|
Name |
Accession |
Description |
Interval |
E-value |
| SAM_liprin-alpha1,2,3,4_repeat2 |
cd09565 |
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ... |
1027-1092 |
1.13e-42 |
|
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: 149.55 E-value: 1.13e-42
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1800081418 1027 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLRRL 1092
Cdd:cd09565 1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
|
|
| SAM_liprin-alpha1,2,3,4_repeat1 |
cd09562 |
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 ... |
910-980 |
1.58e-42 |
|
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.
Pssm-ID: 188961 Cd Length: 71 Bit Score: 149.25 E-value: 1.58e-42
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1800081418 910 FAQWDGPTVVVWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEIMSLT 980
Cdd:cd09562 1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
|
|
| SAM_liprin-alpha1,2,3,4_repeat3 |
cd09568 |
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ... |
1112-1183 |
3.99e-42 |
|
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: 148.23 E-value: 3.99e-42
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1800081418 1112 DVLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLL 1183
Cdd:cd09568 1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
|
|
| SAM_liprin-kazrin_repeat2 |
cd09495 |
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ... |
1031-1090 |
1.09e-28 |
|
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: 109.55 E-value: 1.09e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 1031 WIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLR 1090
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 ... |
917-975 |
2.19e-26 |
|
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: 102.69 E-value: 2.19e-26
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1800081418 917 TVVVWLELWVGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 975
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 ... |
1120-1181 |
2.43e-24 |
|
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: 97.23 E-value: 2.43e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1800081418 1120 RVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNN 1181
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 ... |
1112-1183 |
8.40e-22 |
|
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: 90.19 E-value: 8.40e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1800081418 1112 DVLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLL 1183
Cdd:cd09570 1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
266-548 |
1.02e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.23 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 266 QSQMKERLASLSSHvteleeDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDK 345
Cdd:COG1196 219 KEELKELEAELLLL------KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 346 LENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSDLLSSGSSAAKEAKLLELTS 425
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 426 KLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLL 505
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1800081418 506 REvESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASLHH 548
Cdd:COG1196 453 EL-EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
272-546 |
1.90e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 85.11 E-value: 1.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 272 RLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIA 351
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 352 NKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKsdllssgSSAAKEAKLLELTSKLRKAE 431
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA-------ELEELEAELEELESRLEELE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 432 ERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALE-DKNSLLREVES 510
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEeELEELQEELER 458
|
250 260 270
....*....|....*....|....*....|....*.
gi 1800081418 511 AKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASL 546
Cdd:TIGR02168 459 LEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
|
|
| SAM_kazrin_repeat1 |
cd09564 |
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ... |
911-975 |
2.86e-16 |
|
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: 74.41 E-value: 2.86e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1800081418 911 AQWDGPTVVVWLELWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 975
Cdd:cd09564 2 SRWKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
|
|
| SAM_liprin-beta1,2_repeat3 |
cd09569 |
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ... |
1112-1183 |
1.36e-15 |
|
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.
Pssm-ID: 188968 Cd Length: 72 Bit Score: 72.49 E-value: 1.36e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1800081418 1112 DVLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLL 1183
Cdd:cd09569 1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
|
|
| SAM_kazrin_repeat2 |
cd09567 |
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ... |
1026-1090 |
4.29e-15 |
|
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: 70.90 E-value: 4.29e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1800081418 1026 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLR 1090
Cdd:cd09567 1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
|
|
| SAM_liprin-beta1,2_repeat2 |
cd09566 |
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ... |
1026-1090 |
5.05e-15 |
|
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: 70.80 E-value: 5.05e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1800081418 1026 DMNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRNSFQCGIMCLR 1090
Cdd:cd09566 1 KLDTHWV-LRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDLL-HLKVTSALHHASIRRGIQVLR 63
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
246-467 |
5.72e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.82 E-value: 5.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 246 EEDLAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTL 325
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 326 EKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKS 405
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1800081418 406 DllssgssAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEE 467
Cdd:COG1196 444 L-------EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
1026-1090 |
9.59e-13 |
|
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: 64.21 E-value: 9.59e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1800081418 1026 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRNSFQCGIMCLR 1090
Cdd:pfam00536 1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
237-536 |
2.12e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 72.02 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 237 RSSDGSLSHEEDLAKVIELQEIISKqsreqsqMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKE 316
Cdd:TIGR02169 661 APRGGILFSRSEPAELQRLRERLEG-------LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 317 DMEERITTLEKRYLAAQREATSVHDLNDKLENEIAnkdsmhRQTEDKNrQLQERLE-----LAEQKLQQTLRKAETLPEV 391
Cdd:TIGR02169 734 KLKERLEELEEDLSSLEQEIENVKSELKELEARIE------ELEEDLH-KLEEALNdlearLSHSRIPEIQAELSKLEEE 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 392 EAELAQRVAALSKSDLLSSGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKR 471
Cdd:TIGR02169 807 VSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 472 LSDTVDKL-------------LSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEE---TQHDKDQLVLNIEALRAE 535
Cdd:TIGR02169 887 LKKERDELeaqlrelerkieeLEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEipeEELSLEDVQAELQRVEEE 966
|
.
gi 1800081418 536 L 536
Cdd:TIGR02169 967 I 967
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
244-517 |
2.31e-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: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 244 SHEEDLAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERIT 323
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 324 TLEKRYLAAQREATSVHDLNDKLENEiankdsmHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALS 403
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDELRAE-------LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 404 KSdLLSSGSSAAKEAKLLELTSKLRKAEERH--------GNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDT 475
Cdd:TIGR02168 859 AE-IEELEELIEELESELEALLNERASLEEAlallrselEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR 937
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1800081418 476 VDKLLSESNERLQL---HLKERMAALEDKNSLLR-EVESAKKQLEE 517
Cdd:TIGR02168 938 IDNLQERLSEEYSLtleEAEALENKIEDDEEEARrRLKRLENKIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
45-687 |
3.33e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.24 E-value: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNvCREQLLEREEEIAELKAE----RNN 120
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE-LEEQLETLRSKVAQLELQiaslNNE 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 121 TRLLLEHLECLVSRHER------SLRMTVVKRQAQSPAGVSSEVE-VLKALKSLFEHHKALDEKVRERLRVALERCSLLE 193
Cdd:TIGR02168 402 IERLEARLERLEDRRERlqqeieELLKKLEEAELKELQAELEELEeELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 194 EELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSdgSLSHEEDLAKVIE------LQEIISKqsREQS 267
Cdd:TIGR02168 482 RELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSE--LISVDEGYEAAIEaalggrLQAVVVE--NLNA 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 268 QMKErLASLSSH----VTELEEDLDTAR--------------------KDLIKSEE-----MNTKLQR-----DVREAMA 313
Cdd:TIGR02168 558 AKKA-IAFLKQNelgrVTFLPLDSIKGTeiqgndreilkniegflgvaKDLVKFDPklrkaLSYLLGGvlvvdDLDNALE 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 314 Q--KEDMEERITTLE-----KRYLAA-QREATSVHDLNdkLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKA 385
Cdd:TIGR02168 637 LakKLRPGYRIVTLDgdlvrPGGVITgGSAKTNSSILE--RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEEL 714
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 386 ETLPEVEAELAQRVAALSKSdllssgssaakeakLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMN 465
Cdd:TIGR02168 715 EQLRKELEELSRQISALRKD--------------LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA 780
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 466 EEHNKRLSDTVDKL----------LSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAE 535
Cdd:TIGR02168 781 EAEIEELEAQIEQLkeelkalreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 536 LDHMRLRGASLHHGRPHLGSVPDFRFPMADGHTDSYSTSAVLRRPQKGRLAALRDEPSKVQTLNEQDWERAQQASV-LAN 614
Cdd:TIGR02168 861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVrIDN 940
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1800081418 615 VAQAFESDAdvSDGEDDRDTLLSSVDLLSPSGQADAHTLAMMLQE----QLDAInkeirliqEEKENTEQRAEEIES 687
Cdd:TIGR02168 941 LQERLSEEY--SLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvNLAAI--------EEYEELKERYDFLTA 1007
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
192-490 |
9.93e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.70 E-value: 9.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 192 LEEELGATHKELMI--LKEQNNQKKTLTDGVLDINHEQENTPST--------SGKRSSDGSLSHEEDLA--KVIELQEII 259
Cdd:TIGR02168 218 LKAELRELELALLVlrLEELREELEELQEELKEAEEELEELTAElqeleeklEELRLEVSELEEEIEELqkELYALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 260 SKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSV 339
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 340 HDLNDKLENEIAnkdsmhrQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSDLlsSGSSAAKEAK 419
Cdd:TIGR02168 378 EEQLETLRSKVA-------QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL--QAELEELEEE 448
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1800081418 420 LLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLH 490
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
305-517 |
3.36e-11 |
|
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: 66.71 E-value: 3.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 305 QRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRK 384
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 385 AETLpevEAELAQRVAALSKS------DLLSSGSSAAKEAKLLELTSKLrkAEERHGNIEE------RLRQMEAQLEEKN 452
Cdd:COG4942 99 LEAQ---KEELAELLRALYRLgrqpplALLLSPEDFLDAVRRLQYLKYL--APARREQAEElradlaELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1800081418 453 QELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEE 517
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| SAM_liprin-beta1,2_repeat1 |
cd09563 |
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
910-974 |
4.82e-11 |
|
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: 59.55 E-value: 4.82e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1800081418 910 FAQWDGPTVVVWL-ELWVGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQ 974
Cdd:cd09563 1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
74-488 |
6.24e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.39 E-value: 6.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 74 ERDSLQRQLNtALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLLLEHLECLVSRHERSLRmTVVKRQAQSPAG 153
Cdd:TIGR02168 678 EIEELEEKIE-ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE-QLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 154 VSS----EVEVLKALKSLFEHHKALDEK---VRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTltdgvldinhe 226
Cdd:TIGR02168 756 LTEleaeIEELEERLEEAEEELAEAEAEieeLEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE----------- 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 227 qentpstsgkrssdGSLSHEEDLAKVIELQEIISKQSReqsQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQR 306
Cdd:TIGR02168 825 --------------RLESLERRIAATERRLEDLEEQIE---ELSEDIESLAAEIEELEELIEELESELEALLNERASLEE 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 307 DVREAMAQKEDMEERITTLEKRYLAAQREAtsvHDLNDKLEneiankdsmhrqtedknrQLQERLELAEQKLQQTLRKAE 386
Cdd:TIGR02168 888 ALALLRSELEELSEELRELESKRSELRREL---EELREKLA------------------QLELRLEGLEVRIDNLQERLS 946
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 387 TLPEVEAELAQRVAALSKSDllssgsSAAKEAKLLELTSKLRK-------AEERHGNIEERLRQMEAQLEeknqELQRAR 459
Cdd:TIGR02168 947 EEYSLTLEEAEALENKIEDD------EEEARRRLKRLENKIKElgpvnlaAIEEYEELKERYDFLTAQKE----DLTEAK 1016
|
410 420 430
....*....|....*....|....*....|....
gi 1800081418 460 QR-----EKMNEEHNKRLSDTVDKLlsesNERLQ 488
Cdd:TIGR02168 1017 ETleeaiEEIDREARERFKDTFDQV----NENFQ 1046
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
54-402 |
5.23e-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: 64.31 E-value: 5.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 54 LRETQETLALTQGKLHEVGHERDSLQRQLNTAlpQEFAALTKELNvcREQLLEREEEIAELKAERNNTRLLLEHLECLVS 133
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKSLERQAEKA--ERYKELKAELR--ELELALLVLRLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 134 RHERSlrmtvvkrqaqspagvssevevLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQk 213
Cdd:TIGR02168 257 ELTAE----------------------LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 214 ktltdgvLDINHEQENTPSTSGKRSSDGSLSHEEDLAKVI-ELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARK 292
Cdd:TIGR02168 314 -------LERQLEELEAQLEELESKLDELAEELAELEEKLeELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 293 DLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHdlNDKLENEIANKDSMHRQTEDKNRQLQERLE 372
Cdd:TIGR02168 387 KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALE 464
|
330 340 350
....*....|....*....|....*....|
gi 1800081418 373 LAEQKLQQTLRKAETLPEVEAELAQRVAAL 402
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQLQARLDSL 494
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
45-517 |
1.80e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLL 124
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 125 LEHLECLVSRHERSLRMTVVKRQAQSpagvssevEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELM 204
Cdd:COG1196 403 EELEEAEEALLERLERLEEELEELEE--------ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 205 ILKEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDLAKVI-ELQEIISKQSREQSQMKERLASLSSH-VTE 282
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAgAVAVLIGVEAAYEAALEAALAAALQNiVVE 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 283 LEEDLDTARKDLikseemntKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDsmhRQTED 362
Cdd:COG1196 555 DDEVAAAAIEYL--------KAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVL---GDTLL 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 363 KNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSDLLSSGSSAAKEAKLLELTSKLRKAEERHGNIEERLR 442
Cdd:COG1196 624 GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE 703
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1800081418 443 QMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEE 517
Cdd:COG1196 704 EEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
152-537 |
4.45e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 4.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 152 AGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTL---TDGVLDINHEQE 228
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELkekAEEYIKLSEFYE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 229 NTpstsgkrsSDGSLSHEEDLAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQR-- 306
Cdd:PRK03918 304 EY--------LDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEle 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 307 --DVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIAN-KDSMHRQTEDK------NRQLQE--RLELAE 375
Cdd:PRK03918 376 rlKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKElKKAIEELKKAKgkcpvcGRELTEehRKELLE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 376 Q------KLQQTLRKA-ETLPEVEAELAQRVAALSKSDLLSSGSSAAKEAKLLE------LTSKLRKAEERHGNIEERLR 442
Cdd:PRK03918 456 EytaelkRIEKELKEIeEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEeklkkyNLEELEKKAEEYEKLKEKLI 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 443 QMEAQLEEKNQELQRARQREKMNEEHNKRLsDTVDKLLSESNERLQL-------HLKERMAALEDKNSLLREVESAKKQL 515
Cdd:PRK03918 536 KLKGEIKSLKKELEKLEELKKKLAELEKKL-DELEEELAELLKELEElgfesveELEERLKELEPFYNEYLELKDAEKEL 614
|
410 420
....*....|....*....|..
gi 1800081418 516 EETQHDKDQLVLNIEALRAELD 537
Cdd:PRK03918 615 EREEKELKKLEEELDKAFEELA 636
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
158-525 |
4.76e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.82 E-value: 4.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 158 VEVLKALKSLFEHHkaldEKVRERLRVALERCSLLEEELGATHKELMILKEQnnqKKTLTDGVLDINHEQENTPSTSGKR 237
Cdd:PRK02224 233 RETRDEADEVLEEH----EERREELETLEAEIEDLRETIAETEREREELAEE---VRDLRERLEELEEERDDLLAEAGLD 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 238 SSDGS--LSHEEDLAKVI-ELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQ 314
Cdd:PRK02224 306 DADAEavEARREELEDRDeELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREE 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 315 KEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQ--------QTLRK-- 384
Cdd:PRK02224 386 IEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEagkcpecgQPVEGsp 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 385 -AETLPEVE---AELAQRVAAL-SKSDLLSSGSSAAKEAKllELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRAR 459
Cdd:PRK02224 466 hVETIEEDRervEELEAELEDLeEEVEEVEERLERAEDLV--EAEDRIERLEERREDLEELIAERRETIEEKRERAEELR 543
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1800081418 460 ------------QREKMNEEHNKrlSDTVDKLLSESNERLQlHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQL 525
Cdd:PRK02224 544 eraaeleaeaeeKREAAAEAEEE--AEEAREEVAELNSKLA-ELKERIESLERIRTLLAAIADAEDEIERLREKREAL 618
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
44-537 |
5.52e-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: 60.75 E-value: 5.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 44 LEERDRLLDTLR-ETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTR 122
Cdd:TIGR00618 417 SAFRDLQGQLAHaKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARL 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 123 LLLEHLECLVSRHERSLRMTVVkrQAQSPAGVSSEVEvlkALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKE 202
Cdd:TIGR00618 497 LELQEEPCPLCGSCIHPNPARQ--DIDNPGPLTRRMQ---RGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQS 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 203 LMILKEQNNQKKTLTDGVLDINHE-QENTPSTSGKRSSDGSLSHEEDLakviELQEIISKQ--SREQSQMKERLASLSSH 279
Cdd:TIGR00618 572 FSILTQCDNRSKEDIPNLQNITVRlQDLTEKLSEAEDMLACEQHALLR----KLQPEQDLQdvRLHLQQCSQELALKLTA 647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 280 VTELEEDLdtarkdlikseemntkLQRDVREAMAQKEDMEERitTLEKRYLAAQREATSVHDLNDKLEnEIANKDSMHR- 358
Cdd:TIGR00618 648 LHALQLTL----------------TQERVREHALSIRVLPKE--LLASRQLALQKMQSEKEQLTYWKE-MLAQCQTLLRe 708
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 359 --QTEDKNRQLQERLELAEQKLQQTLR-KAETLPEVEAEL-AQRVAALSKSDLlssgssaAKEAKLLELTSKLRKAEErh 434
Cdd:TIGR00618 709 leTHIEEYDREFNEIENASSSLGSDLAaREDALNQSLKELmHQARTVLKARTE-------AHFNNNEEVTAALQTGAE-- 779
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 435 gnieerLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQ 514
Cdd:TIGR00618 780 ------LSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLK 853
|
490 500
....*....|....*....|...
