|
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 ... |
997-1062 |
3.87e-43 |
|
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.
Pssm-ID: 188964 Cd Length: 66 Bit Score: 150.70 E-value: 3.87e-43
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568952884 997 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLRRL 1062
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 ... |
909-979 |
6.94e-43 |
|
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: 150.41 E-value: 6.94e-43
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952884 909 FAQWDGPTVVVWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEIMSLT 979
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 ... |
1082-1153 |
2.47e-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: 148.62 E-value: 2.47e-42
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568952884 1082 DVLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLL 1153
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 ... |
1001-1060 |
4.19e-29 |
|
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: 110.70 E-value: 4.19e-29
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 1001 WIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLR 1060
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 ... |
916-974 |
1.15e-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: 103.46 E-value: 1.15e-26
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 568952884 916 TVVVWLELWVGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 974
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 ... |
1090-1151 |
2.26e-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: 2.26e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568952884 1090 RVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNN 1151
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 ... |
1082-1153 |
6.12e-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: 90.58 E-value: 6.12e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568952884 1082 DVLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLL 1153
Cdd:cd09570 1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
246-545 |
4.84e-17 |
|
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: 87.03 E-value: 4.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 246 EDLAKVLELQ-EVIDRQAREQSQMKE--------RLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKED 316
Cdd:TIGR02168 192 EDILNELERQlKSLERQAEKAERYKElkaelrelELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 317 MEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQ 396
Cdd:TIGR02168 272 LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 397 RVAALSKSGplssgssAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVD 476
Cdd:TIGR02168 352 ELESLEAEL-------EELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIE 424
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568952884 477 KLLSESNE----RLQLHLKERMAALEDKNSLLREVENAKKQLEEtqhDKDQLVVTIEALKAELEQMRLRGPSL 545
Cdd:TIGR02168 425 ELLKKLEEaelkELQAELEELEEELEELQEELERLEEALEELRE---ELEEAEQALDAAERELAQLQARLDSL 494
|
|
| SAM_kazrin_repeat1 |
cd09564 |
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ... |
910-974 |
2.16e-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: 74.80 E-value: 2.16e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568952884 910 AQWDGPTVVVWLELWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 974
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 ... |
1082-1153 |
1.11e-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: 72.87 E-value: 1.11e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568952884 1082 DVLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLL 1153
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 ... |
996-1060 |
2.81e-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: 71.29 E-value: 2.81e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568952884 996 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLR 1060
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 ... |
996-1060 |
2.85e-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: 71.19 E-value: 2.85e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568952884 996 DMNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRNSFQCGIMCLR 1060
Cdd:cd09566 1 KLDTHWV-LRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDLL-HLKVTSALHHASIRRGIQVLR 63
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
221-538 |
1.06e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 76.26 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 221 LDGNHEQESAPSTNGKRSSDG--SLSHEDLAKVLELQEVIDrqareqsQMKERLASLSSHAAELEEDLDTARKDLIKSEE 298
Cdd:TIGR02169 644 LEGELFEKSGAMTGGSRAPRGgiLFSRSEPAELQRLRERLE-------GLKRELSSLQSELRRIENRLDELSQELSDASR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 299 MNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIAnkdsmhRQTEDKNrQLQERLE-----LA 373
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE------ELEEDLH-KLEEALNdlearLS 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 374 EQKLQQTLRKAETLPEVEAELAQRVAALSKSGPLSSGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQE 453
Cdd:TIGR02169 790 HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 454 LQRARQREKMNEEHNKRLSDTVDKL-------------LSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEE---T 517
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDELeaqlrelerkieeLEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEipeE 949
|
330 340
....*....|....*....|.
gi 568952884 518 QHDKDQLVVTIEALKAELEQM 538
Cdd:TIGR02169 950 ELSLEDVQAELQRVEEEIRAL 970
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
155-687 |
3.69e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.20 E-value: 3.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 155 SSEVEVLKALKSL--FEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGLLDGNHEQESAps 232
Cdd:COG1196 219 KEELKELEAELLLlkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE-- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 233 tngKRSSDGSLSHEdLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMA 312
Cdd:COG1196 297 ---LARLEQDIARL-EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 313 QKEDMEERITTLEKRYLAAQREATsvhdlndKLENEIANKdsmhRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEA 392
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAA-------ELAAQLEEL----EEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 393 ELAQrvaalsksgplssgssaAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLS 472
Cdd:COG1196 442 EALE-----------------EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 473 DtvdkllsESNERLQLHLKERMAALEDKNSLLREVENAKKQLEET----------QHDKDQLVVTIEALKAELEQMRLRG 542
Cdd:COG1196 505 G-------FLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAalaaalqnivVEDDEVAAAAIEYLKAAKAGRATFL 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 543 PSLHHGRPHLGSVPDFRFSVADGHVDAystsAVLRRPQKGRLAALRDEpSKVQTLNEQDWERAQQASVLANVAQAFES-- 620
Cdd:COG1196 578 PLDKIRARAALAAALARGAIGAAVDLV----ASDLREADARYYVLGDT-LLGRTLVAARLEAALRRAVTLAGRLREVTle 652
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568952884 621 -DVDVSDGEDDRDTLLSSVDLLSPSGQADAQTLAMMLQEQLDAINKEIRLIQEEKENTEQRAEEIESR 687
Cdd:COG1196 653 gEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEE 720
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
996-1060 |
5.42e-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: 64.98 E-value: 5.42e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568952884 996 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRNSFQCGIMCLR 1060
Cdd:pfam00536 1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
244-541 |
7.26e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.55 E-value: 7.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 244 SHEDLAKVLE-LQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERIT 322
Cdd:TIGR02168 706 ELEELEEELEqLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 323 TLEKRYLAAQREATSVHDLNDKLENEIAN-KDSMHRQTEDKNrQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAAL 401
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDELRAELTLlNEEAANLRERLE-SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 402 SKSGPLSSGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSE 481
Cdd:TIGR02168 865 EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952884 482 SNERLQLHLkerMAALEDKNSLLREVENAKKQLEETQHDKDQL-VVTIEALkAELEQMRLR 541
Cdd:TIGR02168 945 LSEEYSLTL---EEAEALENKIEDDEEEARRRLKRLENKIKELgPVNLAAI-EEYEELKER 1001
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
304-541 |
1.47e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.40 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 304 QREVREAMAQKEDMEERITTLEKrylaaqrEATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRK 383
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEK-------ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 384 AETLPEVEAELAQRVAALSKSGPLSSGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKM 463
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 464 NEEHNKRLSDTVDKL------------------------LSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQH 519
Cdd:TIGR02168 829 LERRIAATERRLEDLeeqieelsedieslaaeieeleelIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
250 260
....*....|....*....|..
gi 568952884 520 DKDQLVVTIEALKAELEQMRLR 541
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELR 930
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
192-489 |
1.51e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.40 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 192 LEEELGATHKELMI--LKEQNNQKKTLTDGLLDGNHEQESApsTNGKRSSDGSLS------HEDLAKVLELQEVIDRQAR 263
Cdd:TIGR02168 218 LKAELRELELALLVlrLEELREELEELQEELKEAEEELEEL--TAELQELEEKLEelrlevSELEEEIEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 264 EQSQM-------KERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREAT 336
Cdd:TIGR02168 296 EISRLeqqkqilRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 337 SVHDLNDKLENEIAnkdsmhrQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSgpLSSGSSAAKE 416
Cdd:TIGR02168 376 ELEEQLETLRSKVA-------QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK--ELQAELEELE 446
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568952884 417 AKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLH 489
Cdd:TIGR02168 447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
253-541 |
3.96e-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: 3.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 253 ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQ 332
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 333 REATSVHDLNDKLENEIAnkdsmhrQTEDKNRQLQERLELAEQKLQQTlrkAETLPEVEAELAQrvaalsksgplSSGSS 412
Cdd:TIGR02168 761 AEIEELEERLEEAEEELA-------EAEAEIEELEAQIEQLKEELKAL---REALDELRAELTL-----------LNEEA 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 413 AAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRAR-QREKMNEEHNKrlsdtvdklLSESNERLQLHLK 491
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEeLIEELESELEA---------LLNERASLEEALA 890
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 568952884 492 ERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLR 541
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
304-544 |
1.31e-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: 67.87 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 304 QREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRK 383
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 384 AETLpevEAELAQRVAALSKSGP------LSSGSSAAKEAKLLELTSKLrkAEERHGNIEErLRQMEAQLEEKNQELQRA 457
Cdd:COG4942 99 LEAQ---KEELAELLRALYRLGRqpplalLLSPEDFLDAVRRLQYLKYL--APARREQAEE-LRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 458 RQrekmneehnkRLSDTVDKlLSESNERLQLHLKERMAALedkNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQ 537
Cdd:COG4942 173 RA----------ELEALLAE-LEEERAALEALKAERQKLL---ARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
....*..
gi 568952884 538 MRLRGPS 544
Cdd:COG4942 239 AAERTPA 245
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
54-401 |
2.62e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.54 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 54 LRETQETLALTQGKLHEVGHERDSLQRQLNTAlpQEFAALTKELNvcREQLLEREEEIAELKAERNNTRLLLEHLECLVS 133
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKSLERQAEKA--ERYKELKAELR--ELELALLVLRLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 134 RHERSlrmtvvkrqaqspagvssevevLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQk 213
Cdd:TIGR02168 257 ELTAE----------------------LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 214 ktltdglLDGNHEQESAPSTNGKRSSDgsLSHEDLA----KVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTA 289
Cdd:TIGR02168 314 -------LERQLEELEAQLEELESKLD--ELAEELAeleeKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 290 RKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHdlNDKLENEIANKDSMHRQTEDKNRQLQER 369
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEA 462
|
330 340 350
....*....|....*....|....*....|..
gi 568952884 370 LELAEQKLQQTLRKAETLPEVEAELAQRVAAL 401
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQARLDSL 494
|
|
| SAM_liprin-beta1,2_repeat1 |
cd09563 |
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
909-973 |
3.37e-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: 59.93 E-value: 3.37e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568952884 909 FAQWDGPTVVVWL-ELWVGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQ 973
Cdd:cd09563 1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
74-487 |
5.02e-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: 5.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 74 ERDSLQRQLNtALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLLLEHLECLVSRHERSLRmTVVKRQAQSPAG 153
Cdd:TIGR02168 678 EIEELEEKIE-ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE-QLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 154 VSS----EVEVLKALKSLFEHHKALDEK---VRERLRVALERCSLLEEELGATHKELMILKEqnnqkktltdglldGNHE 226
Cdd:TIGR02168 756 LTEleaeIEELEERLEEAEEELAEAEAEieeLEAQIEQLKEELKALREALDELRAELTLLNE--------------EAAN 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 227 QESAPSTNGKRSSDGSLSHEDLAKVLElqevidrqareqsQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQRE 306
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIE-------------ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 307 VREAMAQKEDMEERITTLEKRYLAAQREAtsvHDLNDKLEneiankdsmhrqtedknrQLQERLELAEQKLQQTLRKAET 386
Cdd:TIGR02168 889 LALLRSELEELSEELRELESKRSELRREL---EELREKLA------------------QLELRLEGLEVRIDNLQERLSE 947
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 387 LPEVEAELAQRVAALSKSgplssgSSAAKEAKLLELTSKLRK-------AEERHGNIEERLRQMEAQLEeknqELQRARQ 459
Cdd:TIGR02168 948 EYSLTLEEAEALENKIED------DEEEARRRLKRLENKIKElgpvnlaAIEEYEELKERYDFLTAQKE----DLTEAKE 1017
|
410 420 430
....*....|....*....|....*....|...
