332 RHgnieERMRHLEGQLEEKNQELQRARQ-REKMNE-EHNKRLSDTVDRLLTESNERLQLHLkERMAALEEknvLIQESET 409
Cdd:PRK04863 494 AW----DVARELLRRLREQRHLAEQLQQlRMRLSElEQRLRQQQRAERLLAEFCKRLGKNL-DDEDELEQ---LQEELEA 565
|
330 340 350
....*....|....*....|....*....|....*.
gi 2462535318 410 FRKNLEESlhdKERLAEEIEKLRSELDQLKMRTGSL 445
Cdd:PRK04863 566 RLESLSES---VSEARERRMALRQQLEQLQARIQRL 598
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
7-441 |
4.57e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 4.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 7 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSL 86
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 87 FEHHKALDEKVRERLRVsLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHEKRLSNGS 166
Cdd:COG1196 403 EELEEAEEALLERLERL-EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 167 IDSTDETSQIVELQELLEKQNYE------MAQMKERLAALSSRVGEVEQEAETARKDLIKTEE---MNTKYQRDIREAMA 237
Cdd:COG1196 482 LLEELAEAAARLLLLLEAEADYEgflegvKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALaaaLQNIVVEDDEVAAA 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 238 Q----KEDMEERITTLEKRyLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLP 313
Cdd:COG1196 562 AieylKAAKAGRATFLPLD-KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV 640
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 314 EVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQRE-KMNEEHNKRLSDTVDRLLTESNERLQLHLKE 392
Cdd:COG1196 641 TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLaEEELELEEALLAEEEEERELAEAEEERLEEE 720
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2462535318 393 RMAALEEKNVLIQESETFRKNLEESLHDKERLAEE------IEKLRSELDQLKMR 441
Cdd:COG1196 721 LEEEALEEQLEAEREELLEELLEEEELLEEEALEElpeppdLEELERELERLERE 775
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
15-420 |
5.36e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.01 E-value: 5.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 15 ELNACREQLLEKEEEISELKAERNNTRLLLEHLEcLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALD 94
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAE-EKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 95 E--KVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMAssEGSTESEHLEGMEPGQKVHEKRLSNgSIDSTDE 172
Cdd:PTZ00121 1474 EakKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKA--EEAKKADEAKKAEEAKKADEAKKAE-EKKKADE 1550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 173 TSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDliktEEMNTKYQRDIREAMAQKEDMEERITTLEKR 252
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIE----EVMKLYEEEKKMKAEEAKKAEEAKIKAEELK 1626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 253 ylSAQRESTSIHDMNDKLENEL--------ANKEAILRQMEEKNRQLQERLELAE-QKLQQTMRKAETLPEVEAELAQRI 323
Cdd:PTZ00121 1627 --KAEEEKKKVEQLKKKEAEEKkkaeelkkAEEENKIKAAEEAKKAEEDKKKAEEaKKAEEDEKKAAEALKKEAEEAKKA 1704
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 324 AALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKR---LSDTVDRLLTESNERLQLHLKERMAALEEK 400
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKdeeEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE 1784
|
410 420
....*....|....*....|
gi 2462535318 401 nvLIQESETFRKNLEESLHD 420
Cdd:PTZ00121 1785 --LDEEDEKRRMEVDKKIKD 1802
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
7-357 |
1.19e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 7 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLeclvsrheRSLRMTVVKRQAQSPSGVSSEVEVLKALksl 86
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEA--------QAEEYELLAELARLEQDIARLEERRREL--- 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 87 fehhKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEgmepgQKVHEKRLSNGS 166
Cdd:COG1196 315 ----EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE-----LAEAEEELEELA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 167 IDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERI 246
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 247 TTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQtmRKAETLPEVEAELAQRIAAL 326
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA--GAVAVLIGVEAAYEAALEAA 543
|
330 340 350
....*....|....*....|....*....|.
gi 2462535318 327 TKAEERHGNIEERMRHLEGQLEEKNQELQRA 357
Cdd:COG1196 544 LAAALQNIVVEDDEVAAAAIEYLKAAKAGRA 574
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
174-366 |
1.20e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 61.77 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 174 SQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAmaqKEDMEERITTLEKRY 253
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA---EAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 254 LSAQR------------ESTSIHDMNDKLEN----ELANKEAILRQMEEKNR--QLQERLELAEQKLQQTMRKAET-LPE 314
Cdd:COG3883 93 RALYRsggsvsyldvllGSESFSDFLDRLSAlskiADADADLLEELKADKAEleAKKAELEAKLAELEALKAELEAaKAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462535318 315 VEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEE 366
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
190-601 |
1.24e-09 |
|
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: 62.83 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 190 MAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEerITTLEKRYLSAQRESTSIHDMNDK 269
Cdd:pfam15921 226 LRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVE--ITGLTEKASSARSQANSIQSQLEI 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 270 LENELANKEAI-LRQMEEknrqlqerLELAEQKLQQTMRKA-----ETLPEVEAELAQRIAALTKAEERHGNIEERMRHL 343
Cdd:pfam15921 304 IQEQARNQNSMyMRQLSD--------LESTVSQLRSELREAkrmyeDKIEELEKQLVLANSELTEARTERDQFSQESGNL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 344 EGQLEEKNQELQRARQREKMNEEHNKRLSD-------TVDRLLTESNER-----------------LQLHLKERMAALEE 399
Cdd:pfam15921 376 DDQLQKLLADLHKREKELSLEKEQNKRLWDrdtgnsiTIDHLRRELDDRnmevqrleallkamkseCQGQMERQMAAIQG 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 400 KNVLIQESETFRKNLEESlhdKERLAEEIEKLRSELDQLKmrtgsliepTIPRTHLDTSAELRYSVGSLVDSQSDyrTTK 479
Cdd:pfam15921 456 KNESLEKVSSLTAQLEST---KEMLRKVVEELTAKKMTLE---------SSERTVSDLTASLQEKERAIEATNAE--ITK 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 480 VirrprRGRMGVRRDEPK-VKSLGDHEWNRTQQIGVLSSHPFESDTEMSDIddddRETIFSSMDLLSPSGHSDA--QTLA 556
Cdd:pfam15921 522 L-----RSRVDLKLQELQhLKNEGDHLRNVQTECEALKLQMAEKDKVIEIL----RQQIENMTQLVGQHGRTAGamQVEK 592
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2462535318 557 MMLQEQLDAINKEIRLIQEEKESTELRAEEIENRVASVSLEGLNL 601
Cdd:pfam15921 593 AQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKL 637
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
81-445 |
1.54e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 81 KALKSLFEHHKALDEKvRERLRVSLERVSALEEELAAANQEIvalrEQNVHIQRKMASSEGSTESEhLEGMEPGQKVHEK 160
Cdd:PRK03918 162 NAYKNLGEVIKEIKRR-IERLEKFIKRTENIEELIKEKEKEL----EEVLREINEISSELPELREE-LEKLEKEVKELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 161 RlsngsidstdeTSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVE---QEAETARKDLIKTEEMNTKYQRDIR---E 234
Cdd:PRK03918 236 L-----------KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKkeiEELEEKVKELKELKEKAEEYIKLSEfyeE 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 235 AMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQME---------EKNRQLQERLELAEQKLqqt 305
Cdd:PRK03918 305 YLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEeleerhelyEEAKAKKEELERLKKRL--- 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 306 mrKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ---ELQRARQR-----EKMNEEHNKRLSDTVDR 377
Cdd:PRK03918 382 --TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKaieELKKAKGKcpvcgRELTEEHRKELLEEYTA 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 378 LLTESNERLQ-LHLKERMAALEEKNV---LIQESETFR--------KNLEESL--HDKERL---AEEIEKLRSELDQLKM 440
Cdd:PRK03918 460 ELKRIEKELKeIEEKERKLRKELRELekvLKKESELIKlkelaeqlKELEEKLkkYNLEELekkAEEYEKLKEKLIKLKG 539
|
....*
gi 2462535318 441 RTGSL 445
Cdd:PRK03918 540 EIKSL 544
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
229-444 |
1.54e-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: 61.32 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 229 QRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK 308
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 309 AETLpevEAELAQRIAALTK------------------AEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKR 370
Cdd:COG4942 99 LEAQ---KEELAELLRALYRlgrqpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462535318 371 LSDTVDRLLTEsNERLQLHLKERMAALEEKNvliQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGS 444
Cdd:COG4942 176 LEALLAELEEE-RAALEALKAERQKLLARLE---KELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
171-591 |
1.86e-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: 62.39 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 171 DETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEemntKYQrdirEAMAQKEDMEERITTLE 250
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE----RYQ----ALLKEKREYEGYELLKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 251 KRYLSAQREstsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAelaqrIAALTKAE 330
Cdd:TIGR02169 232 KEALERQKE---------AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ-----LRVKEKIG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 331 ERHGNIEErmrhLEGQLEEKNQELQRA-RQREKMNEEHNKrlsdtvdrlltesnerlqlhLKERMAALEEKnvliqeset 409
Cdd:TIGR02169 298 ELEAEIAS----LERSIAEKERELEDAeERLAKLEAEIDK--------------------LLAEIEELERE--------- 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 410 frknLEESLHDKERLAEEIEKLRSELDQLKMRTGSLieptiprthldtSAELRYSVGSLVDSQSDYRTTKVIRRPRRGRM 489
Cdd:TIGR02169 345 ----IEEERKRRDKLTEEYAELKEELEDLRAELEEV------------DKEFAETRDELKDYREKLEKLKREINELKREL 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 490 GVRRDEPKVKS--LGDHEwnrtQQIGVLSSHPFESDTEMSDIDDDDRETIFSSMDLLSPSGHSDAQTLAmmLQEQLDAIN 567
Cdd:TIGR02169 409 DRLQEELQRLSeeLADLN----AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD--LKEEYDRVE 482
|
410 420
....*....|....*....|....
gi 2462535318 568 KEIRLIQEEKESTELRAEEIENRV 591
Cdd:TIGR02169 483 KELSKLQRELAEAEAQARASEERV 506
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
14-438 |
1.99e-09 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 61.91 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 14 KELNACREQLLEKEEEISELKAERNNtrlLLEHLECLVsrhERSLRMTVVKRQAQSPSGVSSEvEVLKALKSLFEHHKAL 93
Cdd:TIGR00618 472 EQQLQTKEQIHLQETRKKAVVLARLL---ELQEEPCPL---CGSCIHPNPARQDIDNPGPLTR-RMQRGEQTYAQLETSE 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 94 dEKVRERLRVSLERVSALEEELAAANQEIVALREQnvhiqrkmassegstESEHLEGMEPGQKVHEKRLSNGSIDSTDET 173
Cdd:TIGR00618 545 -EDVYHQLTSERKQRASLKEQMQEIQQSFSILTQC---------------DNRSKEDIPNLQNITVRLQDLTEKLSEAED 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 174 SQIVELQELLEKQNYEMAqmKERLAALSSRVGEVEQEAETArkdliKTEEMNTKYQRDIREAMAQKEDMEERitTLEKRY 253
Cdd:TIGR00618 609 MLACEQHALLRKLQPEQD--LQDVRLHLQQCSQELALKLTA-----LHALQLTLTQERVREHALSIRVLPKE--LLASRQ 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 254 LSAQRESTSIHDMNDKLEnELANKEAILRQMEE---KNRQLQERLELAEQKLQQTMR-KAETLPEVEAEL-AQRIAALTK 328
Cdd:TIGR00618 680 LALQKMQSEKEQLTYWKE-MLAQCQTLLRELEThieEYDREFNEIENASSSLGSDLAaREDALNQSLKELmHQARTVLKA 758
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 329 AEERHGNIEER----------MRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALE 398
Cdd:TIGR00618 759 RTEAHFNNNEEvtaalqtgaeLSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLE 838
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2462535318 399 EKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQL 438
Cdd:TIGR00618 839 EKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
8-435 |
3.98e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 3.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 8 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLF 87
Cdd:PRK03918 315 RLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELE 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 88 EHHKAlDEKVRERLRVSLERVSALEEELAAANQEIVALRE---------------------QNVHIQRKMASSEGSTESE 146
Cdd:PRK03918 395 ELEKA-KEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelteehrkellEEYTAELKRIEKELKEIEE 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 147 HLEGMEPGQKVHEKRLSNGSIDSTDET--SQIVELQELLEKQNYEMAQMKERLA-ALSSRVGEVEQEAETARKDLIKTEE 223
Cdd:PRK03918 474 KERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEELEKKAEEYeKLKEKLIKLKGEIKSLKKELEKLEE 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 224 MNTKyqrdIREAMAQKEDMEERITTLEKRYLSAQREstSIHDMNDKLE---------NELANKEAILRQMEEKNRQLQER 294
Cdd:PRK03918 554 LKKK----LAELEKKLDELEEELAELLKELEELGFE--SVEELEERLKelepfyneyLELKDAEKELEREEKELKKLEEE 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 295 LELAEQKLQQTMRKAEtlpeveaELAQRIAALTK--AEERHGNIEERMRHLEGQLEEKNQELqrarqrekmneEHNKRLS 372
Cdd:PRK03918 628 LDKAFEELAETEKRLE-------ELRKELEELEKkySEEEYEELREEYLELSRELAGLRAEL-----------EELEKRR 689
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462535318 373 DTVDRLLTEsnerlqlhLKERMAALEEKnvlIQESEtfrkNLEESLHDKERLAEEIEKLRSEL 435
Cdd:PRK03918 690 EEIKKTLEK--------LKEELEEREKA---KKELE----KLEKALERVEELREKVKKYKALL 737
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
804-870 |
5.14e-09 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 53.84 E-value: 5.14e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462535318 804 FAQWDGPTVVAWLELwLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 870
Cdd:smart00454 1 VSQWSPESVADWLES-IGLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
6-377 |
5.36e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 5.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 6 LQEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKS 85
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEA 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 86 LFEHH--KALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNvhiqrKMASSEGSTESEHLEGMEPGQKVHEKRLS 163
Cdd:COG1196 535 AYEAAleAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLD-----KIRARAALAAALARGAIGAAVDLVASDLR 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 164 NGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDME 243
Cdd:COG1196 610 EADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 244 ERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRI 323
Cdd:COG1196 690 EEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELEREL 769
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 324 AALTKAEERHGNI-----------EERMRHLEGQLEeknqELQRARQR-----EKMNEEHNKRLSDTVDR 377
Cdd:COG1196 770 ERLEREIEALGPVnllaieeyeelEERYDFLSEQRE----DLEEARETleeaiEEIDRETRERFLETFDA 835
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
25-447 |
6.40e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.54 E-value: 6.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 25 EKEEEISELKAERNNTRLllehlECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVR--ERLR 102
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKA-----DAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKkaDEAK 1437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 103 VSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHE-KRLSNGSIDSTDETSQIVELQE 181
Cdd:PTZ00121 1438 KKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEaKKKADEAKKAAEAKKKADEAKK 1517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 182 LLEKQNYEMAQMKERlaalsSRVGEVEQEAETARK--DLIKTEEMntKYQRDIREAMAQKEDMEERITTLEKRYLSAQRE 259
Cdd:PTZ00121 1518 AEEAKKADEAKKAEE-----AKKADEAKKAEEKKKadELKKAEEL--KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAE 1590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 260 STSIHDMNDKLENELANKEAILRQMEE---------KNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAE 330
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAEEAKKAEEakikaeelkKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA 1670
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 331 ERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLltesnERLQLHLKERMAALEEknvLIQESETF 410
Cdd:PTZ00121 1671 EEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA-----EELKKAEEENKIKAEE---AKKEAEED 1742
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2462535318 411 RKNLEESLHD---KERLAEEIEKLRSELDQLKMRTGSLIE 447
Cdd:PTZ00121 1743 KKKAEEAKKDeeeKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
6-441 |
7.34e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 7.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 6 LQEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAqspsgvsSEVEVLKALKS 85
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE-------AEAELAEAEEA 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 86 LFEHHKALDEKVRERLRVSLERVSALEEELAAANQEI-VALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHEKRLSN 164
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEeLEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 165 GSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSrvgevEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEE 244
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE-----ELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 245 RITTL------EKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEK--------NRQLQERLELAEQKLQQTMRKAE 310
Cdd:COG1196 522 LAGAVavligvEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKagratflpLDKIRARAALAAALARGAIGAAV 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 311 TLPEVEAELAQRIAAL--------TKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTES 382
Cdd:COG1196 602 DLVASDLREADARYYVlgdtllgrTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL 681
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462535318 383 NERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMR 441
Cdd:COG1196 682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
230-441 |
7.37e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.31 E-value: 7.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 230 RDIREAMaqkEDMEERITTLE------KRYLSAQRESTSIHDMNDKLEnelankeaiLRQMEEKNRQLQERLELAEQKLQ 303
Cdd:COG4913 238 ERAHEAL---EDAREQIELLEpirelaERYAAARERLAELEYLRAALR---------LWFAQRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 304 QTMRKAETLPEVEAELAQRIAALTKAEERHGNieERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDrLLTESN 383
Cdd:COG4913 306 RLEAELERLEARLDALREELDELEAQIRGNGG--DRLEQLEREIERLERELEERERRRARLEALLAALGLPLP-ASAEEF 382
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462535318 384 ERLQLHLKERMAALEEknvliqESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMR 441
Cdd:COG4913 383 AALRAEAAALLEALEE------ELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
181-462 |
8.96e-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: 60.07 E-value: 8.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 181 ELLEKQnyemAQMKERLAALSSRVGEVE-----QEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLS 255
Cdd:TIGR02168 203 KSLERQ----AEKAERYKELKAELRELElallvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 256 AQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALtkaeerhgn 335
Cdd:TIGR02168 279 LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL--------- 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 336 iEERMRHLEGQLEEKNQELQRARQREKMNEEHnkrlsdtvdrLLTESNERLQLhlkermaaLEEKNVLIQESETFRKNLE 415
Cdd:TIGR02168 350 -KEELESLEAELEELEAELEELESRLEELEEQ----------LETLRSKVAQL--------ELQIASLNNEIERLEARLE 410
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2462535318 416 ESLHDKERLAEEIEKLRSELDQLKMRTGSLIEPTIPRTHLDTSAELR 462
Cdd:TIGR02168 411 RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE 457
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
3-445 |
1.09e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 59.75 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 3 DLFLQEFAALTKELNACREQLLEKEEEIS---------------------ELKAERNNTRLLLEHLECLVsRHERSLRMT 61
Cdd:pfam15921 366 DQFSQESGNLDDQLQKLLADLHKREKELSlekeqnkrlwdrdtgnsitidHLRRELDDRNMEVQRLEALL-KAMKSECQG 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 62 VVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERL---RVSLER----VSAL-------EEELAAANQEIVALRE 127
Cdd:pfam15921 445 QMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELtakKMTLESsertVSDLtaslqekERAIEATNAEITKLRS 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 128 QnvhIQRKMASSEG-STESEHLEGMEPGQKVHEKRLSngsidstdETSQIVE-LQELLEKQNYEMAQMKERLAALSSRVG 205
Cdd:pfam15921 525 R---VDLKLQELQHlKNEGDHLRNVQTECEALKLQMA--------EKDKVIEiLRQQIENMTQLVGQHGRTAGAMQVEKA 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 206 EVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQME 285
Cdd:pfam15921 594 QLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLS 673
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 286 EKNRQLQERLELAEQKLQQTMRKAET-LPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMN 364
Cdd:pfam15921 674 EDYEVLKRNFRNKSEEMETTTNKLKMqLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFL 753
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 365 EEhnkrlsdtvdrLLTESNerlqlhlKERMAALEEKNVLIQESETFRKnleeslhDKERLAEEIEKLRSELDQLKMRTGS 444
Cdd:pfam15921 754 EE-----------AMTNAN-------KEKHFLKEEKNKLSQELSTVAT-------EKNKMAGELEVLRSQERRLKEKVAN 808
|
.