gi 1800081418 515 LEETQHDKDQLVLNIEALRAELD 537
Cdd:TIGR00618 854 YEECSKQLAQLTQEQAKIIQLSD 876
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
249-534 |
6.32e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 60.74 E-value: 6.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 249 LAKVIE---LQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEmntklqrDVREAMAQKEDMEERITTL 325
Cdd:PRK04863 337 LNLVQTalrQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEE-------EVDELKSQLADYQQALDVQ 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 326 EKR---YLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTlRKAETLPEVEAELAQRVAA- 401
Cdd:PRK04863 410 QTRaiqYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVA-QAAHSQFEQAYQLVRKIAGe 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 402 LSKSDllssgssAAKEAKlleltSKLRKAEErHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDklls 481
Cdd:PRK04863 489 VSRSE-------AWDVAR-----ELLRRLRE-QRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLD---- 551
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1800081418 482 eSNERLQLHLKERMAALEDKNSllrEVESAKKQLEETQHDKDQLVLNIEALRA 534
Cdd:PRK04863 552 -DEDELEQLQEELEARLESLSE---SVSEARERRMALRQQLEQLQARIQRLAA 600
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
256-486 |
1.08e-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: 58.62 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 256 QEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQRE 335
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 336 AtsvhdlnDKLENEIANkdsMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSDLLSSGSSAA 415
Cdd:COG4942 99 L-------EAQKEELAE---LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1800081418 416 KEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNER 486
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
285-546 |
1.11e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 285 EDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTED-- 362
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElk 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 363 --------KNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSDLLSSGSSAAKEAKLlELTSKLRKAEERH 434
Cdd:PRK03918 238 eeieelekELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYE-EYLDELREIEKRL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 435 GNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDtvdklLSESNERLQ--LHLKERMAALEDKNSLLrEVESAK 512
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEE-----LEERHELYEeaKAKKEELERLKKRLTGL-TPEKLE 390
|
250 260 270
....*....|....*....|....*....|....
gi 1800081418 513 KQLEETQHDKDQLVLNIEALRAELDHMRLRGASL 546
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKEL 424
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
246-450 |
1.34e-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: 56.86 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 246 EEDLAKVIELQEIISkqsrEQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTL 325
Cdd:COG1579 3 PEDLRALLDLQELDS----ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 326 EKRylaaQREATSVHDLNDkLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQqtlrkaetlpEVEAELAQRVAALsks 405
Cdd:COG1579 79 EEQ----LGNVRNNKEYEA-LQKEIESLKRRISDLEDEILELMERIEELEEELA----------ELEAELAELEAEL--- 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1800081418 406 dllssgssAAKEAKLLELTSKLRKAEERhgnIEERLRQMEAQLEE 450
Cdd:COG1579 141 --------EEKKAELDEELAELEAELEE---LEAEREELAAKIPP 174
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
268-521 |
1.68e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.20 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 268 QMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMA-QKEDMEERITTLEKRYLAAQREATSVhDLNDKL 346
Cdd:PRK04863 841 QLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLlADETLADRVEEIREQLDEAEEAKRFV-QQHGNA 919
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 347 ENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLpeveAELAQRVAALSKSDllsSGSSAAKEAKLLE-LTS 425
Cdd:PRK04863 920 LAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFAL----TEVVQRRAHFSYED---AAEMLAKNSDLNEkLRQ 992
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 426 KLRKAEERHGNIEERLRQMEAQLEEKNQ---ELQRARQR-EKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAAL--- 498
Cdd:PRK04863 993 RLEQAEQERTRAREQLRQAQAQLAQYNQvlaSLKSSYDAkRQMLQELKQELQDLGVPADSGAEERARARRDELHARLsan 1072
|
250 260 270
....*....|....*....|....*....|.
gi 1800081418 499 -EDKNSLLR-------EVESAKKQLEETQHD 521
Cdd:PRK04863 1073 rSRRNQLEKqltfceaEMDNLTKKLRKLERD 1103
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
45-525 |
2.52e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNtALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLL 124
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRR-ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 125 LEHLECLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELM 204
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 205 ILKEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSRE--QSQMKERLASLSSHVTE 282
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLllLLEAEADYEGFLEGVKA 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 283 LEEDLDTARKDLIKSEEMNTK--------------LQRDVREAMAQ--------KEDMEERITTLEKRyLAAQREATSVH 340
Cdd:COG1196 513 ALLLAGLRGLAGAVAVLIGVEaayeaaleaalaaaLQNIVVEDDEVaaaaieylKAAKAGRATFLPLD-KIRARAALAAA 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 341 DLNDKLENEIANKDSMHRQTEDKNRQLQERLE---LAEQKLQQTLRKAETLPEVEAELAQRVAALSKSDLLSSGSSAAKE 417
Cdd:COG1196 592 LARGAIGAAVDLVASDLREADARYYVLGDTLLgrtLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 418 AKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAA 497
Cdd:COG1196 672 AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
|
490 500
....*....|....*....|....*...
gi 1800081418 498 LEDKNSLLREVESAKKQLEETQHDKDQL 525
Cdd:COG1196 752 ALEELPEPPDLEELERELERLEREIEAL 779
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
68-680 |
3.00e-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: 58.59 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 68 LHEVGHERDSLQRQLNTA-----------------LPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLLLEHLEC 130
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESnelhekqkfylrqsvidLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 131 LVSR--HERSLRMTVVKRQAQSPAGVSSEVEVL------KALKSLFEHH-------KALDEKVRERLRVALERCSLLEEE 195
Cdd:pfam15921 160 LKEDmlEDSNTQIEQLRKMMLSHEGVLQEIRSIlvdfeeASGKKIYEHDsmstmhfRSLGSAISKILRELDTEISYLKGR 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 196 LGATHKELMILKEQNNQKKTL-----TDGV--LDINHEQENTPST---SGKRSSDGSLSHEedlakvielQEIISKQSRE 265
Cdd:pfam15921 240 IFPVEDQLEALKSESQNKIELllqqhQDRIeqLISEHEVEITGLTekaSSARSQANSIQSQ---------LEIIQEQARN 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 266 QSQMKER-LASLSSHVTELEEDLDTARKD-------------LIKSEEMNTKLQRD--VREAMAQKEDMEERITTLEKRY 329
Cdd:pfam15921 311 QNSMYMRqLSDLESTVSQLRSELREAKRMyedkieelekqlvLANSELTEARTERDqfSQESGNLDDQLQKLLADLHKRE 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 330 LAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQeRLELAEQKLqqtlrKAETLPEVEAELAQ---RVAALSKSD 406
Cdd:pfam15921 391 KELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQ-RLEALLKAM-----KSECQGQMERQMAAiqgKNESLEKVS 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 407 LLSSGSSAAKEA--KLLE-LTSK---LRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLL 480
Cdd:pfam15921 465 SLTAQLESTKEMlrKVVEeLTAKkmtLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 481 SESNE----RLQLHLKERM-----------------------AALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALR 533
Cdd:pfam15921 545 NVQTEcealKLQMAEKDKVieilrqqienmtqlvgqhgrtagAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELE 624
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 534 AELDHMRLRGASL-HHGRPHLGSVPDF---RFPMADGHTDSYSTSAVLRRPQKGRLAALRDEPSKVQ-TLNEQDWERAQQ 608
Cdd:pfam15921 625 ARVSDLELEKVKLvNAGSERLRAVKDIkqeRDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMEtTTNKLKMQLKSA 704
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1800081418 609 ASVLANVAQAFESdADVSDGEDDRDTLLSSVDLLSPSGQADA-HTLAMMLQEQLDAINKEIRLIQEEKENTEQ 680
Cdd:pfam15921 705 QSELEQTRNTLKS-MEGSDGHAMKVAMGMQKQITAKRGQIDAlQSKIQFLEEAMTNANKEKHFLKEEKNKLSQ 776
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
38-533 |
5.10e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 57.75 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 38 QLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHER--DSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELK 115
Cdd:TIGR00606 353 QLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERqiKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIR 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 116 AERNNTRLLLEHLECLVSRHERSLRMtvVKRQAQSPAGVSSEV-----EVLKALK--SLFEHHKALDEKVRERLRVALER 188
Cdd:TIGR00606 433 DEKKGLGRTIELKKEILEKKQEELKF--VIKELQQLEGSSDRIleldqELRKAERelSKAEKNSLTETLKKEVKSLQNEK 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 189 CSLLEE--ELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPStsgkRSSDGSLSHEEDLAKVIELQEIISKQSREQ 266
Cdd:TIGR00606 511 ADLDRKlrKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKS----RHSDELTSLLGYFPNKKQLEDWLHSKSKEI 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 267 SQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQkEDMEERITTLEKRYLAAQREA---TSVHDLN 343
Cdd:TIGR00606 587 NQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS-QDEESDLERLKEEIEKSSKQRamlAGATAVY 665
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 344 DKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAET-LPEVEAELAQrvaalsksdllssgssaaKEAKLLE 422
Cdd:TIGR00606 666 SQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDkLKSTESELKK------------------KEKRRDE 727
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 423 LtskLRKAEERHGNIEERLRQMEaQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESN---------ERLQLHLKE 493
Cdd:TIGR00606 728 M---LGLAPGRQSIIDLKEKEIP-ELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKvcltdvtimERFQMELKD 803
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1800081418 494 ------RMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALR 533
Cdd:TIGR00606 804 verkiaQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNR 849
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
254-526 |
7.03e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 57.27 E-value: 7.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 254 ELQEIiskqSREQSQMKERLASLSSHVTELEEDLDTARKDLikseemnTKLQRDVREAMA-QKEDMEERITTLEKRYLAA 332
Cdd:COG3096 837 ELAAL----RQRRSELERELAQHRAQEQQLRQQLDQLKEQL-------QLLNKLLPQANLlADETLADRLEELREELDAA 905
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 333 QREATSVHDLNDKLEnEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLpeveAELAQRVAALSKSDL--LSS 410
Cdd:COG3096 906 QEAQAFIQQHGKALA-QLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFAL----SEVVQRRPHFSYEDAvgLLG 980
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 411 GSSAAKEAklleLTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQ----RARQREKMNEEHNKRLSDTVDKLLSESNER 486
Cdd:COG3096 981 ENSDLNEK----LRARLEQAEEARREAREQLRQAQAQYSQYNQVLAslksSRDAKQQTLQELEQELEELGVQADAEAEER 1056
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1800081418 487 LQLHLKERMAALEDKNSLLREVEsakKQLEETQHDKDQLV 526
Cdd:COG3096 1057 ARIRRDELHEELSQNRSRRSQLE---KQLTRCEAEMDSLQ 1093
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
37-540 |
9.31e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 9.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 37 EQLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHERDSLqrqlnTALPQEFAALTKELNVCREQLLEREEEIAELKA 116
Cdd:PRK03918 199 EKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEI-----EELEKELESLEGSKRKLEEKIRELEERIEELKK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 117 ERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpagVSSEVEvlKALKSLFEHHKALDEKVRErLRVALERCSLLEEEL 196
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAEEYIKLSEFYEEYLD---ELREIE--KRLSRLEEEINGIEERIKE-LEEKEERLEELKKKL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 197 GATHKELMILKEqnnqKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDLAKV-IELQEIISKQSREQSQMKERLAS 275
Cdd:PRK03918 348 KELEKRLEELEE----RHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAkEEIEEEISKITARIGELKKEIKE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 276 LSSHVTELE-----------EDLDTARKDLIK--SEEMNtKLQRDVREAMAQKEDMEERITTLEKrYLAAQREATSVHDL 342
Cdd:PRK03918 424 LKKAIEELKkakgkcpvcgrELTEEHRKELLEeyTAELK-RIEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKEL 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 343 NDKLENeiankdsmhrqtedknrqLQERLE-LAEQKLQQTLRKAETLPEVEAELAQRVAALsKSDLlssGSSAAKEAKLL 421
Cdd:PRK03918 502 AEQLKE------------------LEEKLKkYNLEELEKKAEEYEKLKEKLIKLKGEIKSL-KKEL---EKLEELKKKLA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 422 ELTSKLRKAEERHGNIEERLRQM----EAQLEEKNQELQR----------ARQREKMNEEHNKRLSDTVDKL---LSESN 484
Cdd:PRK03918 560 ELEKKLDELEEELAELLKELEELgfesVEELEERLKELEPfyneylelkdAEKELEREEKELKKLEEELDKAfeeLAETE 639
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1800081418 485 ERLQlHLKERMAALEDKNS-------------LLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMR 540
Cdd:PRK03918 640 KRLE-ELRKELEELEKKYSeeeyeelreeyleLSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
254-540 |
9.83e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 56.72 E-value: 9.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 254 ELQEIISKQSREQSQMKE---RLASLSSHVTELEEDLDTARKDLIKSEemntKLQRDVREAM-AQKEDMEERI-TTLEKR 328
Cdd:pfam01576 244 ELQAALARLEEETAQKNNalkKIRELEAQISELQEDLESERAARNKAE----KQRRDLGEELeALKTELEDTLdTTAAQQ 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 329 YLAAQREaTSVHDLNDKLENEIANKDSMHRQTEDKNRQ----LQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSK 404
Cdd:pfam01576 320 ELRSKRE-QEVTELKKALEEETRSHEAQLQEMRQKHTQaleeLTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQ 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 405 SDLLSSGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRArqrEKMNEEHNKRLSdTVDKLLSESN 484
Cdd:pfam01576 399 AKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEA---EGKNIKLSKDVS-SLESQLQDTQ 474
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1800081418 485 ERLQ------LHLKERMAALEDKNSLLREvesakkQLEETQHDKDQLVLNIEALRAELDHMR 540
Cdd:pfam01576 475 ELLQeetrqkLNLSTRLRQLEDERNSLQE------QLEEEEEAKRNVERQLSTLQAQLSDMK 530
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
257-462 |
1.00e-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: 56.61 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 257 EIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREA 336
Cdd:TIGR02169 280 KIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEY 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 337 TSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELA----------EQKLQQTLRKA---------------ETLPEV 391
Cdd:TIGR02169 360 AELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLkreinelkreLDRLQEELQRLseeladlnaaiagieAKINEL 439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1800081418 392 EAELAQRVAALSKSDLLSSGSSAAK---EAKLLELTSKLRKaeerhgnIEERLRQMEAQLEEKNQELQRARQRE 462
Cdd:TIGR02169 440 EEEKEDKALEIKKQEWKLEQLAADLskyEQELYDLKEEYDR-------VEKELSKLQRELAEAEAQARASEERV 506
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
251-467 |
1.51e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.22 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 251 KVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAmaqKEDMEERITTLEKRYL 330
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA---EAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 331 AAQR------------EATSVHDLNDKLE--NEI--ANKDSMHRQTEDKnrqlqERLELAEQKLQQTLRKAETLpevEAE 394
Cdd:COG3883 94 ALYRsggsvsyldvllGSESFSDFLDRLSalSKIadADADLLEELKADK-----AELEAKKAELEAKLAELEAL---KAE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1800081418 395 LAQRVAALsksdllssgssaakEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEE 467
Cdd:COG3883 166 LEAAKAEL--------------EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
282-475 |
1.52e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 282 ELEEDLD-----TARKDLIKSEEMNtKLQRDVREAMAQKED---MEERITTLEKRYLAAQREATSVHDLNDKLENEIANK 353
Cdd:COG4717 50 RLEKEADelfkpQGRKPELNLKELK-ELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 354 DSMHRQTEDKNR--QLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALsksDLLSSGSSAAKEAKLLELTSKLRKAE 431
Cdd:COG4717 129 PLYQELEALEAElaELPERLEELEERLEELRELEEELEELEAELAELQEEL---EELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1800081418 432 ERHGNIEERLRQMEAQLEEKNQELQRArQREKMNEEHNKRLSDT 475
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQL-ENELEAAALEERLKEA 248
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
32-560 |
2.01e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 32 ADSHFEQLMVSMLEER-DRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTA-------LPQEFAALTKELNVCREQ 103
Cdd:COG4913 281 LRLWFAQRRLELLEAElEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrleqLEREIERLERELEERERR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 104 LLEREEEIA-----------ELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSP--AGVSSEVEVLKALKSLFEH 170
Cdd:COG4913 361 RARLEALLAalglplpasaeEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRelRELEAEIASLERRKSNIPA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 171 HkalDEKVRERLRvalERCSLLEEEL---GathkELMILKEQ------------NNQKKTL------------------T 217
Cdd:COG4913 441 R---LLALRDALA---EALGLDEAELpfvG----ELIEVRPEeerwrgaiervlGGFALTLlvppehyaaalrwvnrlhL 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 218 DGVLDINHEQENTPSTSGKRSSDGSLSHeedlakvielqEIISKQSREQSQMKERLASLSSHVT-ELEEDLDTARKD--- 293
Cdd:COG4913 511 RGRLVYERVRTGLPDPERPRLDPDSLAG-----------KLDFKPHPFRAWLEAELGRRFDYVCvDSPEELRRHPRAitr 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 294 --LIKSEemNTKLQRDVREAMAQK----EDMEERITTLEKRYLAAQREATSVHDLNDKLENEIankdsmhrqtedknRQL 367
Cdd:COG4913 580 agQVKGN--GTRHEKDDRRRIRSRyvlgFDNRAKLAALEAELAELEEELAEAEERLEALEAEL--------------DAL 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 368 QERLElAEQKLQQTLRKAETLPEVEAELAQRVAALSKsdlLSSGSSaakeaKLLELTSKLRKAEERHGNIEERLRQMEAQ 447
Cdd:COG4913 644 QERRE-ALQRLAEYSWDEIDVASAEREIAELEAELER---LDASSD-----DLAALEEQLEELEAELEELEEELDELKGE 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 448 LEEKNQELQRARQREkmneehnKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVL 527
Cdd:COG4913 715 IGRLEKELEQAEEEL-------DELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
|
570 580 590
....*....|....*....|....*....|...