gi 568952884 460 R-----EKMNEEHNKRLSDTVDKLlsesNERLQ 487
Cdd:TIGR02168 1018 TleeaiEEIDREARERFKDTFDQV----NENFQ 1046
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
227-539 |
8.44e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.09 E-value: 8.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 227 QESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDrQAREQSQMKERLASLSSHAAELEEDLDTARKdliKSEEmnTKLQRE 306
Cdd:PTZ00121 1441 EEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD-EAKKKAEEAKKADEAKKKAEEAKKKADEAKK---AAEA--KKKADE 1514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 307 VREAmAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRqlqerlelAEQKLQQTLRKAET 386
Cdd:PTZ00121 1515 AKKA-EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKK--------AEEDKNMALRKAEE 1585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 387 LPEVEAELAQRVAALSKSGPLSSGSSAAKEAKLLELTSKLRKAEERHGNIEErLRQMEAQLEEKNQELQRARQREKMNEE 466
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQ-LKKKEAEEKKKAEELKKAEEENKIKAA 1664
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568952884 467 HNKRLSDTvDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMR 539
Cdd:PTZ00121 1665 EEAKKAEE-DKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAK 1736
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
205-536 |
1.04e-10 |
|
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: 66.30 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 205 ILKEQNNQKKTLTDGLLDGNHEQESAPSTNGKRSSDGSLSHEDLAKVL---------------ELQEVIDRQAREQSQMK 269
Cdd:pfam15921 132 IRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMlshegvlqeirsilvDFEEASGKKIYEHDSMS 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 270 E-RLASLSSHAAELEEDLDTARKDLI--------KSEEMNTKLQREVREAMAQKEDMEER--------ITTLEKRYLAAQ 332
Cdd:pfam15921 212 TmHFRSLGSAISKILRELDTEISYLKgrifpvedQLEALKSESQNKIELLLQQHQDRIEQliseheveITGLTEKASSAR 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 333 REATSVHDLNDKLENEIANKDSMHRqtedknRQLQErLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSgplssgss 412
Cdd:pfam15921 292 SQANSIQSQLEIIQEQARNQNSMYM------RQLSD-LESTVSQLRSELREAKRMYEDKIEELEKQLVLANS-------- 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 413 aakeaKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQrarqrekMNEEHNKRLSD-------TVDKLLSESNER 485
Cdd:pfam15921 357 -----ELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELS-------LEKEQNKRLWDrdtgnsiTIDHLRRELDDR 424
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568952884 486 -----------------LQLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELE 536
Cdd:pfam15921 425 nmevqrleallkamkseCQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLE 492
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
158-524 |
1.78e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.45 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 158 VEVLKALKSLFEHHkaldEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGLLDGNHEQESAPSTNGKR 237
Cdd:PRK02224 233 RETRDEADEVLEEH----EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDAD 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 238 SSDGSLSHEDLAKVL-ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKED 316
Cdd:PRK02224 309 AEAVEARREELEDRDeELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 317 MEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQ--------QTLRK---AE 385
Cdd:PRK02224 389 LEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEagkcpecgQPVEGsphVE 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 386 TLPEVE---AELAQRVAAL-SKSGPLSSGSSAAKEAKllELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRAR--- 458
Cdd:PRK02224 469 TIEEDRervEELEAELEDLeEEVEEVEERLERAEDLV--EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRera 546
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568952884 459 ---------QREKMNEEHNKrlSDTVDKLLSESNERLQlHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQL 524
Cdd:PRK02224 547 aeleaeaeeKREAAAEAEEE--AEEAREEVAELNSKLA-ELKERIESLERIRTLLAAIADAEDEIERLREKREAL 618
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
179-533 |
1.79e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 65.75 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 179 RERLRVALERCSLLEEELGATHKELmiLKEQnnQKKTLTDGLLDGNHEQESAPSTNGKRSSDgslsHedLAKVLE---LQ 255
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTSRRQL--AAEQ--YRLVEMARELAELNEAESDLEQDYQAASD----H--LNLVQTalrQQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 256 EVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEmntklqrEVREAMAQKEDMEERITTLEKR---YLAAQ 332
Cdd:PRK04863 348 EKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEE-------EVDELKSQLADYQQALDVQQTRaiqYQQAV 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 333 REATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKlqqtLRKAETLPEVEAELAQRVAALSKSGPLSSGSS 412
Cdd:PRK04863 421 QALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQK----LSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWD 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 413 AAKEAklleltskLRKAEErHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDkllseSNERLQLHLKE 492
Cdd:PRK04863 497 VAREL--------LRRLRE-QRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLD-----DEDELEQLQEE 562
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 568952884 493 RMAALEDKNSllrEVENAKKQLEETQHDKDQLVVTIEALKA 533
Cdd:PRK04863 563 LEARLESLSE---SVSEARERRMALRQQLEQLQARIQRLAA 600
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
246-536 |
5.27e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.93 E-value: 5.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 246 EDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNtKLQREVREA-----MAQKEDMEER 320
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQ-ALLKEKREYegyelLKEKEALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 321 ITTLEKRYLAAQREATSVHDLNDKLENEIAnkdsmhrQTEDKNRQLQERLELAEQKLQQTLRkaETLPEVEAELAQRVAA 400
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLE-------EIEQLLEELNKKIKDLGEEEQLRVK--EKIGELEAEIASLERS 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 401 LsksgplssgssAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKnqelqrARQREKMNEEHnKRLSDTVDKLLS 480
Cdd:TIGR02169 310 I-----------AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEE------RKRRDKLTEEY-AELKEELEDLRA 371
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568952884 481 E------SNERLQLHLKERMAALED----KNSLLREVE---NAKKQLEETQHDKDQLVVTIEALKAELE 536
Cdd:TIGR02169 372 EleevdkEFAETRDELKDYREKLEKlkreINELKRELDrlqEELQRLSEELADLNAAIAGIEAKINELE 440
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
245-449 |
9.38e-10 |
|
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: 60.32 E-value: 9.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 245 HEDLAKVLELQEvIDRQAReqsQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTL 324
Cdd:COG1579 3 PEDLRALLDLQE-LDSELD---RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 325 EKRylaaQREATSVHDLNDkLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQqtlrkaetlpEVEAELAQRVAALsks 404
Cdd:COG1579 79 EEQ----LGNVRNNKEYEA-LQKEIESLKRRISDLEDEILELMERIEELEEELA----------ELEAELAELEAEL--- 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568952884 405 gplssgssAAKEAKLLELTSKLRKAEERhgnIEERLRQMEAQLEE 449
Cdd:COG1579 141 --------EEKKAELDEELAELEAELEE---LEAEREELAAKIPP 174
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
152-536 |
1.34e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.77 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 152 AGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLtDGLLDGNHEQESAP 231
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKEL-KEKAEEYIKLSEFY 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 232 STNGKRSSDGSlshEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQR----EV 307
Cdd:PRK03918 303 EEYLDELREIE---KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEElerlKK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 308 REAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIAN-KDSMHRQTEDK------NRQLQE--RLELAEQ--- 375
Cdd:PRK03918 380 RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKElKKAIEELKKAKgkcpvcGRELTEehRKELLEEyta 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 376 ---KLQQTLRKA-ETLPEVEAELAQRVAALSKSGPLSSGSSAAKEAKLLE------LTSKLRKAEERHGNIEERLRQMEA 445
Cdd:PRK03918 460 elkRIEKELKEIeEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEeklkkyNLEELEKKAEEYEKLKEKLIKLKG 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 446 QLEEKNQELQRARQREKMNEEHNKRLsDTVDKLLSESNERLQL-------HLKERMAALEDKNSLLREVENAKKQLEETQ 518
Cdd:PRK03918 540 EIKSLKKELEKLEELKKKLAELEKKL-DELEEELAELLKELEElgfesveELEERLKELEPFYNEYLELKDAEKELEREE 618
|
410
....*....|....*...
gi 568952884 519 HDKDQLVVTIEALKAELE 536
Cdd:PRK03918 619 KELKKLEEELDKAFEELA 636
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
255-485 |
2.42e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.93 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 255 QEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQRE 334
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 335 AtsvhdlnDKLENEIANkdsMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSGPLSSGSSAA 414
Cdd:COG4942 99 L-------EAQKEELAE---LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952884 415 KEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNER 485
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
284-545 |
2.60e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 2.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 284 EDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTED-- 361
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElk 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 362 --------KNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSGPLSSGSSAAKEAKLlELTSKLRKAEERH 433
Cdd:PRK03918 238 eeieelekELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYE-EYLDELREIEKRL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 434 GNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDtvdklLSESNERLQ--LHLKERMAALEDKNSLLrEVENAK 511
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEE-----LEERHELYEeaKAKKEELERLKKRLTGL-TPEKLE 390
|
250 260 270
....*....|....*....|....*....|....
gi 568952884 512 KQLEETQHDKDQLVVTIEALKAELEQMRLRGPSL 545
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKEL 424
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
157-539 |
3.08e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 3.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 157 EVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGL---------LDGNHE- 226
Cdd:PRK03918 284 ELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLkelekrleeLEERHEl 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 227 ----QESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQ-SQMKERLASLSSHAAELE---EDLDTA--------- 289
Cdd:PRK03918 364 yeeaKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEiSKITARIGELKKEIKELKkaiEELKKAkgkcpvcgr 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 290 ------RKDLIKS--EEMNtKLQREVREAMAQKEDMEERITTLEKrYLAAQREATSVHDLNDKLENeiankdsmhrqted 361
Cdd:PRK03918 444 elteehRKELLEEytAELK-RIEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQLKE-------------- 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 362 knrqLQERLE-LAEQKLQQTLRKAETLPEVEAELAQRVAALSKSgpLSSGssAAKEAKLLELTSKLRKAEERHGNIEERL 440
Cdd:PRK03918 508 ----LEEKLKkYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKE--LEKL--EELKKKLAELEKKLDELEEELAELLKEL 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 441 RQM----EAQLEEKNQELQR----------ARQREKMNEEHNKRLSDTVDKL---LSESNERLQlHLKERMAALEDKNS- 502
Cdd:PRK03918 580 EELgfesVEELEERLKELEPfyneylelkdAEKELEREEKELKKLEEELDKAfeeLAETEKRLE-ELRKELEELEKKYSe 658
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 568952884 503 ------------LLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMR 539
Cdd:PRK03918 659 eeyeelreeyleLSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
68-679 |
5.45e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 60.90 E-value: 5.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 68 LHEVGHERDSLQRQLNTA-----------------LPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLLLEHLEC 130
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESnelhekqkfylrqsvidLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 131 LVSR--HERSLRMTVVKRQAQSPAGVSSEVEVL------KALKSLFEHH-------KALDEKVRERLRVALERCSLLEEE 195
Cdd:pfam15921 160 LKEDmlEDSNTQIEQLRKMMLSHEGVLQEIRSIlvdfeeASGKKIYEHDsmstmhfRSLGSAISKILRELDTEISYLKGR 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 196 LGATHKELMILKEQNNQKKTL-----TDGL--LDGNHEQESAPSTNgKRSSDGSLSHEDLAKVlelqEVIDRQAREQSQM 268
Cdd:pfam15921 240 IFPVEDQLEALKSESQNKIELllqqhQDRIeqLISEHEVEITGLTE-KASSARSQANSIQSQL----EIIQEQARNQNSM 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 269 KER-LASLSSHAAELEEDLDTARKDL-IKSEEMNTKL---QREVREAMAQKEDMEERITTLE---KRYLA----AQREAT 336
Cdd:pfam15921 315 YMRqLSDLESTVSQLRSELREAKRMYeDKIEELEKQLvlaNSELTEARTERDQFSQESGNLDdqlQKLLAdlhkREKELS 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 337 SVHDLNDKL-ENEIANK---DSMHRQTEDKNRQLQeRLELAEQKLqqtlrKAETLPEVEAELAQ---RVAALSKSGPLSS 409
Cdd:pfam15921 395 LEKEQNKRLwDRDTGNSitiDHLRRELDDRNMEVQ-RLEALLKAM-----KSECQGQMERQMAAiqgKNESLEKVSSLTA 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 410 GSSAAKEA--KLLE-LTSK---LRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESN 483
Cdd:pfam15921 469 QLESTKEMlrKVVEeLTAKkmtLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQT 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 484 E----RLQLHLKERM-----------------------AALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELE 536