gi 2462535318 445 L 445
Cdd:pfam15921 809 M 809
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
120-436 |
1.53e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 59.20 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 120 QEIVALREQNVHIQRKMASSEGSTE--SEHLEGMEPGQKVHEKRLSNGSI-DSTDETSQIVELQELLEKQNYEMAQMKER 196
Cdd:COG3096 836 AELAALRQRRSELERELAQHRAQEQqlRQQLDQLKEQLQLLNKLLPQANLlADETLADRLEELREELDAAQEAQAFIQQH 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 197 LAALSsrvgEVEQEAETARKDLIKTEEMNTKYQRdireAMAQKEDMEERITTLEkrYLSAQRESTSIHD----------M 266
Cdd:COG3096 916 GKALA----QLEPLVAVLQSDPEQFEQLQADYLQ----AKEQQRRLKQQIFALS--EVVQRRPHFSYEDavgllgensdL 985
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 267 NDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAAL-----TKAEERhgnIEERMR 341
Cdd:COG3096 986 NEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELgvqadAEAEER---ARIRRD 1062
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 342 HLEGQL----EEKNQ-ELQRARQREKMnEEHNKRLSDtVDRLLTESNERLQLHLKERMAALEeknvLIQESetfrkNLEE 416
Cdd:COG3096 1063 ELHEELsqnrSRRSQlEKQLTRCEAEM-DSLQKRLRK-AERDYKQEREQVVQAKAGWCAVLR----LARDN-----DVER 1131
|
330 340
....*....|....*....|
gi 2462535318 417 SLHDKERLAEEIEKLRSELD 436
Cdd:COG3096 1132 RLHRRELAYLSADELRSMSD 1151
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
197-445 |
1.56e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 197 LAALSSRVGEVEQ--EAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKrYLSAQREstsIHDMNDKLENEL 274
Cdd:PRK03918 127 LNAIYIRQGEIDAilESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEK-FIKRTEN---IEELIKEKEKEL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 275 ANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQ---LEEKN 351
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEieeLEEKV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 352 QELQRARQREKMNEEHNKRLSDTVDRL-----LTESNERLQLHLKERMAALEEKNVLIQESETFRKNLE---ESLHDKER 423
Cdd:PRK03918 283 KELKELKEKAEEYIKLSEFYEEYLDELreiekRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEkrlEELEERHE 362
|
250 260
....*....|....*....|..
gi 2462535318 424 LAEEIEKLRSELDQLKMRTGSL 445
Cdd:PRK03918 363 LYEEAKAKKEELERLKKRLTGL 384
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
174-385 |
1.69e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.85 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 174 SQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRY 253
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 254 ----LSAQREST--------SIHDMNDkLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQ 321
Cdd:COG4942 107 aellRALYRLGRqpplalllSPEDFLD-AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462535318 322 RIAALTKAEERHgniEERMRHLEGQLEEKNQELQRARQREkmneehnKRLSDTVDRLLTESNER 385
Cdd:COG4942 186 ERAALEALKAER---QKLLARLEKELAELAAELAELQQEA-------EELEALIARLEAEAAAA 239
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
175-332 |
3.99e-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: 3.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 175 QIVELQELLEkqnyEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKR-- 252
Cdd:COG1579 8 ALLDLQELDS----ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 253 -------YLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlpEVEAELAQRIAA 325
Cdd:COG1579 84 nvrnnkeYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD---EELAELEAELEE 160
|
....*..
gi 2462535318 326 LTKAEER 332
Cdd:COG1579 161 LEAEREE 167
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
12-446 |
4.78e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 57.34 E-value: 4.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 12 LTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHeRSLrmtvvkrqaqspsgvSSEVEVLKALKSLFEhhK 91
Cdd:TIGR04523 171 LENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKN-KSL---------------ESQISELKKQNNQLK--D 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 92 ALDEKVRErlrvslerVSALEEELAAANQEIVALREQNVHIQRKMA--SSEGSTESEHLEGMEPGQKVHEKRLSNgsIDS 169
Cdd:TIGR04523 233 NIEKKQQE--------INEKTTEISNTQTQLNQLKDEQNKIKKQLSekQKELEQNNKKIKELEKQLNQLKSEISD--LNN 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 170 TDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREamaqKEDMEERIttl 249
Cdd:TIGR04523 303 QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE----KQNEIEKL--- 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 250 ekrylsaQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKA 329
Cdd:TIGR04523 376 -------KKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQ 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 330 ----EERHGNIEERMRHLEGQ--------------LEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNErlqlhLK 391
Cdd:TIGR04523 449 dsvkELIIKNLDNTRESLETQlkvlsrsinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS-----LK 523
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462535318 392 ERMAALE----EKNVLIQESETFRKNLEESLhDKERLAEEIEKLRSELDQLKMRTGSLI 446
Cdd:TIGR04523 524 EKIEKLEsekkEKESKISDLEDELNKDDFEL-KKENLEKEIDEKNKEIEELKQTQKSLK 581
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
6-439 |
5.52e-08 |
|
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: 57.54 E-value: 5.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 6 LQEFAALTKELNacrEQLLEKEEEISELKAERNNTRLLL--------EHLECLVSRHERSLRMTVVKR---QAQSPSgVS 74
Cdd:pfam12128 278 QEERQETSAELN---QLLRTLDDQWKEKRDELNGELSAAdaavakdrSELEALEDQHGAFLDADIETAaadQEQLPS-WQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 75 SEVEVL-KALKSLFEHHKALDEKVrERLRvsLERVSALEEELAAANQEIVALREQnvhIQRKMASSEGsteseHLEGME- 152
Cdd:pfam12128 354 SELENLeERLKALTGKHQDVTAKY-NRRR--SKIKEQNNRDIAGIKDKLAKIREA---RDRQLAVAED-----DLQALEs 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 153 PGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEmAQMKERLAALSSRVGEVEQEAETARKDLikteemnTKYQRDI 232
Cdd:pfam12128 423 ELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATAT-PELLLQLENFDERIERAREEQEAANAEV-------ERLQSEL 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 233 REAMAQKEDMEERITTLEKRYLSAQRESTSIHDMND----KLENELANKEAILRQMEEK--NRQLQERLELAEQKLQQTM 306
Cdd:pfam12128 495 RQARKRRDQASEALRQASRRLEERQSALDELELQLFpqagTLLHFLRKEAPDWEQSIGKviSPELLHRTDLDPEVWDGSV 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 307 RKAETL-------------------PEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEH 367
Cdd:pfam12128 575 GGELNLygvkldlkridvpewaaseEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLD 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 368 NKRLSDTVDRL---LTESNERLQLHLKERMAALE-EKNVLIQESETF-----RKNLEESLHDKERLAEEIEKLRSELDQL 438
Cdd:pfam12128 655 LRRLFDEKQSEkdkKNKALAERKDSANERLNSLEaQLKQLDKKHQAWleeqkEQKREARTEKQAYWQVVEGALDAQLALL 734
|
.
gi 2462535318 439 K 439
Cdd:pfam12128 735 K 735
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
7-402 |
6.40e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.97 E-value: 6.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 7 QEFAALTKELNACREQLLEKEEEISELKAERNNTRL-----------LLEHLECLVSRHERslrmtVVKRQAQSPSGVSS 75
Cdd:PRK02224 363 EEAAELESELEEAREAVEDRREEIEELEEEIEELRErfgdapvdlgnAEDFLEELREERDE-----LREREAELEATLRT 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 76 EVEVLKALKSLFEHHKA-------LDEKVRERLRVSLERVSALEEELAAANQEIVALREQnvhIQRKMASSEGSTESEHL 148
Cdd:PRK02224 438 ARERVEEAEALLEAGKCpecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEER---LERAEDLVEAEDRIERL 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 149 EgmepgqkvhEKRLSngsidstdetsqiveLQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKdlikteemntky 228
Cdd:PRK02224 515 E---------ERRED---------------LEELIAERRETIEEKRERAEELRERAAELEAEAEEKRE------------ 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 229 qrDIREAMAQKEDMEERITTLEKRylsaQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK 308
Cdd:PRK02224 559 --AAAEAEEEAEEAREEVAELNSK----LAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEK 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 309 AETLPEVEAELAQriAALTKAEERHGNIEERMRHLEG---QLEEKNQELQRA--------RQREKMNEEHnKRLSDTVDR 377
Cdd:PRK02224 633 RERKRELEAEFDE--ARIEEAREDKERAEEYLEQVEEkldELREERDDLQAEigavenelEELEELRERR-EALENRVEA 709
|
410 420
....*....|....*....|....*..
gi 2462535318 378 L--LTESNERLQLHLKERMAALEEKNV 402
Cdd:PRK02224 710 LeaLYDEAEELESMYGDLRAELRQRNV 736
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
230-439 |
7.45e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 7.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 230 RDIREAMAQKED----MEERITTLEKRYLSAQRestsIHDMNDKLENelANKEAILRQMEEKNRQLqERLELAEQKLQQT 305
Cdd:TIGR02168 182 ERTRENLDRLEDilneLERQLKSLERQAEKAER----YKELKAELRE--LELALLVLRLEELREEL-EELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 306 MRKAET-LPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL------ 378
Cdd:TIGR02168 255 LEELTAeLQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELesklde 334
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462535318 379 ----LTESNERLQLhLKERMAALEEKnvlIQESETFRKNLEESLHDKErlaEEIEKLRSELDQLK 439
Cdd:TIGR02168 335 laeeLAELEEKLEE-LKEELESLEAE---LEELEAELEELESRLEELE---EQLETLRSKVAQLE 392
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
21-426 |
8.11e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 56.98 E-value: 8.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 21 EQLLEKEEEISELKAERNNTRLL----LEHLECLVSRHERSLRMTVVKRQAQSpsgvsSEVE-VLKALKSLFEHHKALDE 95
Cdd:TIGR00606 684 QRVFQTEAELQEFISDLQSKLRLapdkLKSTESELKKKEKRRDEMLGLAPGRQ-----SIIDlKEKEIPELRNKLQKVNR 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 96 KVrERLRVSLERVSAL------EEELAAANQEIVA----LREQNVHIQRKMASSEGSTESEHLEG--MEPGQKVHEKRLS 163
Cdd:TIGR00606 759 DI-QRLKNDIEEQETLlgtimpEEESAKVCLTDVTimerFQMELKDVERKIAQQAAKLQGSDLDRtvQQVNQEKQEKQHE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 164 NGSIdstdeTSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDME 243
Cdd:TIGR00606 838 LDTV-----VSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDS 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 244 ERITTLEKrylSAQRESTSIHDMNDklENELANKEaiLRQMEEKNRQLQERLELAEQKLQQTmrKAETLPEVEAELAQRI 323
Cdd:TIGR00606 913 PLETFLEK---DQQEKEELISSKET--SNKKAQDK--VNDIKEKVKNIHGYMKDIENKIQDG--KDDYLKQKETELNTVN 983
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 324 AALTKAEERHGNIEERMRHLEGQLEEKNQE---LQRARQREKMNEEHnKRLSDTVDRLLTESNERLQLHLKERMAALEEK 400
Cdd:TIGR00606 984 AQLEECEKHQEKINEDMRLMRQDIDTQKIQerwLQDNLTLRKRENEL-KEVEEELKQHLKEMGQMQVLQMKQEHQKLEEN 1062
|
410 420 430
....*....|....*....|....*....|.
gi 2462535318 401 NVLIQESETF-----RKNLEESLHDKERLAE 426
Cdd:TIGR00606 1063 IDLIKRNHVLalgrqKGYEKEIKHFKKELRE 1093
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7-594 |
8.24e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 8.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 7 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQA--QSPSGVSSEVEVLKA-- 82
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANleRQLEELEAQLEELESkl 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 83 -------------LKSLFEHHKALDEKV---RERLRVSLERVSALEEELAAANQEIVALREQ----NVHIQR---KMASS 139
Cdd:TIGR02168 333 delaeelaeleekLEELKEELESLEAELeelEAELEELESRLEELEEQLETLRSKVAQLELQiaslNNEIERleaRLERL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 140 EGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLI 219
Cdd:TIGR02168 413 EDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 220 KTEEM---NTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIH-----DMNDKL-ENELANKEAI--LRQME--- 285
Cdd:TIGR02168 493 SLERLqenLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEaalggRLQAVVvENLNAAKKAIafLKQNElgr 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 286 --------EKNRQLQERLELAEQKLQQTMRKAETLPEVEAEL-------------------AQRIAALTKAEER------ 332
Cdd:TIGR02168 573 vtflpldsIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLrkalsyllggvlvvddldnALELAKKLRPGYRivtldg 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 333 -----HG---------------------NIEERMRHLEGQLEEKNQELQRAR-QREKMNEEHNK--RLSDTVDRLLTESN 383
Cdd:TIGR02168 653 dlvrpGGvitggsaktnssilerrreieELEEKIEELEEKIAELEKALAELRkELEELEEELEQlrKELEELSRQISALR 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 384 ERLQLHLKERMAALE-------EKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIEptiprthld 456
Cdd:TIGR02168 733 KDLARLEAEVEQLEEriaqlskELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE--------- 803
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 457 tsaelrysvgSLVDSQSDYRTTKviRRPRRGRMGVRRDEPKVKSLGDHEWNRTQQIGVLSSHPFESDTEMSDIDDDDRE- 535
Cdd:TIGR02168 804 ----------ALDELRAELTLLN--EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEl 871
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 536 --------TIFSSMDLLSPSGHSDAQTLAMMLQE---QLDAINKEIRLIQEEKESTELRAEEIENRVASV 594
Cdd:TIGR02168 872 eseleallNERASLEEALALLRSELEELSEELRElesKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
75-439 |
1.09e-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: 56.29 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 75 SEVEVLKALKSLFEHHKALDEKVRERL--RVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGME 152
Cdd:pfam17380 266 TENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 153 PGQKV-----HEKRLSNGSIDSTDETSQIVELQELlEKQNYEMAQMKERlaalssrvgeVEQEAETARKDLIKTEEMntk 227
Cdd:pfam17380 346 RERELerirqEERKRELERIRQEEIAMEISRMREL-ERLQMERQQKNER----------VRQELEAARKVKILEEER--- 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 228 yQRDIREAMAQKEDMeerittlekrylsaqrestsihdmndKLENELANKEAILRQMEEKNRQLqERLELAEQKLQQTMr 307
Cdd:pfam17380 412 -QRKIQQQKVEMEQI--------------------------RAEQEEARQREVRRLEEERAREM-ERVRLEEQERQQQV- 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 308 kaETLPEVEAELAQRIAALTKAEERHGNIEERMRH-LEGQLEEKnqelqrarqREKMNEEHNKRlsdtvdrlltesnERL 386
Cdd:pfam17380 463 --ERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKiLEKELEER---------KQAMIEEERKR-------------KLL 518
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2462535318 387 QLHLKERMAALEEKNVLIQESETFRKNLEesLHDKERLAEEIEKLRSELDQLK 439
Cdd:pfam17380 519 EKEMEERQKAIYEEERRREAEEERRKQQE--MEERRRIQEQMRKATEERSRLE 569
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
936-991 |
1.10e-07 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 49.99 E-value: 1.10e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462535318 936 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 991
Cdd:smart00454 11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
268-434 |
1.10e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 268 DKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtLPEVEAELA---QRIAALTKAEERHGNIEERMRHLE 344
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID-VASAEREIAeleAELERLDASSDDLAALEEQLEELE 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 345 GQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLT-------ESNERLQLHLKERMAALEEKNVLIQESETFRKNLEES 417
Cdd:COG4913 699 AELEELEEELDELKGEIGRLEKELEQAEEELDELQDrleaaedLARLELRALLEERFAAALGDAVERELRENLEERIDAL 778
|
170
....*....|....*..
gi 2462535318 418 LHDKERLAEEIEKLRSE 434
Cdd:COG4913 779 RARLNRAEEELERAMRA 795
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
284-439 |
1.21e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 54.16 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 284 MEEKNRQLqERLELAEQKLQQTMRKAETLP----EVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARq 359
Cdd:COG1579 2 MPEDLRAL-LDLQELDSELDRLEHRLKELPaelaELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 360 rEKMNEEHNKRLSDTVDR---LLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESL-HDKERLAEEIEKLRSEL 435
Cdd:COG1579 80 -EQLGNVRNNKEYEALQKeieSLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELeEKKAELDEELAELEAEL 158
|
....