gi 1800081418 528 NIEALRAEldHMRLRGASLHHGRPHLGSVPDFR 560
Cdd:COG4913 788 ELERAMRA--FNREWPAETADLDADLESLPEYL 818
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
303-519 |
2.06e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 303 KLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIAnkdsmhrqtedknrQLQERLELAEQKLQQTl 382
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID--------------KLQAEIAEAEAEIEER- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 383 rkaetlpevEAELAQRVAALSKSDLLSSGSSAAKEAK----LLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRA 458
Cdd:COG3883 85 ---------REELGERARALYRSGGSVSYLDVLLGSEsfsdFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1800081418 459 RQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQ 519
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
55-537 |
2.44e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 55 RETQETLALTQGKLHevGHERDSLQRQLNTALpQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLLLEHLeclvsr 134
Cdd:COG1196 216 RELKEELKELEAELL--LLKLRELEAELEELE-AELEELEAELEELEAELAELEAELEELRLELEELELELEEA------ 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 135 heRSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKK 214
Cdd:COG1196 287 --QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 215 TLTDGVLDINHEQEntpstsgKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDL 294
Cdd:COG1196 365 EALLEAEAELAEAE-------EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 295 IKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELA 374
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 375 EQK-LQQTLRKAETLPEVEAELAQRVAALSKSDLLSSGSSAAKEAKLLELTSKLRKAEERHGNIEERlRQMEAQLEEKNQ 453
Cdd:COG1196 518 GLRgLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRA-RAALAAALARGA 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 454 ELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAA--LEDKNSLLREVESAKKQLEETQHDKDQLVLNIEA 531
Cdd:COG1196 597 IGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVtlAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLE 676
|
....*.
gi 1800081418 532 LRAELD 537
Cdd:COG1196 677 AEAELE 682
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
1113-1183 |
2.47e-07 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 48.83 E-value: 2.47e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1800081418 1113 VLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDfsalaLLLQIPTQNTQARAVLEREFNNLL 1183
Cdd:smart00454 1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEE-----DLKELGITKLGHRKKILKAIQKLK 66
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
250-541 |
2.55e-07 |
|
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: 54.69 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 250 AKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRY 329
Cdd:pfam19220 48 SRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 330 LAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALsksdlls 409
Cdd:pfam19220 128 AAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAEL------- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 410 SGSSAAKEAKLLELTSKLrkAEERhgniEERLRQMEAQLEEKN-QELQRARQREKMnEEHNKRLSDTvDKLLSESNErlq 488
Cdd:pfam19220 201 ETQLDATRARLRALEGQL--AAEQ----AERERAEAQLEEAVEaHRAERASLRMKL-EALTARAAAT-EQLLAEARN--- 269
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1800081418 489 lHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMRL 541
Cdd:pfam19220 270 -QLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARA 321
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
365-535 |
2.96e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 365 RQLQERLELAEQKLQQTLRKAETLPEVEAELAQrvAALSKSDLLSSGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQM 444
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEE--LEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 445 EAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQ 524
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
170
....*....|.
gi 1800081418 525 LVLNIEALRAE 535
Cdd:COG4717 232 LENELEAAALE 242
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
244-539 |
4.79e-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: 54.41 E-value: 4.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 244 SHEEDLAKVIELQEIIS--KQSREQSQMKERLAS--LSSHVTELEEDLDTARKdlikSEEMNTKLQRDVREAmaqKEDME 319
Cdd:pfam01576 265 KIRELEAQISELQEDLEseRAARNKAEKQRRDLGeeLEALKTELEDTLDTTAA----QQELRSKREQEVTEL---KKALE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 320 ERITTLEKRYLA-AQREATSVHDLNDKLENEIANKDSMHRQT---EDKNRQLQERLEL--------------AEQKLQQT 381
Cdd:pfam01576 338 EETRSHEAQLQEmRQKHTQALEELTEQLEQAKRNKANLEKAKqalESENAELQAELRTlqqakqdsehkrkkLEGQLQEL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 382 LRKAETLPEVEAELAQRVAAL-----SKSDLLSS----GSSAAKEAKLLEL----TSKLRKAEERHG-NIEERLRQMEaq 447
Cdd:pfam01576 418 QARLSESERQRAELAEKLSKLqseleSVSSLLNEaegkNIKLSKDVSSLESqlqdTQELLQEETRQKlNLSTRLRQLE-- 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 448 lEEKNQELQRARQREKMNEEHNKRLSdTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVL 527
Cdd:pfam01576 496 -DERNSLQEQLEEEEEAKRNVERQLS-TLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEK 573
|
330
....*....|..
gi 1800081418 528 NIEALRAELDHM 539
Cdd:pfam01576 574 TKNRLQQELDDL 585
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
236-535 |
4.86e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 236 KRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKErlASLSSHVTELEEDLDTARK--DLIKSEEMNTKLQRDVREAMA 313
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK--AEEAKKADEAKKKAEEAKKadEAKKKAEEAKKKADEAKKAAE 1507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 314 QKEDMEERITTLEKRYLAAQREATSVHDLND-KLENEIANKDSMHRQTEDKNRQLQERLE---LAEQKLQQTLRKAETLP 389
Cdd:PTZ00121 1508 AKKKADEAKKAEEAKKADEAKKAEEAKKADEaKKAEEKKKADELKKAEELKKAEEKKKAEeakKAEEDKNMALRKAEEAK 1587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 390 EVEAELAQRVAALSKSDLLSSGSSAAKEAKLLELTSKLRKAEERHGNIEErLRQMEAQLEEKNQELQRARQREKMNEEHN 469
Cdd:PTZ00121 1588 KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQ-LKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1800081418 470 KRLSDTVDKLLSESNerlqlhlKERMAALEDKNSLLREVESAKKqLEETQHDKDQLVLNIEALRAE 535
Cdd:PTZ00121 1667 AKKAEEDKKKAEEAK-------KAEEDEKKAAEALKKEAEEAKK-AEELKKKEAEEKKKAEELKKA 1724
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
40-689 |
5.73e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 5.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 40 MVSMLEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNtALPQEFAALTKELNVCREQLLEREEEIAELKAERN 119
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS-ELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 120 NTRLLLEHLECLVSRHERSLrmtvvKRQAQSPAGVSSEVEVLKALKSLFEhhKALDEKvRERLRVALERCSLLEEELGAT 199
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKL-----DELAEELAELEEKLEELKEELESLE--AELEEL-EAELEELESRLEELEEQLETL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 200 HKELMILKEQ----NNQKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDL-AKVIELQEIISKQSREQSQMKERLA 274
Cdd:TIGR02168 385 RSKVAQLELQiaslNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELqAELEELEEELEELQEELERLEEALE 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 275 SLSSHVTELEEDLDTARKDLIKS----------EEMNTKLQRDVREAMAQKEDME-------ERITTLEK------RYLA 331
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQLqarldslerlQENLEGFSEGVKALLKNQSGLSgilgvlsELISVDEGyeaaieAALG 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 332 AQREATSVHDLNDKLE-----------------------NEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTL------ 382
Cdd:TIGR02168 545 GRLQAVVVENLNAAKKaiaflkqnelgrvtflpldsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALsyllgg 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 383 -----------------RKAETLPEVEAELAQRVAALSKSDLLSSGSSAAKEAKLLELTSKLRKAEE------------- 432
Cdd:TIGR02168 625 vlvvddldnalelakklRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEkiaelekalaelr 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 433 -RHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNErLQLHLKERMAALEDKNSLLREVESA 511
Cdd:TIGR02168 705 kELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE-LEAEIEELEERLEEAEEELAEAEAE 783
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 512 KKQLEET-QHDKDQLVLNIE---ALRAELDHMRLRGASLHHGRPHLgsvpdfRFPMADGHTDSYSTSAVLRRpQKGRLAA 587
Cdd:TIGR02168 784 IEELEAQiEQLKEELKALREaldELRAELTLLNEEAANLRERLESL------ERRIAATERRLEDLEEQIEE-LSEDIES 856
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 588 LRDEPSKVQTLNEQdwERAQQASVLANVAQAFESDADVSDGEDDRDTllssvDLLSPSGQADAhtlammLQEQLDAINKE 667
Cdd:TIGR02168 857 LAAEIEELEELIEE--LESELEALLNERASLEEALALLRSELEELSE-----ELRELESKRSE------LRRELEELREK 923
|
730 740
....*....|....*....|..
gi 1800081418 668 IRLIQEEKENTEQRAEEIESRV 689
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQERL 945
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
1035-1090 |
5.74e-07 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 48.06 E-value: 5.74e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1800081418 1035 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLR 1090
Cdd:smart00454 11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
910-976 |
6.09e-07 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 48.06 E-value: 6.09e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1800081418 910 FAQWDGPTVVVWLELWvGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEI 976
Cdd:smart00454 1 VSQWSPESVADWLESI-GLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
362-540 |
1.05e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 362 DKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALsksdllssgssaakEAKLLELTSKLRKAEERHGNIEERL 441
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL--------------ERRIAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 442 RQMEAQLEEKNQELQRARQR--EKMNEEHNKRLSDTVDKLLSESN--------ERLQLHLKERMAALEDKNSLLREVESA 511
Cdd:COG4942 86 AELEKEIAELRAELEAQKEElaELLRALYRLGRQPPLALLLSPEDfldavrrlQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180
....*....|....*....|....*....
gi 1800081418 512 KKQLEETQHDKDQLVLNIEALRAELDHMR 540
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALK 194
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
335-548 |
1.19e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 335 EATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQ--ERLELAEQKLQQTLRKAETLPEVEAEL----AQRVAALSKSDLL 408
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALrlwfAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 409 SSGSSAAK-EAKLLELTSKLRKAEERHGNIEERLRQ--------MEAQLEEKNQELQRARQREKmneehnkRLSDTVDKL 479
Cdd:COG4913 299 ELRAELARlEAELERLEARLDALREELDELEAQIRGnggdrleqLEREIERLERELEERERRRA-------RLEALLAAL 371
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1800081418 480 ---LSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQlvlNIEALRAELDHMRLRGASLHH 548
Cdd:COG4913 372 glpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR---ELRELEAEIASLERRKSNIPA 440
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
45-548 |
1.20e-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: 53.10 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTaLPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLL 124
Cdd:TIGR04523 124 VELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYND-LKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 125 LEHLECLVSRHeRSLRMTVVKRQAQSpagvSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELm 204
Cdd:TIGR04523 203 LSNLKKKIQKN-KSLESQISELKKQN----NQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL- 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 205 ilkEQNNQK-KTLTDGVLDINHEQENTPStsgKRSSDGSLSHEEDLA----KVIELQEIISKQSREQSQMKERLASLSSH 279
Cdd:TIGR04523 277 ---EQNNKKiKELEKQLNQLKSEISDLNN---QKEQDWNKELKSELKnqekKLEEIQNQISQNNKIISQLNEQISQLKKE 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 280 VTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITtlekrylaaqreatsvhDLNDKLENEiankdsmhrq 359
Cdd:TIGR04523 351 LTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIN-----------------DLESKIQNQ---------- 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 360 tEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSDllssgssAAKEAKLLELTSKLRKAEERHGNIEE 439
Cdd:TIGR04523 404 -EKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQD-------SVKELIIKNLDNTRESLETQLKVLSR 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 440 RLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNErlqlhLKERMAALEdknSLLREVESAKKQLEEtQ 519
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS-----LKEKIEKLE---SEKKEKESKISDLED-E 546
|
490 500
....*....|....*....|....*....
gi 1800081418 520 HDKDQLVLNIEALRAELDHMRLRGASLHH 548
Cdd:TIGR04523 547 LNKDDFELKKENLEKEIDEKNKEIEELKQ 575
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
45-456 |
1.72e-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: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALpqEFAALTKElnvcreqllereeeiaelKAERNNTRLL 124
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE--RYQALLKE------------------KREYEGYELL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 125 LEHLEclvsrHERSLRmtvvkrqaqspagvssevEVLKALKSLFEHHKALDEKVRERLrvalERCSLLEEELGATHKELM 204
Cdd:TIGR02169 230 KEKEA-----LERQKE------------------AIERQLASLEEELEKLTEEISELE----KRLEEIEQLLEELNKKIK 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 205 ILKEqnNQKKTLTDGVLDINHEQENTpstsgKRSSDGSLSHEEDLA-KVIELQEIISKQ-------SREQSQMKERLASL 276
Cdd:TIGR02169 283 DLGE--EEQLRVKEKIGELEAEIASL-----ERSIAEKERELEDAEeRLAKLEAEIDKLlaeieelEREIEEERKRRDKL 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 277 SSHVTELEEDLDTARKDLiksEEMNTKLQRDVREAMAQKEDME---ERITTLEKRYLAAQREATSVHDLNDKLENEIANK 353
Cdd:TIGR02169 356 TEEYAELKEELEDLRAEL---EEVDKEFAETRDELKDYREKLEklkREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 354 DSMHRQTEDKNRQLQERLELAEQKLQQTlrkAETLPEVEAELAQRVAALSKSdllssgssaakEAKLLELTSKLRKAEER 433
Cdd:TIGR02169 433 EAKINELEEEKEDKALEIKKQEWKLEQL---AADLSKYEQELYDLKEEYDRV-----------EKELSKLQRELAEAEAQ 498
|
410 420
....*....|....*....|...