Cdd:pfam15921 549 EcealKLQMAEKDKVieilrqqienmtqlvgqhgrtagAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVS 628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 537 QMRLRGPSL-HHGRPHLGSVPDFR-------FSVADGHVDAYSTS---AVLRRpqkgrlaALRDEPSKVQ-TLNEQDWER 604
Cdd:pfam15921 629 DLELEKVKLvNAGSERLRAVKDIKqerdqllNEVKTSRNELNSLSedyEVLKR-------NFRNKSEEMEtTTNKLKMQL 701
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568952884 605 AQQASVLANVAQAFESdVDVSDGEDDRDTLLSSVDLLSPSGQADA-QTLAMMLQEQLDAINKEIRLIQEEKENTEQ 679
Cdd:pfam15921 702 KSAQSELEQTRNTLKS-MEGSDGHAMKVAMGMQKQITAKRGQIDAlQSKIQFLEEAMTNANKEKHFLKEEKNKLSQ 776
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
45-538 |
6.18e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 6.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNtALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLL 124
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRR-ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 125 LEHLECLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELM 204
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 205 ILKEQNNQKKTLTDGLLDGNHEQEsapstngKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEE 284
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEE-------EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 285 DLDTARKDLIKS----------------EEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENE 348
Cdd:COG1196 506 FLEGVKAALLLAglrglagavavligveAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRAR 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 349 IANKDSMHRQTEDKNR----QLQERLELAEQKLQQTL-------RKAETLPEVEAELAQRVAALSKSGPLSSGSSAAKEA 417
Cdd:COG1196 586 AALAAALARGAIGAAVdlvaSDLREADARYYVLGDTLlgrtlvaARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 418 KLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAAL 497
Cdd:COG1196 666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 568952884 498 EDKNSLLREVENAKKQLEETQHDkdqlvvtIEALKAELEQM 538
Cdd:COG1196 746 ELLEEEALEELPEPPDLEELERE-------LERLEREIEAL 779
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
45-537 |
1.00e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 59.65 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTaLPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLL 124
Cdd:TIGR04523 124 VELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYND-LKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 125 LEHLECLVSRHeRSLRMTVVKRQAQSpagvSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKEL- 203
Cdd:TIGR04523 203 LSNLKKKIQKN-KSLESQISELKKQN----NQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELe 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 204 ---MILKEQNNQKKTLTDGLLDGNHEQEsapstngkrssdgslshEDLAKvlELQEVIDRQAREQSQMKERLASLSSHAA 280
Cdd:TIGR04523 278 qnnKKIKELEKQLNQLKSEISDLNNQKE-----------------QDWNK--ELKSELKNQEKKLEEIQNQISQNNKIIS 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 281 ELEEDLDTARKDLIKSEEMNTKLQREVREamaqKEDMEERIttlekrylaaQREATSVHDLNDKLENEIANKDSMHRQTE 360
Cdd:TIGR04523 339 QLNEQISQLKKELTNSESENSEKQRELEE----KQNEIEKL----------KKENQSYKQEIKNLESQINDLESKIQNQE 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 361 DKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKsgplssgSSAAKEAKLLELTS-------KLRKAEERH 433
Cdd:TIGR04523 405 KLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTN-------QDSVKELIIKNLDNtresletQLKVLSRSI 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 434 GNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLsESNERLQLHLKERMAALEDKNSLLREV------ 507
Cdd:TIGR04523 478 NKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLK-EKIEKLESEKKEKESKISDLEDELNKDdfelkk 556
|
490 500 510
....*....|....*....|....*....|
gi 568952884 508 ENAKKQLEETQHDKDQLVVTIEALKAELEQ 537
Cdd:TIGR04523 557 ENLEKEIDEKNKEIEELKQTQKSLKKKQEE 586
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
31-533 |
1.04e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 59.75 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 31 DADSHFEQLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQ---LNTALPQEFAAL---TKELNVCREQL 104
Cdd:pfam15921 321 DLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQEsgnLDDQLQKLLADLhkrEKELSLEKEQN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 105 LE-------REEEIAELKAERNNTRLLLEHLECLVsRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEK 177
Cdd:pfam15921 401 KRlwdrdtgNSITIDHLRRELDDRNMEVQRLEALL-KAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRK 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 178 VRERL---RVALER---------CSLLEEE--LGATHKELMILKEQNNQK-KTLTDGLLDGNHEQESAPSTNGKRssdgs 242
Cdd:pfam15921 480 VVEELtakKMTLESsertvsdltASLQEKEraIEATNAEITKLRSRVDLKlQELQHLKNEGDHLRNVQTECEALK----- 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 243 LSHEDLAKVLE-LQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEeri 321
Cdd:pfam15921 555 LQMAEKDKVIEiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLE--- 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 322 ttLEKRYL--AAQREATSVHDLN---DKLENEIAN-KDSMHRQTEDKN------RQLQERLELAEQKLQQTLRKAET-LP 388
Cdd:pfam15921 632 --LEKVKLvnAGSERLRAVKDIKqerDQLLNEVKTsRNELNSLSEDYEvlkrnfRNKSEEMETTTNKLKMQLKSAQSeLE 709
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 389 EVEAELAQRVAALSKSGPLSSGSS---AAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQR-ARQREKMN 464
Cdd:pfam15921 710 QTRNTLKSMEGSDGHAMKVAMGMQkqiTAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTvATEKNKMA 789
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568952884 465 EEHNkrlsdtvdklLSESNERlqlHLKERMAALE---DKNSL-LREVEN-AKKQLEETQHDKDQLVVTIEALKA 533
Cdd:pfam15921 790 GELE----------VLRSQER---RLKEKVANMEvalDKASLqFAECQDiIQRQEQESVRLKLQHTLDVKELQG 850
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
44-538 |
1.22e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 59.60 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 44 LEERDRLLDTLR-ETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTR 122
Cdd:TIGR00618 417 SAFRDLQGQLAHaKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARL 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 123 LLLEHLECLVSRHERSLRMTVVkrQAQSPAGVSSEVEvlkALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKE 202
Cdd:TIGR00618 497 LELQEEPCPLCGSCIHPNPARQ--DIDNPGPLTRRMQ---RGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQS 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 203 LMILKEQNNQKKTLTDGLLdgNHEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQ--AREQSQMKERLASLSSHAA 280
Cdd:TIGR00618 572 FSILTQCDNRSKEDIPNLQ--NITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQdvRLHLQQCSQELALKLTALH 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 281 ELEEDLdtarkdlikseemntkLQREVREAMAQKEDMEERitTLEKRYLAAQREATSVHDLNDKLEnEIANKDSMHR--- 357
Cdd:TIGR00618 650 ALQLTL----------------TQERVREHALSIRVLPKE--LLASRQLALQKMQSEKEQLTYWKE-MLAQCQTLLRele 710
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 358 QTEDKNRQLQERLELAEQKLQQTLR-KAETLPEVEAEL-AQRVAALSKSgplssgsSAAKEAKLLELTSKLRKAEErhgn 435
Cdd:TIGR00618 711 THIEEYDREFNEIENASSSLGSDLAaREDALNQSLKELmHQARTVLKAR-------TEAHFNNNEEVTAALQTGAE---- 779
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 436 ieerLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLE 515
Cdd:TIGR00618 780 ----LSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYE 855
|
490 500
....*....|....*....|...
gi 568952884 516 ETQHDKDQLVVTIEALKAELEQM 538
Cdd:TIGR00618 856 ECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
252-533 |
3.74e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.04 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 252 LELQEVIDRQAREQ-SQMKERLASLSSHAAELeedldtarkDLIKSEEmntkLQREVREAMAQKEDMEErittlEKRYLA 330
Cdd:PRK04863 853 LADHESQEQQQRSQlEQAKEGLSALNRLLPRL---------NLLADET----LADRVEEIREQLDEAEE-----AKRFVQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 331 AQREATSvhdlndKLENEIankdSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLpeveAELAQRVAALSKSgplSSG 410
Cdd:PRK04863 915 QHGNALA------QLEPIV----SVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFAL----TEVVQRRAHFSYE---DAA 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 411 SSAAKEAKLLE-LTSKLRKAEERHGNIEERLRQMEAQLEEKNQ---ELQRARQR-EKMNEEHNKRLSDTVDKLLSESNER 485
Cdd:PRK04863 978 EMLAKNSDLNEkLRQRLEQAEQERTRAREQLRQAQAQLAQYNQvlaSLKSSYDAkRQMLQELKQELQDLGVPADSGAEER 1057
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 568952884 486 LQLHLKERMAAL----EDKNSLLR-------EVENAKKQLEETQHDKDQLVVTIEALKA 533
Cdd:PRK04863 1058 ARARRDELHARLsanrSRRNQLEKqltfceaEMDNLTKKLRKLERDYHEMREQVVNAKA 1116
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
160-538 |
3.86e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 3.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 160 VLKALKSLFEhhKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGLLDGNHEQESApstnGKRSS 239
Cdd:COG4717 39 LLAFIRAMLL--ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEEL----EAELE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 240 DGSLSHEDLAKVLELQEVIDRQAREQSQMK---ERLASLSSHAA---ELEEDLDTARKDLIKSEEMNTKLQREVREAMAQ 313
Cdd:COG4717 113 ELREELEKLEKLLQLLPLYQELEALEAELAelpERLEELEERLEelrELEEELEELEAELAELQEELEELLEQLSLATEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 314 K-EDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELA------------------- 373
Cdd:COG4717 193 ElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLiaaallallglggsllsli 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 374 ------------------------EQKLQQTLRKAETLPEVEAELAQRVAALSKSGPLSSGSSAAKEAKLLELTSKLRKA 429
Cdd:COG4717 273 ltiagvlflvlgllallflllareKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 430 EERHGNIEERLRQMEAQlEEKNQELQRA--------RQREKMNEEHNKRLsdtvdKLLSESNERLQLHLKERMAALE--D 499
Cdd:COG4717 353 LREAEELEEELQLEELE-QEIAALLAEAgvedeeelRAALEQAEEYQELK-----EELEELEEQLEELLGELEELLEalD 426
|
410 420 430
....*....|....*....|....*....|....*....
gi 568952884 500 KNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQM 538
Cdd:COG4717 427 EEELEEELEELEEELEELEEELEELREELAELEAELEQL 465
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
246-460 |
4.04e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 4.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 246 EDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLdtarkdlikseemntkLQREVREAMAQKEDMEERITTLE 325
Cdd:COG4913 252 ELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL----------------LEAELEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 326 KRYLAAQREATSVHdlNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQkLQQTLRKAE-TLPEVEAELAQRVAALsks 404
Cdd:COG4913 316 ARLDALREELDELE--AQIRGNGGDRLEQLEREIERLERELEERERRRAR-LEALLAALGlPLPASAEEFAALRAEA--- 389
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568952884 405 gplssgssaakEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQR 460
Cdd:COG4913 390 -----------AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
302-518 |
5.37e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.76 E-value: 5.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 302 KLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIAnkdsmhrqtedknrQLQERLELAEQKLQQTl 381
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID--------------KLQAEIAEAEAEIEER- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 382 rkaetlpevEAELAQRVAALSKSGPLSSGSSAAKEAK----LLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRA 457
Cdd:COG3883 85 ---------REELGERARALYRSGGSVSYLDVLLGSEsfsdFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952884 458 RQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQ 518
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
264-461 |
5.51e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 5.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 264 EQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLND 343
Cdd:TIGR02169 288 EQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 344 KLENEIANKDSMHRQTEDKNRQLQERLELA----------EQKLQQTLRKA---------------ETLPEVEAELAQRV 398
Cdd:TIGR02169 368 DLRAELEEVDKEFAETRDELKDYREKLEKLkreinelkreLDRLQEELQRLseeladlnaaiagieAKINELEEEKEDKA 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568952884 399 AALSKS-GPLSSGSS--AAKEAKLLELTSKLRKaeerhgnIEERLRQMEAQLEEKNQELQRARQRE 461
Cdd:TIGR02169 448 LEIKKQeWKLEQLAAdlSKYEQELYDLKEEYDR-------VEKELSKLQRELAEAEAQARASEERV 506
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
249-541 |
6.74e-08 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 56.23 E-value: 6.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 249 AKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRY 328
Cdd:pfam19220 48 SRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 329 LAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSGPLS 408
Cdd:pfam19220 128 AAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDAT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 409 SGSSAAKEAKLLELTSKLRKAEERHGNIEERLRqmeaqleeknqeLQRARQREKMnEEHNKRLSDTvDKLLSESNERLQl 488
Cdd:pfam19220 208 RARLRALEGQLAAEQAERERAEAQLEEAVEAHR------------AERASLRMKL-EALTARAAAT-EQLLAEARNQLR- 272
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 568952884 489 hlkermaaleDKNSLLREVENAkkqLEETQHDKDQLVVTIEALKAELEQMRLR 541
Cdd:pfam19220 273 ----------DRDEAIRAAERR---LKEASIERDTLERRLAGLEADLERRTQQ 312
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
236-523 |
8.74e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.07 E-value: 8.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 236 KRSSDGSLSHEDLAKVLELQEVID--RQAREQSQMKE-RLASLSSHAAELEEDLDTARKD-LIKSEEMntKLQREVREAM 311