gi 2462535318 436 DQLK 439
Cdd:COG1579 159 EELE 162
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
99-447 |
1.34e-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: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 99 ERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMepgQKVHEKRLSNgsidstdetsQIVE 178
Cdd:TIGR00618 212 CMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQ---LRARIEELRA----------QEAV 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 179 LQELLEKQNYemAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEkrylSAQR 258
Cdd:TIGR00618 279 LEETQERINR--ARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQ----TLHS 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 259 ESTSIHDMNDKlenELANKEAILRQMEEKN--RQLQERLELAEQKLQQTMRKAETLPE----VEAELAQRIAALTKAEER 332
Cdd:TIGR00618 353 QEIHIRDAHEV---ATSIREISCQQHTLTQhiHTLQQQKTTLTQKLQSLCKELDILQReqatIDTRTSAFRDLQGQLAHA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 333 HGNIEERMRHLEGQ----------LEEKNQELQRARQR---EKMNEEHNKRLSDTVDRLLTESNERLQLH------LKER 393
Cdd:TIGR00618 430 KKQQELQQRYAELCaaaitctaqcEKLEKIHLQESAQSlkeREQQLQTKEQIHLQETRKKAVVLARLLELqeepcpLCGS 509
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2462535318 394 MAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIE 447
Cdd:TIGR00618 510 CIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKE 563
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
174-464 |
1.48e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.91 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 174 SQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRY 253
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 254 LSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMrkaetlpevEAELAQRIAALTKAEERH 333
Cdd:COG4372 125 QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS---------EAEAEQALDELLKEANRN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 334 GNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKN 413
Cdd:COG4372 196 AEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEE 275
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2462535318 414 LEESLHDKERLAEEIEKLRSELDQLKMRTGSLIEPTIPRTHLDTSAELRYS 464
Cdd:COG4372 276 EELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAK 326
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
98-433 |
1.56e-07 |
|
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: 56.11 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 98 RERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTE---------SEHLEGMEPGQKVHEKrlsngsID 168
Cdd:COG3096 277 ANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESdleqdyqaaSDHLNLVQTALRQQEK------IE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 169 STDEtsQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLikteemnTKYQRDIREAMAQKEDMEERITT 248
Cdd:COG3096 351 RYQE--DLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQL-------ADYQQALDVQQTRAIQYQQAVQA 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 249 LEKrylsaQRESTSIHDMN-DKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETL----PEVEAELA-QR 322
Cdd:COG3096 422 LEK-----ARALCGLPDLTpENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVckiaGEVERSQAwQT 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 323 IAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDrllteSNERLQLHLKERMAALEEknv 402
Cdd:COG3096 497 ARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLD-----AAEELEELLAELEAQLEE--- 568
|
330 340 350
....*....|....*....|....*....|.
gi 2462535318 403 LIQESETFRKNLEESLHDKERLAEEIEKLRS 433
Cdd:COG3096 569 LEEQAAEAVEQRSELRQQLEQLRARIKELAA 599
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
147-438 |
1.64e-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: 55.75 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 147 HLEGMEPGQKVHEKRLSNGSIdSTDETSQIVELQELLEKQNYEMAqmkERLAALSS-RVGEVEQEAETARKDLIKTEEMN 225
Cdd:TIGR00618 100 HRKTEQPEQLYLEQKKGRGRI-LAAKKSETEEVIHDLLKLDYKTF---TRVVLLPQgEFAQFLKAKSKEKKELLMNLFPL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 226 TKYQRDIREAMAQKEDMEERITTLEKRY----LSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQK 301
Cdd:TIGR00618 176 DQYTQLALMEFAKKKSLHGKAELLTLRSqlltLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQ 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 302 ------LQQTMRKAETLPEVEAELAQRIAALTKA--EERHGNIEERMRHLEGQLEEKNQELQ-RARQREKMNEEHNKRLS 372
Cdd:TIGR00618 256 lkkqqlLKQLRARIEELRAQEAVLEETQERINRArkAAPLAAHIKAVTQIEQQAQRIHTELQsKMRSRAKLLMKRAAHVK 335
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 373 DTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLH----DKERLAEEIEKLRSELDQL 438
Cdd:TIGR00618 336 QQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHtlqqQKTTLTQKLQSLCKELDIL 405
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
20-444 |
1.79e-07 |
|
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: 55.60 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 20 REQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRmtvvkRQAQSPSGVSSEVEVLKAL------KSLFEHHK-- 91
Cdd:pfam10174 330 KESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQ-----DLTEEKSTLAGEIRDLKDMldvkerKINVLQKKie 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 92 ALDEKVRERLRV---------SLERVSA--------LEEELAAANQEIVALREQNvhiqrkmaSSEGSTESEHLEGMEPG 154
Cdd:pfam10174 405 NLQEQLRDKDKQlaglkervkSLQTDSSntdtalttLEEALSEKERIIERLKEQR--------EREDRERLEELESLKKE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 155 QKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALssrvgevEQEAETARKDLIKTEEMNTKYQrDIRE 234
Cdd:pfam10174 477 NKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSL-------EIAVEQKKEECSKLENQLKKAH-NAEE 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 235 AMAQKEDMEERITTLEKRYLSAQRESTsihdmndKLENELANKEAILRQME----EKNRQLQERLELAEQKLQQTMRKAE 310
Cdd:pfam10174 549 AVRTNPEINDRIRLLEQEVARYKEESG-------KAQAEVERLLGILREVEneknDKDKKIAELESLTLRQMKEQNKKVA 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 311 TLPEVEAELAQRIAALTkaEERHGNIEERMR-HLEGQLEEKNQELQRARQREkmnEEHNKRLSDTV------DRLLTESN 383
Cdd:pfam10174 622 NIKHGQQEMKKKGAQLL--EEARRREDNLADnSQQLQLEELMGALEKTRQEL---DATKARLSSTQqslaekDGHLTNLR 696
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462535318 384 ERLQLHLKERM--------AALEEKNVLIQEsetfrknLEESLHDKERLAEEIEKLRSELD----QLKMRTGS 444
Cdd:pfam10174 697 AERRKQLEEILemkqeallAAISEKDANIAL-------LELSSSKKKKTQEEVMALKREKDrlvhQLKQQTQN 762
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1-445 |
2.14e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.46 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 1 MNDLFlQEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHL-ECLVSRHERSLRM-----TVVKRQAQSPSGVS 74
Cdd:TIGR02169 366 LEDLR-AELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLqEELQRLSEELADLnaaiaGIEAKINELEEEKE 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 75 SEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRkmASSEGSTESEHLEGMEPG 154
Cdd:TIGR02169 445 DKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE--RVRGGRAVEEVLKASIQG 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 155 --------QKVHEK-----------RLSNGSIDsTDETSQivELQELLEKQNY---------EMAQMkERLAALSSRVGE 206
Cdd:TIGR02169 523 vhgtvaqlGSVGERyataievaagnRLNNVVVE-DDAVAK--EAIELLKRRKAgratflplnKMRDE-RRDLSILSEDGV 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 207 VE--------------------------QEAETARKDLI-------------------------KTEEMNTKYQRD-IRE 234
Cdd:TIGR02169 599 IGfavdlvefdpkyepafkyvfgdtlvvEDIEAARRLMGkyrmvtlegelfeksgamtggsrapRGGILFSRSEPAeLQR 678
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 235 AMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAET--- 311
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENvks 758
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 312 -LPEVEAELAQRIAALTKAEERHGNIEERMRHleGQLEEKNQELqrarqrEKMNEEHnKRLSDTVDRLLTESNERLQL-- 388
Cdd:TIGR02169 759 eLKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAEL------SKLEEEV-SRIEARLREIEQKLNRLTLEke 829
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462535318 389 HLKERMAALEEKNVLIQES-ETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSL 445
Cdd:TIGR02169 830 YLEKEIQELQEQRIDLKEQiKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDL 887
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2-440 |
2.27e-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: 55.18 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 2 NDLFLQEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSlRMTVVKRQAQSPSGVSSEVEVLK 81
Cdd:pfam01576 147 NSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKG-RQELEKAKRKLEGESTDLQEQIA 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 82 ALKSLFEHHKALDEKVRERLRVSLERvsaLEEELAAANQEIVALREQNVHI------------QRKMASSEGSTESEHLE 149
Cdd:pfam01576 226 ELQAQIAELRAQLAKKEEELQAALAR---LEEETAQKNNALKKIRELEAQIselqedleseraARNKAEKQRRDLGEELE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 150 GMepgqkvheKRLSNGSIDST--------DETSQIVELQELLEKQ----NYEMAQMKERLAALSSRVGEVEQEAETARKD 217
Cdd:pfam01576 303 AL--------KTELEDTLDTTaaqqelrsKREQEVTELKKALEEEtrshEAQLQEMRQKHTQALEELTEQLEQAKRNKAN 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 218 LIKT----EEMNTKYQRDIREAMAQKEDMEER-------ITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEE 286
Cdd:pfam01576 375 LEKAkqalESENAELQAELRTLQQAKQDSEHKrkklegqLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEG 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 287 KNRQLQERLELAEQKLQQTMrkaETLPEveaELAQRIAALTKAEErhgnIEERMRHLEGQLEEknqELQRARQREKMNEE 366
Cdd:pfam01576 455 KNIKLSKDVSSLESQLQDTQ---ELLQE---ETRQKLNLSTRLRQ----LEDERNSLQEQLEE---EEEAKRNVERQLST 521
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462535318 367 HNKRLSDTVDRLLTESnerlqlhlkERMAALEE-KNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKM 440
Cdd:pfam01576 522 LQAQLSDMKKKLEEDA---------GTLEALEEgKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLV 587
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
126-438 |
2.45e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 55.18 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 126 REQNVHIQRKMASSEGSTESEHLEGMEPG-QKVH-EKRLSNGSIDSTDETSQIVELQEllEKQNYEMAQMKERLAALSSR 203
Cdd:pfam01576 90 RSQQLQNEKKKMQQHIQDLEEQLDEEEAArQKLQlEKVTTEAKIKKLEEDILLLEDQN--SKLSKERKLLEERISEFTSN 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 204 VGEVEQEAETARKDLIKTEEMNTkyqrDIREAMAQKEDMEERittLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQ 283
Cdd:pfam01576 168 LAEEEEKAKSLSKLKNKHEAMIS----DLEERLKKEEKGRQE---LEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 284 MEEKNRQLQERLE---LAEQKLQQTMRKAET-LPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEK------NQE 353
Cdd:pfam01576 241 KEEELQAALARLEeetAQKNNALKKIRELEAqISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTldttaaQQE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 354 LQRARQRE--------------------KMNEEHNKRLSDTVDRLltESNERLQLHLKERMAALEEKNVLI--------- 404
Cdd:pfam01576 321 LRSKREQEvtelkkaleeetrsheaqlqEMRQKHTQALEELTEQL--EQAKRNKANLEKAKQALESENAELqaelrtlqq 398
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2462535318 405 --QESETFRKNLEESLHD-----------KERLAEEIEKLRSELDQL 438
Cdd:pfam01576 399 akQDSEHKRKKLEGQLQElqarlseserqRAELAEKLSKLQSELESV 445
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
249-441 |
2.58e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 249 LEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTK 328
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 329 AEERHgNIEERMRHLEGQLEE---KNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKErmaaleeknvLIQ 405
Cdd:COG4717 131 YQELE-ALEAELAELPERLEEleeRLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD----------LAE 199
|
170 180 190
....*....|....*....|....*....|....*.
gi 2462535318 406 ESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMR 441
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
256-443 |
2.74e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.05 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 256 AQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGN 335
Cdd:PRK02224 197 EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 336 IEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLH-------------LKERMAALEE 399
Cdd:PRK02224 277 LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELedrDEELRDRLEECrvaaqahneeaesLREDADDLEE 356
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462535318 400 KNVLIQE-SETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTG 443
Cdd:PRK02224 357 RAEELREeAAELESELEEAREAVEDRREEIEELEEEIEELRERFG 401
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
190-398 |
4.43e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 4.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 190 MAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQREStsihdmnDK 269
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREEL-------EK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 270 LENELANKEAI--LRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGN-IEERMRHLEGQ 346
Cdd:COG4717 121 LEKLLQLLPLYqeLEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLaTEEELQDLAEE 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462535318 347 LEEKNQELQRARQREKMNEEHNKRLSDTVDRLlteSNERLQLHLKERMAALE 398
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQL---ENELEAAALEERLKEAR 249
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
175-359 |
5.02e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 5.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 175 QIVELQELLEKQNyEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEmnTKYQRDIREAMAQKEDMEERITTLEKRYL 254
Cdd:COG4913 250 QIELLEPIRELAE-RYAAARERLAELEYLRAALRLWFAQRRLELLEAEL--EELRAELARLEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 255 SAQREstsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQkLQQTMRKAE-TLPEVEAELAQRI----AALTKA 329
Cdd:COG4913 327 ELEAQ---------IRGNGGDRLEQLEREIERLERELEERERRRAR-LEALLAALGlPLPASAEEFAALRaeaaALLEAL 396
|
170 180 190
....*....|....*....|....*....|
gi 2462535318 330 EERHGNIEERMRHLEGQLEEKNQELQRARQ 359
Cdd:COG4913 397 EEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
111-341 |
5.32e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 5.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 111 LEEELAAANQEIVALREQNVHIQRKMASSEgstesehlegmepgQKVHEKRLSNGSIDSTDET----SQIVELQELLEKQ 186
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAE--------------AALEEFRQKNGLVDLSEEAklllQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 187 NYEMAQMKERLAALSSRVGEVEQEAETARKDlikteEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQREstsIHDM 266
Cdd:COG3206 232 RAELAEAEARLAALRAQLGSGPDALPELLQS-----PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ---IAAL 303
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462535318 267 NDKLENELankEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMR 341
Cdd:COG3206 304 RAQLQQEA---QRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
12-430 |
5.42e-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: 53.87 E-value: 5.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 12 LTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTvvKRQAQSpsgVSSEVEVLKALKSlfehhK 91
Cdd:TIGR04523 237 KQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKEL--EKQLNQ---LKSEISDLNNQKE-----Q 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 92 ALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIqrkmassegstesehlegmepgqkvhEKRLSNGSIDSTD 171
Cdd:TIGR04523 307 DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQL--------------------------KKELTNSESENSE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 172 ETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAEtarkdliKTEEMNTKYQRDIREAMAQKEDMEERITTLEK 251
Cdd:TIGR04523 361 KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ-------NQEKLNQQKDEQIKKLQQEKELLEKEIERLKE 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 252 RYLSAQREstsIHDmndkLENELANKEAILRQMEEKNRQLQERLEL-------AEQKLQQTMR-------KAETLPEVEA 317
Cdd:TIGR04523 434 TIIKNNSE---IKD----LTNQDSVKELIIKNLDNTRESLETQLKVlsrsinkIKQNLEQKQKelkskekELKKLNEEKK 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 318 ELAQRIAALTKaeeRHGNIEERMRHLEGQLEEKNQEL-QRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAA 396
Cdd:TIGR04523 507 ELEEKVKDLTK---KISSLKEKIEKLESEKKEKESKIsDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKK 583
|
410 420 430
....*....|....*....|....*....|....
gi 2462535318 397 LEEKNVLIQESETFRKNLEESLHDKERLAEEIEK 430
Cdd:TIGR04523 584 QEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEK 617
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
15-387 |
6.21e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 53.75 E-value: 6.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 15 ELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHErSLRMtvvKRQAQSPSGVSSEVEVLKALKSLFEHHKALD 94
Cdd:PRK01156 333 VLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIE-SLKK---KIEEYSKNIERMSAFISEILKIQEIDPDAIK 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 95 eKVRERLRVSLERVSAleeELAAANQEIVALREQNVHIQRKMASSEGSTESEhLEGMEPGQKVHEKRLSNGSIDSTDETS 174
Cdd:PRK01156 409 -KELNEINVKLQDISS---KVSSLNQRIRALRENLDELSRNMEMLNGQSVCP-VCGTTLGEEKSNHIINHYNEKKSRLEE 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 175 QIVELQELLEKQNYEMAQMKERLAALSSrvGEVEQ------EAETARKDL--IKTEEMNTKYQRDIREAMAQK------E 240
Cdd:PRK01156 484 KIREIEIEVKDIDEKIVDLKKRKEYLES--EEINKsineynKIESARADLedIKIKINELKDKHDKYEEIKNRykslklE 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 241 DMEERITTLEKryLSAQRESTSIhDMNDKLENELANK----------------------EAILRQMEEKNRQLQERLELA 298
Cdd:PRK01156 562 DLDSKRTSWLN--ALAVISLIDI-ETNRSRSNEIKKQlndlesrlqeieigfpddksyiDKSIREIENEANNLNNKYNEI 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 299 EQK--LQQTMR-KAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTV 375
Cdd:PRK01156 639 QENkiLIEKLRgKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRI 718
|
410
....*....|..