gi 1800081418 434 HGNIEERLRQMEAQLEEKNQELQ 456
Cdd:TIGR02169 499 ARASEERVRGGRAVEEVLKASIQ 521
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
44-488 |
1.78e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 44 LEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTA-LPQEFAALTKELNVCREQLLEREEEIAELKAERNNTR 122
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLpLYQELEALEAELAELPERLEELEERLEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 123 LLLEHLECLVSRHERSLRmtvvkrqaqspagvSSEVEVLKALKSLFEHHKALDEKV---RERLRVALERCSLLEEELGAT 199
Cdd:COG4717 167 ELEAELAELQEELEELLE--------------QLSLATEEELQDLAEELEELQQRLaelEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 200 HKELMILKEQNNQKKT-----LTDGVLDINHEQENTPSTSGKRSSDGSLsheedLAKVIELQEIISKQSREQSQMKERLA 274
Cdd:COG4717 233 ENELEAAALEERLKEArllllIAAALLALLGLGGSLLSLILTIAGVLFL-----VLGLLALLFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 275 SLSSHVTELE-EDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANK 353
Cdd:COG4717 308 QALPALEELEeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 354 DSMHRQTEDKnRQLQERLELAEQKLQQTLRKAETLPEV--EAELAQRVAALsksdllssgssaakEAKLLELTSKLRKAE 431
Cdd:COG4717 388 RAALEQAEEY-QELKEELEELEEQLEELLGELEELLEAldEEELEEELEEL--------------EEELEELEEELEELR 452
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1800081418 432 ERHGNIEERLRQMEAQ--LEEKNQELQRARQREKMNEEHNKRLsDTVDKLLSESNERLQ 488
Cdd:COG4717 453 EELAELEAELEQLEEDgeLAELLQELEELKAELRELAEEWAAL-KLALELLEEAREEYR 510
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
264-457 |
1.82e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 264 REQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVH--D 341
Cdd:COG4913 671 AELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELraL 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 342 LNDKLENEIANK--DSMHRQTEDKNRQLQERLELAEQKLQQTLRK---------------AETLPEVEAELAQrvaaLSK 404
Cdd:COG4913 751 LEERFAAALGDAveRELRENLEERIDALRARLNRAEEELERAMRAfnrewpaetadldadLESLPEYLALLDR----LEE 826
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1800081418 405 SDLlssgssAAKEAKLLELtskLRKAEER-----HGNIEERLRQMEAQLEEKNQELQR 457
Cdd:COG4913 827 DGL------PEYEERFKEL---LNENSIEfvadlLSKLRRAIREIKERIDPLNDSLKR 875
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
113-543 |
2.10e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 113 ELKAERNNTRLLLEHLECLVSRHERSLRmtVVKRQAQSPAGVSSEV-EVLKALKSLFEHHKALDEKVR--ERLRVALERC 189
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRLEEEIN--GIEERIKELEEKEERLeELKKKLKELEKRLEELEERHElyEEAKAKKEEL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 190 SLLEEELGATHKELMI--LKEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSD--------------GSLSHEEDLAkvi 253
Cdd:PRK03918 375 ERLKKRLTGLTPEKLEkeLEELEKAKEEIEEEISKITARIGELKKEIKELKKAieelkkakgkcpvcGRELTEEHRK--- 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 254 elqEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMntklqRDVREAMAQKEDMEERITTLEKRYL-AA 332
Cdd:PRK03918 452 ---ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEL-----IKLKELAEQLKELEEKLKKYNLEELeKK 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 333 QREATSVHDLNDKLENEIAN-KDSMHRQTEDKNR--QLQERLELAEQKLQQTLRKAETLP-EVEAELAQRVAALSKSdll 408
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSlKKELEKLEELKKKlaELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPF--- 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 409 ssgssAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREkmnEEHNKRLSDTVDKLLSESNERLQ 488
Cdd:PRK03918 601 -----YNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL---EELEKKYSEEEYEELREEYLELS 672
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1800081418 489 LHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHM-RLRG 543
Cdd:PRK03918 673 RELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVeELRE 728
|
|
| SAM_superfamily |
cd09487 |
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
1035-1086 |
2.24e-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: 46.08 E-value: 2.24e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1800081418 1035 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRNSFQCGI 1086
Cdd:cd09487 4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
247-521 |
2.25e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 247 EDLAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDliksEEMNTKLQRDVREAMAQKEDMEERITTLE 326
Cdd:PTZ00121 1549 DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIE----EVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 327 KRylAAQREATSVHDLNDKLENEIANKDSMHRQTED-KNRQLQERLELAEQKlqqtlRKAETLPEVEAELAQRVAALSKS 405
Cdd:PTZ00121 1625 LK--KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEnKIKAAEEAKKAEEDK-----KKAEEAKKAEEDEKKAAEALKKE 1697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 406 dllssgssaAKEAKLLELTSK-----LRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKrlsdtVDKLL 480
Cdd:PTZ00121 1698 ---------AEEAKKAEELKKkeaeeKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKK-----IAHLK 1763
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1800081418 481 SESNERLQLHLKERMAALEDKnsLLREVESAKKQLEETQHD 521
Cdd:PTZ00121 1764 KEEEKKAEEIRKEKEAVIEEE--LDEEDEKRRMEVDKKIKD 1802
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
304-517 |
2.46e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.94 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 304 LQRDVREAMAQKEDMEERITTLEKRYLAAQREatsvhdLND-KLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTL 382
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAA------LEEfRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 383 RKAETLPEVEAELAQRVAALSKSDLLSSGSS--AAKEAKLLELTSKLRkaeERHGNIEERLRQMEAQLEEKNQELQRARQ 460
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQSPVIQQLRAqlAELEAELAELSARYT---PNHPDVIALRAQIAALRAQLQQEAQRILA 316
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1800081418 461 REKMNEEHNKRLSDTVDKLLSESNERLQlhlkeRMAALEDK-NSLLREVESAKKQLEE 517
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLA-----ELPELEAElRRLEREVEVARELYES 369
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
247-546 |
3.61e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 247 EDLAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLE 326
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEA 1436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 327 KRylaAQREATSVHDLNDKLEnEIANKDSMHRQTEDKnRQLQERLELAEQ--KLQQTLRKAETLPEVEAELAQRVAALSK 404
Cdd:PTZ00121 1437 KK---KAEEAKKADEAKKKAE-EAKKAEEAKKKAEEA-KKADEAKKKAEEakKADEAKKKAEEAKKKADEAKKAAEAKKK 1511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 405 SDLLSSGSSA--AKEAKLLELTSK---LRKAEERHGNIE----ERLRQMEA---------QLEEKNQELQRARQREKMNE 466
Cdd:PTZ00121 1512 ADEAKKAEEAkkADEAKKAEEAKKadeAKKAEEKKKADElkkaEELKKAEEkkkaeeakkAEEDKNMALRKAEEAKKAEE 1591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 467 EHNKRLSDTVDKLLSESNERLQLHLKERMAALEdknslLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASL 546
Cdd:PTZ00121 1592 ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE-----LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
44-536 |
3.64e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 44 LEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTaLPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRL 123
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEE-LEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRD 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 124 LLEHLECLVSRH--------ERSLRMTVVKRQAQSPAGVsSEVEVLKALKSLFEHHKALDEkVRERLRVALERCSLLEEE 195
Cdd:PRK02224 329 RLEECRVAAQAHneeaeslrEDADDLEERAEELREEAAE-LESELEEAREAVEDRREEIEE-LEEEIEELRERFGDAPVD 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 196 LGATHKELMILKEQnnqkktltdgvLDINHEQENTPSTSGKrssdgslSHEEDLAKVIELQEI----ISKQSREQSQMKE 271
Cdd:PRK02224 407 LGNAEDFLEELREE-----------RDELREREAELEATLR-------TARERVEEAEALLEAgkcpECGQPVEGSPHVE 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 272 RLASLSSHVTELEEDLDTARKDLiksEEMNTKLQR--DVREAMAQKEDMEERITTLEKRylAAQREATsVHDLNDKLENE 349
Cdd:PRK02224 469 TIEEDRERVEELEAELEDLEEEV---EEVEERLERaeDLVEAEDRIERLEERREDLEEL--IAERRET-IEEKRERAEEL 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 350 IANKDSMHRQTEDKNRQLQErlelAEQKLQQTLRKAETLPEVEAELAQRVAALSK-SDLLSSGSSAAKEA-----KLLEL 423
Cdd:PRK02224 543 RERAAELEAEAEEKREAAAE----AEEEAEEAREEVAELNSKLAELKERIESLERiRTLLAAIADAEDEIerlreKREAL 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 424 TSKLRKAEERHGNIEERLRQMEAQLEEKN-----QELQRARQREKMNEEHNKRLSDTVDKLLSE----SNERLQLH-LKE 493
Cdd:PRK02224 619 AELNDERRERLAEKRERKRELEAEFDEARieearEDKERAEEYLEQVEEKLDELREERDDLQAEigavENELEELEeLRE 698
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1800081418 494 RMAALEDKNSLLREVESAKKQLEETQHDkdqlvlnieaLRAEL 536
Cdd:PRK02224 699 RREALENRVEALEALYDEAEELESMYGD----------LRAEL 731
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
254-384 |
3.86e-06 |
|
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: 48.75 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 254 ELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREA-MAQKEDMEERITTLEKRYLAA 332
Cdd:pfam15619 57 ELPQLIARHNEEVRVLRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKnLAEREELQKKLEQLEAKLEDK 136
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1800081418 333 QREatsVHDLNDKLEN-------EIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRK 384
Cdd:pfam15619 137 DEK---IQDLERKLELenksfrrQLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKERE 192
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
46-536 |
3.94e-06 |
|
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: 51.60 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 46 ERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNtalpqefaALTKELNVCREQLLEREEEIAELKAERNNTRLLL 125
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQ--------ELEEKLEELRLEVSELEEEIEELQKELYALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 126 EHLECLVSRH---ERSLRMTVVKRQAQSPAGVSSEVEVLKALK-------SLFEHHKALDEKV---RERLRVALERCSLL 192
Cdd:TIGR02168 298 SRLEQQKQILrerLANLERQLEELEAQLEELESKLDELAEELAeleekleELKEELESLEAELeelEAELEELESRLEEL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 193 EEELGATHKELMILKEQ----NNQKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDL-AKVIELQEIISKQSREQS 267
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQiaslNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELqAELEELEEELEELQEELE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 268 QMKERLASLSSHVTELEEDLDTARKDLIKS----------EEMNTKLQRDVREAMAQKEDME-------ERITTLEK--- 327
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLqarldslerlQENLEGFSEGVKALLKNQSGLSgilgvlsELISVDEGyea 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 328 ---RYLAAQREATSVHDLNDK------LENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAEL--- 395
Cdd:TIGR02168 538 aieAALGGRLQAVVVENLNAAkkaiafLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLrka 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 396 ----------------AQRVAALSKSDL--------------LSSGSSAAKEAKLLELTSKLRkaeerhgNIEERLRQME 445
Cdd:TIGR02168 618 lsyllggvlvvddldnALELAKKLRPGYrivtldgdlvrpggVITGGSAKTNSSILERRREIE-------ELEEKIEELE 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 446 AQLEEKNQELQRAR-QREKMNEEHNK--RLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDK 522
Cdd:TIGR02168 691 EKIAELEKALAELRkELEELEEELEQlrKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
|
570
....*....|....
gi 1800081418 523 DQLVLNIEALRAEL 536
Cdd:TIGR02168 771 EEAEEELAEAEAEI 784
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
34-525 |
4.46e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 51.26 E-value: 4.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 34 SHFEQLMVSMleerDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTK-ELNVCREQLLEREEeia 112
Cdd:pfam05483 296 KELEDIKMSL----QRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEfEATTCSLEELLRTE--- 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 113 ELKAERNNTRLLLEHLEcLVSRHERSLRMTVVKRqaqspagvSSEVEVLKALKSLFEHHKALDEKvrerlrvalERCSLL 192
Cdd:pfam05483 369 QQRLEKNEDQLKIITME-LQKKSSELEEMTKFKN--------NKEVELEELKKILAEDEKLLDEK---------KQFEKI 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 193 EEELGATHKELMILKEQNNQKktltdgVLDInhEQENTPSTSgkrssdgslSHEEDLAKVIELQEIISKQSREQSQMKER 272
Cdd:pfam05483 431 AEELKGKEQELIFLLQAREKE------IHDL--EIQLTAIKT---------SEEHYLKEVEDLKTELEKEKLKNIELTAH 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 273 LASLSSHVTELEEDLDTARKDLIKSEEmntklqrDVREAMAQKEDMEERITTLEKRYLAAQREATSVHD----LNDKLEN 348
Cdd:pfam05483 494 CDKLLLENKELTQEASDMTLELKKHQE-------DIINCKKQEERMLKQIENLEEKEMNLRDELESVREefiqKGDEVKC 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 349 EIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSDLLSSGSSAAKEAKL----LELT 424
Cdd:pfam05483 567 KLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVnkleLELA 646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 425 SKLRKAEERHGNIEERLRQMEAQLEEKNQELQRAR----QREKMNEEHNKRLSDTV--------------DKLLSESNER 486
Cdd:pfam05483 647 SAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKaiadEAVKLQKEIDKRCQHKIaemvalmekhkhqyDKIIEERDSE 726
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1800081418 487 LQLHLKERM------AALEDKNSLLR-EVESAKKQLEETQHDKDQL 525
Cdd:pfam05483 727 LGLYKNKEQeqssakAALEIELSNIKaELLSLKKQLEIEKEEKEKL 772
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
236-534 |
4.64e-06 |
|
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: 51.49 E-value: 4.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 236 KRSSDGSLSHEEDLAKviELQEIISKQSREQSQMKErLASLSSHVTELEEDLDTARKDLIKseemntklqrdVREAMAQK 315
Cdd:COG3096 281 RELSERALELRRELFG--ARRQLAEEQYRLVEMARE-LEELSARESDLEQDYQAASDHLNL-----------VQTALRQQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 316 EDME---ERITTLEKRyLAAQREAtsVHDLNDKLENEIANK-------DSMHRQTEDKNRQL--QERLELAEQKLQQTLR 383
Cdd:COG3096 347 EKIEryqEDLEELTER-LEEQEEV--VEEAAEQLAEAEARLeaaeeevDSLKSQLADYQQALdvQQTRAIQYQQAVQALE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 384 KAETL---PEVEAE-LAQRVAAL-SKSDLLSSG----------SSAAKE--AKLLELTSKLRKAEER------------- 433
Cdd:COG3096 424 KARALcglPDLTPEnAEDYLAAFrAKEQQATEEvleleqklsvADAARRqfEKAYELVCKIAGEVERsqawqtarellrr 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 434 ---HGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDkllseSNERLQLHLKERMAALEDknsLLREVES 510
Cdd:COG3096 504 yrsQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLD-----AAEELEELLAELEAQLEE---LEEQAAE 575
|
330 340
....*....|....*....|....
gi 1800081418 511 AKKQLEETQHDKDQLVLNIEALRA 534
Cdd:COG3096 576 AVEQRSELRQQLEQLRARIKELAA 599
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
365-530 |
5.68e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.55 E-value: 5.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 365 RQLQERLELAEQKLQQTLRKAETlpevEAELAQRVAALsksdllssgssAAKEaKLLELTSKL-RKAEERHGNI---EER 440
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKK----EAEAIKKEALL-----------EAKE-EIHKLRNEFeKELRERRNELqklEKR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 441 LRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLK--ERMAAL---EDKNSLLREVEsakkql 515
Cdd:PRK12704 91 LLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQelERISGLtaeEAKEILLEKVE------ 164
|
170
....*....|....*
gi 1800081418 516 EETQHDKDQLVLNIE 530
Cdd:PRK12704 165 EEARHEAAVLIKEIE 179
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
321-542 |
7.13e-06 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 48.84 E-value: 7.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 321 RITTLEKRYLAAQREATSVHDLNDKLENeIANKDSmhrqTEDKNRQLQERLELAEQKLQQTLRKAETL-PEVEAELAQRV 399
Cdd:pfam12795 1 KLDELEKAKLDEAAKKKLLQDLQQALSL-LDKIDA----SKQRAAAYQKALDDAPAELRELRQELAALqAKAEAAPKEIL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 400 AALSKSDLlssgssaakEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTvDKL 479
Cdd:pfam12795 76 ASLSLEEL---------EQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPP-GEP 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1800081418 480 LSESnerLQLHLKERMAALEDKNSLLRE--------VESAKKQLEETQHDKDQLVLNIEALRAELDHMRLR 542
Cdd:pfam12795 146 LSEA---QRWALQAELAALKAQIDMLEQellsnnnrQDLLKARRDLLTLRIQRLEQQLQALQELLNEKRLQ 213
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
156-489 |
1.42e-05 |
|
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: 49.35 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 156 SEVEVLKALKSLFEHHKALDEKVRERL--RVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPST 233
Cdd:pfam17380 266 TENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 234 SGK---------RSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKERLaslsshvtelEEDLDTARKDLIKSEEMNTKL 304
Cdd:pfam17380 346 RERelerirqeeRKRELERIRQEEIAMEISRMRELERLQMERQQKNERV----------RQELEAARKVKILEEERQRKI 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 305 QRDVREaMAQKEDMEERITTLEKRYLAAQREatsvHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRK 384
Cdd:pfam17380 416 QQQKVE-MEQIRAEQEEARQREVRRLEEERA----REMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 385 AETLPEVEAELAQRVAALsksdLLSSGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKM 464
Cdd:pfam17380 491 EQRRKILEKELEERKQAM----IEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERS 566
|
330 340
....*....|....*....|....*
gi 1800081418 465 NEEHNKRLSDTVDKLLSESNERLQL 489
Cdd:pfam17380 567 RLEAMEREREMMRQIVESEKARAEY 591
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
249-533 |
1.47e-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: 49.44 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 249 LAKVIE-LQEIISKQSREQSQMKERLASLS-------SHVTELEEDLdtARKDLIkSEEMNTKLQRDVREAMAQKEDMEE 320
Cdd:pfam10174 399 LQKKIEnLQEQLRDKDKQLAGLKERVKSLQtdssntdTALTTLEEAL--SEKERI-IERLKEQREREDRERLEELESLKK 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 321 RITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQ---KLQQTLRKAETLPEVE---AE 394
Cdd:pfam10174 476 ENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEecsKLENQLKKAHNAEEAVrtnPE 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 395 LAQRVAALSKSDLLSSGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQME--AQLEEKNQELQRARQREKMNEEHNKRL 472
Cdd:pfam10174 556 INDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELEslTLRQMKEQNKKVANIKHGQQEMKKKGA 635
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1800081418 473 SDTVDKLLSESNER---LQLHLKERMAALEDKNSllrEVESAKKQLEETQ---HDKDQLVLNIEALR 533
Cdd:pfam10174 636 QLLEEARRREDNLAdnsQQLQLEELMGALEKTRQ---ELDATKARLSSTQqslAEKDGHLTNLRAER 699
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
422-542 |
1.47e-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: 49.68 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 422 ELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQR-ARQREKMNEehnkrlsdtVDKLLSESNE-RLQLHLKERMAALE 499
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERlRREREKAER---------YQALLKEKREyEGYELLKEKEALER 237
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1800081418 500 DKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMRLR 542
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKK 280
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
44-335 |
1.47e-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: 49.68 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 44 LEERDRLLDTLRETQETLALTQGKLHE-----VGHERDSLQRQLnTALPQEFAALTKELNVCREQLLEREEEIAELKAER 118
Cdd:TIGR02169 210 AERYQALLKEKREYEGYELLKEKEALErqkeaIERQLASLEEEL-EKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEE 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 119 NNT-RLLLEHLECLVSRHERSLRmtVVKRQAQSPAGVSSEVEV--------LKALKSLFEHHKALDEKVRERLRVALERC 189
Cdd:TIGR02169 289 QLRvKEKIGELEAEIASLERSIA--EKERELEDAEERLAKLEAeidkllaeIEELEREIEEERKRRDKLTEEYAELKEEL 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 190 SLLEEELGATHKELMILKEQNNQKKTLTDgvlDINHEQEntpstsgkrssdgSLSHEEDlakviELQEIISKQSREQSQM 269
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRDELKDYREKLE---KLKREIN-------------ELKRELD-----RLQEELQRLSEELADL 425
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1800081418 270 KERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQRE 335
Cdd:TIGR02169 426 NAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
270-538 |
1.80e-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: 49.25 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 270 KERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEK-------RYLAAQREATSVHDL 342
Cdd:TIGR04523 95 KDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKeleklnnKYNDLKKQKEELENE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 343 NDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQqtlrKAETLPEVEAELAQRVAALSKSDLLssgssaaKEAKLLE 422
Cdd:TIGR04523 175 LNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQ----KNKSLESQISELKKQNNQLKDNIEK-------KQQEINE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 423 LTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRArqrEKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKN 502
Cdd:TIGR04523 244 KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN---NKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQE 320
|
250 260 270
....*....|....*....|....*....|....*.