Cdd:PTZ00121 1490 KKAEEAKKKADEAKKAAEAKKKADeaKKAEEAKKADEaKKAEEAKKADEAKKAEEKKKADeLKKAEEL--KKAEEKKKAE 1567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 312 AQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTED---------KNRQLQERLELAEQKLQQTLR 382
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikaeelkKAEEEKKKVEQLKKKEAEEKK 1647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 383 KAETLPEVEAELAQRVAALSKSgplssgssaAKEAKlleltsklRKAEERHGNIEERlRQMEAQLEEKNQELQRARQREK 462
Cdd:PTZ00121 1648 KAEELKKAEEENKIKAAEEAKK---------AEEDK--------KKAEEAKKAEEDE-KKAAEALKKEAEEAKKAEELKK 1709
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952884 463 MNEEHNKRLsdtvdkllsesnERLQLHLKERMAALEDknsLLREVENAKKQLEETQHDKDQ 523
Cdd:PTZ00121 1710 KEAEEKKKA------------EELKKAEEENKIKAEE---AKKEAEEDKKKAEEAKKDEEE 1755
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
253-466 |
8.93e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.99 E-value: 8.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 253 ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAmaqKEDMEERITTLEKRYLAAQ 332
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA---EAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 333 R------------EATSVHDLNDKLE--NEI--ANKDSMHRQTEDKnrqlqERLELAEQKLQQTLRKAETLpevEAELAQ 396
Cdd:COG3883 97 RsggsvsyldvllGSESFSDFLDRLSalSKIadADADLLEELKADK-----AELEAKKAELEAKLAELEAL---KAELEA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 397 RVAALsksgplssgssaakEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEE 466
Cdd:COG3883 169 AKAEL--------------EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
262-539 |
1.37e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 56.11 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 262 AREQSQMKERLASLSSHAAELEEDLDTARKDLikseemnTKLQREVREAMA-QKEDMEERITTLEKRYLAAQREATSVHD 340
Cdd:COG3096 842 RQRRSELERELAQHRAQEQQLRQQLDQLKEQL-------QLLNKLLPQANLlADETLADRLEELREELDAAQEAQAFIQQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 341 LNDKLEnEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLpeveAELAQRVAALS--KSGPLSSGSSAAKEAk 418
Cdd:COG3096 915 HGKALA-QLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFAL----SEVVQRRPHFSyeDAVGLLGENSDLNEK- 988
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 419 lleLTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQ----RARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERM 494
Cdd:COG3096 989 ---LRARLEQAEEARREAREQLRQAQAQYSQYNQVLAslksSRDAKQQTLQELEQELEELGVQADAEAEERARIRRDELH 1065
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 568952884 495 AALEDKNSLLREVEnakKQLEETQHDKDQLVVTIEALKAELEQMR 539
Cdd:COG3096 1066 EELSQNRSRRSQLE---KQLTRCEAEMDSLQKRLRKAERDYKQER 1107
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
1083-1153 |
1.52e-07 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 49.60 E-value: 1.52e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952884 1083 VLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDfsalaLLLQIPTQNTQARAVLEREFNNLL 1153
Cdd:smart00454 1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEE-----DLKELGITKLGHRKKILKAIQKLK 66
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
44-487 |
3.18e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 44 LEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTA-LPQEFAALTKELNVCREQLLEREEEIAELKAERNNTR 122
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLpLYQELEALEAELAELPERLEELEERLEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 123 LLLEHLECLVSRHERSLRmtvvkrqaqspagvSSEVEVLKALKSLFEHHKALDEKV---RERLRVALERCSLLEEELGAT 199
Cdd:COG4717 167 ELEAELAELQEELEELLE--------------QLSLATEEELQDLAEELEELQQRLaelEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 200 HKELMILKEQNNQKKTLTDGLLDGnheqeSAPSTNGKRSSDGSLSHEDLAKVLELQEVI-------DRQAREQSQMKERL 272
Cdd:COG4717 233 ENELEAAALEERLKEARLLLLIAA-----ALLALLGLGGSLLSLILTIAGVLFLVLGLLallflllAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 273 ASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANK 352
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 353 DSMHRQTEDKnRQLQERLELAEQKLQQTLRKAETLPEV--EAELAQRVAALsksgplssgssaakEAKLLELTSKLRKAE 430
Cdd:COG4717 388 RAALEQAEEY-QELKEELEELEEQLEELLGELEELLEAldEEELEEELEEL--------------EEELEELEEELEELR 452
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 568952884 431 ERHGNIEERLRQMEAQ--LEEKNQELQRARQREKMNEEHNKRLsDTVDKLLSESNERLQ 487
Cdd:COG4717 453 EELAELEAELEQLEEDgeLAELLQELEELKAELRELAEEWAAL-KLALELLEEAREEYR 510
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
909-975 |
3.75e-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: 48.45 E-value: 3.75e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568952884 909 FAQWDGPTVVVWLELWvGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEI 975
Cdd:smart00454 1 VSQWSPESVADWLESI-GLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
1005-1060 |
3.79e-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: 48.45 E-value: 3.79e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 568952884 1005 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLR 1060
Cdd:smart00454 11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
258-461 |
3.82e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.07 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 258 IDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREV----REAMAQKEDMEERITTLEKRYLAAQR 333
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIdklqAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 334 ------------EATSVHDLNDKLE--NEI--ANKDSMHRQTEDKnrqlqERLELAEQKLQQTLRKAETLpevEAELAQR 397
Cdd:COG3883 98 sggsvsyldvllGSESFSDFLDRLSalSKIadADADLLEELKADK-----AELEAKKAELEAKLAELEAL---KAELEAA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568952884 398 VAALSKsgplssgSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQRE 461
Cdd:COG3883 170 KAELEA-------QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
253-546 |
4.13e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 53.75 E-value: 4.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 253 ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQ 332
Cdd:COG4372 49 QLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 333 REATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQtLRKAETLPEVEAELAQ-RVAALSKSGPLSSGS 411
Cdd:COG4372 129 QQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA-LSEAEAEQALDELLKEaNRNAEKEEELAEAEK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 412 SAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLK 491
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 568952884 492 ERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRGPSLH 546
Cdd:COG4372 288 LEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADL 342
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
38-554 |
4.31e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 54.67 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 38 QLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHER--DSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELK 115
Cdd:TIGR00606 353 QLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERqiKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIR 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 116 AERNNTRLLLEHLECLVSRHERSLRMtvVKRQAQSPAGVSSEV-----EVLKALK--SLFEHHKALDEKVRERLRVALER 188
Cdd:TIGR00606 433 DEKKGLGRTIELKKEILEKKQEELKF--VIKELQQLEGSSDRIleldqELRKAERelSKAEKNSLTETLKKEVKSLQNEK 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 189 CSLLEEElgatHKELMILKEQNNQKKTLTDGLL---DGNHEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQ 265
Cdd:TIGR00606 511 ADLDRKL----RKLDQEMEQLNHHTTTRTQMEMltkDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEI 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 266 SQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQkEDMEERITTLEKRYLAAQREA---TSVHDLN 342
Cdd:TIGR00606 587 NQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS-QDEESDLERLKEEIEKSSKQRamlAGATAVY 665
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 343 DKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAET-LPEVEAELAQrvaalsksgplssgssaaKEAKLLE 421
Cdd:TIGR00606 666 SQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDkLKSTESELKK------------------KEKRRDE 727
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 422 LtskLRKAEERHGNIEERLRQMEaQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESN---------ERLQLHLKE 492
Cdd:TIGR00606 728 M---LGLAPGRQSIIDLKEKEIP-ELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKvcltdvtimERFQMELKD 803
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568952884 493 ------RMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRGPSLHHGRPHLGS 554
Cdd:TIGR00606 804 verkiaQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKS 871
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
269-537 |
5.02e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 5.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 269 KERLASLSSHAAELEEDLDTARKDLIKSEEMnTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENE 348
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERLERAEDL-VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAE 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 349 IANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSGPLSSgSSAAKEAKLLELTSKLRK 428
Cdd:PRK02224 553 AEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLRE-KREALAELNDERRERLAE 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 429 AEERHGNIEERLRqmEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSE----SNERLQLH-LKERMAALEDKNSL 503
Cdd:PRK02224 632 KRERKRELEAEFD--EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEigavENELEELEeLRERREALENRVEA 709
|
250 260 270
....*....|....*....|....*....|....
gi 568952884 504 LREVENAKKQLEETQHDkdqlvvtieaLKAELEQ 537
Cdd:PRK02224 710 LEALYDEAEELESMYGD----------LRAELRQ 733
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
38-538 |
5.14e-07 |
|
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: 54.46 E-value: 5.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 38 QLMVSMLEERDR--LLDTLRETQETLALTQGKLHE--VGHERDSLQRQ-----LNTALPQEFAALTKELNvcreqlLERE 108
Cdd:pfam12128 231 QAIAGIMKIRPEftKLQQEFNTLESAELRLSHLHFgyKSDETLIASRQeerqeTSAELNQLLRTLDDQWK------EKRD 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 109 EEIAELKAERNNTRLLLEHLECLVSRHERSLRMTVVKR---QAQSPAgVSSEVEVL-KALKSLFEHHKALDEKVRERLRV 184
Cdd:pfam12128 305 ELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAaadQEQLPS-WQSELENLeERLKALTGKHQDVTAKYNRRRSK 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 185 ALERCSlleEELGATHKELMILKEQNNQKKTLTDGLLDGnheQESApstngkrssdgsLSHEDLAKVLELQEVIDRQARE 264
Cdd:pfam12128 384 IKEQNN---RDIAGIKDKLAKIREARDRQLAVAEDDLQA---LESE------------LREQLEAGKLEFNEEEYRLKSR 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 265 QSQMKERLASLSSHAAELE------EDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSV 338
Cdd:pfam12128 446 LGELKLRLNQATATPELLLqlenfdERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDEL 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 339 --------HDLNDKLENEIAN-KDSMHRQTedkNRQLQERLELAEQKLQQTLRKAETLPEVEAELaQRVAAlsksgPLSS 409
Cdd:pfam12128 526 elqlfpqaGTLLHFLRKEAPDwEQSIGKVI---SPELLHRTDLDPEVWDGSVGGELNLYGVKLDL-KRIDV-----PEWA 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 410 GSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLH 489
Cdd:pfam12128 597 ASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAER 676
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 568952884 490 LK---ERMAALE-DKNSLLREVENAKKQ-----LEETQHDKDQLVVTIEALKAELEQM 538
Cdd:pfam12128 677 KDsanERLNSLEaQLKQLDKKHQAWLEEqkeqkREARTEKQAYWQVVEGALDAQLALL 734
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
31-539 |
6.98e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.97 E-value: 6.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 31 DADSHFEQLMVSMLEERDrlldTLRETQETLALTQGKLHEVGHERDSLQ----RQLNTALPQEFAALTKELNVCREQLLE 106
Cdd:pfam15921 167 DSNTQIEQLRKMMLSHEG----VLQEIRSILVDFEEASGKKIYEHDSMStmhfRSLGSAISKILRELDTEISYLKGRIFP 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 107 REEEIAELKAE-RNNTRLLLEH----LECLVSRHERSLR-MTVVKRQAQSPA-GVSSEVEV------------LKALKSL 167
Cdd:pfam15921 243 VEDQLEALKSEsQNKIELLLQQhqdrIEQLISEHEVEITgLTEKASSARSQAnSIQSQLEIiqeqarnqnsmyMRQLSDL 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 168 FEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQ----KKTLTD---GLLDGNHEQESAPSTNGK---- 236
Cdd:pfam15921 323 ESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQfsqeSGNLDDqlqKLLADLHKREKELSLEKEqnkr 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 237 ---RSSDGSLSHEDLAKVL-------------------ELQEVIDRQAREQSQMKERLASLSSHAAELE----------E 284
Cdd:pfam15921 403 lwdRDTGNSITIDHLRRELddrnmevqrleallkamksECQGQMERQMAAIQGKNESLEKVSSLTAQLEstkemlrkvvE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 285 DLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNR 364
Cdd:pfam15921 483 ELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDK 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 365 QLQERLELAEQKLQQTLRKAETLPEVEAELAQrvaaLSKSgpLSSGSSAAKEAKLLE--LTSKLRKAEERHGNIE-ERLR 441
Cdd:pfam15921 563 VIEILRQQIENMTQLVGQHGRTAGAMQVEKAQ----LEKE--INDRRLELQEFKILKdkKDAKIRELEARVSDLElEKVK 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 442 QMEAQLEeknqelqRARQREKMNEEHnkrlsdtvDKLLSE-SNERLQLHlkermAALEDKNSLLREVENAKKQLEETqhd 520
Cdd:pfam15921 637 LVNAGSE-------RLRAVKDIKQER--------DQLLNEvKTSRNELN-----SLSEDYEVLKRNFRNKSEEMETT--- 693
|
570
....*....|....*....