gi 2462535318 376 drllTESNERLQ 387
Cdd:PRK01156 719 ----NDINETLE 726
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
1014-1085 |
6.35e-07 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 47.68 E-value: 6.35e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535318 1014 VLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDEnfdysSLALLLQIPTQNTQARQILEREYNNLLA 1085
Cdd:smart00454 1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLT-----SEEDLKELGITKLGHRKKILKAIQKLKE 67
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
10-296 |
6.93e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 6.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 10 AALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQspsgvssevevlkalkslfeh 89
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIA--------------------- 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 90 hkALDEKvRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEgstesEHLEGMEPGQKVHEKRLSNGSIDS 169
Cdd:COG4913 672 --ELEAE-LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLE-----KELEQAEEELDELQDRLEAAEDLA 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 170 TDETSQivELQELLEKQNYEmAQMKERLAALSSRVGEVEQEAETARKDLIKT-EEMNTKYQRDIREAMAQKEDMEE---R 245
Cdd:COG4913 744 RLELRA--LLEERFAAALGD-AVERELRENLEERIDALRARLNRAEEELERAmRAFNREWPAETADLDADLESLPEylaL 820
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2462535318 246 ITTLEKRYLSAQREstsihDMNDKL-ENELANKEAILRQMEEKNRQLQERLE 296
Cdd:COG4913 821 LDRLEEDGLPEYEE-----RFKELLnENSIEFVADLLSKLRRAIREIKERID 867
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
174-462 |
7.86e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 7.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 174 SQIVELQELLEKQNYEMAQMKERLAALSSRvGEVEQEAETARKDLIKTEEmntkYQRDIREAMAQKED----------ME 243
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYSWDEIDVAS----AEREIAELEAELERldassddlaaLE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 244 ERITTLEKRYlsaqrestsihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlPEVEAELAQRI 323
Cdd:COG4913 692 EQLEELEAEL--------------EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR--LELRALLEERF 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 324 AALtKAEERHGNIEERmrhLEGQLEEKNQELQRARQR-EKMNEEHNKRLSDTVDRLLT--ESNERLQLHLK----ERMAA 396
Cdd:COG4913 756 AAA-LGDAVERELREN---LEERIDALRARLNRAEEElERAMRAFNREWPAETADLDAdlESLPEYLALLDrleeDGLPE 831
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462535318 397 LEEK--NVLIQESETFRKNLEESLHDKERLAEE-IEKLRSELDQLKMRTGSLIEPTIPRTHLDTSAELR 462
Cdd:COG4913 832 YEERfkELLNENSIEFVADLLSKLRRAIREIKErIDPLNDSLKRIPFGPGRYLRLEARPRPDPEVREFR 900
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
150-439 |
8.76e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.60 E-value: 8.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 150 GMEPGQKVHEKRLSNGSIdSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQ 229
Cdd:COG4372 1 GDRLGEKVGKARLSLFGL-RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 230 RDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKA 309
Cdd:COG4372 80 EELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 310 ETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLH 389
Cdd:COG4372 160 ESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2462535318 390 LKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLK 439
Cdd:COG4372 240 DALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALE 289
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
87-430 |
9.46e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 9.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 87 FEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSteseHLEGMEPGQKVHEKRLSNgS 166
Cdd:PTZ00121 1208 AEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMA----HFARRQAAIKAEEARKAD-E 1282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 167 IDSTDETSQIVELQELLEKQNYE----MAQMKERLAALSSRVGEVEQEAETARKdliKTEEMNTKYQRDIREAMAQKEDM 242
Cdd:PTZ00121 1283 LKKAEEKKKADEAKKAEEKKKADeakkKAEEAKKADEAKKKAEEAKKKADAAKK---KAEEAKKAAEAAKAEAEAAADEA 1359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 243 EERITTLEKRYLSAQRESTSIHDMNDKLEnELANKEAILRQMEEKNRQLQE--RLELAEQKLQQTMRKAETLPEVEaELA 320
Cdd:PTZ00121 1360 EAAEEKAEAAEKKKEEAKKKADAAKKKAE-EKKKADEAKKKAEEDKKKADElkKAAAAKKKADEAKKKAEEKKKAD-EAK 1437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 321 QRIAALTKAEERHGNIEERMRHLEgqLEEKNQELQRARQREKMNEEhnKRLSDTVDRLLTESNERLQlhlkERMAALEEK 400
Cdd:PTZ00121 1438 KKAEEAKKADEAKKKAEEAKKAEE--AKKKAEEAKKADEAKKKAEE--AKKADEAKKKAEEAKKKAD----EAKKAAEAK 1509
|
330 340 350
....*....|....*....|....*....|
gi 2462535318 401 nvliQESETFRKNLEESLHDKERLAEEIEK 430
Cdd:PTZ00121 1510 ----KKADEAKKAEEAKKADEAKKAEEAKK 1535
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
6-398 |
1.29e-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: 52.81 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 6 LQEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKrQAQSPSGVSSEVEVLKALKS 85
Cdd:pfam15921 460 LEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAE-ITKLRSRVDLKLQELQHLKN 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 86 LFEHhkaldekvrerLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHEKR--LS 163
Cdd:pfam15921 539 EGDH-----------LRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRleLQ 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 164 NGSIDSTDETSQIVELQELLEKQNYEMAQM----KERLAALSSRVGEVEQ---EAETARKDLIKTEEMNTKYQRDIREam 236
Cdd:pfam15921 608 EFKILKDKKDAKIRELEARVSDLELEKVKLvnagSERLRAVKDIKQERDQllnEVKTSRNELNSLSEDYEVLKRNFRN-- 685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 237 aQKEDMEERITTLEKRYLSAQRE----STSIHDMNDKLENELANKEAILRQMEEKNRQ---LQERLELAEQKLQQTMRKA 309
Cdd:pfam15921 686 -KSEEMETTTNKLKMQLKSAQSEleqtRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQidaLQSKIQFLEEAMTNANKEK 764
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 310 ETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMneehnkRLSDTVDRLLTESNERLQLH 389
Cdd:pfam15921 765 HFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASL------QFAECQDIIQRQEQESVRLK 838
|
....*....
gi 2462535318 390 LKERMAALE 398
Cdd:pfam15921 839 LQHTLDVKE 847
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
273-430 |
1.34e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.47 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 273 ELANKEAIlRQMEEKNRQLQERLELAEQKLQQTMRKAETlpEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ 352
Cdd:PRK12704 34 KEAEEEAK-RILEEAKKEAEAIKKEALLEAKEEIHKLRN--EFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 353 ELQRARQREKMNEEHNKRLSDTVDRLLTESNERLqlhlkERMAAL---EEKNVLIQESEtfrknlEESLHDKERLAEEIE 429
Cdd:PRK12704 111 ELEKKEKELEQKQQELEKKEEELEELIEEQLQEL-----ERISGLtaeEAKEILLEKVE------EEARHEAAVLIKEIE 179
|
.
gi 2462535318 430 K 430
Cdd:PRK12704 180 E 180
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
7-328 |
1.34e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.76 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 7 QEFAALTKELNACREQLLEKEEEISELKAErnntrllLEHLECLVSRHERSLrmtvvkrqaqspSGVSSEVEVLKA--LK 84
Cdd:TIGR02169 730 QEEEKLKERLEELEEDLSSLEQEIENVKSE-------LKELEARIEELEEDL------------HKLEEALNDLEArlSH 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 85 SLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEhlegmepGQKVHEKRLsn 164
Cdd:TIGR02169 791 SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI-------EKEIENLNG-- 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 165 gsidstdetsQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKdliKTEEMNTKYQRD---IREAMAQKED 241
Cdd:TIGR02169 862 ----------KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELER---KIEELEAQIEKKrkrLSELKAKLEA 928
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 242 MEERITTLEKRYLSAQRESTSIHDMnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQ 321
Cdd:TIGR02169 929 LEEELSEIEDPKGEDEEIPEEELSL-EDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILE 1007
|
....*..
gi 2462535318 322 RIAALTK 328
Cdd:TIGR02169 1008 RIEEYEK 1014
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
98-477 |
3.02e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 98 RERLRVSLERVSALEEELAAANQEIVALR-EQNVHIQRKMASSEGSTESEHLEGMEPGQKVHE------KRLSNGSIDST 170
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEaELDALQERREALQRLAEYSWDEIDVASAEREIAeleaelERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 171 DETSQIVELQEllekqnyEMAQMKERLAALSSRVGEVEQEAETArkdlikteemntkyQRDIREAMAQKEDMEERITTLE 250
Cdd:COG4913 689 ALEEQLEELEA-------ELEELEEELDELKGEIGRLEKELEQA--------------EEELDELQDRLEAAEDLARLEL 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 251 KRYLSAQRESTSIhdmnDKLENELAnkeailRQMEEKNRQLQERLELAEQKLQQTMRKA-ETLPEVEAELAQRIAALTKA 329
Cdd:COG4913 748 RALLEERFAAALG----DAVERELR------ENLEERIDALRARLNRAEEELERAMRAFnREWPAETADLDADLESLPEY 817
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 330 EERHGNIEERmrhlegQLEEKNQELQRARQR----------EKMNEEHN---KRLsDTVDRLLTESN----ERLQLHLKE 392
Cdd:COG4913 818 LALLDRLEED------GLPEYEERFKELLNEnsiefvadllSKLRRAIReikERI-DPLNDSLKRIPfgpgRYLRLEARP 890
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 393 RmaALEEKNVLIQE-----SETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIepTIPRTHLDTSAELRYSV-G 466
Cdd:COG4913 891 R--PDPEVREFRQElravtSGASLFDEELSEARFAALKRLIERLRSEEEESDRRWRARV--LDVRNHLEFDAEEIDREdG 966
|
410
....*....|.
gi 2462535318 467 SLVDSQSDYRT 477
Cdd:COG4913 967 EEVETYSSSGG 977
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
6-363 |
3.61e-06 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 50.84 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 6 LQEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKS 85
Cdd:pfam19220 19 LEDLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 86 LFEHHKALDEkVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGS-TESEHlegmepgqkvhekrlsn 164
Cdd:pfam19220 99 LREAEAAKEE-LRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKAlQRAEG----------------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 165 gSIDSTDETSQIVE-----LQELLEKQNYEmaqmkerLAALSSRVGEVEQEAETARKDLIKTE----EMNTKYQRDIREA 235
Cdd:pfam19220 161 -ELATARERLALLEqenrrLQALSEEQAAE-------LAELTRRLAELETQLDATRARLRALEgqlaAEQAERERAEAQL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 236 MAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQ-------LQERLELAEQKLQQTMRK 308
Cdd:pfam19220 233 EEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEasierdtLERRLAGLEADLERRTQQ 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462535318 309 AETLPEVEAELAQRI-----------AALTKAEERHGNIEERMRHLEGQ-------LEEKNQELQRARQREKM 363
Cdd:pfam19220 313 FQEMQRARAELEERAemltkalaakdAALERAEERIASLSDRIAELTKRfeveraaLEQANRRLKEELQRERA 385
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
231-408 |
5.11e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 5.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 231 DIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKA- 309
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALy 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 310 ---ETLPEVEA--------ELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL 378
Cdd:COG3883 97 rsgGSVSYLDVllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190
....*....|....*....|....*....|
gi 2462535318 379 LTESNERLQLHLKERMAALEEKNVLIQESE 408
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
170-438 |
5.49e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.79 E-value: 5.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 170 TDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKT-----------EEMNTKYQRDIReamaQ 238
Cdd:TIGR04523 92 KKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFlteikkkekelEKLNNKYNDLKK----Q 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 239 KEDMEERITTLEKRYLSAQREstsihdmNDKLENELANKE---AILRQMEEKNRQLQ-ERLELAEQKLQQTmrkaETLPE 314
Cdd:TIGR04523 168 KEELENELNLLEKEKLNIQKN-------IDKIKNKLLKLElllSNLKKKIQKNKSLEsQISELKKQNNQLK----DNIEK 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 315 VEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRArqrEKMNEEHNKRLSDTVDRLLTESNERLQLHLKERM 394
Cdd:TIGR04523 237 KQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN---NKKIKELEKQLNQLKSEISDLNNQKEQDWNKELK 313
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2462535318 395 AALEEKNVLIQESETFRKNLEESLhdkERLAEEIEKLRSELDQL 438
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKII---SQLNEQISQLKKELTNS 354
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
232-399 |
5.56e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.15 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 232 IREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAeqklqQTMRKAET 311
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-----RNNKEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 312 LpevEAELAQriaaltkAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLK 391
Cdd:COG1579 94 L---QKEIES-------LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
....*...
gi 2462535318 392 ERMAALEE 399
Cdd:COG1579 164 EREELAAK 171
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
64-439 |
7.73e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 7.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 64 KRQAQSPSGVSSEVEVL-KALKSLFEHHKALDEKVRERLRVSlERVSALEEELAAANQEIVALREQnvhIQRKMASSEGS 142
Cdd:COG4717 60 KPQGRKPELNLKELKELeEELKEAEEKEEEYAELQEELEELE-EELEELEAELEELREELEKLEKL---LQLLPLYQELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 143 TESEHLEGMEPGQKVHEKRLSngsidstdetsQIVELQELLEKQNYEMAQMKERLAALSSRVG-EVEQEAETARKDLIKT 221
Cdd:COG4717 136 ALEAELAELPERLEELEERLE-----------ELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 222 EEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQREST---------------SIHDMNDKLENELANKEAIL----- 281
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlkearlllliaaallALLGLGGSLLSLILTIAGVLflvlg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 282 ----------RQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKN 351
Cdd:COG4717 285 llallflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 352 QELQRARQREKMNE-------------EHNKRLSDTVDRLlTESNERLQLHLKERMAALE--EKNVLIQESETFRKNLEE 416
Cdd:COG4717 365 LEELEQEIAALLAEagvedeeelraalEQAEEYQELKEEL-EELEEQLEELLGELEELLEalDEEELEEELEELEEELEE 443
|
410 420
....*....|....*....|...
gi 2462535318 417 SLHDKERLAEEIEKLRSELDQLK 439
Cdd:COG4717 444 LEEELEELREELAELEAELEQLE 466
|
|
| SAM_superfamily |
cd09487 |
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
936-987 |
7.75e-06 |
|
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.
Pssm-ID: 188886 [Multi-domain] Cd Length: 56 Bit Score: 44.15 E-value: 7.75e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2462535318 936 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGI 987
Cdd:cd09487 4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
7-438 |
8.40e-06 |
|
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: 50.17 E-value: 8.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 7 QEFAALTKELNACRE---QLLEKEEEISELKAERNNT----RLLLEHLECLVSRHERSLRMTVVKRQAQSPSgvSSEVEV 79
Cdd:pfam01576 254 EETAQKNNALKKIREleaQISELQEDLESERAARNKAekqrRDLGEELEALKTELEDTLDTTAAQQELRSKR--EQEVTE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 80 LKalKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIV-------ALREQNVHIQRKMAS-SEGSTESEHlegm 151
Cdd:pfam01576 332 LK--KALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKAnlekakqALESENAELQAELRTlQQAKQDSEH---- 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 152 epGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEmaqmkerLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRD 231
Cdd:pfam01576 406 --KRKKLEGQLQELQARLSESERQRAELAEKLSKLQSE-------LESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQEL 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 232 IREAMAQKEDMEERITTLEKrylsaqrESTSIHDMndkLENELANKEAILRQMEEKNRQLQErlelAEQKLQQTMRKAET 311
Cdd:pfam01576 477 LQEETRQKLNLSTRLRQLED-------ERNSLQEQ---LEEEEEAKRNVERQLSTLQAQLSD----MKKKLEEDAGTLEA 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 312 LPEVEAELAQRIAALTKAEERHGNIEERM----RHLEGQLEEKNQELQRARQREKMNEEHNKRLsdtvDRLLTESNERLQ 387
Cdd:pfam01576 543 LEEGKKRLQRELEALTQQLEEKAAAYDKLektkNRLQQELDDLLVDLDHQRQLVSNLEKKQKKF----DQMLAEEKAISA 618
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2462535318 388 LHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQL 438
Cdd:pfam01576 619 RYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDL 669
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
171-435 |
9.53e-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: 49.97 E-value: 9.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 171 DETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVE----QEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERI 246
Cdd:pfam02463 159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKlqelKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 247 TTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAA- 325
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKe 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 326 ----LTKAEERHGNIEERMRHLEGQLEEKN---QELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALE 398
Cdd:pfam02463 319 sekeKKKAEKELKKEKEEIEELEKELKELEikrEAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
|
250 260 270
....*....|....*....|....*....|....*..
gi 2462535318 399 EKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSEL 435
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEE 435
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
7-354 |
1.00e-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: 49.82 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 7 QEFAALTKELNACREQLLEKEEEISELKAERNNtrlLLEHLEclvsrhERSLRMTVVKRQAQSPSGVSSEVEVlkALKSL 86
Cdd:pfam10174 373 EEKSTLAGEIRDLKDMLDVKERKINVLQKKIEN---LQEQLR------DKDKQLAGLKERVKSLQTDSSNTDT--ALTTL 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 87 FEhhkALDEKVR--ERLRVSLERVS-ALEEELAAANQEIVALREQNVHIQRKMASSEGSTES--EHLEGMEPGQKVHEKR 161
Cdd:pfam10174 442 EE---ALSEKERiiERLKEQREREDrERLEELESLKKENKDLKEKVSALQPELTEKESSLIDlkEHASSLASSGLKKDSK 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 162 LSNGSIDSTDETSQIVELQELLEK-QNYEMAQMKErlAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKE 240
Cdd:pfam10174 519 LKSLEIAVEQKKEECSKLENQLKKaHNAEEAVRTN--PEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKN 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 241 DMEERITTLEKRYLSaQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELA 320
Cdd:pfam10174 597 DKDKKIAELESLTLR-QMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQELDATK 675
|
330 340 350
....*....|....*....|....*....|....*....