gi 1800081418 503 SLLREVESakkQLEETQHDKDQLVLNIEALRAELDH 538
Cdd:TIGR04523 321 KKLEEIQN---QISQNNKIISQLNEQISQLKKELTN 353
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
266-460 |
1.85e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 266 QSQMKERLASLSSHVTELEEDLDTARKDLIKSEE--MNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLN 343
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAalEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 344 DKLENEIA-NKDSMHRQTEDKN-RQLQERLELAEQKLQQTLRK-AETLPEVEAELAQRVAALSKSDLLSSGSSAAKEAKL 420
Cdd:COG3206 243 AALRAQLGsGPDALPELLQSPViQQLRAQLAELEAELAELSARyTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAEL 322
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1800081418 421 LELTSKLRKAEERHGNIEERLRQM---EAQLEEKNQELQRARQ 460
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARE 365
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
38-521 |
2.30e-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: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 38 QLMVSMLEERDR--LLDTLRETQETLALTQGKLHE--VGHERDSLQRQ-----LNTALPQEFAALTKELNvcreqlLERE 108
Cdd:pfam12128 231 QAIAGIMKIRPEftKLQQEFNTLESAELRLSHLHFgyKSDETLIASRQeerqeTSAELNQLLRTLDDQWK------EKRD 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 109 EEIAELKAERNNTRLLLEHLECLVSRHERSLRMTVVKR---QAQSPAgVSSEVEVL-KALKSLFEHHKALDEKVRERLRV 184
Cdd:pfam12128 305 ELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAaadQEQLPS-WQSELENLeERLKALTGKHQDVTAKYNRRRSK 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 185 ALERCSlleEELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTSGKRS-SDGSLSHEEDL--AKVIELQEIISK 261
Cdd:pfam12128 384 IKEQNN---RDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEfNEEEYRLKSRLgeLKLRLNQATATP 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 262 QSREQ--------SQMKERLASLSSHVTELEEDLDTARKdliKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRylaaq 333
Cdd:pfam12128 461 ELLLQlenfderiERAREEQEAANAEVERLQSELRQARK---RRDQASEALRQASRRLEERQSALDELELQLFPQ----- 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 334 reatsVHDLNDKLENEIAN-KDSMHRQTedkNRQLQERLELAEQKLQQTLRKAETLPEVEAELaQRVAALSKSDllssgS 412
Cdd:pfam12128 533 -----AGTLLHFLRKEAPDwEQSIGKVI---SPELLHRTDLDPEVWDGSVGGELNLYGVKLDL-KRIDVPEWAA-----S 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 413 SAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDtvdkllSESNERLQLHlK 492
Cdd:pfam12128 599 EEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFD------EKQSEKDKKN-K 671
|
490 500
....*....|....*....|....*....
gi 1800081418 493 ERMAALEDKNSLLREVESAKKQLEETQHD 521
Cdd:pfam12128 672 ALAERKDSANERLNSLEAQLKQLDKKHQA 700
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
145-524 |
2.85e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 145 KRQAQSPAGVSSEVEVLKALKSLFEHHKALDE--KVRERLRVALERCSLLEEELGATHkelmiLKEQNNQKKtltdgvld 222
Cdd:PTZ00121 1417 KKKADEAKKKAEEKKKADEAKKKAEEAKKADEakKKAEEAKKAEEAKKKAEEAKKADE-----AKKKAEEAK-------- 1483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 223 iNHEQENTPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKERlASLSSHVTELEEdldtARK--DLIKSEEM 300
Cdd:PTZ00121 1484 -KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE-AKKADEAKKAEE----KKKadELKKAEEL 1557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 301 ntKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQErlelaeqklqq 380
Cdd:PTZ00121 1558 --KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE----------- 1624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 381 tLRKAEtlpeveaELAQRVAALSKsdllssgssaaKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQ 460
Cdd:PTZ00121 1625 -LKKAE-------EEKKKVEQLKK-----------KEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE 1685
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 461 REKMNEE------HNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQ 524
Cdd:PTZ00121 1686 DEKKAAEalkkeaEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE 1755
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
245-537 |
2.90e-05 |
|
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: 48.15 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 245 HEEDLAK-VIELQ---EIISKQSREQSQMKERLASL---SSHVTELEEDLDTARKDLiksEEMNtKLQRDVR-------E 310
Cdd:pfam05622 88 KCEELEKeVLELQhrnEELTSLAEEAQALKDEMDILresSDKVKKLEATVETYKKKL---EDLG-DLRRQVKlleernaE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 311 AMAQKEDMEERIttleKRY--LAAQREATS--VHDLNDKLENEIANKDsmhrQTEDKNRQLQERLELAEQKLQQTLRKAE 386
Cdd:pfam05622 164 YMQRTLQLEEEL----KKAnaLRGQLETYKrqVQELHGKLSEESKKAD----KLEFEYKKLEEKLEALQKEKERLIIERD 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 387 TLPE----------VEAELAQRVAALSKSDllSSGSSAAKEAKLLELTSKLRK--------AEERHGNIEERLRQMEAQL 448
Cdd:pfam05622 236 TLREtneelrcaqlQQAELSQADALLSPSS--DPGDNLAAEIMPAEIREKLIRlqhenkmlRLGQEGSYRERLTELQQLL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 449 EEKNQELQRARQREKMNeehNKRLSdtvdkLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLN 528
Cdd:pfam05622 314 EDANRRKNELETQNRLA---NQRIL-----ELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQ 385
|
....*....
gi 1800081418 529 IEALRAELD 537
Cdd:pfam05622 386 IEELEPKQD 394
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
344-500 |
3.44e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 344 DKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAEtlpEVEAELAQRVAALSKSDLLSSGSSAAKEAKllEL 423
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIK---RLELEIEEVEARIKKYEEQLGNVRNNKEYE--AL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1800081418 424 TSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALED 500
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
418-537 |
4.60e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 4.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 418 AKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEhnkrlsdtvdKLLSESNER----LQL---H 490
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE----------QLGNVRNNKeyeaLQKeieS 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1800081418 491 LKERMAALEDK-NSLLREVESAKKQLEETQHDKDQLVLNIEALRAELD 537
Cdd:COG1579 101 LKRRISDLEDEiLELMERIEELEEELAELEAELAELEAELEEKKAELD 148
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
169-540 |
4.93e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 169 EHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDgvLDINHEQENTPSTSGKRSSDGSLSHEED 248
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE--AKKKAEEDKKKADELKKAAAAKKKADEA 1423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 249 LAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQ--RDVREAMAQKEDMEERITTLE 326
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEeaKKADEAKKKAEEAKKKADEAK 1503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 327 KRYlAAQREATSVHDLNDKLENEIANKDSMHRQTEDKnRQLQERLELAEQKLQQTLRKAETLPEVEA---ELAQRVAALS 403
Cdd:PTZ00121 1504 KAA-EAKKKADEAKKAEEAKKADEAKKAEEAKKADEA-KKAEEKKKADELKKAEELKKAEEKKKAEEakkAEEDKNMALR 1581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 404 KSDLLSSGSSA-AKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEknqELQRARQREKMNEEHNKRLSDTVDKLLSE 482
Cdd:PTZ00121 1582 KAEEAKKAEEArIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE---EEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1800081418 483 SNERlqlhlkermaaledKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMR 540
Cdd:PTZ00121 1659 NKIK--------------AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
255-467 |
5.49e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 5.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 255 LQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQR 334
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 335 EATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSDLLSSGSSA 414
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1800081418 415 AKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEE 467
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA 241
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
391-540 |
5.65e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 391 VEAELAQRVAALSKSDLLSSGSSAakEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQR-EKMNEEHN 469
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAA--QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEiEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 470 KRLSD---------TVDKLL-SESNERL--QLHLKERMAalEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELD 537
Cdd:COG3883 90 ERARAlyrsggsvsYLDVLLgSESFSDFldRLSALSKIA--DADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
...
gi 1800081418 538 HMR 540
Cdd:COG3883 168 AAK 170
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
207-524 |
6.80e-05 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 46.73 E-value: 6.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 207 KEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSHE-----EDLAKVIELQEIISKQSREQSQMKERLASLsshvt 281
Cdd:pfam15905 25 KSQRFRKQKAAESQPNLNNSKDASTPATARKVKSLELKKKsqknlKESKDQKELEKEIRALVQERGEQDKRLQAL----- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 282 elEEDLdtarkdliksEEMNTKLQRDVREamaqKEDMEERITTLEKRylaaQREATSVHDLNDKLENEIANKDSM----- 356
Cdd:pfam15905 100 --EEEL----------EKVEAKLNAAVRE----KTSLSASVASLEKQ----LLELTRVNELLKAKFSEDGTQKKMsslsm 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 357 -----HRQTEDKNRQLQERLELAEQKLQQTLRKaetLPEVEAELAQRVAALSKSDLLSSGSSAAKEaKLLELTSKLRKAE 431
Cdd:pfam15905 160 elmklRNKLEAKMKEVMAKQEGMEGKLQVTQKN---LEHSKGKVAQLEEKLVSTEKEKIEEKSETE-KLLEYITELSCVS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 432 ERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVD---KLLSESNERLQLHLKERmaaledKNSLLREV 508
Cdd:pfam15905 236 EQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNekcKLLESEKEELLREYEEK------EQTLNAEL 309
|
330
....*....|....*...
gi 1800081418 509 ESAKKQL--EETQHDKDQ 524
Cdd:pfam15905 310 EELKEKLtlEEQEHQKLQ 327
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
1113-1183 |
6.92e-05 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 41.87 E-value: 6.92e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1800081418 1113 VLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFsalalLLQIPTQNTQARAVLEREFNNLL 1183
Cdd:pfam07647 1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLRLTLED-----LKRLGITSVGHRRKILKKIQELK 66
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
31-460 |
7.06e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.42 E-value: 7.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 31 DADSHFEQLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQ---LNTALPQEFAAL---TKELNVCREQL 104
Cdd:pfam15921 321 DLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQEsgnLDDQLQKLLADLhkrEKELSLEKEQN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 105 LE-------REEEIAELKAERNNTRLLLEHLECLVsRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEK 177
Cdd:pfam15921 401 KRlwdrdtgNSITIDHLRRELDDRNMEVQRLEALL-KAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRK 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 178 VRERL---RVALER---------CSLLEEE--LGATHKELMILKE-------------------QNNQKK--------TL 216
Cdd:pfam15921 480 VVEELtakKMTLESsertvsdltASLQEKEraIEATNAEITKLRSrvdlklqelqhlknegdhlRNVQTEcealklqmAE 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 217 TDGVLDINHEQ-ENTPSTSGK--RSSDGSLSHEEDLAKVI-----ELQEIISKQSREQSQMKERLASLSS---------- 278
Cdd:pfam15921 560 KDKVIEILRQQiENMTQLVGQhgRTAGAMQVEKAQLEKEIndrrlELQEFKILKDKKDAKIRELEARVSDlelekvklvn 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 279 -------HVTELEEDLD-------TARKDLIKSEEMNTKLQRDVREamaQKEDMEERITTLEKRYLAAQREATSVHDLND 344
Cdd:pfam15921 640 agserlrAVKDIKQERDqllnevkTSRNELNSLSEDYEVLKRNFRN---KSEEMETTTNKLKMQLKSAQSELEQTRNTLK 716
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 345 KLE----NEIANKDSMHRQTEDKNRQ---LQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSksdllssgSSAAKE 417
Cdd:pfam15921 717 SMEgsdgHAMKVAMGMQKQITAKRGQidaLQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVA--------TEKNKM 788
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1800081418 418 AKLLE-LTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQ 460
Cdd:pfam15921 789 AGELEvLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQ 832
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
250-461 |
7.17e-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: 7.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 250 AKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREamaQKEDMEERITTLEKR- 328
Cdd:COG4942 41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA---QKEELAELLRALYRLg 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 329 ---YLAAQREATSVHDLNDKLENEiankDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKs 405
Cdd:COG4942 118 rqpPLALLLSPEDFLDAVRRLQYL----KYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEA- 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1800081418 406 dllssgSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQR 461
Cdd:COG4942 193 ------LKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
47-538 |
7.26e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 7.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 47 RDRLLDTLRETQETLALTQGKLHEVG-HERDSLQRQLNTA--LPQEFAALTKELNvcreqllEREEEIAELKAERNNTRL 123
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNlKELKELEEELKEAeeKEEEYAELQEELE-------ELEEELEELEAELEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 124 LLEHLECLVSRHERSLRMTVVKRQaqspagvssevevlkaLKSLFEHHKALDEKVRERLRvALERCSLLEEELGATHKEL 203
Cdd:COG4717 117 ELEKLEKLLQLLPLYQELEALEAE----------------LAELPERLEELEERLEELRE-LEEELEELEAELAELQEEL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 204 milkeqnnqkktltdgvldiNHEQENTPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKERLASLSSHVTEL 283
Cdd:COG4717 180 --------------------EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 284 EED------------------LDTARKDLIKSEEMNTKLQRDVREAMAqkedMEERITTLEKRYLAAQREATSVHDLNDK 345
Cdd:COG4717 240 ALEerlkearlllliaaallaLLGLGGSLLSLILTIAGVLFLVLGLLA----LLFLLLAREKASLGKEAEELQALPALEE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 346 LENEIAN--KDSMHRQTEDKNRQLQERLELAEQkLQQTLRKAETLpevEAELAQRVAALSKSDLLSSGSSAAKEakllEL 423
Cdd:COG4717 316 LEEEELEelLAALGLPPDLSPEELLELLDRIEE-LQELLREAEEL---EEELQLEELEQEIAALLAEAGVEDEE----EL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 424 TSKLRKAEERHgNIEERLRQMEAQLEEKNQELQRARQREKmNEEHNKRLSDTVDKLLSESNERLQLH-----LKERMAAL 498
Cdd:COG4717 388 RAALEQAEEYQ-ELKEELEELEEQLEELLGELEELLEALD-EEELEEELEELEEELEELEEELEELReelaeLEAELEQL 465
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1800081418 499 EDKNSL---LREVESAKKQLEETQHDKDQLVLNIEALRAELDH 538
Cdd:COG4717 466 EEDGELaelLQELEELKAELRELAEEWAALKLALELLEEAREE 508
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
344-517 |
8.60e-05 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 45.06 E-value: 8.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 344 DKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAEtlPEVEAELAQRVAALSKSdllssgsSAAKEAKLLEL 423
Cdd:pfam04012 39 VKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGN--EELAREALAEKKSLEKQ-------AEALETQLAQQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 424 TSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEehnkrlsdTVDKLLSESNERLQLHLKERMAALEDKNS 503
Cdd:pfam04012 110 RSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAAKAQEAVQT--------SLGSLSTSSATDSFERIEEKIEEREARAD 181
|
170
....*....|....