gi 568952884 521 KDQLVVTIEALKAELEQMR 539
Cdd:pfam15921 694 TNKLKMQLKSAQSELEQTR 712
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
269-536 |
9.54e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.10 E-value: 9.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 269 KERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEK-------RYLAAQREATSVHDL 341
Cdd:TIGR04523 95 KDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKeleklnnKYNDLKKQKEELENE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 342 NDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQqtlrKAETLPEVEAELAQRVAALSKSGPLssgssaaKEAKLLE 421
Cdd:TIGR04523 175 LNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQ----KNKSLESQISELKKQNNQLKDNIEK-------KQQEINE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 422 LTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRArqrEKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKN 501
Cdd:TIGR04523 244 KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN---NKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQE 320
|
250 260 270
....*....|....*....|....*....|....*
gi 568952884 502 SLLREVENakkQLEETQHDKDQLVVTIEALKAELE 536
Cdd:TIGR04523 321 KKLEEIQN---QISQNNKIISQLNEQISQLKKELT 352
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
246-536 |
9.58e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 9.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 246 EDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERItTLE 325
Cdd:PRK03918 221 EELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYI-KLS 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 326 KRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQE---RLELAEQKLQQTLRKAETLPEVEAELAQRVAALS 402
Cdd:PRK03918 300 EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEElkkKLKELEKRLEELEERHELYEEAKAKKEELERLKK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 403 KSGPLSSGSSaakEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQ---ELQRARQR-----EKMNEEHNKRLSDT 474
Cdd:PRK03918 380 RLTGLTPEKL---EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKaieELKKAKGKcpvcgRELTEEHRKELLEE 456
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568952884 475 VDKLLSESNERlqlhLKERMAALEDKNSLLREVENAKKQLEETQHDKdQLVVTIEALKAELE 536
Cdd:PRK03918 457 YTAELKRIEKE----LKEIEEKERKLRKELRELEKVLKKESELIKLK-ELAEQLKELEEKLK 513
|
|
| SAM_superfamily |
cd09487 |
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
1005-1056 |
1.42e-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: 46.46 E-value: 1.42e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 568952884 1005 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRNSFQCGI 1056
Cdd:cd09487 4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
246-688 |
1.45e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 246 EDLAKVLELQEVID-RQAREQSQMKERLASLSSHAAELEEDLDTARK-DLIKSEEMNTKLQREVREAMAQKEDMEERITT 323
Cdd:PTZ00121 1185 EEVRKAEELRKAEDaRKAEAARKAEEERKAEEARKAEDAKKAEAVKKaEEAKKDAEEAKKAEEERNNEEIRKFEEARMAH 1264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 324 LEKRYLAAQ----REATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQE--RLELAEQKLQQTLRKAETLPEvEAELAQR 397
Cdd:PTZ00121 1265 FARRQAAIKaeeaRKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEakKADEAKKKAEEAKKKADAAKK-KAEEAKK 1343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 398 VAALSKSGPLSSGSSA-----AKEAKLLELTSKLRKAEERHGNIEERLRQMEA-----QLEEKNQELQRARQREKMNEEH 467
Cdd:PTZ00121 1344 AAEAAKAEAEAAADEAeaaeeKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAkkkaeEDKKKADELKKAAAAKKKADEA 1423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 468 NKRLSDT--VDKLLSESNErlqlhlKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAE-----LEQMRL 540
Cdd:PTZ00121 1424 KKKAEEKkkADEAKKKAEE------AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADeakkkAEEAKK 1497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 541 RGPSLHHGRPHLGSVPDFRFSVADGHVDAYSTSAVLRRPQKGRLAalrDEPSKVQTLNEQdwERAQQASVLANVAQAFES 620
Cdd:PTZ00121 1498 KADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKA---EEKKKADELKKA--EELKKAEEKKKAEEAKKA 1572
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 621 dvdvsdgEDDRDTLLSSVDLLSPSGQADAQTLAMMLQEQLDAINKEIRLIQEEKENTEQ--RAEEIESRV 688
Cdd:PTZ00121 1573 -------EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkKAEEEKKKV 1635
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
113-541 |
1.54e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 113 ELKAERNNTRLLLEHLECLVSRHERSLRmtVVKRQAQSPAGVSSEV-EVLKALKSLFEHHKALDEKVR--ERLRVALERC 189
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRLEEEIN--GIEERIKELEEKEERLeELKKKLKELEKRLEELEERHElyEEAKAKKEEL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 190 SLLEEELGATHKELMI--LKEQNNQKKTLTDGLLDGNHEQESAPstngKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQ 267
Cdd:PRK03918 375 ERLKKRLTGLTPEKLEkeLEELEKAKEEIEEEISKITARIGELK----KEIKELKKAIEELKKAKGKCPVCGRELTEEHR 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 268 ---MKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQRE-----VREAMAQKEDMEERITTLEKRYL-AAQREATSV 338
Cdd:PRK03918 451 kelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKEselikLKELAEQLKELEEKLKKYNLEELeKKAEEYEKL 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 339 HDLNDKLENEIAN-KDSMHRQTEDKNR--QLQERLELAEQKLQQTLRKA-----ETLPEVEAELAQRVAALSKSGPLSSG 410
Cdd:PRK03918 531 KEKLIKLKGEIKSlKKELEKLEELKKKlaELEKKLDELEEELAELLKELeelgfESVEELEERLKELEPFYNEYLELKDA 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 411 SS--AAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEehNKRLSDTVDKLLSESnERLQL 488
Cdd:PRK03918 611 EKelEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREE--YLELSRELAGLRAEL-EELEK 687
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 568952884 489 HLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIE---ALKAELEQMRLR 541
Cdd:PRK03918 688 RREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREkvkKYKALLKERALS 743
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
364-536 |
2.26e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.70 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 364 RQLQERLELAEQKLQQTLRKAETlpevEAELAQRVAALsksgplssgssAAKEaKLLELTSKL-RKAEERHGNI---EER 439
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKK----EAEAIKKEALL-----------EAKE-EIHKLRNEFeKELRERRNELqklEKR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 440 LRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLK--ERMAAL---EDKNSLLREVEnakkql 514
Cdd:PRK12704 91 LLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQelERISGLtaeEAKEILLEKVE------ 164
|
170 180
....*....|....*....|..
gi 568952884 515 EETQHDKDQLVVTIEAlKAELE 536
Cdd:PRK12704 165 EEARHEAAVLIKEIEE-EAKEE 185
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
45-455 |
3.28e-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: 51.61 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALpqEFAALTKELnvcreqlleREEEIAELKAERNNTRLL 124
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE--RYQALLKEK---------REYEGYELLKEKEALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 125 LEHLECLVSRHERSLRmtvvKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKvrERLRValercsllEEELGATHKELM 204
Cdd:TIGR02169 239 KEAIERQLASLEEELE----KLTEEISELEKRLEEIEQLLEELNKKIKDLGEE--EQLRV--------KEKIGELEAEIA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 205 ILKEQNNQKKtltdglldgnHEQESApstNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLAslsshaaELEE 284
Cdd:TIGR02169 305 SLERSIAEKE----------RELEDA---EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYA-------ELKE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 285 DLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNR 364
Cdd:TIGR02169 365 ELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKE 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 365 QLQERLELAEQKLQQTlrkAETLPEVEAELAQRVAALSKSgplssgssaakEAKLLELTSKLRKAEERHGNIEERLRQME 444
Cdd:TIGR02169 445 DKALEIKKQEWKLEQL---AADLSKYEQELYDLKEEYDRV-----------EKELSKLQRELAEAEAQARASEERVRGGR 510
|
410
....*....|.
gi 568952884 445 AQLEEKNQELQ 455
Cdd:TIGR02169 511 AVEEVLKASIQ 521
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
303-516 |
3.40e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 303 LQREVREAMAQKEDMEERITTLEKRYLAAQREatsvhdLND-KLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTL 381
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAA------LEEfRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 382 RKAETLPEVEAELAQRVAALSKSGPLSSGSS--AAKEAKLLELTSKLRkaeERHGNIEERLRQMEAQLEEKNQELQRARQ 459
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQSPVIQQLRAqlAELEAELAELSARYT---PNHPDVIALRAQIAALRAQLQQEAQRILA 316
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568952884 460 REKMNEEHNKRLSDTVDKLLSESNERLQlhlkeRMAALEDK-NSLLREVENAKKQLEE 516
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLA-----ELPELEAElRRLEREVEVARELYES 369
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
32-534 |
3.45e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 32 ADSHFEQLMVSMLEER-DRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTA-------LPQEFAALTKELNVCREQ 103
Cdd:COG4913 281 LRLWFAQRRLELLEAElEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrleqLEREIERLERELEERERR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 104 LLEREEEIA-----------ELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSP--AGVSSEVEVLKALKSLFEH 170
Cdd:COG4913 361 RARLEALLAalglplpasaeEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRelRELEAEIASLERRKSNIPA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 171 HkalDEKVRERLRvalERCSLLEEEL---GathkELMILKEQ------------NNQKKTL------------------T 217
Cdd:COG4913 441 R---LLALRDALA---EALGLDEAELpfvG----ELIEVRPEeerwrgaiervlGGFALTLlvppehyaaalrwvnrlhL 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 218 DGLLDGNHEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQareqsqmkerLASLSSHA-AELEEDLDTARKD---- 292
Cdd:COG4913 511 RGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAE----------LGRRFDYVcVDSPEELRRHPRAitra 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 293 -LIKSE----EMNTklQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIankdsmhrqtedknRQLQ 367
Cdd:COG4913 581 gQVKGNgtrhEKDD--RRRIRSRYVLGFDNRAKLAALEAELAELEEELAEAEERLEALEAEL--------------DALQ 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 368 ERLElAEQKLQQTLRKAETLPEVEAELAQRVAALSKsgpLSSGSSaakeaKLLELTSKLRKAEERHGNIEERLRQMEAQL 447
Cdd:COG4913 645 ERRE-ALQRLAEYSWDEIDVASAEREIAELEAELER---LDASSD-----DLAALEEQLEELEAELEELEEELDELKGEI 715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 448 EEKNQELQRARQREkmneehnKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVT 527
Cdd:COG4913 716 GRLEKELEQAEEEL-------DELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEE 788
|
....*..
gi 568952884 528 IEALKAE 534
Cdd:COG4913 789 LERAMRA 795
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
416-539 |
3.48e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 416 EAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQR-EKMNEEHNKRLSD---------TVDKLL-SESNE 484
Cdd:COG3883 36 QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEiEERREELGERARAlyrsggsvsYLDVLLgSESFS 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 568952884 485 RL--QLHLKERMAalEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMR 539
Cdd:COG3883 116 DFldRLSALSKIA--DADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
37-477 |
3.63e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 37 EQLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELnvcreqllEREEEIAELKA 116
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA--------LLEAALAELLE 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 117 ERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKslfehhKALDEKVRERLRVALERCSLLEEEL 196
Cdd:COG1196 485 ELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVE------AAYEAALEAALAAALQNIVVEDDEV 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 197 GATHKELmiLKEQNNQKKTLTDGLLDGNHEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASLS 276
Cdd:COG1196 559 AAAAIEY--LKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAAL 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 277 SHAAELEEDLdtarkdLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMH 356
Cdd:COG1196 637 RRAVTLAGRL------REVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA 710
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 357 RQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSGPlssgssaaKEAKLLELTSKLRKAEERHGNI 436
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP--------DLEELERELERLEREIEALGPV 782
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 568952884 437 -----------EERLRQMEAQLEeknqELQRARQR-----EKMNEEHNKRLSDTVDK 477
Cdd:COG1196 783 nllaieeyeelEERYDFLSEQRE----DLEEARETleeaiEEIDRETRERFLETFDA 835
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
334-541 |
3.78e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 334 EATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQ--ERLELAEQKLQQTLRKAETLPEVEAEL-----AQRVAALSKSGP 406
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALrlwfaQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 407 LSSGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQM----EAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSES 482
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 483 NERLQLHLKERMAALEDKNSLLREVEN----AKKQLEETQHDKDQLVVTIEALK-------AELEQMRLR 541
Cdd:COG4913 379 AEEFAALRAEAAALLEALEEELEALEEalaeAEAALRDLRRELRELEAEIASLErrksnipARLLALRDA 448
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
46-537 |
3.93e-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: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 46 ERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNtalpqefaALTKELNVCREQLLEREEEIAELKAERNNTRLLL 125
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQ--------ELEEKLEELRLEVSELEEEIEELQKELYALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 126 EHLECLVSRH---ERSLRMTVVKRQAQSPAGVSSEVEVLKALK-------SLFEHHKALDEKV---RERLRVALERCSLL 192
Cdd:TIGR02168 298 SRLEQQKQILrerLANLERQLEELEAQLEELESKLDELAEELAeleekleELKEELESLEAELeelEAELEELESRLEEL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 193 EEELGATHKELMILKEQ----NNQKKTLTDGLLDGNHEQESAPSTNGKRSSDGSLS--HEDLAKVLELQEVIDRQAREQS 266
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQiaslNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAelKELQAELEELEEELEELQEELE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 267 QMKERLASLSSHAAELEEDLDTARKDLIKS----------EEMNTKLQREVREAMAQKEDME-------ERITTLEK--- 326
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLqarldslerlQENLEGFSEGVKALLKNQSGLSgilgvlsELISVDEGyea 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 327 ---RYLAAQREATSVHDLNDKLE-----------------------NEIANKDSMHRQTEDKNRQLQERLELAEQKLQ-- 378
Cdd:TIGR02168 538 aieAALGGRLQAVVVENLNAAKKaiaflkqnelgrvtflpldsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRka 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 379 -----QTLRKAETLP---EVEAELAQRVAALSKSGPL------SSGSSAAKEAKLLELTSKLRkaeerhgNIEERLRQME 444
Cdd:TIGR02168 618 lsyllGGVLVVDDLDnalELAKKLRPGYRIVTLDGDLvrpggvITGGSAKTNSSILERRREIE-------ELEEKIEELE 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 445 AQLEEKNQELQRAR-QREKMNEEHNK--RLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQHDK 521
Cdd:TIGR02168 691 EKIAELEKALAELRkELEELEEELEQlrKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
|
570
....*....|....*.