gi 2462535318 321 QRIAALTKA-EERHGNIE----ERMRHLEGQLEEKNQEL 354
Cdd:pfam10174 676 ARLSSTQQSlAEKDGHLTnlraERRKQLEEILEMKQEAL 714
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
8-289 |
1.03e-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: 50.07 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 8 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRhERSLRMTVVKRQAQSpsgVSSEVEVLK-ALKSL 86
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKD-LGEEEQLRVKEKIGE---LEAEIASLErSIAEK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 87 FEHHKALDEKVR---ERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKV--HEKR 161
Cdd:TIGR02169 314 ERELEDAEERLAkleAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELkdYREK 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 162 LSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKED 241
Cdd:TIGR02169 394 LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD 473
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2462535318 242 MEERITTLEKRYLSAQREstsihdmndkleneLANKEAILRQMEEKNR 289
Cdd:TIGR02169 474 LKEEYDRVEKELSKLQRE--------------LAEAEAQARASEERVR 507
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
25-400 |
1.07e-05 |
|
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: 49.72 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 25 EKEEEISELKAERNNTRLLLEHLECLVSRHERSLR------------MTVVKRQAQSPSgvsSEVEVLKALKS-----LF 87
Cdd:pfam05483 332 EKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRteqqrleknedqLKIITMELQKKS---SELEEMTKFKNnkeveLE 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 88 EHHKALDEKvrERLRVSLERVSALEEELAAANQEIVAL---REQNVH---IQ------------RKMASSEGSTESEHLE 149
Cdd:pfam05483 409 ELKKILAED--EKLLDEKKQFEKIAEELKGKEQELIFLlqaREKEIHdleIQltaiktseehylKEVEDLKTELEKEKLK 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 150 GMEPGQKVHEKRLSNGSI--DSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLI-------- 219
Cdd:pfam05483 487 NIELTAHCDKLLLENKELtqEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIqkgdevkc 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 220 ---KTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMN---------------------DKLENELA 275
Cdd:pfam05483 567 kldKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENkalkkkgsaenkqlnayeikvNKLELELA 646
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 276 NKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETL--------PEVEAELAQRIAALTKAEERHGN-----IEERMRH 342
Cdd:pfam05483 647 SAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIadeavklqKEIDKRCQHKIAEMVALMEKHKHqydkiIEERDSE 726
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462535318 343 LeGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLT---ESNERLQLHLKERMAALEEK 400
Cdd:pfam05483 727 L-GLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEiekEEKEKLKMEAKENTAILKDK 786
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
175-447 |
1.31e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.63 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 175 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQK----------EDMEE 244
Cdd:TIGR04523 132 QKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLlklelllsnlKKKIQ 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 245 RITTLEKRYLSAQRESTSIHDMNDKLENELANKEAI-------LRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEA 317
Cdd:TIGR04523 212 KNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEisntqtqLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLN 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 318 ELAQRIAALTKAEERH---------GNIEERMRHLEGQLEEKNQELQRARQ------REKMNEEHNKRlsdTVDRLLTES 382
Cdd:TIGR04523 292 QLKSEISDLNNQKEQDwnkelkselKNQEKKLEEIQNQISQNNKIISQLNEqisqlkKELTNSESENS---EKQRELEEK 368
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462535318 383 NERLQLHLKERMAALEEKNVL----------IQESETFRKNLEESLH----DKERLAEEIEKLRSELDQLKMRTGSLIE 447
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLesqindleskIQNQEKLNQQKDEQIKklqqEKELLEKEIERLKETIIKNNSEIKDLTN 447
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
191-439 |
1.34e-05 |
|
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: 49.35 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 191 AQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRylsaqrestsihdmndkl 270
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKR------------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 271 eneLANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHgnieermrhlEGQLEEK 350
Cdd:pfam05557 64 ---EAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRA----------ELELQST 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 351 NQELQRARQRekmNEEHNKRLSDtvdrlLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAeEIEK 430
Cdd:pfam05557 131 NSELEELQER---LDLLKAKASE-----AEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELA-RIPE 201
|
....*....
gi 2462535318 431 LRSELDQLK 439
Cdd:pfam05557 202 LEKELERLR 210
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
271-439 |
1.63e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 271 ENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlpEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEK 350
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN---ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 351 NQELQRARQREKMNEE--HNKRLSDTVDRL-----LTESNERLQLHLKERMAALEEKnvliqesetfRKNLEESLHDKER 423
Cdd:COG3883 92 ARALYRSGGSVSYLDVllGSESFSDFLDRLsalskIADADADLLEELKADKAELEAK----------KAELEAKLAELEA 161
|
170
....*....|....*.
gi 2462535318 424 LAEEIEKLRSELDQLK 439
Cdd:COG3883 162 LKAELEAAKAELEAQQ 177
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
104-308 |
1.97e-05 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 46.82 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 104 SLERVSALEEELAAANQEIVALREQNVHIQRKmassegstesehlegmepgQKVHEKRLSNgsIDSTDEtsqivELQELL 183
Cdd:pfam15619 9 RLHKIKELQNELAELQSKLEELRKENRLLKRL-------------------QKRQEKALGK--YEGTES-----ELPQLI 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 184 EKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREA-MAQKEDMEERITTLEKRYLSAQREsts 262
Cdd:pfam15619 63 ARHNEEVRVLRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKnLAEREELQKKLEQLEAKLEDKDEK--- 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462535318 263 IHDMNDKLEN-------ELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK 308
Cdd:pfam15619 140 IQDLERKLELenksfrrQLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKERE 192
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
96-439 |
2.08e-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: 48.70 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 96 KVRERLRVSLERVSALEEELAAANQEIVALREQNvhiqrkmasSEGSTESEHLEGM--EPGQKVHEKRLSNG-SIDSTDE 172
Cdd:pfam06160 83 KAKKALDEIEELLDDIEEDIKQILEELDELLESE---------EKNREEVEELKDKyrELRKTLLANRFSYGpAIDELEK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 173 T-----SQIVELQELLEKQNYEMA-----QMKERLAALSSRVGEVEQEAETARKDLikTEEMNtkyqrDIREAMAQkedM 242
Cdd:pfam06160 154 QlaeieEEFSQFEELTESGDYLEArevleKLEEETDALEELMEDIPPLYEELKTEL--PDQLE-----ELKEGYRE---M 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 243 EERITTLEkrYLSAQRESTSIHDMNDKLENELANKEaiLRQMEEKNRQLQERLElaeqKLQQTMRKaetlpEVEAELaqr 322
Cdd:pfam06160 224 EEEGYALE--HLNVDKEIQQLEEQLEENLALLENLE--LDEAEEALEEIEERID----QLYDLLEK-----EVDAKK--- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 323 iaaltKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEH-------NKRLsDTVDRLLTESNERLQLH------ 389
Cdd:pfam06160 288 -----YVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYTLNENElervrglEKQL-EELEKRYDEIVERLEEKevayse 361
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2462535318 390 LKERMAALEEKNVLIQES-ETFRKNLeESLHDKERLA-EEIEKLRSELDQLK 439
Cdd:pfam06160 362 LQEELEEILEQLEEIEEEqEEFKESL-QSLRKDELEArEKLDEFKLELREIK 412
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
92-435 |
2.17e-05 |
|
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: 49.07 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 92 ALDEKVRERLRV-------SLERVSALEEELAAANqeiVALREQNVHIQRKMASSEGSTES-EHLEGMEPGQKVHEKRLS 163
Cdd:pfam12128 597 ASEEELRERLDKaeealqsAREKQAAAEEQLVQAN---GELEKASREETFARTALKNARLDlRRLFDEKQSEKDKKNKAL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 164 NGSIDSTDETSQIVELQE--LLEKQNYEMAQMKERLAALSSRVGEVEQEAETARK---DLIKTEEMNTKYQRDiREAMAQ 238
Cdd:pfam12128 674 AERKDSANERLNSLEAQLkqLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDaqlALLKAAIAARRSGAK-AELKAL 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 239 KEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQmeekNRQLQERLELAEQKLQQTMRKAET-LPEVEA 317
Cdd:pfam12128 753 ETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRY----FDWYQETWLQRRPRLATQLSNIERaISELQQ 828
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 318 ELAQRIAaltKAEERHGNIEERMRHLEGQLEEKNQELQRARQR-EKMNEEHnkrlsdtvdrlLTESNERLQLHLKERMAA 396
Cdd:pfam12128 829 QLARLIA---DTKLRRAKLEMERKASEKQQVRLSENLRGLRCEmSKLATLK-----------EDANSEQAQGSIGERLAQ 894
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2462535318 397 LEE-KNVLIQESETFRKNLEE-----SLHDKERLAEEIEKLRSEL 435
Cdd:pfam12128 895 LEDlKLKRDYLSESVKKYVEHfknviADHSGSGLAETWESLREED 939
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
261-371 |
2.69e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.28 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 261 TSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAEL---AQRIA--ALTKAEERHGN 335
Cdd:PRK00409 509 KLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLleeAEKEAqqAIKEAKKEADE 588
|
90 100 110
....*....|....*....|....*....|....*....
gi 2462535318 336 IEERMRHLE--GQLEEKNQELQRARQR-EKMNEEHNKRL 371
Cdd:PRK00409 589 IIKELRQLQkgGYASVKAHELIEARKRlNKANEKKEKKK 627
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
168-440 |
3.39e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 48.28 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 168 DSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKT-EEMNTKYQrdIREAMAQKEDMEERI 246
Cdd:pfam10174 158 ESIKKLLEMLQSKGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLrEELHRRNQ--LQPDPAKTKALQTVI 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 247 TTLEKRYLSAQRestSIHDMNDKLENELAN-------KEAILRQME----------EKNRQLQERLELAEQKLQQTMRKA 309
Cdd:pfam10174 236 EMKDTKISSLER---NIRDLEDEVQMLKTNgllhtedREEEIKQMEvykshskfmkNKIDQLKQELSKKESELLALQTKL 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 310 ETLPEVEAELAQRI----AALTKAEERHGNIEERMRHLEGQLEEKNQEL-QRARQREKMNEE---------HNKRLSDTV 375
Cdd:pfam10174 313 ETLTNQNSDCKQHIevlkESLTAKEQRAAILQTEVDALRLRLEEKESFLnKKTKQLQDLTEEkstlageirDLKDMLDVK 392
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462535318 376 DR---LLTESNERLQLHLKERMAALEEKNVLIQESETFRKN-------LEESLHDKERLAEEIEKLRSELDQLKM 440
Cdd:pfam10174 393 ERkinVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNtdtalttLEEALSEKERIIERLKEQREREDRERL 467
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
79-441 |
4.48e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 4.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 79 VLKALKSLFEhhKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSteSEHLEGMEPGQKVH 158
Cdd:COG4717 39 LLAFIRAMLL--ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEEL--EEELEELEAELEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 159 EKRLsngsidstDETSQIVELQELLEkqnyEMAQMKERLAALSSRVGEVEQEAET---ARKDLIKTEEMNTKYQRDIREA 235
Cdd:COG4717 115 REEL--------EKLEKLLQLLPLYQ----ELEALEAELAELPERLEELEERLEElreLEEELEELEAELAELQEELEEL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 236 MAQK-EDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQK-----------LQ 303
Cdd:COG4717 183 LEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliaaallaLL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 304 QTMRKAETLPEVEAELAQRIAAL--------TKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEhnkrLSDTV 375
Cdd:COG4717 263 GLGGSLLSLILTIAGVLFLVLGLlallflllAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPD----LSPEE 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462535318 376 DRLLTESNERLQLHLKERMAALEEknVLIQESETFRKNL--------EESLHDKERLAEEIEKLRSELDQLKMR 441
Cdd:COG4717 339 LLELLDRIEELQELLREAEELEEE--LQLEELEQEIAALlaeagvedEEELRAALEQAEEYQELKEELEELEEQ 410
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
87-434 |
4.78e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 87 FEHHKALDEKVRERLRVSLERVSALEEELAAANQeivALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHEKRLSNGS 166
Cdd:PTZ00121 1093 TEEAFGKAEEAKKTETGKAEEARKAEEAKKKAED---ARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEA 1169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 167 iDSTDETSQIVELQELLE-KQNYEMAQMKERLAALSSRVGEVEQEAETARK--DLIKTEEMNTKYQRDIREAMAQKEDmE 243
Cdd:PTZ00121 1170 -RKAEDAKKAEAARKAEEvRKAEELRKAEDARKAEAARKAEEERKAEEARKaeDAKKAEAVKKAEEAKKDAEEAKKAE-E 1247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 244 ERITTLEKRYLSAQRESTSIHDMNDKLENelANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRI 323
Cdd:PTZ00121 1248 ERNNEEIRKFEEARMAHFARRQAAIKAEE--ARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAE 1325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 324 AALTKAEERHGNIEERMRHLE---GQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNE-RLQLHLKERMAALEE 399
Cdd:PTZ00121 1326 EAKKKADAAKKKAEEAKKAAEaakAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkKKADEAKKKAEEDKK 1405
|
330 340 350
....*....|....*....|....*....|....*..
gi 2462535318 400 KNVLIQESETFRKNLEESLHDKE--RLAEEIEKLRSE 434
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKKAEekKKADEAKKKAEE 1442
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
78-259 |
5.46e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 5.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 78 EVLKALKSLFEHHKALDEkVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEgstesEHLEGMEPGQKV 157
Cdd:COG1579 4 EDLRALLDLQELDSELDR-LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLE-----LEIEEVEARIKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 158 HEKRLsnGSIDSTDEtsqivelQELLEKqnyEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMA 237
Cdd:COG1579 78 YEEQL--GNVRNNKE-------YEALQK---EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA 145
|
170 180
....*....|....*....|..
gi 2462535318 238 QKEDMEERITTLEKRyLSAQRE 259
Cdd:COG1579 146 ELDEELAELEAELEE-LEAERE 166
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
80-313 |
6.13e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 6.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 80 LKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEgstesEHLEGMEPGQKVHE 159
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE-----KEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 160 KRLSNgSIDSTDETSQIVELQELLEKQNyeMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQK 239
Cdd:COG4942 104 EELAE-LLRALYRLGRQPPLALLLSPED--FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462535318 240 EDMEERITTLEKryLSAQRESTSihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLP 313
Cdd:COG4942 181 AELEEERAALEA--LKAERQKLL-----ARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
289-486 |
7.04e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 47.01 E-value: 7.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 289 RQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERmrhlegqlEEKNQELQRARQREKMNEEHN 368
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRER--------EELQREEERLVQKEEQLDARA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 369 KRLSDTVDRLLTESN----ERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHD--KERLAEEIEKLRSELD-QLKMR 441
Cdd:PRK12705 98 EKLDNLENQLEEREKalsaRELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAelEEEKAQRVKKIEEEADlEAERK 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462535318 442 TGSLIEPTIPRTHLDTSAELRYSVgslVDSQSDYRTTKVIRRPRR 486
Cdd:PRK12705 178 AQNILAQAMQRIASETASDLSVSV---VPIPSDAMKGRIIGREGR 219
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
179-441 |
7.83e-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: 46.81 E-value: 7.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 179 LQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLiktEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQR 258
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQW---ERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 259 ESTSIHdmndklenelANKEAILRQMEEKNRQLQErLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEE-RHGNIE 337
Cdd:pfam07888 109 SSEELS----------EEKDALLAQRAAHEARIRE-LEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEaERKQLQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 338 ERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLH--LKERMAALEEK-NVLIQESETFR 411
Cdd:pfam07888 178 AKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLtqkLTTAHRKEAENeaLLEELRSLQERlNASERKVEGLG 257
|
250 260 270
....*....|....*....|....*....|
gi 2462535318 412 KNLEESLHDKERLAEEIEKLRSELDQLKMR 441
Cdd:pfam07888 258 EELSSMAAQRDRTQAELHQARLQAAQLTLQ 287
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
178-360 |
8.09e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.61 E-value: 8.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 178 ELQELLEKQNyEMAQMKERL-------AALSSRVGEVEQ-EAEtaRKDLIKTEEMNTKYQRdIREAMAQKED-MEERITT 248
Cdd:COG0497 173 ELEELRADEA-ERARELDLLrfqleelEAAALQPGEEEElEEE--RRRLSNAEKLREALQE-ALEALSGGEGgALDLLGQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 249 LEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQ---ERLELAEQKLQ---QTMRK----AETLPEVEAE 318
Cdd:COG0497 249 ALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEfdpERLEEVEERLAllrRLARKygvtVEELLAYAEE 328
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462535318 319 LAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQR 360
Cdd:COG0497 329 LRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKK 370
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
4-279 |
8.46e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 8.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 4 LFLQEFAALTKELNACREQLLEKEEEISELKAERNNTRlllehleclvsrherslrmtvvkrqaqspsgvSSEVEVLKAL 83
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALK--------------------------------KEEKALLKQL 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 84 KSLfehhkaldekvRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMAssegsTESEHLEGMEPGQKVHEKRLS 163
Cdd:COG4942 58 AAL-----------ERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE-----AQKEELAELLRALYRLGRQPP 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 164 NGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDM- 242
Cdd:COG4942 122 LALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLl 201
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2462535318 243 ---EERITTLEKRYLSAQRESTSIHDMNDKLENELANKEA 279
Cdd:COG4942 202 arlEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
239-438 |
1.01e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.83 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 239 KEDMEERITTLEKRYLSAQRESTSIHDmndkLENELANKEAILRQmEEKNRQLQERLELAEQKLQQTMRKAETLPEVEA- 317
Cdd:PRK11281 38 EADVQAQLDALNKQKLLEAEDKLVQQD----LEQTLALLDKIDRQ-KEETEQLKQQLAQAPAKLRQAQAELEALKDDNDe 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 318 ELAQRIAALTkaeerhgnieerMRHLEGQLEEKNQELQRARqrekmneehnKRLSDTVDRLLTESN--ERLQlhlkermA 395
Cdd:PRK11281 113 ETRETLSTLS------------LRQLESRLAQTLDQLQNAQ----------NDLAEYNSQLVSLQTqpERAQ-------A 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2462535318 396 ALEEKNVLIQESETFRKNLEESlhDKERLAEEIEKLRSELDQL 438
Cdd:PRK11281 164 ALYANSQRLQQIRNLLKGGKVG--GKALRPSQRVLLQAEQALL 204
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
806-870 |
1.07e-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: 1.07e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462535318 806 QWDGPTVVAWLElWLGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQEM 870
Cdd:pfam00536 2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
324-447 |
1.14e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.39 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 324 AALTKAEERHGNIEErmrhlegqlEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTEsNERLQLHLKERMAALEEknvL 403
Cdd:COG2433 380 EALEELIEKELPEEE---------PEAEREKEHEERELTEEEEEIRRLEEQVERLEAE-VEELEAELEEKDERIER---L 446
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2462535318 404 IQESETFRKNLEESLH-DKE--RLAEEIEKLRSELDQLKMRTGSLIE 447
Cdd:COG2433 447 ERELSEARSEERREIRkDREisRLDREIERLERELEEERERIEELKR 493
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
196-455 |
1.22e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 46.00 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 196 RLAALSSRVGEVEQEAET-----ARKDLIKTEEMNTKYQRDIR-------EAMAQKEDMEERITTLEKRY------LSAQ 257
Cdd:pfam06160 61 SLPDIEELLFEAEELNDKyrfkkAKKALDEIEELLDDIEEDIKqileeldELLESEEKNREEVEELKDKYrelrktLLAN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 258 RES--TSIhdmnDKLENELANKEAILRQMEEKN--------RQLQERLELAEQKLQQTMRK--------AETLPEVEAEL 319
Cdd:pfam06160 141 RFSygPAI----DELEKQLAEIEEEFSQFEELTesgdyleaREVLEKLEEETDALEELMEDipplyeelKTELPDQLEEL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 320 AQRIAALTKAEER--HGNIEERMRHLEGQLEE-----KNQELQRArqrEKMNEEHNKRLSDTVDRLLTESNERLQLH--- 389
Cdd:pfam06160 217 KEGYREMEEEGYAleHLNVDKEIQQLEEQLEEnlallENLELDEA---EEALEEIEERIDQLYDLLEKEVDAKKYVEknl 293
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462535318 390 --LKERMAALEEKNVLIQE-----SETFRKNlEESLHDKERLAEEIEKLRSELDQLKMRtgsLIEPTIPRTHL 455
Cdd:pfam06160 294 peIEDYLEHAEEQNKELKEelervQQSYTLN-ENELERVRGLEKQLEELEKRYDEIVER---LEEKEVAYSEL 362
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
95-332 |
1.36e-04 |
|
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: 45.53 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 95 EKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEgstesEHLEGMEPGQKVHEKRLSNGsidstdeTS 174
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA-----RRIRALEQELAALEAELAEL-------EK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 175 QIVELQELLEKQNYEMAQMKeRLAALSSRVGEVEQ--EAETArKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKR 252
Cdd:COG4942 91 EIAELRAELEAQKEELAELL-RALYRLGRQPPLALllSPEDF-LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 253 yLSAQREstsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEER 332
Cdd:COG4942 169 -LEAERA---------ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
1014-1084 |
1.38e-04 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 41.10 E-value: 1.38e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462535318 1014 VLVWSNDRVIRWIQAIGLREYANNILESGVHG--SLIALDENFdysslalLLQIPTQNTQARQILEREYNNLL 1084
Cdd:pfam07647 1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGaeLLLRLTLED-------LKRLGITSVGHRRKILKKIQELK 66
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
85-371 |
1.40e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 85 SLFEHHKALDEKVR--ERLRVSLERVSALEEELAAA---NQEIVALREQNVHIQRKMASSEGSTE--SEHLEGMEPGQKV 157
Cdd:PRK04863 797 ELAERYATLSFDVQklQRLHQAFSRFIGSHLAVAFEadpEAELRQLNRRRVELERALADHESQEQqqRSQLEQAKEGLSA 876
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 158 HEKRLsnGSIDSTDETSQIVELQELLEkQNYEMAQMKERLAALSSRVGEVEQEAETARKDliktEEMNTKYQRDIREAMA 237
Cdd:PRK04863 877 LNRLL--PRLNLLADETLADRVEEIRE-QLDEAEEAKRFVQQHGNALAQLEPIVSVLQSD----PEQFEQLKQDYQQAQQ 949
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 238 QKEDMEERITTL----EKR----YLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKA 309
Cdd:PRK04863 950 TQRDAKQQAFALtevvQRRahfsYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSY 1029
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535318 310 ETLPEVEAELAQRIAALT---------KAEERHGNIEERMRHLEGQleeKNQ-ELQRARQREKMNEEhNKRL 371
Cdd:PRK04863 1030 DAKRQMLQELKQELQDLGvpadsgaeeRARARRDELHARLSANRSR---RNQlEKQLTFCEAEMDNL-TKKL 1097
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
95-337 |
1.75e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 95 EKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEgstesehlegmepgqkvhekrlsngsidstdetS 174
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQ---------------------------------A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 175 QIVELQELLEKQNyemAQMKERLAAL---SSRVGEVEQ--EAETARKDLIKTEEMNTKYQRD---IREAMAQKEDMEERI 246
Cdd:COG3883 73 EIAEAEAEIEERR---EELGERARALyrsGGSVSYLDVllGSESFSDFLDRLSALSKIADADadlLEELKADKAELEAKK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 247 TTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAAL 326
Cdd:COG3883 150 AELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
250
....*....|.