gi 1800081418 504 LLREVESAKKQLEE 517
Cdd:pfam04012 182 AAAELASAVDLDAK 195
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
129-541 |
8.70e-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: 8.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 129 ECLVSRHErslrmtVVKRQAQSPAGVSSEVEVLKALKSLFEH-HKALDEKVrERLRVALERCSLLEEELGATHKELMILK 207
Cdd:pfam07888 38 ECLQERAE------LLQAQEAANRQREKEKERYKRDREQWERqRRELESRV-AELKEELRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 208 EQNNQKKTLTdgvldinheqentpstsgkrssdgSLSHEEDLAKVIELQEIIskqsreqsqmkerlASLSSHVTELEEDL 287
Cdd:pfam07888 111 EELSEEKDAL------------------------LAQRAAHEARIRELEEDI--------------KTLTQRVLERETEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 288 DtarkdlikseemntKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQL 367
Cdd:pfam07888 153 E--------------RMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 368 QERLELAEQK---LQQTLRKAETLPEVeAELAQRVAALSKSDLLSSGSsaAKEAKLLELTSKLRKAEERHGNIEE---RL 441
Cdd:pfam07888 219 TQKLTTAHRKeaeNEALLEELRSLQER-LNASERKVEGLGEELSSMAA--QRDRTQAELHQARLQAAQLTLQLADaslAL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 442 RQMEAQLEEKNQELQRARQREKmneEHNKRLSDTVDKLlsesNERLQlhlKERMAALEDKNSLLREVESAKKQLEETQHD 521
Cdd:pfam07888 296 REGRARWAQERETLQQSAEADK---DRIEKLSAELQRL----EERLQ---EERMEREKLEVELGREKDCNRVQLSESRRE 365
|
410 420
....*....|....*....|
gi 1800081418 522 KDQLVLNIEALRAELDHMRL 541
Cdd:pfam07888 366 LQELKASLRVAQKEKEQLQA 385
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
358-550 |
9.63e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 9.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 358 RQTEDKNRQLQE---RLELAEQKLQQTLRKAETL---PEVEAELAQRVAALSKSDLLSSGSSA-AKEAKLLELTSKLRKA 430
Cdd:COG4913 221 PDTFEAADALVEhfdDLERAHEALEDAREQIELLepiRELAERYAAARERLAELEYLRAALRLwFAQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 431 EERHGNIEERLRQMEAQLEEKNQELQRARQR------------EKMNEEHNKRLSDTVDKL--LSESNERLQLHLKERMA 496
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEAQirgnggdrleqlEREIERLERELEERERRRarLEALLAALGLPLPASAE 380
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1800081418 497 ALEDKNSLLRE-VESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASLHHGR 550
Cdd:COG4913 381 EFAALRAEAAAlLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK 435
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
86-516 |
1.12e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 86 LPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALK 165
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEK 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 166 SLFEHHKAlDEKVRERLRVALERCSLLEEELGATHKELMILKeqnnqkktltdgvldinheqentpSTSGKRSSDGSLSH 245
Cdd:PRK03918 392 ELEELEKA-KEEIEEEISKITARIGELKKEIKELKKAIEELK------------------------KAKGKCPVCGRELT 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 246 EEDLAkvielqEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMntklqRDVREAMAQKEDMEERITTL 325
Cdd:PRK03918 447 EEHRK------ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEL-----IKLKELAEQLKELEEKLKKY 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 326 EKRYL-AAQREATSVHDLNDKLENEIAN-KDSMHRQTEDKNR--QLQERLELAEQKLQQTLRKAETLP-EVEAELAQRVA 400
Cdd:PRK03918 516 NLEELeKKAEEYEKLKEKLIKLKGEIKSlKKELEKLEELKKKlaELEKKLDELEEELAELLKELEELGfESVEELEERLK 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 401 ALSKS-----DLLSSGSSAAKEAKLLE-LTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEehNKRLSD 474
Cdd:PRK03918 596 ELEPFyneylELKDAEKELEREEKELKkLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREE--YLELSR 673
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1800081418 475 TVDKLLSESnERLQLHLKERMAALEDKNSLLREVESAKKQLE 516
Cdd:PRK03918 674 ELAGLRAEL-EELEKRREEIKKTLEKLKEELEEREKAKKELE 714
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
37-478 |
1.21e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 37 EQLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELKA 116
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 117 ERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPAGV-SSEVEVLKALKSLFEHH-----KALDEKVRERLRVALERCS 190
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEaAARLLLLLEAEADYEGFlegvkAALLLAGLRGLAGAVAVLI 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 191 LLEEELGATHKELMILKEQNNQKKTLTDGVLDINHEQEN-----TPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSRE 265
Cdd:COG1196 531 GVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAkagraTFLPLDKIRARAALAAALARGAIGAAVDLVASDLRE 610
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 266 QSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDK 345
Cdd:COG1196 611 ADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAE 690
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 346 LENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSDLLSSGSSAAKEAKLLELTS 425
Cdd:COG1196 691 EELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELE 770
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1800081418 426 KLRKAEERHGNI-----------EERLRQMEAQLEeknqELQRARQR-----EKMNEEHNKRLSDTVDK 478
Cdd:COG1196 771 RLEREIEALGPVnllaieeyeelEERYDFLSEQRE----DLEEARETleeaiEEIDRETRERFLETFDA 835
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
192-519 |
1.24e-04 |
|
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: 46.55 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 192 LEEELGATHKELMILKEQNNQK----KTLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSREQS 267
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKdeqiKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 268 QMKERLASLSSHVTELEE---DLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREatsVHDLND 344
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQkqkELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESK---ISDLED 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 345 KLENEIANKDSmhRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSdllssgsSAAKEAKLLELT 424
Cdd:TIGR04523 546 ELNKDDFELKK--ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE-------IEEKEKKISSLE 616
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 425 SKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQ-----REKMNE--EHNKRLSDTVD---KLLSESNERLQLHLKER 494
Cdd:TIGR04523 617 KELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKEtikeiRNKWPEiiKKIKESKTKIDdiiELMKDWLKELSLHYKKY 696
|
330 340
....*....|....*....|....*
gi 1800081418 495 MAALEDKNSLLREVESAKKQLEETQ 519
Cdd:TIGR04523 697 ITRMIRIKDLPKLEEKYKEIEKELK 721
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
423-542 |
1.48e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 44.43 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 423 LTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLlsesNERLQLHLK---ERMA--A 497
Cdd:COG1842 14 INALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKW----EEKARLALEkgrEDLAreA 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1800081418 498 LEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMRLR 542
Cdd:COG1842 90 LERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAK 134
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
315-546 |
2.09e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 315 KEDMEERITTLEKRYLAAQREATSVHDLNDKLEnEIANKDsmhrQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEA- 393
Cdd:PRK11281 38 EADVQAQLDALNKQKLLEAEDKLVQQDLEQTLA-LLDKID----RQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDe 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 394 ELAQRVAALSksdllssgssaakeaklleltsklrkaeerhgnieerLRQMEAQLEEKNQELQRARqrekmneehnKRLS 473
Cdd:PRK11281 113 ETRETLSTLS-------------------------------------LRQLESRLAQTLDQLQNAQ----------NDLA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1800081418 474 DTVDKLLSESN--ERLQLHLKERMAALEDKNSLLREVESAKKQLEETQhdKDQLVLNIEALRAELDHMR--LRGASL 546
Cdd:PRK11281 146 EYNSQLVSLQTqpERAQAALYANSQRLQQIRNLLKGGKVGGKALRPSQ--RVLLQAEQALLNAQNDLQRksLEGNTQ 220
|
|
| SAM_STIM-1,2-like |
cd09504 |
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ... |
913-971 |
2.26e-04 |
|
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like (Stromal interaction molecule) proteins is a putative protein-protein interaction domain. STIM1 and STIM2 human proteins are type I transmembrane proteins. The N-terminal part of them includes "hidden" EF-hand and SAM domains. This region is responsible for sensing changes in store-operated and basal cytoplasmic Ca2+ levels and initiates oligomerization. "Hidden" EF hand and SAM domains have a stable intramolecular association, and the SAM domain is a component that regulates stability within STIM proteins. Destabilization of the EF-SAM association during Ca2+ depletion leads to partial unfolding and aggregation (homooligomerization), thus activating the store-operated Ca2+ entry. Immunoprecipitation analysis indicates that STIM1 and STIM2 can form co-precipitable oligomeric associations in vivo. It was suggested that STIM1 and STIM2 are involved in opposite regulation of store operated channels in plasma membrane.
Pssm-ID: 188903 Cd Length: 74 Bit Score: 40.78 E-value: 2.26e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1800081418 913 WDGPTVVVWLELWVGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNPLHRLKLRL 971
Cdd:cd09504 5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
366-536 |
2.66e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 366 QLQERLELAE--QKLQQTLRKAETLPEVEAELAQRVAALSKSdllssgsSAAKEAKLLELTSKLRKAEERHGNIEERLRQ 443
Cdd:COG1579 5 DLRALLDLQEldSELDRLEHRLKELPAELAELEDELAALEAR-------LEAAKTELEDLEKEIKRLELEIEEVEARIKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 444 MEAQLEE-KNQELQRARQREKmnEEHNKRLSDTVDKLLsESNERLQlHLKERMAALEDK-NSLLREVESAKKQLEETQHD 521
Cdd:COG1579 78 YEEQLGNvRNNKEYEALQKEI--ESLKRRISDLEDEIL-ELMERIE-ELEEELAELEAElAELEAELEEKKAELDEELAE 153
|
170
....*....|....*
gi 1800081418 522 KDQLVLNIEALRAEL 536
Cdd:COG1579 154 LEAELEELEAEREEL 168
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
1035-1090 |
2.96e-04 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 40.33 E-value: 2.96e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1800081418 1035 EWLPSLGLPQYRSYFMECLVD-ARMLDHLTKKDLrGQLKMVDSFHRNSFQCGIMCLR 1090
Cdd:pfam07647 11 DWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDL-KRLGITSVGHRRKILKKIQELK 66
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
154-542 |
3.34e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.10 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 154 VSSEVEVLKALKSLFEHHKALD--EKVRERLRVALERCSLLEEELGATHKELMilkEQNNQKKTLTDGVldinheqENTP 231
Cdd:pfam05483 95 VSIEAELKQKENKLQENRKIIEaqRKAIQELQFENEKVSLKLEEEIQENKDLI---KENNATRHLCNLL-------KETC 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 232 STSGKRSSDGSLSHEEDLAKVIELQEIISKqsreqsqmkerlasLSSHVTELEEDLDTARKdlikseEMNTKLQRDVREA 311
Cdd:pfam05483 165 ARSAEKTKKYEYEREETRQVYMDLNNNIEK--------------MILAFEELRVQAENARL------EMHFKLKEDHEKI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 312 MAQKEDMEERITTLEKRYLAAQREATsvhdlndKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRK----AET 387
Cdd:pfam05483 225 QHLEEEYKKEINDKEKQVSLLLIQIT-------EKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKkdhlTKE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 388 LPEVEAELAQRVA---ALSKSDLLSSGS----SAAKEAKLLELTsklrKAEERHGNIEERLRQMEAQLEEKnqeLQRARQ 460
Cdd:pfam05483 298 LEDIKMSLQRSMStqkALEEDLQIATKTicqlTEEKEAQMEELN----KAKAAHSFVVTEFEATTCSLEEL---LRTEQQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 461 REKMNEEHNKRLSDTVDKLLSESNERLQL------HLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRA 534
Cdd:pfam05483 371 RLEKNEDQLKIITMELQKKSSELEEMTKFknnkevELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREK 450
|
....*...
gi 1800081418 535 ELDHMRLR 542
Cdd:pfam05483 451 EIHDLEIQ 458
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
245-485 |
3.91e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.53 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 245 HEEDLAKVIELQEI-----ISKQSREQSQMKERLASLSSHVTELEEDLDTARK-------DLIKSEEMNT-KLQRDVREA 311
Cdd:PRK05771 26 HELGVVHIEDLKEElsnerLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKvsvksleELIKDVEEELeKIEKEIKEL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 312 MAQKEDMEERITTLEKRylaaQREATSVHDLNDKLENEIANKdSMHRQTEDKNRQLQERLELAEqklqqTLRKAETLPEV 391
Cdd:PRK05771 106 EEEISELENEIKELEQE----IERLEPWGNFDLDLSLLLGFK-YVSVFVGTVPEDKLEELKLES-----DVENVEYISTD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 392 EAELAqrVAALSKSDLLSSgssAAKEAKLLELtskLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQR-EKMNEEHNK 470
Cdd:PRK05771 176 KGYVY--VVVVVLKELSDE---VEEELKKLGF---ERLELEEEGTPSELIREIKEELEEIEKERESLLEElKELAKKYLE 247
|
250
....*....|....*
gi 1800081418 471 RLSDTVDKLLSESNE 485
Cdd:PRK05771 248 ELLALYEYLEIELER 262
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
365-531 |
3.98e-04 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 42.95 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 365 RQLQERLELAEQKLQQTLRKAETLPEvEAEL-AQRVAALSKSDLlssgssaakEAKLLELTSKLRKAEERHGNIEERLRQ 443
Cdd:pfam12072 27 AKIGSAEELAKRIIEEAKKEAETKKK-EALLeAKEEIHKLRAEA---------ERELKERRNELQRQERRLLQKEETLDR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 444 MEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLqlhlkERMAAL---EDKNSLLREVEsakkqlEETQH 520
Cdd:pfam12072 97 KDESLEKKEESLEKKEKELEAQQQQLEEKEEELEELIEEQRQEL-----ERISGLtseEAKEILLDEVE------EELRH 165
|
170
....*....|.
gi 1800081418 521 DKDQLVLNIEA 531
Cdd:pfam12072 166 EAAVMIKEIEE 176
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
193-517 |
4.44e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.78 E-value: 4.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 193 EEELGATHKELMILKEQNNQ-KKTLTDgvldinHEQENTPSTSGKRSSDGSLSHEEDL------------AKVIELQEII 259
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKaESELKE------LEKKHQQLCEEKNALQEQLQAETELcaeaeemrarlaARKQELEEIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 260 --------SKQSREQSQMKERlASLSSHVTELEEDLDtarkdliKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLA 331
Cdd:pfam01576 78 helesrleEEEERSQQLQNEK-KKMQQHIQDLEEQLD-------EEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 332 AQREATSVHDLNDKLENEIANKDSMHRQ-TEDKNRQ------LQERLElAEQKLQQTLRKAETLPEVEA-ELAQRVAALS 403
Cdd:pfam01576 150 LSKERKLLEERISEFTSNLAEEEEKAKSlSKLKNKHeamisdLEERLK-KEEKGRQELEKAKRKLEGEStDLQEQIAELQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 404 KSDLLSSGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSEs 483
Cdd:pfam01576 229 AQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTE- 307
|
330 340 350
....*....|....*....|....*....|....
gi 1800081418 484 nerLQLHLKERMAALEDKNSLLREVESAKKQLEE 517
Cdd:pfam01576 308 ---LEDTLDTTAAQQELRSKREQEVTELKKALEE 338
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
222-501 |
5.10e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.51 E-value: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 222 DINHEQENTPSTSGKRSSDGSLSHEED--LAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEE 299
Cdd:PLN02939 70 DENGQLENTSLRTVMELPQKSTSSDDDhnRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 300 MNTKLQRDVREAMAQKEDMEERITTLEKRY--------LAAQrEATSVHDLNDKLENeiANKDSMHRQTEDKNRQLQERL 371
Cdd:PLN02939 150 ARLQALEDLEKILTEKEALQGKINILEMRLsetdarikLAAQ-EKIHVEILEEQLEK--LRNELLIRGATEGLCVHSLSK 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 372 ELAEQKLQQTLRKA------ETLPEVeAELAQRVAALSKsdllssgSSAAKEAKLLELTSKLRKAEERHGNIEErlRQME 445
Cdd:PLN02939 227 ELDVLKEENMLLKDdiqflkAELIEV-AETEERVFKLEK-------ERSLLDASLRELESKFIVAQEDVSKLSP--LQYD 296
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1800081418 446 AqLEEKNQELQRARQREKMNEEH-------NKRLSDTVDKL---LSESN------ERLQLhLKERMAALEDK 501
Cdd:PLN02939 297 C-WWEKVENLQDLLDRATNQVEKaalvldqNQDLRDKVDKLeasLKEANvskfssYKVEL-LQQKLKLLEER 366
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
160-688 |
5.24e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.58 E-value: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 160 VLKALKSLFEHHKALDEK--VRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTSGKR 237
Cdd:pfam02463 228 YLDYLKLNEERIDLLQELlrDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 238 SSDGSLS----HEEDLAKVIELQEIISKQSREQSQMKERL----ASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVR 309
Cdd:pfam02463 308 RKVDDEEklkeSEKEKKKAEKELKKEKEEIEELEKELKELeikrEAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLS 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 310 EAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSM--HRQTEDKNRQLQERLELAEQKL-QQTLRKAE 386
Cdd:pfam02463 388 SAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEeeESIELKQGKLTEEKEELEKQELkLLKDELEL 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 387 TLPEVEAELAQRVAALSKSDLLSSgssaakEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNE 466
Cdd:pfam02463 468 KKSEDLLKETQLVKLQEQLELLLS------RQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENY 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 467 EHNKRLSDTVDkllsESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASL 546
Cdd:pfam02463 542 KVAISTAVIVE----VSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADE 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 547 HHGRPHLGSVPDFRFPMADGHTDSYSTSAVLRRPQ---KGRLAALRDEPSKVQTLNEQDWERAQQASVLANVAQAFESDA 623
Cdd:pfam02463 618 DDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVsleEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRR 697
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1800081418 624 DVSDGEDDRDTLLSSVDLLspsgQADAHTLAMMLQEQLDAINKEIRLIQEEKENTEQRAEEIESR 688
Cdd:pfam02463 698 QLEIKKKEQREKEELKKLK----LEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLK 758
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
244-510 |
5.48e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.40 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 244 SHEEDLakvIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNT--------------------- 302
Cdd:pfam01576 135 KLEEDI---LLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISdleerlkkeekgrqelekakr 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 303 --------------KLQRDVREAMAQKEDMEERITTLEKRY-------LAAQREATSVHDLNDKLENEIANKDSMHRQTE 361
Cdd:pfam01576 212 klegestdlqeqiaELQAQIAELRAQLAKKEEELQAALARLeeetaqkNNALKKIRELEAQISELQEDLESERAARNKAE 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 362 DKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSDLLSSGSSAAK--------EAKLLELTSKLRKAEER 433
Cdd:pfam01576 292 KQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQlqemrqkhTQALEELTEQLEQAKRN 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 434 HGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESN--ERLQLHLKERMAA----LEDKNSLLRE 507
Cdd:pfam01576 372 KANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSesERQRAELAEKLSKlqseLESVSSLLNE 451
|
...