gi 568952884 522 DQLVVTIEALKAELEQ 537
Cdd:TIGR02168 771 EEAEEELAEAEAEIEE 786
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
236-534 |
4.16e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 4.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 236 KRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKE 315
Cdd:PTZ00121 1230 KKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKK 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 316 DMEE--RITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEV--- 390
Cdd:PTZ00121 1310 KAEEakKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKaee 1389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 391 --EAELAQRVAALSKSGPLSSGSSAAKEAKLLELTSK---LRKAEERHGNIEERLRQMEAQleEKNQELQRARQREKMNE 465
Cdd:PTZ00121 1390 kkKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKaeeKKKADEAKKKAEEAKKADEAK--KKAEEAKKAEEAKKKAE 1467
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568952884 466 EhnKRLSDTVDKLLSESneRLQLHLKERMAALEDKNSLLREVENAKKQLEETQHDK-----DQLVVTIEALKAE 534
Cdd:PTZ00121 1468 E--AKKADEAKKKAEEA--KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEeakkaDEAKKAEEAKKAD 1537
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
232-466 |
5.26e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.29 E-value: 5.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 232 STNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAM 311
Cdd:COG4372 14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 312 AQKEDMEERITTLEKRYLAAQREAtsvhdlnDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVE 391
Cdd:COG4372 94 AELAQAQEELESLQEEAEELQEEL-------EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568952884 392 AELAQRVAALSKSGPLSSGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEE 466
Cdd:COG4372 167 AALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA 241
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
421-685 |
6.04e-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: 50.84 E-value: 6.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 421 ELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQR-ARQREKMNEehnkrlsdtVDKLLSESNE-RLQLHLKERMAALE 498
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERlRREREKAER---------YQALLKEKREyEGYELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 499 DKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRGPSLHHGRphlgsVPDFRFSVADGHVD---AYSTSAV 575
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEE-----QLRVKEKIGELEAEiasLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 576 LRRPQK---GRLAALRDEPSKVQ-TLNEQDWERAQQASVLANVAQAFESDvdvsdgEDDRDTLLSSVDLLSPSGQA---- 647
Cdd:TIGR02169 313 KERELEdaeERLAKLEAEIDKLLaEIEELEREIEEERKRRDKLTEEYAEL------KEELEDLRAELEEVDKEFAEtrde 386
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 568952884 648 --DAQTLAMMLQEQLDAINKEIRLIQEEKENTEQRAEEIE 685
Cdd:TIGR02169 387 lkDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN 426
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
44-539 |
7.16e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 7.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 44 LEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTaLPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRL 123
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEE-LEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRD 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 124 LLEhleclvsrhERSLRMTVVKRQAQSPAGVSSEVEvlKALKSLFEHHKALD---EKVRERLRVALERCSLLEEELGATH 200
Cdd:PRK02224 329 RLE---------ECRVAAQAHNEEAESLREDADDLE--ERAEELREEAAELEselEEAREAVEDRREEIEELEEEIEELR 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 201 KELMILKEQNNQKKTLTDGLLDgnhEQESAPSTNGKRSSDGSLSHEDLAKVLELQEviDRQAREQSQMKERlaslSSHAA 280
Cdd:PRK02224 398 ERFGDAPVDLGNAEDFLEELRE---ERDELREREAELEATLRTARERVEEAEALLE--AGKCPECGQPVEG----SPHVE 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 281 ELEEDldtarkdliksEEMNTKLQREVREAMAQKEDMEERITTLEKrYLAAQREATSVHDLNDKLENEIANKDSMHRQTE 360
Cdd:PRK02224 469 TIEED-----------RERVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIERLEERREDLEELIAERRETIEEKR 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 361 DKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALsksgplssgssaakEAKLLELTSKLrkaeERHGNIEERL 440
Cdd:PRK02224 537 ERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAEL--------------NSKLAELKERI----ESLERIRTLL 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 441 rqmeAQLEEKNQELQRARQREK----MNEEHNKRLS---DTVDKLLSESNE-RLQlhlkermAALEDKNSLLREVENAKK 512
Cdd:PRK02224 599 ----AAIADAEDEIERLREKREalaeLNDERRERLAekrERKRELEAEFDEaRIE-------EAREDKERAEEYLEQVEE 667
|
490 500
....*....|....*....|....*..
gi 568952884 513 QLEETQHDKDQLVVTIEALKAELEQMR 539
Cdd:PRK02224 668 KLDELREERDDLQAEIGAVENELEELE 694
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
417-537 |
8.89e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 8.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 417 AKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEhnkrlsdtvdKLLSESNER----LQL---H 489
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE----------QLGNVRNNKeyeaLQKeieS 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 568952884 490 LKERMAALEDK-NSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQ 537
Cdd:COG1579 101 LKRRISDLEDEiLELMERIEELEEELAELEAELAELEAELEEKKAELDE 149
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
258-456 |
1.17e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 258 IDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATS 337
Cdd:COG4913 666 AEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 338 VH--DLNDKLENEIANK--DSMHRQTEDKNRQLQERLELAEQKLQQTLRK---------------AETLPEVEAELAQrv 398
Cdd:COG4913 746 ELraLLEERFAAALGDAveRELRENLEERIDALRARLNRAEEELERAMRAfnrewpaetadldadLESLPEYLALLDR-- 823
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568952884 399 aaLSKSGpLssgssAAKEAKLLELtskLRKAEER-----HGNIEERLRQMEAQLEEKNQELQR 456
Cdd:COG4913 824 --LEEDG-L-----PEYEERFKEL---LNENSIEfvadlLSKLRRAIREIKERIDPLNDSLKR 875
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
156-488 |
1.19e-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: 49.74 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 156 SEVEVLKALKSLFEHHKALDEKVR---------ERLRVA-------LERCSLLEEELGATHKEL----MILKEQNNQKkt 215
Cdd:pfam17380 266 TENEFLNQLLHIVQHQKAVSERQQqekfekmeqERLRQEkeekareVERRRKLEEAEKARQAEMdrqaAIYAEQERMA-- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 216 ltdglLDGNHEQESAPSTNGKRSSDgSLSHEDLAKVLELQEVIDRQAREQSQMKERLaslsshaaelEEDLDTARKDLIK 295
Cdd:pfam17380 344 -----MERERELERIRQEERKRELE-RIRQEEIAMEISRMRELERLQMERQQKNERV----------RQELEAARKVKIL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 296 SEEMNTKLQREVREaMAQKEDMEERITTLEKRYLAAQREatsvHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQ 375
Cdd:pfam17380 408 EEERQRKIQQQKVE-MEQIRAEQEEARQREVRRLEEERA----REMERVRLEEQERQQQVERLRQQEEERKRKKLELEKE 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 376 KLQQTLRKAETLPEVEAELAQRVAALSKSgplsSGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQ 455
Cdd:pfam17380 483 KRDRKRAEEQRRKILEKELEERKQAMIEE----ERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQM 558
|
330 340 350
....*....|....*....|....*....|...
gi 568952884 456 RARQREKMNEEHNKRLSDTVDKLLSESNERLQL 488
Cdd:pfam17380 559 RKATEERSRLEAMEREREMMRQIVESEKARAEY 591
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
256-506 |
1.33e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 256 EVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREA 335
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 336 TSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKlqqtlRKAETLPEVEAELAQRVAALSKSgplssgssaAK 415
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEK-----KKAEELKKAEEENKIKAEEAKKE---------AE 1740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 416 EAKlleltsklRKAEErhgnieerLRQMEaqlEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMA 495
Cdd:PTZ00121 1741 EDK--------KKAEE--------AKKDE---EEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIK 1801
|
250
....*....|.
gi 568952884 496 ALEDKNSLLRE 506
Cdd:PTZ00121 1802 DIFDNFANIIE 1812
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
245-540 |
1.33e-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: 49.12 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 245 HEDL-AKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITT 323
Cdd:pfam07888 96 HEELeEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQ 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 324 LEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQK---LQQTLRKAETLPEVEAELAQRVAA 400
Cdd:pfam07888 176 LQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKeaeNEALLEELRSLQERLNASERKVEG 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 401 LskSGPLSSGSSAAKEAKlleltSKLRKAEERHGNIEERLRQMEAQLEEKN----QELQRARQREKMNEEHNKRLSDTVD 476
Cdd:pfam07888 256 L--GEELSSMAAQRDRTQ-----AELHQARLQAAQLTLQLADASLALREGRarwaQERETLQQSAEADKDRIEKLSAELQ 328
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568952884 477 KLlsesNERLQlhlKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRL 540
Cdd:pfam07888 329 RL----EERLQ---EERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQA 385
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
246-537 |
1.85e-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: 48.92 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 246 EDLAK-VLELQEVID---RQAREQSQMKERLASL---SSHAAELEEDLDTARKDLiksEEMNtKLQREVR-------EAM 311
Cdd:pfam05622 90 EELEKeVLELQHRNEeltSLAEEAQALKDEMDILresSDKVKKLEATVETYKKKL---EDLG-DLRRQVKlleernaEYM 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 312 AQKEDMEERIttleKRY--LAAQREATS--VHDLNDKLENEIANKDsmhrQTEDKNRQLQERLELAEQKLQQTLRKAETL 387
Cdd:pfam05622 166 QRTLQLEEEL----KKAnaLRGQLETYKrqVQELHGKLSEESKKAD----KLEFEYKKLEEKLEALQKEKERLIIERDTL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 388 PE----------VEAELAQRVAALSKSGPlsSGSSAAKEAKLLELTSKLRK--------AEERHGNIEERLRQMEAQLEE 449
Cdd:pfam05622 238 REtneelrcaqlQQAELSQADALLSPSSD--PGDNLAAEIMPAEIREKLIRlqhenkmlRLGQEGSYRERLTELQQLLED 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 450 KNQELQRARQREKMNeehNKRLSdtvdkLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIE 529
Cdd:pfam05622 316 ANRRKNELETQNRLA---NQRIL-----ELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIE 387
|
....*...
gi 568952884 530 ALKAELEQ 537
Cdd:pfam05622 388 ELEPKQDS 395
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
295-537 |
2.38e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 295 KSEEMNTKLQREVREAMAQKED---MEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKnRQLQERLE 371
Cdd:PTZ00121 1105 KTETGKAEEARKAEEAKKKAEDarkAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDA-KKAEAARK 1183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 372 LAEQKLQQTLRKAETLPEVEA----------------ELAQRVAALSKSGPLSSGSSAAKEAKLLELTSKLRKAEE-RHG 434
Cdd:PTZ00121 1184 AEEVRKAEELRKAEDARKAEAarkaeeerkaeearkaEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEaRMA 1263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 435 NIEERLRQMEAQLEEKNQELQRARQREKMNEehnKRLSDTVDKLlsesnERLQLHLKERMAALEDKnsllREVENAKKQL 514
Cdd:PTZ00121 1264 HFARRQAAIKAEEARKADELKKAEEKKKADE---AKKAEEKKKA-----DEAKKKAEEAKKADEAK----KKAEEAKKKA 1331
|
250 260
....*....|....*....|...
gi 568952884 515 EETQHDKDQLVVTIEALKAELEQ 537
Cdd:PTZ00121 1332 DAAKKKAEEAKKAAEAAKAEAEA 1354
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
253-538 |
2.53e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.63 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 253 ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREamaqkedmeerittLEKRYLAAQ 332
Cdd:pfam01576 360 ELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQE--------------LQARLSESE 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 333 REATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTlrkAETLPEveaELAQRvaalsksgplssgss 412
Cdd:pfam01576 426 RQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDT---QELLQE---ETRQK--------------- 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 413 aakeaklLELTSKLRKAEERHGNIEErlrqmeaQLEEknqELQRARQREKMNEEHNKRLSDTvDKLLSESNERLQlhlke 492
Cdd:pfam01576 485 -------LNLSTRLRQLEDERNSLQE-------QLEE---EEEAKRNVERQLSTLQAQLSDM-KKKLEEDAGTLE----- 541
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 568952884 493 rmAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQM 538
Cdd:pfam01576 542 --ALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDL 585
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
113-549 |
2.71e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.63 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 113 ELKAERNNTRLLLEH-LECLVSRHERSLRmTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKvrERLRVALERCSL 191
Cdd:pfam01576 320 ELRSKREQEVTELKKaLEEETRSHEAQLQ-EMRQKHTQALEELTEQLEQAKRNKANLEKAKQALES--ENAELQAELRTL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 192 LEEELGATHK---------ELMI-LKEQNNQKKTLTDGLLDGNHEQESAPSTNGKRSSDGSLSHEDLAKV-LELQeviDR 260
Cdd:pfam01576 397 QQAKQDSEHKrkklegqlqELQArLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLeSQLQ---DT 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 261 QAREQSQMKERLaSLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQ----KEDMEERITTLEKRYLAAQREAT 336
Cdd:pfam01576 474 QELLQEETRQKL-NLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQlsdmKKKLEEDAGTLEALEEGKKRLQR 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 337 SVHDLNDKLENEIANKDSMHRQTE-------------DKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSK 403
Cdd:pfam01576 553 ELEALTQQLEEKAAAYDKLEKTKNrlqqelddllvdlDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAR 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 404 SgplssgssaaKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEE---------KN-QELQRA-RQREKMNEEHNKRLS 472
Cdd:pfam01576 633 E----------KETRALSLARALEEALEAKEELERTNKQLRAEMEDlvsskddvgKNvHELERSkRALEQQVEEMKTQLE 702
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 473 DTVDKLLSESNERLQLHLKerMAAL----------------EDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELE 536
Cdd:pfam01576 703 ELEDELQATEDAKLRLEVN--MQALkaqferdlqardeqgeEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLK 780
|
490
....*....|...