gi 2462535318 327 TKAEERHGNIE 337
Cdd:COG3883 230 AAAAAAAAAAA 240
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
232-439 |
1.78e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 232 IREAMAQKEDMEERITTLEKRYlsaqresTSIHDMNDKLEnELANKEAILRQMEEKNRQLQE-RLELAEQKLQQTMRKAE 310
Cdd:COG4913 213 VREYMLEEPDTFEAADALVEHF-------DDLERAHEALE-DAREQIELLEPIRELAERYAAaRERLAELEYLRAALRLW 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 311 TLPEVEAELAQRIAALtkaEERHGNIEERMRHLEGQLEEKNQELQRARQRekmneehnkRLSDTVDRL--LTESNERLQL 388
Cdd:COG4913 285 FAQRRLELLEAELEEL---RAELARLEAELERLEARLDALREELDELEAQ---------IRGNGGDRLeqLEREIERLER 352
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462535318 389 HLKERMAALEEKNVLIQ--------ESETFRKNLEESLHDKERLAEEIEKLRSELDQLK 439
Cdd:COG4913 353 ELEERERRRARLEALLAalglplpaSAEEFAALRAEAAALLEALEEELEALEEALAEAE 411
|
|
| pepcterm_ChnLen |
TIGR03007 |
polysaccharide chain length determinant protein, PEP-CTERM locus subfamily; Members of this ... |
106-321 |
2.06e-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: 45.43 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 106 ERVSALEEELAAANQEIVALREQNVhiqrkmassegstesehleGMEPGQkvhekrlsngsidSTDETSQIVELQELLEK 185
Cdd:TIGR03007 168 EQIKTYEKKLEAAENRLKAFKQENG-------------------GILPDQ-------------EGDYYSEISEAQEELEA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 186 QNYEMAQMKERLAALSSRVGEVEQEAETARKDL-----IKTEEMNTKYQR----------DIREAMAQKEDMEERITTLE 250
Cdd:TIGR03007 216 ARLELNEAIAQRDALKRQLGGEEPVLLAGSSVAnseldGRIEALEKQLDAlrlrytdkhpDVIATKREIAQLEEQKEEEG 295
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462535318 251 KRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLElaeqklqQTMRKAETLPEVEAELAQ 321
Cdd:TIGR03007 296 SAKNGGPERGEIANPVYQQLQIELAEAEAEIASLEARVAELTARIE-------RLESLLRTIPEVEAELTQ 359
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
178-406 |
2.09e-04 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 44.33 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 178 ELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKryLSAQ 257
Cdd:pfam06008 27 QLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKE--INEK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 258 RESTSIHDM---NDKLENELANKEAILRQMeeKNRQLQERLELAEQKLqqtmRKAETLPEVEAELAQRIAALTKAeerhg 334
Cdd:pfam06008 105 VATLGENDFalpSSDLSRMLAEAQRMLGEI--RSRDFGTQLQNAEAEL----KAAQDLLSRIQTWFQSPQEENKA----- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 335 nIEERMRHLEGQLEEKNQELQ--------RARQREKMNEEHNKRLSDTVDRLLT--ESNERLQLHLKERMAALEEKNVLI 404
Cdd:pfam06008 174 -LANALRDSLAEYEAKLSDLRellreaaaKTRDANRLNLANQANLREFQRKKEEvsEQKNQLEETLKTARDSLDAANLLL 252
|
..
gi 2462535318 405 QE 406
Cdd:pfam06008 253 QE 254
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
178-441 |
2.59e-04 |
|
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: 44.52 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 178 ELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRE--AMAQKEDMEERITTLE--KRY 253
Cdd:pfam13868 56 ALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEedQAEAEEKLEKQRQLREeiDEF 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 254 LSAQRESTSIHDMNDKLENElANKEAILRQMEEKNRQLQERLELAEQK----------LQQTMRKAETLPEVEAELAQ-- 321
Cdd:pfam13868 136 NEEQAEWKELEKEEEREEDE-RILEYLKEKAEREEEREAEREEIEEEKereiarlraqQEKAQDEKAERDELRAKLYQee 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 322 -----RIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAA 396
Cdd:pfam13868 215 qerkeRQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRE 294
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2462535318 397 LEEknvLIQESE-TFRKNLEESLHDKERLAEEIEKLRSELDQLKMR 441
Cdd:pfam13868 295 LEK---QIEEREeQRAAEREEELEEGERLREEEAERRERIEEERQK 337
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
206-432 |
4.02e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.44 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 206 EVEQEAET-----ARKDLIKTEEMNTKYQRD---IREAMA----QKEDMEERITTLEKRYLSAQRE----STSIHDMNDK 269
Cdd:PRK04778 90 EAEELNDKfrfrkAKHEINEIESLLDLIEEDieqILEELQelleSEEKNREEVEQLKDLYRELRKSllanRFSFGPALDE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 270 LENELANKEAILRQMEEKN-----RQLQERLELAEQKLQQTMRKAETLPEVEAELAQRI-AALTKAEE------------ 331
Cdd:PRK04778 170 LEKQLENLEEEFSQFVELTesgdyVEAREILDQLEEELAALEQIMEEIPELLKELQTELpDQLQELKAgyrelveegyhl 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 332 RHGNIEERMRHLEGQLEEKNQELQR---ARQREKmNEEHNKRLSDTVDRLLTEsnerlqlhlkerMAAleeKNVLIQESE 408
Cdd:PRK04778 250 DHLDIEKEIQDLKEQIDENLALLEEldlDEAEEK-NEEIQERIDQLYDILERE------------VKA---RKYVEKNSD 313
|
250 260
....*....|....*....|....
gi 2462535318 409 TFRKNLEESLHDKERLAEEIEKLR 432
Cdd:PRK04778 314 TLPDFLEHAKEQNKELKEEIDRVK 337
|
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
99-526 |
4.33e-04 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 44.73 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 99 ERLRVSLERVsalEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHEK--RLSNGSID----STDE 172
Cdd:COG5192 363 EKMKMQLQEI---EQDPGVDGVGLQLFSNSDAIDTVDRESSEIDNVGRKTRRQPTGKAIAEEtsREDELSFDdsdvSTSD 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 173 TSQIVELQELLEKQNYEMAQMKERLAALSSRVGEvEQEAETARKDLIKTEEMNTkyQRDIREAMAQKEDMEERITTlEKR 252
Cdd:COG5192 440 ENEDVDFTGKKGAINNEDESDNEEVAFDSDSQFD-ESEGNLRWKEGLASKLAYS--QSGKRGRNIQKIFYDESLSP-EEC 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 253 YLSAQRESTSIHDMNDKLENElanKEAILRQMEEKNRQLQERLE-LAEQKLQQTMRKAETLPEVEAELAQriAALTKAEE 331
Cdd:COG5192 516 IEEYKGESAKSSESDLVVQDE---PEDFFDVSKVANESISSNHEkLMESEFEELKKKWSSLAQLKSRFQK--DATLDSIE 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 332 RHgniEErmrhLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEK---NVLIQESE 408
Cdd:COG5192 591 GE---EE----LIQDDEKGNFEDLEDEENSSDNEMEESRGSSVTAENEESADEVDYETEREENARKKEElrgNFELEERG 663
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 409 TFRKN-LEESLHDKERLAEEIEKLRSELDQLKMRTGSLIEPT------------IPRTHLDTSaELRYSV--GSLVDSQS 473
Cdd:COG5192 664 DPEKKdVDWYTEEKRKIEEQLKINRSEFETMVPESRVVIEGYragryvrivlshVPLEFVDEF-NSRYPIvlGGLLPAEK 742
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2462535318 474 DYRTTKV-IRRPRRGRMGVRRDEPKVKSLGdheWNRTQQIGVLSSHPFESDTEM 526
Cdd:COG5192 743 EMGIVQGrIKRHRWHKKILKTNDPLIFSVG---WRRFQSIPVYSMKDSRTRNRM 793
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
186-416 |
4.39e-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: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 186 QNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQR--DIREAMAQKEDMEERITTLEKRYLSAQREstsi 263
Cdd:COG3206 159 EAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQknGLVDLSEEAKLLLQQLSELESQLAEARAE---- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 264 hdmndklenelankeaiLRQMEEKNRQLQERLELAEQKLQQTMRkAETLPEVEAELAQRIAALTKAEERHGNIEERMRHL 343
Cdd:COG3206 235 -----------------LAEAEARLAALRAQLGSGPDALPELLQ-SPVIQQLRAQLAELEAELAELSARYTPNHPDVIAL 296
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462535318 344 EGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEE 416
Cdd:COG3206 297 RAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES 369
|
|
| SAM_STIM-1,2-like |
cd09504 |
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ... |
807-865 |
5.02e-04 |
|
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like (Stromal interaction molecule) proteins is a putative protein-protein interaction domain. STIM1 and STIM2 human proteins are type I transmembrane proteins. The N-terminal part of them includes "hidden" EF-hand and SAM domains. This region is responsible for sensing changes in store-operated and basal cytoplasmic Ca2+ levels and initiates oligomerization. "Hidden" EF hand and SAM domains have a stable intramolecular association, and the SAM domain is a component that regulates stability within STIM proteins. Destabilization of the EF-SAM association during Ca2+ depletion leads to partial unfolding and aggregation (homooligomerization), thus activating the store-operated Ca2+ entry. Immunoprecipitation analysis indicates that STIM1 and STIM2 can form co-precipitable oligomeric associations in vivo. It was suggested that STIM1 and STIM2 are involved in opposite regulation of store operated channels in plasma membrane.
Pssm-ID: 188903 Cd Length: 74 Bit Score: 39.62 E-value: 5.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535318 807 WDGPTVVAWLELWLGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNPLHRLKLRL 865
Cdd:cd09504 5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
268-442 |
5.46e-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: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 268 DKLENELANKEAILRQME------------EKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIaaltkaEERHGN 335
Cdd:cd00176 10 DELEAWLSEKEELLSSTDygddlesveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI------QERLEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 336 IEERMRHLEGQLEEKNQELQRARQREKMNEEH---NKRLSDTVDRLLTESN-------ERLQLHLKERMAALEEKNVLIQ 405
Cdd:cd00176 84 LNQRWEELRELAEERRQRLEEALDLQQFFRDAddlEQWLEEKEAALASEDLgkdlesvEELLKKHKELEEELEAHEPRLK 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462535318 406 ESETFRKNLEESLH--DKERLAEEIEKLRSELDQLKMRT 442
Cdd:cd00176 164 SLNELAEELLEEGHpdADEEIEEKLEELNERWEELLELA 202
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
173-438 |
5.61e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.06 E-value: 5.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 173 TSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLE-- 250
Cdd:PRK04778 111 ESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEEEFSQFVELTes 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 251 ------KRYLSAQRESTS------------IHDMNDKLENELANKEAILRQMEEKN-----RQLQERLELAEQKLQQTMR 307
Cdd:PRK04778 191 gdyveaREILDQLEEELAaleqimeeipelLKELQTELPDQLQELKAGYRELVEEGyhldhLDIEKEIQDLKEQIDENLA 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 308 KAETLpeveaelaqriaALTKAEERHGNIEERMRHLEGQLE---------EKNQElqRARQREKMNEEHNKRLSDTVDRL 378
Cdd:PRK04778 271 LLEEL------------DLDEAEEKNEEIQERIDQLYDILErevkarkyvEKNSD--TLPDFLEHAKEQNKELKEEIDRV 336
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462535318 379 -----LTESNERLQLHLKERMAALEEKNVLIQE---------SETfRKNLEESLHDKERLAEEIEKLRSELDQL 438
Cdd:PRK04778 337 kqsytLNESELESVRQLEKQLESLEKQYDEITEriaeqeiaySEL-QEELEEILKQLEEIEKEQEKLSEMLQGL 409
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
83-467 |
6.43e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 6.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 83 LKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEgstesehlegmepgqkvhekrl 162
Cdd:COG4372 15 LFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQAR---------------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 163 sngsidstdetSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLikteemnTKYQRDIREAMAQKEDM 242
Cdd:COG4372 73 -----------SELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL-------EELQKERQDLEQQRKQL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 243 EERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQME--EKNRQLQERLELAEQKLQQTMRKAETLPEVEAELA 320
Cdd:COG4372 135 EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSeaEAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 321 QRIAALT--KAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALE 398
Cdd:COG4372 215 ELAEELLeaKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALE 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462535318 399 EKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIEPTIPRTHLDTSAELRYSVGS 467
Cdd:COG4372 295 LKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGA 363
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
83-354 |
6.75e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.06 E-value: 6.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 83 LKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQnVHIQRKMASSEGSTESEHLEGMEPGQKVHEKrl 162
Cdd:pfam12128 260 LSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDE-LNGELSAADAAVAKDRSELEALEDQHGAFLD-- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 163 sngsidstDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETaRKDLIKtEEMNTKYQRDIREAMAQKEDM 242
Cdd:pfam12128 337 --------ADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNR-RRSKIK-EQNNRDIAGIKDKLAKIREAR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 243 EERITTLEKRYlsAQRESTSIHDMN-DKLENELANKEAILRQMEEKNR---------------QLQERLELAEQKLQQTM 306
Cdd:pfam12128 407 DRQLAVAEDDL--QALESELREQLEaGKLEFNEEEYRLKSRLGELKLRlnqatatpelllqleNFDERIERAREEQEAAN 484
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2462535318 307 RKAETLpevEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQEL 354
Cdd:pfam12128 485 AEVERL---QSELRQARKRRDQASEALRQASRRLEERQSALDELELQL 529
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
224-439 |
7.29e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.53 E-value: 7.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 224 MNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQREstsihdmndkLENELANKEAILRQMEEKNRQLQErleLAEQKLQ 303
Cdd:COG0497 138 LDPDAQRELLDAFAGLEELLEEYREAYRAWRALKKE----------LEELRADEAERARELDLLRFQLEE---LEAAALQ 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 304 qtmrkaetlPEVEAELAQRIAALTKAEERHGNIEERMRHLEGqlEEKN--QELQRARQR-EKMnEEHNKRLSDTVDRL-- 378
Cdd:COG0497 205 ---------PGEEEELEEERRRLSNAEKLREALQEALEALSG--GEGGalDLLGQALRAlERL-AEYDPSLAELAERLes 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 379 ----LTESNERLQLHLK------ERMAALEEK-----------NVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQ 437
Cdd:COG0497 273 alieLEEAASELRRYLDslefdpERLEEVEERlallrrlarkyGVTVEELLAYAEELRAELAELENSDERLEELEAELAE 352
|
..