gi 1800081418 508 VES 510
Cdd:pfam01576 452 AEG 454
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
176-353 |
5.57e-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: 43.98 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 176 EKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDLAKVIEL 255
Cdd:COG4942 58 AALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 256 QEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDM----EERITTLEKRYLA 331
Cdd:COG4942 138 LQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLlarlEKELAELAAELAE 217
|
170 180
....*....|....*....|..
gi 1800081418 332 AQREATSVHDLNDKLENEIANK 353
Cdd:COG4942 218 LQQEAEELEALIARLEAEAAAA 239
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
172-546 |
6.48e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 172 KALDEKVRErLRVALERCSLLEEELGATHKELMILKEQnnqKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSH------ 245
Cdd:COG4717 74 KELEEELKE-AEEKEEEYAELQEELEELEEELEELEAE---LEELREELEKLEKLLQLLPLYQELEALEAELAElperle 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 246 --EEDLAKVIELQEIISKQSREQSQMKERLASLSSHVT-ELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERI 322
Cdd:COG4717 150 elEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 323 TTLEKRYLAAQRE-------------------ATSVHDLNDKLEN-----------------EIANKDSMHRQTEDKNRQ 366
Cdd:COG4717 230 EQLENELEAAALEerlkearlllliaaallalLGLGGSLLSLILTiagvlflvlgllallflLLAREKASLGKEAEELQA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 367 LQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKS--DLLSSGSSAAKEAKLLELTSKLRK-AEERHGNIEERLRQ 443
Cdd:COG4717 310 LPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEElqELLREAEELEEELQLEELEQEIAAlLAEAGVEDEEELRA 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 444 MEAQLEEKNQELQRARQREKMNEEHNK----RLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEEtQ 519
Cdd:COG4717 390 ALEQAEEYQELKEELEELEEQLEELLGeleeLLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE-D 468
|
410 420
....*....|....*....|....*..
gi 1800081418 520 HDKDQLVLNIEALRAELDHMRLRGASL 546
Cdd:COG4717 469 GELAELLQELEELKAELRELAEEWAAL 495
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
176-455 |
7.32e-04 |
|
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: 44.04 E-value: 7.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 176 EKVRERLRVALER-CSLLEEELGATHKELMILKEQ-NNQKKTLTDGVLDINHEQENTPS--------TSGKRSSDGSLSH 245
Cdd:pfam10174 449 ERIIERLKEQREReDRERLEELESLKKENKDLKEKvSALQPELTEKESSLIDLKEHASSlassglkkDSKLKSLEIAVEQ 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 246 EEDLAKVIELQEIISKQSREQSQMKErlaSLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTL 325
Cdd:pfam10174 529 KKEECSKLENQLKKAHNAEEAVRTNP---EINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAEL 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 326 EKRYLAAQREATSvhdlndklenEIANKDSMhrQTEDKNRQLQErlelaeqkLQQTLRKAETLPEVEAE--LAQRVAALS 403
Cdd:pfam10174 606 ESLTLRQMKEQNK----------KVANIKHG--QQEMKKKGAQL--------LEEARRREDNLADNSQQlqLEELMGALE 665
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1800081418 404 KSDLlssgssaAKEAKLLELTSKLRKAEERHGNIE----ERLRQMEAQLEEKNQEL 455
Cdd:pfam10174 666 KTRQ-------ELDATKARLSSTQQSLAEKDGHLTnlraERRKQLEEILEMKQEAL 714
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
44-450 |
8.23e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 8.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 44 LEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRL 123
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 124 LLEHLECLVSRHERSLRmtvVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKEL 203
Cdd:COG4717 228 ELEQLENELEAAALEER---LKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 204 MILKEQNNQKKTltdgvldinhEQENTPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKErlASLSSHVTEL 283
Cdd:COG4717 305 EELQALPALEEL----------EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE--LQLEELEQEI 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 284 EEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSvhdlnDKLENEIANKDSMHRQTEDK 363
Cdd:COG4717 373 AALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE-----EELEEELEELEEELEELEEE 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 364 NRQLQERLELAEQKLQQtLRKAETLPEVEAELAQRVAALsksdllssgSSAAKEAKLLELTSK-LRKAEERHgnIEERLR 442
Cdd:COG4717 448 LEELREELAELEAELEQ-LEEDGELAELLQELEELKAEL---------RELAEEWAALKLALElLEEAREEY--REERLP 515
|
....*...
gi 1800081418 443 QMEAQLEE 450
Cdd:COG4717 516 PVLERASE 523
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
177-564 |
8.44e-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: 43.67 E-value: 8.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 177 KVRERLRVALERCSLLEEELGATHKEL------MILKEQNNQKKTLTDGVLDINHEQE----NTPSTSGKRSSDGSLSHE 246
Cdd:pfam12128 608 KAEEALQSAREKQAAAEEQLVQANGELekasreETFARTALKNARLDLRRLFDEKQSEkdkkNKALAERKDSANERLNSL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 247 EDLAKVIELQEIISKQSrEQSQMKERLASLSSHVTELEEDLDtARKDLIKSEEMNTKLQRDVReamaQKEDMEERITTLE 326
Cdd:pfam12128 688 EAQLKQLDKKHQAWLEE-QKEQKREARTEKQAYWQVVEGALD-AQLALLKAAIAARRSGAKAE----LKALETWYKRDLA 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 327 KRYLAAQREAtsvhdlndKLENEIANkdsMHRQTEDKNRQLQERLE----LAEQKLQQTLRKAETLPEVEAELaqrvaal 402
Cdd:pfam12128 762 SLGVDPDVIA--------KLKREIRT---LERKIERIAVRRQEVLRyfdwYQETWLQRRPRLATQLSNIERAI------- 823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 403 skSDLLSsgssaakeakllELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQR-EKMNEEHnkrlsdtvdklLS 481
Cdd:pfam12128 824 --SELQQ------------QLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEmSKLATLK-----------ED 878
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 482 ESNERLQLHLKERMAALED-KNSLLREVESAKKQLEE-----TQHDKDQLVLNIEALRAELDHMRLRGASLHHGRPHLGS 555
Cdd:pfam12128 879 ANSEQAQGSIGERLAQLEDlKLKRDYLSESVKKYVEHfknviADHSGSGLAETWESLREEDHYQNDKGIRLLDYRKLVPY 958
|
....*....
gi 1800081418 556 VPDFRFPMA 564
Cdd:pfam12128 959 LEQWFDVRV 967
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
260-519 |
8.96e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 8.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 260 SKQSREQSQMKERLAslsshvTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKED---MEERITTLEKRYLAAQREA 336
Cdd:PTZ00121 1075 SYKDFDFDAKEDNRA------DEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDarkAEEARKAEDARKAEEARKA 1148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 337 TSVHDLNDKLENEIANKDSMHRQTEDKnRQLQERLELAEQKLQQTLRKAETLPEVEAelAQRVAALSKsdllssgssaAK 416
Cdd:PTZ00121 1149 EDAKRVEIARKAEDARKAEEARKAEDA-KKAEAARKAEEVRKAEELRKAEDARKAEA--ARKAEEERK----------AE 1215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 417 EAKLLEltsKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMA 496
Cdd:PTZ00121 1216 EARKAE---DAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKA 1292
|
250 260
....*....|....*....|...
gi 1800081418 497 ALEDKNSLLREVESAKKQLEETQ 519
Cdd:PTZ00121 1293 DEAKKAEEKKKADEAKKKAEEAK 1315
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
134-484 |
9.22e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 43.32 E-value: 9.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 134 RHERSLRMTVvkRQAQSPAGVSSEVEVLKAlKSLFEHHKALDEKVRERLRvalERCSLLEEELGATHKELMILKEQNNQK 213
Cdd:pfam02029 13 RRAREERRRQ--KEEEEPSGQVTESVEPNE-HNSYEEDSELKPSGQGGLD---EEEAFLDRTAKREERRQKRLQEALERQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 214 K----TLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSREQ--SQMKERLASLSSHVTELEEDL 287
Cdd:pfam02029 87 KefdpTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENkwSTEVRQAEEEGEEEEDKSEEA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 288 DTARKDLIKSEEM---NTKLQRDVREAMAQKEDMEERITTLekrylAAQREATSVHDLNDKLENEIANKDSMHRQTEDKN 364
Cdd:pfam02029 167 EEVPTENFAKEEVkdeKIKKEKKVKYESKVFLDQKRGHPEV-----KSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 365 RQLQerlelAEQKLQQTLRKAETLPEVEAE-LAQRVAalsksdllssgssaakEAKLlELTSKLRKAEERHGNIEERLRQ 443
Cdd:pfam02029 242 VFLE-----AEQKLEELRRRRQEKESEEFEkLRQKQQ----------------EAEL-ELEELKKKREERRKLLEEEEQR 299
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1800081418 444 MEAqlEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESN 484
Cdd:pfam02029 300 RKQ--EEAERKLREEEEKRRMKEEIERRRAEAAEKRQKLPE 338
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
268-539 |
1.14e-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: 43.24 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 268 QMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDM-------EERITTLEKRYL-------AAQ 333
Cdd:pfam01576 774 KLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEIlaqskesEKKLKNLEAELLqlqedlaASE 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 334 REATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSkSDLLSSGSS 413
Cdd:pfam01576 854 RARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLT-TELAAERST 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 414 AAK---------------EAKLLELTSKLR-KAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEehnKRLSDTVd 477
Cdd:pfam01576 933 SQKsesarqqlerqnkelKAKLQEMEGTVKsKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTE---KKLKEVL- 1008
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1800081418 478 kLLSESNERLQLHLKERMaalEDKNSLLREVesaKKQLEETQHDKDQLVLNIEALRAELDHM 539
Cdd:pfam01576 1009 -LQVEDERRHADQYKDQA---EKGNSRMKQL---KRQLEEAEEEASRANAARRKLQRELDDA 1063
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
297-531 |
1.60e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 297 SEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQ 376
Cdd:COG4372 1 GDRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 377 KLQQTLRKAETLPEVEAELAQRVAALSKsdllssgSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQ 456
Cdd:COG4372 81 ELEELNEQLQAAQAELAQAQEELESLQE-------EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1800081418 457 RARQREKMNEEHNKRLSDTVDKL-LSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEA 531
Cdd:COG4372 154 ELEEQLESLQEELAALEQELQALsEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEA 229
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
113-462 |
1.74e-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: 42.65 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 113 ELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLL 192
Cdd:pfam02463 674 ELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEE 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 193 EEELGATHKELMILKEQNNQKKTLTDGVLDINHEQEntpstsgKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKER 272
Cdd:pfam02463 754 KSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVE-------EEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQ 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 273 LASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRD---VREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKL--- 346
Cdd:pfam02463 827 EEKIKEEELEELALELKEEQKLEKLAEEELERLEEeitKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEees 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 347 ---------ENEIANKDSMHRQTEDKNRQLQERLELAEQKLQqtlRKAETLPEVEAELAQRvaALSKSDLLSSGSSAAKE 417
Cdd:pfam02463 907 qklnlleekENEIEERIKEEAEILLKYEEEPEELLLEEADEK---EKEENNKEEEEERNKR--LLLAKEELGKVNLMAIE 981
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1800081418 418 AKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQRE 462
Cdd:pfam02463 982 EFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELF 1026
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
256-472 |
2.07e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 41.95 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 256 QEIISKQSREQSQMKERLASLSShvtELEEDLDTARKDLIKSEEmntKLQRDVREAMAQKEDMEERittleKRYLAAQRE 335
Cdd:pfam15558 54 LLLQQSQEQWQAEKEQRKARLGR---EERRRADRREKQVIEKES---RWREQAEDQENQRQEKLER-----ARQEAEQRK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 336 ATSVHDLNDKLENEiankdsmHRQTEDKNRQLQERLELAEQKLQqtLRKAETLPEVEAE-LAQRVAALSKSDLLSSGSSA 414
Cdd:pfam15558 123 QCQEQRLKEKEEEL-------QALREQNSLQLQERLEEACHKRQ--LKEREEQKKVQENnLSELLNHQARKVLVDCQAKA 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 415 AKEAKLLELTSKLRKAEERH-GNIEERLRQMEAQLEEKNQELQRARQR-EKMNEEHNKRL 472
Cdd:pfam15558 194 EELLRRLSLEQSLQRSQENYeQLVEERHRELREKAQKEEEQFQRAKWRaEEKEEERQEHK 253
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
206-683 |
2.11e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.65 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 206 LKEQNNQKKTLTDGVLDIN-HEQENTPSTSGKRSSDGSLSHEEDLAKVIEL---QEIISKQSREQSQMKErLASLSSHVT 281
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDqYTQLALMEFAKKKSLHGKAELLTLRSQLLTLctpCMPDTYHERKQVLEKE-LKHLREALQ 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 282 ELEEDLDTARKDLIKSEEmNTKLQRDVREAMAQkedmEERITTLEKRyLAAQREATSVHDLNDKLENEIANKDSMHRQTE 361
Cdd:TIGR00618 237 QTQQSHAYLTQKREAQEE-QLKKQQLLKQLRAR----IEELRAQEAV-LEETQERINRARKAAPLAAHIKAVTQIEQQAQ 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 362 DKNRQLQERLELAEQKLQQTlrkaetlpevEAELAQRVAALSKSDLLSSGSSAAKEAKLLELTSKLRKAE-ERHGNIEER 440
Cdd:TIGR00618 311 RIHTELQSKMRSRAKLLMKR----------AAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREIsCQQHTLTQH 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 441 LRQMEAQLEEKNQELQRARQR-EKMNEEHNKRLSDTVD---------------KLLSESNERLQLHLKERMAALEDKNSL 504
Cdd:TIGR00618 381 IHTLQQQKTTLTQKLQSLCKElDILQREQATIDTRTSAfrdlqgqlahakkqqELQQRYAELCAAAITCTAQCEKLEKIH 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 505 LREVESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASLHhgRPHLGSVPDFRFPMadghTDSYSTSAVLRRPQKG- 583
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEP--CPLCGSCIHPNPAR----QDIDNPGPLTRRMQRGe 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 584 -RLAALRDEPSKV----QTLNEQDWERAQQASVLANVAQAFESDADVSdgEDDRDTLLSSVDLLSPSGQADA-------- 650
Cdd:TIGR00618 535 qTYAQLETSEEDVyhqlTSERKQRASLKEQMQEIQQSFSILTQCDNRS--KEDIPNLQNITVRLQDLTEKLSeaedmlac 612
|
490 500 510
....*....|....*....|....*....|....*
gi 1800081418 651 --HTLAMMLQEQLDaiNKEIRLIQEEKENTEQRAE 683
Cdd:TIGR00618 613 eqHALLRKLQPEQD--LQDVRLHLQQCSQELALKL 645
|
|
| SAM_SARM1-like_repeat1 |
cd09501 |
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
1035-1082 |
2.21e-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: 38.05 E-value: 2.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1800081418 1035 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSF 1082
Cdd:cd09501 11 TWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLRKRF 58
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
912-974 |
2.81e-03 |
|
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.