gi 568952884 537 QMRLRGPSLHHGR 549
Cdd:pfam01576 781 ELEAQIDAANKGR 793
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
250-538 |
3.17e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.18 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 250 KVLELQevidRQAREQSQMKERLASLsshaaELEEDLDTaRKDLIKSEEMNTKLQREVREAMAqkedmeeRITTLEKRYL 329
Cdd:pfam05483 113 KIIEAQ----RKAIQELQFENEKVSL-----KLEEEIQE-NKDLIKENNATRHLCNLLKETCA-------RSAEKTKKYE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 330 AAQREATSVH-DLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQtlrkaetlpeVEAELAQRVAALSKSGPLS 408
Cdd:pfam05483 176 YEREETRQVYmDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQH----------LEEEYKKEINDKEKQVSLL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 409 SGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQE--------------LQRARQREKMNEEHNKRLSDT 474
Cdd:pfam05483 246 LIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKkdhltkeledikmsLQRSMSTQKALEEDLQIATKT 325
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952884 475 VDKLLSESNERLQLHLKERMA----ALEDKNSLLREVENAKKQLEETQHDKDQL-VVTIEALK--AELEQM 538
Cdd:pfam05483 326 ICQLTEEKEAQMEELNKAKAAhsfvVTEFEATTCSLEELLRTEQQRLEKNEDQLkIITMELQKksSELEEM 396
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
343-533 |
3.27e-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: 46.60 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 343 DKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAEtlPEVEAELAQRVAALSKSgplssgsSAAKEAKLLEL 422
Cdd:pfam04012 39 VKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGN--EELAREALAEKKSLEKQ-------AEALETQLAQQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 423 TSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEehnkrlsdTVDKLLSESNERLQLHLKERMAALEDKNS 502
Cdd:pfam04012 110 RSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAAKAQEAVQT--------SLGSLSTSSATDSFERIEEKIEEREARAD 181
|
170 180 190
....*....|....*....|....*....|....
gi 568952884 503 LLREVENA---KKQLEETQHDKDQLVVTIEALKA 533
Cdd:pfam04012 182 AAAELASAvdlDAKLEQAGIQMEVSEDVLARLKA 215
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
422-541 |
3.81e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 46.36 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 422 LTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLlsesNERLQLHLK---ERMA--A 496
Cdd:COG1842 14 INALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKW----EEKARLALEkgrEDLAreA 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 568952884 497 LEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLR 541
Cdd:COG1842 90 LERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAK 134
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
224-523 |
4.08e-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: 47.11 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 224 NHEQESAPSTNGKRSSDGSL------SHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSE 297
Cdd:pfam15905 42 NNSKDASTPATARKVKSLELkkksqkNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 298 EMNTKLQREVREAMAQKEDMEERI--TTLEKRYLAAQREATsvhdlndKLENEIANKDsmhRQTEDKNRQLQERLELAEQ 375
Cdd:pfam15905 122 ASVASLEKQLLELTRVNELLKAKFseDGTQKKMSSLSMELM-------KLRNKLEAKM---KEVMAKQEGMEGKLQVTQK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 376 KLQQTlrkaetlpevEAELAQRVAALSKSGPLSSGSSAAKEaKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQ 455
Cdd:pfam15905 192 NLEHS----------KGKVAQLEEKLVSTEKEKIEEKSETE-KLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIE 260
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568952884 456 RARQREKMNEEHNKRLSDTVD---KLLSESNERLQLHLKERmaaledKNSLLREVENAKKQL--EETQHDKDQ 523
Cdd:pfam15905 261 SLKQSLEEKEQELSKQIKDLNekcKLLESEKEELLREYEEK------EQTLNAELEELKEKLtlEEQEHQKLQ 327
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
129-536 |
4.26e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.58 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 129 ECLVSRHErslrmtVVKRQAQSPAGVSSEVEVLKALKSLFEH-HKALDEKVrERLRVALERCSLLEEELGATHKELMILK 207
Cdd:pfam07888 38 ECLQERAE------LLQAQEAANRQREKEKERYKRDREQWERqRRELESRV-AELKEELRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 208 EQNNQKKtltDGLLDGNHEQESAPSTNGKRSSdgSLSHEDLAKVLELQEVIDRQAREQSQMKERlaslsshaaeleedlD 287
Cdd:pfam07888 111 EELSEEK---DALLAQRAAHEARIRELEEDIK--TLTQRVLERETELERMKERAKKAGAQRKEE---------------E 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 288 TARKDLikseemNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLeNEIANKDSMHRQTEDKNRQLQ 367
Cdd:pfam07888 171 AERKQL------QAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKL-TTAHRKEAENEALLEELRSLQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 368 ERLELAEQK---LQQTLRKAETLPE-VEAELAQ-RVAALSKSGPLSSGSSAAKEAK---LLELTSKLRKAEERHgnieER 439
Cdd:pfam07888 244 ERLNASERKvegLGEELSSMAAQRDrTQAELHQaRLQAAQLTLQLADASLALREGRarwAQERETLQQSAEADK----DR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 440 LRQMEAQLEEKNQELQRAR-QREKMNEEHNkRLSDTVDKLLSESNERLQlhlkermaalEDKNSLlrevENAKKQLEETQ 518
Cdd:pfam07888 320 IEKLSAELQRLEERLQEERmEREKLEVELG-REKDCNRVQLSESRRELQ----------ELKASL----RVAQKEKEQLQ 384
|
410
....*....|....*...
gi 568952884 519 HDKDQLVVTIEALKAELE 536
Cdd:pfam07888 385 AEKQELLEYIRQLEQRLE 402
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
1083-1153 |
4.56e-05 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 42.64 E-value: 4.56e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952884 1083 VLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFsalalLLQIPTQNTQARAVLEREFNNLL 1153
Cdd:pfam07647 1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLRLTLED-----LKRLGITSVGHRRKILKKIQELK 66
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
162-518 |
4.58e-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: 47.71 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 162 KALKSLFEHHKALDEKVRERLRValercslLEEELGATHKELMILKEQNN-QKKTLTDglldgnheqesapstngkrssd 240
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKK-------LQQEKELLEKEIERLKETIIkNNSEIKD---------------------- 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 241 gsLSHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEE---DLDTARKDLIKSEEMNTKLQREVREAMAQKEDM 317
Cdd:TIGR04523 445 --LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQkqkELKSKEKELKKLNEEKKELEEKVKDLTKKISSL 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 318 EERITTLEKRYLAAQREatsVHDLNDKLENEIANKDSmhRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQR 397
Cdd:TIGR04523 523 KEKIEKLESEKKEKESK---ISDLEDELNKDDFELKK--ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKE 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 398 VAALSKSgplssgsSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQ-----REKMNE--EHNKR 470
Cdd:TIGR04523 598 KKDLIKE-------IEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKEtikeiRNKWPEiiKKIKE 670
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 568952884 471 LSDTVD---KLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQ 518
Cdd:TIGR04523 671 SKTKIDdiiELMKDWLKELSLHYKKYITRMIRIKDLPKLEEKYKEIEKELK 721
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
253-383 |
4.61e-05 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 45.66 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 253 ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREA-MAQKEDMEERITTLEKRYLAA 331
Cdd:pfam15619 57 ELPQLIARHNEEVRVLRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKnLAEREELQKKLEQLEAKLEDK 136
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 568952884 332 QREatsVHDLNDKLEN-------EIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRK 383
Cdd:pfam15619 137 DEK---IQDLERKLELenksfrrQLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKERE 192
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
193-539 |
4.90e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.86 E-value: 4.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 193 EEELGATHKELMILKEQNNQ-KKTLTDglLDGNHEQESAPST--NGKRSSDGSLSHED-------LAKVLELQEVIDRQA 262
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKaESELKE--LEKKHQQLCEEKNalQEQLQAETELCAEAeemrarlAARKQELEEILHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 263 REQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLN 342
Cdd:pfam01576 82 SRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 343 DKLENEIANKDSMHRQ-TEDKNRQ------LQERLElAEQKLQQTLRKAETLPEVEA-ELAQRVAALSKSGPLSSGSSAA 414
Cdd:pfam01576 162 SEFTSNLAEEEEKAKSlSKLKNKHeamisdLEERLK-KEEKGRQELEKAKRKLEGEStDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 415 KEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSEsnerLQLHLKERM 494
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTE----LEDTLDTTA 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 568952884 495 AALEDKNSLLREVENAKKQLEETQHDKDQLVV--------TIEALKAELEQMR 539
Cdd:pfam01576 317 AQQELRSKREQEVTELKKALEEETRSHEAQLQemrqkhtqALEELTEQLEQAK 369
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
360-559 |
4.96e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 360 EDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSGPLSSGS--SAAKEAKLLELTSKLRKAEERHG--- 434
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEidVASAEREIAELEAELERLDASSDdla 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 435 NIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQL 514
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELR 768
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568952884 515 EETQHDKDQLVVTIEALKAELEQMRLR-----GPSLHHGRPHLGSVPDFR 559
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERAMRAfnrewPAETADLDADLESLPEYL 818
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
314-539 |
7.01e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.21 E-value: 7.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 314 KEDMEERITTLEKRYLAAQREATSVHDLNDKLEnEIANKDsmhrQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEA- 392
Cdd:PRK11281 38 EADVQAQLDALNKQKLLEAEDKLVQQDLEQTLA-LLDKID----RQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDe 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 393 ELAQRVAALSksgplssgssaakeaklleltsklrkaeerhgnieerLRQMEAQLEEKNQELQRARqrekmneehnKRLS 472
Cdd:PRK11281 113 ETRETLSTLS-------------------------------------LRQLESRLAQTLDQLQNAQ----------NDLA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568952884 473 DTVDKLLSESN--ERLQLHLKERMAALEDKNSLLREVENAKKQLEETQhdKDQLVVTIEALKAELEQMR 539
Cdd:PRK11281 146 EYNSQLVSLQTqpERAQAALYANSQRLQQIRNLLKGGKVGGKALRPSQ--RVLLQAEQALLNAQNDLQR 212
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
365-539 |
8.79e-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: 45.30 E-value: 8.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 365 QLQERLELAE--QKLQQTLRKAETLPEVEAELAQRVAALSKSgplssgsSAAKEAKLLELTSKLRKAEERHGNIEERLRQ 442
Cdd:COG1579 5 DLRALLDLQEldSELDRLEHRLKELPAELAELEDELAALEAR-------LEAAKTELEDLEKEIKRLELEIEEVEARIKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 443 MEAQLEE-KNQELQRARQREKmnEEHNKRLSDTVDKLLsESNERLQlHLKERMAALEDknsllrEVENAKKQLEETQHDK 521
Cdd:COG1579 78 YEEQLGNvRNNKEYEALQKEI--ESLKRRISDLEDEIL-ELMERIE-ELEEELAELEA------ELAELEAELEEKKAEL 147
|
170
....*....|....*...
gi 568952884 522 DQLVVTIEALKAELEQMR 539
Cdd:COG1579 148 DEELAELEAELEELEAER 165
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
44-449 |
1.02e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 44 LEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRL 123
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 124 LLEHLECLVSRHERSLRmtvVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKEL 203
Cdd:COG4717 228 ELEQLENELEAAALEER---LKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 204 MILKEQNNQKKTltdglldgnhEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLAsLSSHAAELE 283
Cdd:COG4717 305 EELQALPALEEL----------EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ-LEELEQEIA 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 284 EDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSvhdlnDKLENEIANKDSMHRQTEDKN 363
Cdd:COG4717 374 ALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE-----EELEEELEELEEELEELEEEL 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 364 RQLQERLELAEQKLQQtLRKAETLPEVEAELAQRVAALsksgplssgSSAAKEAKLLELTSK-LRKAEERHgnIEERLRQ 442
Cdd:COG4717 449 EELREELAELEAELEQ-LEEDGELAELLQELEELKAEL---------RELAEEWAALKLALElLEEAREEY--REERLPP 516
|
....*..