gi 2462535318 438 LK 439
Cdd:COG0497 353 AE 354
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
174-326 |
7.92e-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: 41.82 E-value: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 174 SQIVELQELLEKQNYEMA-------QMKERLAALSSRVGEVEQEAETARKD---LIKTEEMNTKYQRDIREAMAQKEDME 243
Cdd:pfam13851 33 EEIAELKKKEERNEKLMSeiqqenkRLTEPLQKAQEEVEELRKQLENYEKDkqsLKNLKARLKVLEKELKDLKWEHEVLE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 244 ERITTLEKRY--LSAQREStSIHDMNDKLENE---LANK-EAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEA 317
Cdd:pfam13851 113 QRFEKVERERdeLYDKFEA-AIQDVQQKTGLKnllLEKKlQALGETLEKKEAQLNEVLAAANLDPDALQAVTEKLEDVLE 191
|
....*....
gi 2462535318 318 ELAQRIAAL 326
Cdd:pfam13851 192 SKNQLIKDL 200
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
6-597 |
8.09e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.91 E-value: 8.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 6 LQEFAALTKELNACREQLLEKEEEISELKAERNNTRlllehLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKS 85
Cdd:COG5022 884 LQELKIDVKSISSLKLVNLELESEIIELKKSLSSDL-----IENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNK 958
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 86 LFEHHKALDEKVRERLRVsLERVSALEEELAAANQEIVALreqnvhiQRKMASsegstesehlegmepgqkvhekrLSNG 165
Cdd:COG5022 959 LHEVESKLKETSEEYEDL-LKKSTILVREGNKANSELKNF-------KKELAE-----------------------LSKQ 1007
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 166 SIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQE-AETARKDLIKTEEMNTKYQRDIREAMAQKEDMEE 244
Cdd:COG5022 1008 YGALQESTKQLKELPVEVAELQSASKIISSESTELSILKPLQKLKgLLLLENNQLQARYKALKLRRENSLLDDKQLYQLE 1087
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 245 RITTLEKRYLSAQRESTSIHDMNDKLENELANKEAI----LRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAela 320
Cdd:COG5022 1088 STENLLKTINVKDLEVTNRNLVKPANVLQFIVAQMIklnlLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEAN--- 1164
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 321 qrIAALTKAEERHGNIEERMRHlEGQLEEKNqelqrarqreKMNEEHNKRLSDTVDRLLTESNERLQLHLKERmAALEEK 400
Cdd:COG5022 1165 --LEALPSPPPFAALSEKRLYQ-SALYDEKS----------KLSSSEVNDLKNELIALFSKIFSGWPRGDKLK-KLISEG 1230
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 401 NVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQL-KMRTGSLIEPTIprthldTSAELRYSVGSLVDSQSDyrttK 479
Cdd:COG5022 1231 WVPTEYSTSLKGFNNLNKKFDTPASMSNEKLLSLLNSIdNLLSSYKLEEEV------LPATINSLLQYINVGLFN----A 1300
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 480 VIRRPRRGRMGVRRDEPKVKSLgDHEWNRTQQIGVLSSHpFESDTEMSDI------DDDDRETIFSSMDLLSPsghsdAQ 553
Cdd:COG5022 1301 LRTKASSLRWKSATEVNYNSEE-LDDWCREFEISDVDEE-LEELIQAVKVlqllkdDLNKLDELLDACYSLNP-----AE 1373
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 2462535318 554 TLAMMLQEQL--------DAINKEI---RLIQEEKESTELRAEEIENRVASVSLE 597
Cdd:COG5022 1374 IQNLKSRYDPadkennlpKEILKKIealLIKQELQLSLEGKDETEVHLSEIFSEE 1428
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
292-430 |
9.36e-04 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 40.75 E-value: 9.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 292 QERLELAEQKLQQtmrkaetLPEVEAELAQRIAALTKaeeRHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRL 371
Cdd:pfam12718 13 QERAEELEEKVKE-------LEQENLEKEQEIKSLTH---KNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNENLTRKI 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462535318 372 sdtvdRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEK 430
Cdd:pfam12718 83 -----QLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEE 136
|
|
| PRK03992 |
PRK03992 |
proteasome-activating nucleotidase; Provisional |
392-450 |
1.04e-03 |
|
proteasome-activating nucleotidase; Provisional
Pssm-ID: 179699 [Multi-domain] Cd Length: 389 Bit Score: 42.90 E-value: 1.04e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 392 ERMAALEEKNV-LIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKmrTGSLIEPTI 450
Cdd:PRK03992 1 ERLEALEERNSeLEEQIRQLELKLRDLEAENEKLERELERLKSELEKLK--SPPLIVATV 58
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
206-439 |
1.08e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.17 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 206 EVEQEAETARKdlikteEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTsihdmndKLENELANKEAILRQME 285
Cdd:pfam05483 201 ELRVQAENARL------EMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQIT-------EKENKMKDLTFLLEESR 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 286 EKNRQLQERLELAEQKLQQTMRK----AETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQRE 361
Cdd:pfam05483 268 DKANQLEEKTKLQDENLKELIEKkdhlTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAH 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 362 KMNEEHNKRLSDTVDRLLTESNERLQLH---LKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQL 438
Cdd:pfam05483 348 SFVVTEFEATTCSLEELLRTEQQRLEKNedqLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQF 427
|
.
gi 2462535318 439 K 439
Cdd:pfam05483 428 E 428
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
7-146 |
1.21e-03 |
|
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: 41.83 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 7 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgVSSEVEVLKALKSL 86
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEA---LQKEIESLKRRISD 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 87 FEhhkaldekvrERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESE 146
Cdd:COG1579 108 LE----------DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
226-439 |
1.33e-03 |
|
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: 43.04 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 226 TKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIhDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQK---- 301
Cdd:pfam02463 165 SRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKL-KEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIdllq 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 302 -----LQQTMRKAETLPEVEAELAQRIAALTKAEERhgnIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRlsdtVD 376
Cdd:pfam02463 244 ellrdEQEEIESSKQEIEKEEEKLAQVLKENKEEEK---EKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE----KL 316
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462535318 377 RLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLK 439
Cdd:pfam02463 317 KESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKK 379
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
58-597 |
1.35e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.11 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 58 LRMTVVKRQAQspsgVSSEVEVLKALKSLFEHHKALDEKVRErlrvSLERVSALEEELAAANQEIVALREQNVHIQRKMA 137
Cdd:TIGR00606 222 IRDQITSKEAQ----LESSREIVKSYENELDPLKNRLKEIEH----NLSKIMKLDNEIKALKSRKKQMEKDNSELELKME 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 138 SSEGSTESEHLEgmepgqkVHEKRLSNGSidstDETSQIVELQELLEKQNYEMAQMKERLAALSSRVG------EVEQEA 211
Cdd:TIGR00606 294 KVFQGTDEQLND-------LYHNHQRTVR----EKERELVDCQRELEKLNKERRLLNQEKTELLVEQGrlqlqaDRHQEH 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 212 ETARKDLIKTEEMNTKY---------QRDIREAMA-QKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAIL 281
Cdd:TIGR00606 363 IRARDSLIQSLATRLELdgfergpfsERQIKNFHTlVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTI 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 282 RQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEErHGNIEERMRHLEGQLEEKNQELQRARQRE 361
Cdd:TIGR00606 443 ELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEK-NSLTETLKKEVKSLQNEKADLDRKLRKLD 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 362 KMNEEHNkRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETF--RKNLEESLH----DKERLAEEIEKLRSEL 435
Cdd:TIGR00606 522 QEMEQLN-HHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFpnKKQLEDWLHskskEINQTRDRLAKLNKEL 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 436 DQLKMRTGSLIEPTIPRTHLDTSAELR-YSVGSLVDSQSDY-RTTKVIRRPRRGRMGVRRDEPKVKSLGDHEWNRTQQIG 513
Cdd:TIGR00606 601 ASLEQNKNHINNELESKEEQLSSYEDKlFDVCGSQDEESDLeRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCC 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 514 VLSSHPFESDTEMSDIDDDdretiFSSMDLLSPSGHSDAQTLAMMLQEQLDAINKEIRLIQEEKESTELRAEEIENRVAS 593
Cdd:TIGR00606 681 PVCQRVFQTEAELQEFISD-----LQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQK 755
|
....
gi 2462535318 594 VSLE 597
Cdd:TIGR00606 756 VNRD 759
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
95-393 |
1.37e-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: 42.81 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 95 EKVRERLRVSLERVSALEEELAAANQeivALREQNVHIQRKMASSEGSTESEHlegmEPGQKVHEKRLSNGSI-DSTDET 173
Cdd:pfam05557 44 DRESDRNQELQKRIRLLEKREAEAEE---ALREQAELNRLKKKYLEALNKKLN----EKESQLADAREVISCLkNELSEL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 174 SQIVELQEL-LEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEE-------- 244
Cdd:pfam05557 117 RRQIQRAELeLQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIvknsksel 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 245 -RITTLEKRyLSAQRE-----STSIHDmNDKLENELANKEAILRQME---EKNRQLQERLELAEQKLQQ----------T 305
Cdd:pfam05557 197 aRIPELEKE-LERLREhnkhlNENIEN-KLLLKEEVEDLKRKLEREEkyrEEAATLELEKEKLEQELQSwvklaqdtglN 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 306 MRKAETLPEVEAELAQRIAALTkaeERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLltesNER 385
Cdd:pfam05557 275 LRSPEDLSRRIEQLQQREIVLK---EENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRL----QRR 347
|
....*...
gi 2462535318 386 LQLHLKER 393
Cdd:pfam05557 348 VLLLTKER 355
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
262-439 |
1.41e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 41.35 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 262 SIHDMND---KLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK---------AETLPEVEAELAQRIAALTKA 329
Cdd:COG1842 31 AIRDMEEdlvEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKgredlareaLERKAELEAQAEALEAQLAQL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 330 EERHGNIEERMRHLEGQLEEKNQELQRARQREKMNeEHNKRLSDTVDRLLTESNErlqlhlkERMAALEEKnvliQESET 409
Cdd:COG1842 111 EEQVEKLKEALRQLESKLEELKAKKDTLKARAKAA-KAQEKVNEALSGIDSDDAT-------SALERMEEK----IEEME 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 2462535318 410 FRKNLEESLHDKERLAEEIEKLRS------ELDQLK 439
Cdd:COG1842 179 ARAEAAAELAAGDSLDDELAELEAdsevedELAALK 214
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
178-444 |
1.75e-03 |
|
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: 42.25 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 178 ELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETAR-----KDLIKTEEMNTKYQRDIREA----MAQKEDMEERITT 248
Cdd:COG5185 272 ENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKateslEEQLAAAEAEQELEESKRETetgiQNLTAEIEQGQES 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 249 LEKRYLSAQRESTSIHDMND------KLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPE-------- 314
Cdd:COG5185 352 LTENLEAIKEEIENIVGEVElsksseELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEelqrqieq 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 315 VEAELAQRIAALTKAEERhgnIEERMRHLEGQLEEKNQELQRARQRE--KMNEEHNKRLSDTVDRLLT--ESNERLQLHL 390
Cdd:COG5185 432 ATSSNEEVSKLLNELISE---LNKVMREADEESQSRLEEAYDEINRSvrSKKEDLNEELTQIESRVSTlkATLEKLRAKL 508
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2462535318 391 KERMAALEEKNVLIQESETFRKNLEESLHDKERlaEEIEKLRSELDQLKMRTGS 444
Cdd:COG5185 509 ERQLEGVRSKLDQVAESLKDFMRARGYAHILAL--ENLIPASELIQASNAKTDG 560
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
215-438 |
1.82e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.76 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 215 RKDLIKTEEMNTKYQRDIREAMAQKEdMEERITTLEkrylsaqreSTSIHdmNDKLENELANKEAILRQMEEKNRQLQER 294
Cdd:COG5022 809 RKEYRSYLACIIKLQKTIKREKKLRE-TEEVEFSLK---------AEVLI--QKFGRSLKAKKRFSLLKKETIYLQSAQR 876
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 295 LELAEQK---LQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIE-----ERMRHLEGQLEEKNQELQRARQREKmNEE 366
Cdd:COG5022 877 VELAERQlqeLKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENlefktELIARLKKLLNNIDLEEGPSIEYVK-LPE 955
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535318 367 HNKRLsdTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQL 438
Cdd:COG5022 956 LNKLH--EVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEV 1025
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
165-348 |
1.86e-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: 41.59 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 165 GSIDSTDETSQIVELQELLEKQNYEMAQM---------KERLAALSSRVGEVEQEAETARKDLikteemnTKYQRDIrea 235
Cdd:cd22656 82 AQNAGGTIDSYYAEILELIDDLADATDDEeleeakktiKALLDDLLKEAKKYQDKAAKVVDKL-------TDFENQT--- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 236 MAQKEDMEERITTLEKRYlsaQRESTSIHDMN-DKLENELAN-KEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLP 313
Cdd:cd22656 152 EKDQTALETLEKALKDLL---TDEGGAIARKEiKDLQKELEKlNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLT 228
|
170 180 190
....*....|....*....|....*....|....*
gi 2462535318 314 EVEAELAQRIAALTKAEERHGNIEERMRHLEGQLE 348
Cdd:cd22656 229 AADTDLDNLLALIGPAIPALEKLQGAWQAIATDLD 263
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
936-991 |
2.64e-03 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 37.63 E-value: 2.64e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462535318 936 EWLPSLGLPQYRSYFMECLVD-ARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 991
Cdd:pfam07647 11 DWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLK-RLGITSVGHRRKILKKIQELK 66
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
289-437 |
2.74e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 289 RQLQERLELAEQKLQQTMRKAETlpevEAELAQRIAALTKAEERHgnieERMRHLEGQLEEKNQELQRARQREKMNEEHn 368
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKK----EAEAIKKEALLEAKEEIH----KLRNEFEKELRERRNELQKLEKRLLQKEEN- 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462535318 369 krlsdtvdrlltesnerlqlhLKERMAALEEKNvliQESETFRKNLEESLHDKERLAEEIEKLRSELDQ 437
Cdd:PRK12704 98 ---------------------LDRKLELLEKRE---EELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
64-287 |
2.80e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.60 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 64 KRQAQSPSGVSSEvEVLKALKSLFEHhKALDEK----VRERLRVSLERVSALE--EELAAAN-QEIVALREQNVHIQRKM 136
Cdd:pfam05622 189 KRQVQELHGKLSE-ESKKADKLEFEY-KKLEEKlealQKEKERLIIERDTLREtnEELRCAQlQQAELSQADALLSPSSD 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 137 ASSEGSTESEHLEGMEPGQKV-HE-KRLSNGSIDSTDEtsQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETA 214
Cdd:pfam05622 267 PGDNLAAEIMPAEIREKLIRLqHEnKMLRLGQEGSYRE--RLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEEL 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 215 RK----------DLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEkrylsaQRESTSIHDMNDKLENELANKEAILRQM 284
Cdd:pfam05622 345 QKalqeqgskaeDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELE------PKQDSNLAQKIDELQEALRKKDEDMKAM 418
|
...
gi 2462535318 285 EEK 287
Cdd:pfam05622 419 EER 421
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
180-358 |
2.94e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 40.51 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 180 QELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLikteEMNTKYQRDIREAmaqkEDMEERITTLEKRYLSaqre 259
Cdd:cd00176 64 EQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRL----EEALDLQQFFRDA----DDLEQWLEEKEAALAS---- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 260 stsihdmnDKLENELANKEAILRQMEEknrqLQERLELAEQKLQQTMRKAETLPEveaelAQRIAALTKAEERHGNIEER 339
Cdd:cd00176 132 --------EDLGKDLESVEELLKKHKE----LEEELEAHEPRLKSLNELAEELLE-----EGHPDADEEIEEKLEELNER 194
|
170
....*....|....*....
gi 2462535318 340 MRHLEGQLEEKNQELQRAR 358
Cdd:cd00176 195 WEELLELAEERQKKLEEAL 213
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
268-435 |
3.09e-03 |
|
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: 40.43 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 268 DKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlPEVEAELAQRIAALTKAEERHG-----------NI 336
Cdd:pfam04012 39 VKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGN--EELAREALAEKKSLEKQAEALEtqlaqqrsaveQL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 337 EERMRHLEGQLEEKNQE-------LQRARQREKMNEehnkrlsdTVDRLLTESNERLQLHLKERMAALEEKNVLIQESEt 409
Cdd:pfam04012 117 RKQLAALETKIQQLKAKknllkarLKAAKAQEAVQT--------SLGSLSTSSATDSFERIEEKIEEREARADAAAELA- 187
|
170 180
....*....|....*....|....*.