Pssm-ID: 425739 Cd Length: 64 Bit Score: 37.25 E-value: 2.81e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1800081418 912 QWDGPTVVVWLElWVGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQ 974
Cdd:pfam00536 2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQ 61
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
321-555 |
2.91e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.80 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 321 RITTLEKRYLAAQREATSVHDL----NDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELA 396
Cdd:pfam07888 28 RAELLQNRLEECLQERAELLQAqeaaNRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 397 QRVAALSKSDLLSSGSSAAKEAKLLELtsklrkaeerhgniEERLRQMEAQLEEKNQELQRARQREKM------NEEHNK 470
Cdd:pfam07888 108 ASSEELSEEKDALLAQRAAHEARIREL--------------EEDIKTLTQRVLERETELERMKERAKKagaqrkEEEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 471 RLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASLHHGR 550
Cdd:pfam07888 174 KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKV 253
|
....*
gi 1800081418 551 PHLGS 555
Cdd:pfam07888 254 EGLGE 258
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
194-450 |
3.48e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 194 EELGATHKELMILKEQnnqKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKERL 273
Cdd:COG4913 235 DDLERAHEALEDAREQ---IELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 274 ASLSSHVTELEEDLDTARKDLikseemntkLQRDVReamaQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIAnk 353
Cdd:COG4913 312 ERLEARLDALREELDELEAQI---------RGNGGD----RLEQLEREIERLERELEERERRRARLEALLAALGLPLP-- 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 354 dsmhrqtedknrqlQERLELAEQKlQQTLRKAETLPEVEAELAQRVAALsksdllsSGSSAAKEAKLLELTSKLRKAEER 433
Cdd:COG4913 377 --------------ASAEEFAALR-AEAAALLEALEEELEALEEALAEA-------EAALRDLRRELRELEAEIASLERR 434
|
250
....*....|....*..
gi 1800081418 434 HGNIEERLRQMEAQLEE 450
Cdd:COG4913 435 KSNIPARLLALRDALAE 451
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
264-447 |
3.63e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 264 REQSQMKERLASLSSHVTELEEDLDTARKDLIK----------SEEMNTKLQR------DVREAMAQKEDMEERITTLEK 327
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdlSEEAKLLLQQlselesQLAEARAELAEAEARLAALRA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 328 RY------LAAQREATSVHDLNDKLENEIANKDSMHRQTEDKN---RQLQERLELAEQKLQQTLRKAETLPEVEAE-LAQ 397
Cdd:COG3206 248 QLgsgpdaLPELLQSPVIQQLRAQLAELEAELAELSARYTPNHpdvIALRAQIAALRAQLQQEAQRILASLEAELEaLQA 327
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1800081418 398 RVAALSK--SDLLS-SGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQ 447
Cdd:COG3206 328 REASLQAqlAQLEArLAELPELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| SAM_Neurabin-like |
cd09512 |
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ... |
1113-1177 |
4.27e-03 |
|
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like (Neural actin-binding) subfamily is a putative protein-protein interaction domain. This group currently includes the SAM domains of neurobin-I, SAMD14 and neurobin-I/SAMD14-like proteins. Most are multidomain proteins and in addition to SAM domain they contain other protein-binding domains such as PDZ and actin-binding domains. Members of this subfamily participate in signal transduction. Neurabin-I is involved in the regulation of Ca signaling intensity in alpha-adrenergic receptors; it forms a functional pair of opposing regulators with neurabin-II. Neurabins are expressed almost exclusively in neuronal cells. They are known to interact with protein phosphatase 1 and inhibit its activity; they also can bind actin filaments; however, the exact role of the SAM domain is unclear, since SAM doesn't participate in these interactions.
Pssm-ID: 188911 [Multi-domain] Cd Length: 70 Bit Score: 37.25 E-value: 4.27e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1800081418 1113 VLVWSNDRVIRWILSIGLKEYANNLIESGVHG-ALLALDETfDFSALALllqiptQNTQARAVLER 1177
Cdd:cd09512 4 VSEWSVQQVCQWLMGLGLEQYIPEFTANNIDGqQLLQLDSS-KLKALGI------TSSSDRSLLKK 62
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
237-550 |
4.36e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 237 RSSDGSLSHEEDLAKvielqeiiSKQSREQSQmkERLASLSSHVTELEEdldtARKDL-IKSEEMNTKLQRdVREAMAQK 315
Cdd:PRK04863 283 VHLEEALELRRELYT--------SRRQLAAEQ--YRLVEMARELAELNE----AESDLeQDYQAASDHLNL-VQTALRQQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 316 EDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQL---QERLELAE------QKLQQTLRKAE 386
Cdd:PRK04863 348 EKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLadyQQALDVQQtraiqyQQAVQALERAK 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 387 TL---PEVEAELAqrvaalskSDLLSSGSSAAKEA--KLLELTSKLRKAEERHGNIE---ERLRQMEAQLEeKNQELQRA 458
Cdd:PRK04863 428 QLcglPDLTADNA--------EDWLEEFQAKEQEAteELLSLEQKLSVAQAAHSQFEqayQLVRKIAGEVS-RSEAWDVA 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 459 RQREKMNEEHnkrlsdtvdKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDH 538
Cdd:PRK04863 499 RELLRRLREQ---------RHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLES 569
|
330
....*....|..
gi 1800081418 539 MRLRGASLHHGR 550
Cdd:PRK04863 570 LSESVSEARERR 581
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
177-537 |
4.45e-03 |
|
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: 41.38 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 177 KVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTsgKRSSDGS--------LSH-EE 247
Cdd:pfam06160 83 KAKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLA--NRFSYGPaidelekqLAEiEE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 248 DLAKVIEL---------QEIISKQSRE----QSQMK--------------ERLASLSSHVTELEED------------LD 288
Cdd:pfam06160 161 EFSQFEELtesgdyleaREVLEKLEEEtdalEELMEdipplyeelktelpDQLEELKEGYREMEEEgyalehlnvdkeIQ 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 289 TARKDLIKSEEMNTKLqrDVREAMAQKEDMEERITTL----EKRYLAAQreatSVHDLNDKLENEIankdsmhRQTEDKN 364
Cdd:pfam06160 241 QLEEQLEENLALLENL--ELDEAEEALEEIEERIDQLydllEKEVDAKK----YVEKNLPEIEDYL-------EHAEEQN 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 365 RQLQERLELaeqkLQQTLRKAETLPEVEAELAQRVAALSKSDLLSSGSSAAKEAKLLELTSKLRKaeerhgnIEERLRQM 444
Cdd:pfam06160 308 KELKEELER----VQQSYTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEE-------ILEQLEEI 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 445 EAQLEEKNQELQRARQREKmneEHNKRLsDTVDKLLSESNERLQlhlKERMAALEDknSLLREVESAKKQLEETQHDKDQ 524
Cdd:pfam06160 377 EEEQEEFKESLQSLRKDEL---EAREKL-DEFKLELREIKRLVE---KSNLPGLPE--SYLDYFFDVSDEIEDLADELNE 447
|
410
....*....|...
gi 1800081418 525 LVLNIEALRAELD 537
Cdd:pfam06160 448 VPLNMDEVNRLLD 460
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
343-472 |
4.85e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 343 NDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRvaalsksdllssgssAAKEAKlle 422
Cdd:PRK00409 515 KEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEE---------------AEKEAQ--- 576
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1800081418 423 ltSKLRKAEERHGNIEERLRQMEAQL--EEKNQELQRARQR-EKMNEEHNKRL 472
Cdd:PRK00409 577 --QAIKEAKKEADEIIKELRQLQKGGyaSVKAHELIEARKRlNKANEKKEKKK 627
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
251-397 |
4.89e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 251 KVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRD--VREAMAQKEDMEERITTLEKR 328
Cdd:COG3206 206 GLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSAR 285
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 329 YLAAQREATSVHDLNDKLENEIAN-KDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQ 397
Cdd:COG3206 286 YTPNHPDVIALRAQIAALRAQLQQeAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
175-511 |
4.89e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 175 DEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDgvlDINHEQENTPSTSGKRSSDGSLSHEEDLAKVIE 254
Cdd:PRK01156 464 EEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKE---YLESEEINKSINEYNKIESARADLEDIKIKINE 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 255 LQEIISKQSreqsQMKERLASLSShvteleEDLDTARKDLIKSEEMNTKLqrDVREAMAQKEDMEERITTLEKRylaaqr 334
Cdd:PRK01156 541 LKDKHDKYE----EIKNRYKSLKL------EDLDSKRTSWLNALAVISLI--DIETNRSRSNEIKKQLNDLESR------ 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 335 eatsVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTlrkaETLPEVEAELAQRVAALSksdllssgssa 414
Cdd:PRK01156 603 ----LQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILI----EKLRGKIDNYKKQIAEID----------- 663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 415 AKEAKLLELTSKLRKaeerhgnIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVdkllSESNERLqlhlkER 494
Cdd:PRK01156 664 SIIPDLKEITSRIND-------IEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRI----NDINETL-----ES 727
|
330
....*....|....*..
gi 1800081418 495 MAALEDKNSLLREVESA 511
Cdd:PRK01156 728 MKKIKKAIGDLKRLREA 744
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
258-525 |
5.36e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 258 IISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEmntklqrdvreamaQKEDMEERITTLEKRylaaqreat 337
Cdd:TIGR04523 27 IANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEE--------------KINNSNNKIKILEQQ--------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 338 sVHDLNDKLENEIA-----NKDSMHRQTEDKN-RQLQERLELAEQKLQQTLRkaetlpEVEAELAQRVAALSKsdllssg 411
Cdd:TIGR04523 84 -IKDLNDKLKKNKDkinklNSDLSKINSEIKNdKEQKNKLEVELNKLEKQKK------ENKKNIDKFLTEIKK------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 412 ssaaKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQR-----------EKMNEEHNKRLSDTVDklL 480
Cdd:TIGR04523 150 ----KEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKllklelllsnlKKKIQKNKSLESQISE--L 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1800081418 481 SESNERLQLHLKERMAALEDKNSLLREVESAKKQL-EETQHDKDQL 525
Cdd:TIGR04523 224 KKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLkDEQNKIKKQL 269
|
|
| NIP100 |
COG5244 |
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ... |
382-542 |
6.09e-03 |
|
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227569 [Multi-domain] Cd Length: 669 Bit Score: 40.82 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 382 LRKAETLPEVEaELAQRVaalskSDLLSSGSSAAKEAKLLELTsklrkaeerHGNIEERLRQMEAQLEEKN---QELQRA 458
Cdd:COG5244 442 IARIDKLIGKE-EISKQD-----NRLFLYPSCDITLSSILTIL---------FSDKLEVFFQGIESLLENItifPEQPSQ 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 459 RQREKMNEEHNKRLSDTvdklLSESNERL--QLHLKERMAALEDKNSLLREVESAKKQLEEtqhdkdqlvlNIEALRAEL 536
Cdd:COG5244 507 QTSDSENIKENSLLSDR----LNEENIRLkeVLVQKENMLTEETKIKIIIGRDLERKTLEE----------NIKTLKVEL 572
|
....*.
gi 1800081418 537 DHMRLR 542
Cdd:COG5244 573 NNKNNK 578
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
389-527 |
6.18e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 40.42 E-value: 6.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 389 PEVEAELAQRVAALsksdllssgssAAKEAKLLELTSKLRKAEERHGnIEERLRQMEAQLEEKNQELQRARQ-------- 460
Cdd:COG1566 79 TDLQAALAQAEAQL-----------AAAEAQLARLEAELGAEAEIAA-AEAQLAAAQAQLDLAQRELERYQAlykkgavs 146
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1800081418 461 REKMNEEHNKRlsDTVDKLLSESNERLQLhLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVL 527
Cdd:COG1566 147 QQELDEARAAL--DAAQAQLEAAQAQLAQ-AQAGLREEEELAAAQAQVAQAEAALAQAELNLARTTI 210
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
45-277 |
7.42e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNtALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLL 124
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA-ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 125 LEHLECLVSRHERSLRMTVVKRQAQ---SPAGVSSEVEVLKALKSLFEHhkalDEKVRERLRVALERCSLLEEELGATHK 201
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPA----RREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1800081418 202 ELM-ILKEQNNQKKTLTDGVldinHEQENTPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKERLASLS 277
Cdd:COG4942 175 ELEaLLAELEEERAALEALK----AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
345-536 |
7.46e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.42 E-value: 7.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 345 KLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETlpeveaELAqRVAALSKSDLlssgssaakEAKLLELT 424
Cdd:COG1842 41 EARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKGRE------DLA-REALERKAEL---------EAQAEALE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 425 SKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNeEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSL 504
Cdd:COG1842 105 AQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAA-KAQEKVNEALSGIDSDDATSALERMEEKIEEMEARAEA 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 1800081418 505 LREVESAK---KQLEETQHDK---DQLvlniEALRAEL 536
Cdd:COG1842 184 AAELAAGDsldDELAELEADSeveDEL----AALKAKM 217
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
193-541 |
8.58e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.49 E-value: 8.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 193 EEELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTSgkrssdgsLSHEEdlaKVIELQEIISKQ---SREQSQM 269
Cdd:pfam05557 124 ELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSL--------AEAEQ---RIKELEFEIQSQeqdSEIVKNS 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 270 KERLASLSshvtELEedldtarKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEkRYLAAQREATSVHDLNDKLENE 349
Cdd:pfam05557 193 KSELARIP----ELE-------KELERLREHNKHLNENIENKLLLKEEVEDLKRKLE-REEKYREEAATLELEKEKLEQE 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 350 iankdsmhrqtedknrqLQERLELAeQKLQQTLRKAETLPEVEAELAQRVAALSKSDLLSSGSSAAKEAKLLELTSK--- 426
Cdd:pfam05557 261 -----------------LQSWVKLA-QDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQElaq 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 427 -------LRKAEERHGNIEERLRQ-----------MEAQLEEKNQELQRARQREKMNEEHnKRLSDTVDK---LLSESNE 485
Cdd:pfam05557 323 ylkkiedLNKKLKRHKALVRRLQRrvllltkerdgYRAILESYDKELTMSNYSPQLLERI-EEAEDMTQKmqaHNEEMEA 401
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1800081418 486 RLQLHLKERMAALEDKNSLLREVESAKKQleETQHDKDQLVLNIEALRAELDHMRL 541
Cdd:pfam05557 402 QLSVAEEELGGYKQQAQTLERELQALRQQ--ESLADPSYSKEEVDSLRRKLETLEL 455
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
276-457 |
9.12e-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: 39.28 E-value: 9.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 276 LSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERIT-TLEKRYLAAQREATSVhdlNDKLENEIANKD 354
Cdd:pfam04012 27 LEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQaALTKGNEELAREALAE---KKSLEKQAEALE 103
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 355 SMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLpEVEAELAQRVAALSKSDLLSSGSSAAK-----EAKLLELTSKLRK 429
Cdd:pfam04012 104 TQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLL-KARLKAAKAQEAVQTSLGSLSTSSATDsferiEEKIEEREARADA 182
|
170 180 190
....*....|....*....|....*....|
gi 1800081418 430 AEERHG--NIEERLRQMEAQLEEKNQELQR 457
Cdd:pfam04012 183 AAELASavDLDAKLEQAGIQMEVSEDVLAR 212
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| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
256-537 |
9.33e-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: 40.54 E-value: 9.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 256 QEIISKQSREQSQMKERLASLSSHVTELE--------------EDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEER 321
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEkkhqqlceeknalqEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 322 ITTLEKRYLAAQRE----ATSVHDLNDKLENEIANKDSMHRQ---TEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAE 394
Cdd:pfam01576 84 LEEEEERSQQLQNEkkkmQQHIQDLEEQLDEEEAARQKLQLEkvtTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 395 LAQRVAALSKSDLLSSGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQR----EKMNEEHNK 470
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQiaelRAQLAKKEE 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1800081418 471 RLSDTVDKLLSESNERLQLHLKERmaALEDKNSLLRE-VESAKKQLEETQHDKDQLVLNIEALRAELD 537
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIR--ELEAQISELQEdLESERAARNKAEKQRRDLGEELEALKTELE 309
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| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
250-538 |
9.42e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.11 E-value: 9.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 250 AKVIELQEIISKQSREQSQM----KERLASLSSHVTELEEDLDTARKdliKSEEMNTKLQ----RDVREAMAQKEDMEEr 321
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMelehKRARIELEKKASALKRQLDRESD---RNQELQKRIRllekREAEAEEALREQAEL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 322 iTTLEKRYLAAQREA--------TSVHDLNDKLENEIA-------NKDSMHRQTEDKNRQLQERLEL-------AEQKLQ 379
Cdd:pfam05557 78 -NRLKKKYLEALNKKlnekesqlADAREVISCLKNELSelrrqiqRAELELQSTNSELEELQERLDLlkakaseAEQLRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 380 QTLRKAETLPEVEA---ELAQRVAAL---------SKSDLLSSGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQ 447
Cdd:pfam05557 157 NLEKQQSSLAEAEQrikELEFEIQSQeqdseivknSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800081418 448 LE--EKNQ------ELQRARQREKMNE----EHNKRLSDTVDKLLSESNERLQlhlKERMAALEDKNSLLREVESAKKQL 515
Cdd:pfam05557 237 LEreEKYReeaatlELEKEKLEQELQSwvklAQDTGLNLRSPEDLSRRIEQLQ---QREIVLKEENSSLTSSARQLEKAR 313
|
330 340
....*....|....*....|...
gi 1800081418 516 EETQHDKDQLVLNIEALRAELDH 538
Cdd:pfam05557 314 RELEQELAQYLKKIEDLNKKLKR 336
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