gi 2462535318 410 FRKNLEESLHDKERLAEEIEKLRSEL 435
Cdd:pfam04012 188 SAVDLDAKLEQAGIQMEVSEDVLARL 213
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
281-394 |
3.15e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 281 LRQMEEKNRQLQ-ERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQ 359
Cdd:COG0542 413 LDELERRLEQLEiEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEK 492
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462535318 360 R----EKMNEEHNKRLSDTVD-----------------RLLTESNERLqLHLKERM 394
Cdd:COG0542 493 ElaelEEELAELAPLLREEVTeediaevvsrwtgipvgKLLEGEREKL-LNLEEEL 547
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
98-434 |
3.17e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 41.39 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 98 RERLRVSLERVSAlEEELAAANQEIVALREQNVHIQRKMASSEGSTESEH----LEGMEPGQKVHEKRLSNGSIDSTDET 173
Cdd:pfam02029 12 RRRAREERRRQKE-EEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEeeafLDRTAKREERRQKRLQEALERQKEFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 174 SQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAmAQKEDMEERITTLEKRY 253
Cdd:pfam02029 91 PTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQA-EEEGEEEEDKSEEAEEV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 254 LSAQRESTSIHDMNDKLENELANKEAILRQMEEK--NRQLQERLELAEQKLQQTMRKAETLPEV---EAELAQRIAALTK 328
Cdd:pfam02029 170 PTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGhpEVKSQNGEEEVTKLKVTTKRRQGGLSQSqerEEEAEVFLEAEQK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 329 AEErhgnieERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLsdtvdrlltesnerlqlhlKERMAALEEKNVLIQESE 408
Cdd:pfam02029 250 LEE------LRRRRQEKESEEFEKLRQKQQEAELELEELKKKR-------------------EERRKLLEEEEQRRKQEE 304
|
330 340
....*....|....*....|....*.
gi 2462535318 409 TFRKNLEEslHDKERLAEEIEKLRSE 434
Cdd:pfam02029 305 AERKLREE--EEKRRMKEEIERRRAE 328
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
209-366 |
4.13e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 209 QEAETARKDLIKTEEmntkyqrdiREAMAQKEDMEerittlekryLSAQREstsIHDMNDKLENELANKEAILRQMEEKN 288
Cdd:PRK12704 34 KEAEEEAKRILEEAK---------KEAEAIKKEAL----------LEAKEE---IHKLRNEFEKELRERRNELQKLEKRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 289 RQLQERLElaeqklqqtmRKAETLPEVEAELAQRIAALTKAEErhgNIEERmrhlEGQLEEK----NQELQR-------- 356
Cdd:PRK12704 92 LQKEENLD----------RKLELLEKREEELEKKEKELEQKQQ---ELEKK----EEELEELieeqLQELERisgltaee 154
|
170
....*....|..
gi 2462535318 357 ARQR--EKMNEE 366
Cdd:PRK12704 155 AKEIllEKVEEE 166
|
|
| BAR_SNX7 |
cd07666 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 7; BAR domains are dimerization, lipid ... |
183-374 |
4.14e-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: 40.27 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 183 LEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQrDIREAMAQK----EDMEERITTLEKRYLSAQR 258
Cdd:cd07666 14 LTAQAWELSSHKKQGPGLLSRMGQTVKAVASSVRGVKNRPEEFTEMN-EYVEAFSQKinvlDKISQRIYKEQREYFEELK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 259 ESTSIHDMNDKLENELANK--------EAILRQMEEKNRQLQERLE-------LAEQKLQQTMRKAEtlpEVEAELAQRI 323
Cdd:cd07666 93 EYGPIYTLWSASEEELADSlkgmasciDRCCKATDKRMKGLSEQLLpviheyvLYSETLMGVIKRRD---QIQAELDSKV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2462535318 324 AALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDT 374
Cdd:cd07666 170 EALANKKADRDLLKEEIEKLEDKVECANNALKADWERWKQNMQTDLRSAFT 220
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
175-386 |
4.85e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 175 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTlekryl 254
Cdd:pfam01576 890 RIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKS------ 963
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 255 saqrestsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK-AETLPEVEAElaQRIAALTKAEERH 333
Cdd:pfam01576 964 --------------KFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKlKEVLLQVEDE--RRHADQYKDQAEK 1027
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2462535318 334 GNIeeRMRHLEGQLEEKNQELQRAR-QREKMNEEhnkrLSDTvdrllTESNERL 386
Cdd:pfam01576 1028 GNS--RMKQLKRQLEEAEEEASRANaARRKLQRE----LDDA-----TESNESM 1070
|
|
| SAM_superfamily |
cd09487 |
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
812-869 |
5.27e-03 |
|
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.
Pssm-ID: 188886 [Multi-domain] Cd Length: 56 Bit Score: 36.45 E-value: 5.27e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462535318 812 VVAWLElWLGMPaWYVAACRANVKSGAIMSALSDTEIQrEIGISNPLHRLKLRLAIQE 869
Cdd:cd09487 2 VAEWLE-SLGLE-QYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAIQR 56
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
93-395 |
5.67e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 40.62 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 93 LDEKVRERLRVSLERVSALEEELAAANqEIVALREQNVHIQRKmassEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDE 172
Cdd:pfam02029 71 REERRQKRLQEALERQKEFDPTIADEK-ESVAERKENNEEEEN----SSWEKEEKRDSRLGRYKEEETEIREKEYQENKW 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 173 TSQIVELQELLEKQNYEMAQMKERLAAlssRVGEVEQEAETARKDLIKTEEMNTKYQRD---IREAMAQKEDMEERITTL 249
Cdd:pfam02029 146 STEVRQAEEEGEEEEDKSEEAEEVPTE---NFAKEEVKDEKIKKEKKVKYESKVFLDQKrghPEVKSQNGEEEVTKLKVT 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 250 EKRYLSAQRESTSIH-DMNDKLENELAnkeailrqMEEKNRQLQERLELAEQKLQQTMRKAEtlpeveAELaqriaaltk 328
Cdd:pfam02029 223 TKRRQGGLSQSQEREeEAEVFLEAEQK--------LEELRRRRQEKESEEFEKLRQKQQEAE------LEL--------- 279
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462535318 329 aEERHGNIEERMRHLEgqlEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMA 395
Cdd:pfam02029 280 -EELKKKREERRKLLE---EEEQRRKQEEAERKLREEEEKRRMKEEIERRRAEAAEKRQKLPEDSSS 342
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
289-429 |
7.11e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 39.10 E-value: 7.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 289 RQLQERLELAEQKLQQTMRKAETLP----------------EVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ 352
Cdd:pfam12072 27 AKIGSAEELAKRIIEEAKKEAETKKkealleakeeihklraEAERELKERRNELQRQERRLLQKEETLDRKDESLEKKEE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 353 ELQRARQREKMNEEHNKRLSDTVDRLLTESNERLqlhlkERMAAL---EEKNVLIQESEtfrknlEESLHDKERLAEEIE 429
Cdd:pfam12072 107 SLEKKEKELEAQQQQLEEKEEELEELIEEQRQEL-----ERISGLtseEAKEILLDEVE------EELRHEAAVMIKEIE 175
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
84-373 |
7.13e-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: 40.51 E-value: 7.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 84 KSLFEHHKALDEKVRERLRvSLERVSALEEELAAANQEIVALREQNVH--IQRKMASSEGSTESEHLEGMEPGQKVHEKR 161
Cdd:pfam09731 121 KSEQEKEKALEEVLKEAIS-KAESATAVAKEAKDDAIQAVKAHTDSLKeaSDTAEISREKATDSALQKAEALAEKLKEVI 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 162 LSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAE-TARKDLIKTEEM---------------- 224
Cdd:pfam09731 200 NLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKElVASERIVFQQELvsifpdiipvlkednl 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 225 --NTKYQRDIREAMAQKEDMEERITTLEKR-YLSAQRESTSIHDMNDKLENELAnkEAILRQMEEKNRQLQERLELAEQK 301
Cdd:pfam09731 280 lsNDDLNSLIAHAHREIDQLSKKLAELKKReEKHIERALEKQKEELDKLAEELS--ARLEEVRAADEAQLRLEFEREREE 357
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462535318 302 LQQTMRKaetlpEVEAELAQRIAALTKaeerhgnieermrHLEGQLEEKNQELQRARQR---EKMNEEHNKRLSD 373
Cdd:pfam09731 358 IRESYEE-----KLRTELERQAEAHEE-------------HLKDVLVEQEIELQREFLQdikEKVEEERAGRLLK 414
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2-327 |
7.20e-03 |
|
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: 40.33 E-value: 7.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 2 NDLFLQEF---AALTKELNACREQLL----EKEEEISElKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVS 74
Cdd:COG5185 263 TDLRLEKLgenAESSKRLNENANNLIkqfeNTKEKIAE-YTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 75 SEvEVLKALKSLFEHHKALDEKVRERlrVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSegstESEHLEGMEPG 154
Cdd:COG5185 342 TA-EIEQGQESLTENLEAIKEEIENI--VGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGY----AQEILATLEDT 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 155 QKVHEKrlsngsidstdetsQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAetarkDLIKTEEMNTKYQRDIRE 234
Cdd:COG5185 415 LKAADR--------------QIEELQRQIEQATSSNEEVSKLLNELISELNKVMREA-----DEESQSRLEEAYDEINRS 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 235 AMAQKEDMEERITTLEKRYLSAQREstsIHDMNDKLENELANKEAILRQMEEK-NRQLQERLELAEQKLQQTMRKAETLP 313
Cdd:COG5185 476 VRSKKEDLNEELTQIESRVSTLKAT---LEKLRAKLERQLEGVRSKLDQVAESlKDFMRARGYAHILALENLIPASELIQ 552
|
330
....*....|....
gi 2462535318 314 EVEAELAQRIAALT 327
Cdd:COG5185 553 ASNAKTDGQAANLR 566
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
118-333 |
7.28e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 7.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 118 ANQEIVALREQNVHIQRKMAssegsTESEHLEGMEPGQKVHEKRLSNgSIDSTDET-----SQIVELQELL-------EK 185
Cdd:PHA02562 179 LNQQIQTLDMKIDHIQQQIK-----TYNKNIEEQRKKNGENIARKQN-KYDELVEEaktikAEIEELTDELlnlvmdiED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 186 QNYEMAQMKERLAALSSRVGEVEQEAE---------TARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSA 256
Cdd:PHA02562 253 PSAALNKLNTAAAKIKSKIEQFQKVIKmyekggvcpTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEF 332
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462535318 257 QRESTSIHDMNDKLENelaNKEAILRqMEEKNRQLQERLELAEqklQQTMRKAETLPEVEAELAQRIAALTK-AEERH 333
Cdd:PHA02562 333 NEQSKKLLELKNKIST---NKQSLIT-LVDKAKKVKAAIEELQ---AEFVDNAEELAKLQDELDKIVKTKSElVKEKY 403
|
|
| SAM_SARM1-like_repeat1 |
cd09501 |
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
936-980 |
7.73e-03 |
|
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of SARM1-like adaptor proteins is a protein-protein interaction domain. SARM1-like proteins contain two tandem SAM domains. SARM1-like proteins are involved in TLR (Toll-like receptor) signaling. They are responsible for targeted localization of the whole protein to post-synaptic regions of axons. In humans SARM1 expression is detected in kidney and liver.
Pssm-ID: 188900 [Multi-domain] Cd Length: 69 Bit Score: 36.13 E-value: 7.73e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2462535318 936 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHR 980
Cdd:cd09501 11 TWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLR 55
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
108-438 |
7.76e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 40.44 E-value: 7.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 108 VSALEEELAAANQEIVALREQnvhiqrkMASSEGSTESEHLEGMEPG--QKVHEK------RLSNGSID----STDETSQ 175
Cdd:pfam05622 23 VSLLQEEKNSLQQENKKLQER-------LDQLESGDDSGTPGGKKYLllQKQLEQlqeenfRLETARDDyrikCEELEKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 176 IVELQ---ELLEKQNYEMAQMKERLAAL---SSRVGEVEQEAETARK------DLIKT----EEMNTKYqrdireaMAQK 239
Cdd:pfam05622 96 VLELQhrnEELTSLAEEAQALKDEMDILresSDKVKKLEATVETYKKkledlgDLRRQvkllEERNAEY-------MQRT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 240 EDMEE---RITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQ---ERLELAEQKLQQTMRKAETLP 313
Cdd:pfam05622 169 LQLEEelkKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQkekERLIIERDTLRETNEELRCAQ 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 314 EVEAELAQRIAALTKAEERHGNIEERMRHLEgqLEEKNQELQRARQREKMNEEHNKRLSDT-VDRLLTESNER------- 385
Cdd:pfam05622 249 LQQAELSQADALLSPSSDPGDNLAAEIMPAE--IREKLIRLQHENKMLRLGQEGSYRERLTeLQQLLEDANRRkneletq 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462535318 386 ----------LQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQL 438
Cdd:pfam05622 327 nrlanqrileLQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEEL 389
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
178-371 |
7.86e-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: 40.02 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 178 ELQELLEKQNYEMAQMKERLAALSSRvgEVEQEAETARKDLIKTEEmntKYQRDIRE-AMAQKEDMEERITTLEKRYLSA 256
Cdd:pfam15558 35 EELRRRDQKRQETLERERRLLLQQSQ--EQWQAEKEQRKARLGREE---RRRADRREkQVIEKESRWREQAEDQENQRQE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 257 QRESTSIHDMNDKLENE--LANKEAILRQMEEKNR-QLQERLELAEQKLQQ--------------------TMRKAETLP 313
Cdd:pfam15558 110 KLERARQEAEQRKQCQEqrLKEKEEELQALREQNSlQLQERLEEACHKRQLkereeqkkvqennlsellnhQARKVLVDC 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462535318 314 EVEAELAQRIAAL----TKAEERH-GNIEERMRHLEGQLEEKNQELQRARQR-EKMNEEHNKRL 371
Cdd:pfam15558 190 QAKAEELLRRLSLeqslQRSQENYeQLVEERHRELREKAQKEEEQFQRAKWRaEEKEEERQEHK 253
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
298-439 |
8.29e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 39.58 E-value: 8.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 298 AEQKLQQTMRKAETlpeVEAELAQRIAALTKAE----ERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSD 373
Cdd:pfam02841 174 AEEVLQEFLQSKEA---VEEAILQTDQALTAKEkaieAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIE 250
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462535318 374 TVdrlltESNERLQLHLKERMAALEEknvliQESETFRKnleeslhdkERLAEEIEKLRSELDQLK 439
Cdd:pfam02841 251 KM-----EAEREQLLAEQERMLEHKL-----QEQEELLK---------EGFKTEAESLQKEIQDLK 297
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
200-439 |
8.72e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.00 E-value: 8.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 200 LSSRVGEVEQEAET--ARKDLIKTE-EMNTKYQRDIREAMAQkedmeeRITTLEKRYLSAQRESTSIHDMNDKLENELAN 276
Cdd:PHA02562 172 NKDKIRELNQQIQTldMKIDHIQQQiKTYNKNIEEQRKKNGE------NIARKQNKYDELVEEAKTIKAEIEELTDELLN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 277 keaILRQMEEKNRQLQE-RLELAEQKLQ-QTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQEL 354
Cdd:PHA02562 246 ---LVMDIEDPSAALNKlNTAAAKIKSKiEQFQKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAI 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 355 QRARQREKMNEEHNKRLSDTvdrlltesneRLQLHLKERMAALEEKNVLIQESETfrKNLEESLHDKErlaEEIEKLRSE 434
Cdd:PHA02562 323 DELEEIMDEFNEQSKKLLEL----------KNKISTNKQSLITLVDKAKKVKAAI--EELQAEFVDNA---EELAKLQDE 387
|
....*
gi 2462535318 435 LDQLK 439
Cdd:PHA02562 388 LDKIV 392
|
|
| Kre28 |
pfam17097 |
Spindle pole body component; In Saccharomyces cerevisae Kre28 and Spc105 form a kinetochore ... |
228-459 |
9.31e-03 |
|
Spindle pole body component; In Saccharomyces cerevisae Kre28 and Spc105 form a kinetochore microtubule binding complex, which bridges between centromeric heterochromatin and kinetochore MAPs (microtubule associated protein, such as Bim1, Bik1 and SIk19) and motors (Cin8, Kar3). It may be regulated by sumoylation.
Pssm-ID: 407241 [Multi-domain] Cd Length: 360 Bit Score: 39.79 E-value: 9.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 228 YQRDIREAMAQKEDM-EERITTLEKRYLSAQREST-SIHDMND-----KLENELANKEAILRQMEEKNRQLQERLELaeq 300
Cdd:pfam17097 9 YEAQLRELEEQTAHSsEQVLTEQDKRLLGALRELTqSVIQLIEenslvTVSGDAANLLIDPSGIEVKIRQLDQLVEL--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 301 kLQQTMRKAETLPEVEAELAQRIAAL---TKAEERHGNIEERMRHLE-GQLEEKNQELQRAR------------QREKMN 364
Cdd:pfam17097 86 -LKVTHLEQETLDNFLRYTISSTDLLqleSVSDPKYASLEDEVSQLEdDTLTVLNQEIDQIKgdilqvaqeiadKQDQVN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 365 EE--HNKRLSDTVDRLLTESNE-RLQLHLKERMAALEEKNVLIQESETFR--KNLEESLHDKERLAEEIEKLRSELDQLK 439
Cdd:pfam17097 165 ELclETSNELDECWELLNELERlRDQRITVEEQTSNEKDTELDPVEETYEewKSLQESLQQLEHLKEELDQLQKQKDSLE 244
|
250 260
....*....|....*....|
gi 2462535318 440 MRTGSliepTIPRTHLDTSA 459
Cdd:pfam17097 245 KVDKS----SINRTQNDEES 260
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
237-358 |
9.73e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.56 E-value: 9.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535318 237 AQKEDMEERITTLEKRYLSAQREstsihdmNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVE 316
Cdd:PRK09039 74 QGNQDLQDSVANLRASLSAAEAE-------RSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQI 146
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2462535318 317 AELAQRIAAL--------TKAEERHGNIEERMRHLEGQLEEKNQELQRAR 358
Cdd:PRK09039 147 AALRRQLAALeaaldaseKRDRESQAKIADLGRRLNVALAQRVQELNRYR 196
|
|
| |