gi 568952884 443 MEAQLEE 449
Cdd:COG4717 517 VLERASE 523
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
244-539 |
1.04e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.89 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 244 SHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELE---EDLDTARKDL-------------IKSEEMNTKLQ--- 304
Cdd:TIGR00618 241 SHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEetqERINRARKAAplaahikavtqieQQAQRIHTELQskm 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 305 REVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKN--RQLQERLELAEQKLQQTLR 382
Cdd:TIGR00618 321 RSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQhiHTLQQQKTTLTQKLQSLCK 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 383 KAETLPEVEAE----------LAQRVAALSKSGPLSSGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQ 452
Cdd:TIGR00618 401 ELDILQREQATidtrtsafrdLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQ 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 453 ELQRARQREKMNEEHNKRLSDT---------------VDKLLSESNERLQLHLKERMAALEDK--------NSLLREVEN 509
Cdd:TIGR00618 481 IHLQETRKKAVVLARLLELQEEpcplcgscihpnparQDIDNPGPLTRRMQRGEQTYAQLETSeedvyhqlTSERKQRAS 560
|
330 340 350
....*....|....*....|....*....|
gi 568952884 510 AKKQLEETQHDKDQLVVTIEALKAELEQMR 539
Cdd:TIGR00618 561 LKEQMQEIQQSFSILTQCDNRSKEDIPNLQ 590
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
343-499 |
1.08e-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: 45.30 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 343 DKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAEtlpEVEAELAQRVAALSKSGPLSSGSSAAKEAKllEL 422
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIK---RLELEIEEVEARIKKYEEQLGNVRNNKEYE--AL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568952884 423 TSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALED 499
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
320-541 |
1.60e-04 |
|
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: 44.60 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 320 RITTLEKRYLAAQREATSVHDLNDKLENeIANKDSmhrqTEDKNRQLQERLELAEQKLQQtLRKaetlpEVEAELAQRVA 399
Cdd:pfam12795 1 KLDELEKAKLDEAAKKKLLQDLQQALSL-LDKIDA----SKQRAAAYQKALDDAPAELRE-LRQ-----ELAALQAKAEA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 400 ALSKSgpLSSGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTvDKLL 479
Cdd:pfam12795 70 APKEI--LASLSLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPP-GEPL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 480 SESnerLQLHLKERMAALEDKNSLLR-EVENA-------KKQLEETQHDKDQLVVTIEALKAELEQMRLR 541
Cdd:pfam12795 147 SEA---QRWALQAELAALKAQIDMLEqELLSNnnrqdllKARRDLLTLRIQRLEQQLQALQELLNEKRLQ 213
|
|
| SAM_STIM-1,2-like |
cd09504 |
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ... |
912-970 |
1.90e-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: 41.16 E-value: 1.90e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568952884 912 WDGPTVVVWLELWVGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNPLHRLKLRL 970
Cdd:cd09504 5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
1005-1060 |
1.99e-04 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 40.72 E-value: 1.99e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 568952884 1005 EWLPSLGLPQYRSYFMECLVD-ARMLDHLTKKDLrGQLKMVDSFHRNSFQCGIMCLR 1060
Cdd:pfam07647 11 DWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDL-KRLGITSVGHRRKILKKIQELK 66
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
298-541 |
2.22e-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: 45.48 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 298 EMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATsvhdlndKLENEIANKDSMHRQTEDKNRQLQERLELAEQKL 377
Cdd:pfam05483 212 EMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQIT-------EKENKMKDLTFLLEESRDKANQLEEKTKLQDENL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 378 QQTLRK----AETLPEVEAELAQRVA---ALSKSGPLSSGS----SAAKEAKLLELTsklrKAEERHGNIEERLRQMEAQ 446
Cdd:pfam05483 285 KELIEKkdhlTKELEDIKMSLQRSMStqkALEEDLQIATKTicqlTEEKEAQMEELN----KAKAAHSFVVTEFEATTCS 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 447 LEEKnqeLQRARQREKMNEEHNKRLSDTVDKLLSESNERLQL------HLKERMAALEDKNSLLREVENAKKQLEETQHD 520
Cdd:pfam05483 361 LEEL---LRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFknnkevELEELKKILAEDEKLLDEKKQFEKIAEELKGK 437
|
250 260
....*....|....*....|.
gi 568952884 521 KDQLVVTIEALKAELEQMRLR 541
Cdd:pfam05483 438 EQELIFLLQAREKEIHDLEIQ 458
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
206-683 |
2.29e-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: 45.48 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 206 LKEQNNQKKTLTDGLLDGNHEQESAPSTNGKRSSDGSLSHEDLAKVLELQEV-IDRQAREQSQMKERLASLSSHAAELEE 284
Cdd:pfam05483 284 LKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAqMEELNKAKAAHSFVVTEFEATTCSLEE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 285 DLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLE------KRYLAAQREATSVHDLNDKLENEIANKDS---- 354
Cdd:pfam05483 364 LLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEveleelKKILAEDEKLLDEKKQFEKIAEELKGKEQelif 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 355 MHRQTEDKNRQLQERLELAEQKLQQTLRKAETLP-EVEAELAQRVAALSKSGPLS-SGSSAAKEAKllELTSKLRKAEER 432
Cdd:pfam05483 444 LLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKtELEKEKLKNIELTAHCDKLLlENKELTQEAS--DMTLELKKHQED 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 433 HGNIEERLRQMEAQLEE-KNQELQRARQREKMNEEHnKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAK 511
Cdd:pfam05483 522 IINCKKQEERMLKQIENlEEKEMNLRDELESVREEF-IQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLK 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 512 KQLEETQHDKDQLVVTIEALK----AELEQMRLRGPSLHHGRPHLGSVPDFRFSVADGH-----VDAYSTSAVLRRPQKG 582
Cdd:pfam05483 601 KQIENKNKNIEELHQENKALKkkgsAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYqkeieDKKISEEKLLEEVEKA 680
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 583 RLAAlrDEPSKVQtlNEQDWERAQQASVLANVAQAFESDVD-VSDGEDDRDTLLSSVDLLSPSGQADAQTLAMMLQEQLD 661
Cdd:pfam05483 681 KAIA--DEAVKLQ--KEIDKRCQHKIAEMVALMEKHKHQYDkIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELL 756
|
490 500
....*....|....*....|..
gi 568952884 662 AINKEIRLIQEEKENTEQRAEE 683
Cdd:pfam05483 757 SLKKQLEIEKEEKEKLKMEAKE 778
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
251-508 |
3.86e-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: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 251 VLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNT---------------------KLQREVRE 309
Cdd:pfam01576 140 ILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISdleerlkkeekgrqelekakrKLEGESTD 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 310 AMAQKEDMEERITTL-------EKRYLAAQ-----------------REATS-VHDLNDKLENEIAnkdsMHRQTEDKNR 364
Cdd:pfam01576 220 LQEQIAELQAQIAELraqlakkEEELQAALarleeetaqknnalkkiRELEAqISELQEDLESERA----ARNKAEKQRR 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 365 QLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSGPLSSGSSAAK--------EAKLLELTSKLRKAEERHGNI 436
Cdd:pfam01576 296 DLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQlqemrqkhTQALEELTEQLEQAKRNKANL 375
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568952884 437 EERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESN--ERLQLHLKERMAA----LEDKNSLLREVE 508
Cdd:pfam01576 376 EKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSesERQRAELAEKLSKlqseLESVSSLLNEAE 453
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
296-536 |
4.45e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 296 SEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQ 375
Cdd:COG4372 1 GDRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 376 KLQQTLRKAETLPEVEAELAQRVAALSKsgplssgSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQ 455
Cdd:COG4372 81 ELEELNEQLQAAQAELAQAQEELESLQE-------EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 456 RARQREKMNEEHNKRLSDTVDKL-LSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAE 534
Cdd:COG4372 154 ELEEQLESLQEELAALEQELQALsEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233
|
..
gi 568952884 535 LE 536
Cdd:COG4372 234 AL 235
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
253-460 |
6.39e-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: 43.60 E-value: 6.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 253 ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRY---- 328
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELaell 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 329 ---------------------LAAQREATSVHDLNDKLENEIankdsmhRQTEDKNRQLQERLELAEQKLQQtlrkaetL 387
Cdd:COG4942 111 ralyrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQA-------EELRADLAELAALRAELEAERAE-------L 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568952884 388 PEVEAELAQRVAALSKsgplssgSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQR 460
Cdd:COG4942 177 EALLAELEEERAALEA-------LKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
179-543 |
6.73e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.12 E-value: 6.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 179 RERLRVAlerCSLLEEELGATHKELMILKEQNNQKKTLTDGLLDGNHEQE-------SAPSTNGKRSSDGSLSHEDLAKV 251
Cdd:PLN02939 28 RRRLAVS---CRARRRGFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQlentslrTVMELPQKSTSSDDDHNRASMQR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 252 LELQEVIDRQAREQSQMKERLASLssHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRY--- 328
Cdd:PLN02939 105 DEAIAAIDNEQQTNSKDGEQLSDF--QLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLset 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 329 -----LAAQrEATSVHDLNDKLENeiANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKA------ETLPEVeAELAQR 397
Cdd:PLN02939 183 darikLAAQ-EKIHVEILEEQLEK--LRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDdiqflkAELIEV-AETEER 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 398 VAALSKsgplssgSSAAKEAKLLELTSKLRKAEERHGNIEErlRQMEAqLEEKNQELQRARQREKMNEEH-------NKR 470
Cdd:PLN02939 259 VFKLEK-------ERSLLDASLRELESKFIVAQEDVSKLSP--LQYDC-WWEKVENLQDLLDRATNQVEKaalvldqNQD 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 471 LSDTVDKL---LSESN------ERLQLhLKERMAALEDKnsLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLR 541
Cdd:PLN02939 329 LRDKVDKLeasLKEANvskfssYKVEL-LQQKLKLLEER--LQASDHEIHSYIQLYQESIKEFQDTLSKLKEESKKRSLE 405
|
..
gi 568952884 542 GP 543
Cdd:PLN02939 406 HP 407
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
290-539 |
7.26e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.80 E-value: 7.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 290 RKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRY----LAAQREATSVHDLNDKLENEIAN---KDSMHRQTEDK 362
Cdd:TIGR00618 165 KKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSqlltLCTPCMPDTYHERKQVLEKELKHlreALQQTQQSHAY 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 363 NRQLQERLELA---EQKLQQTLRKAETLPEVEAELAQRVAALSKSgplssgssaAKEAKLLELTSKLRKAEERHGNIEER 439
Cdd:TIGR00618 245 LTQKREAQEEQlkkQQLLKQLRARIEELRAQEAVLEETQERINRA---------RKAAPLAAHIKAVTQIEQQAQRIHTE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 440 LRQMEAQLEEKNQELQRARQREKMNEEHNKRLsdtvDKLLSESNERLQLHLKErMAALEDKNSLLREVENAKKQLEETQH 519
Cdd:TIGR00618 316 LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLL----QTLHSQEIHIRDAHEVA-TSIREISCQQHTLTQHIHTLQQQKTT 390
|
250 260
....*....|....*....|
gi 568952884 520 DKDQLvvtiEALKAELEQMR 539
Cdd:TIGR00618 391 LTQKL----QSLCKELDILQ 406
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
162-352 |
9.27e-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: 43.21 E-value: 9.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 162 KALKSLFEHHKALDEKV---RERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGLLDGNHEQESAPSTNGKRS 238
Cdd:COG4942 48 KEEKALLKQLAALERRIaalARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLS 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 239 SDGSLsheDLAKVLE-LQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDM 317
Cdd:COG4942 128 PEDFL---DAVRRLQyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARL 204
|
170 180 190
....*....|....*....|....*....|....*
gi 568952884 318 EERITTLEKRYLAAQREATSVHDLNDKLENEIANK 352
Cdd:COG4942 205 EKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
259-446 |
1.06e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 259 DRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIK----------SEEMNTKLQR------EVREAMAQKEDMEERIT 322
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdlSEEAKLLLQQlselesQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 323 TLEKR------YLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKN---RQLQERLELAEQKLQQTLRK--------AE 385
Cdd:COG3206 244 ALRAQlgsgpdALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHpdvIALRAQIAALRAQLQQEAQRilasleaeLE 323
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952884 386 TLPEVEAELAQRVAALSKSgplsSGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQ 446
Cdd:COG3206 324 ALQAREASLQAQLAQLEAR----LAELPELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
206-682 |
1.38e-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: 43.03 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 206 LKEQNNQKKTLTDGLLDGN-HEQESAPSTNGKRSSDGSLSHEDL-AKVLEL---QEVIDRQAREQSQMKErLASLSSHAA 280
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDqYTQLALMEFAKKKSLHGKAELLTLrSQLLTLctpCMPDTYHERKQVLEKE-LKHLREALQ 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 281 ELEEDLDTARKDLIKSEEmNTKLQREVREAMAQkedmEERITTLEKRyLAAQREATSVHDLNDKLENEIANKDSMHRQTE 360
Cdd:TIGR00618 237 QTQQSHAYLTQKREAQEE-QLKKQQLLKQLRAR----IEELRAQEAV-LEETQERINRARKAAPLAAHIKAVTQIEQQAQ 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 361 DKNRQLQERLELAEQKLQQTlrkaetlpevEAELAQRVAALSKSGPLSSGSSAAKEAKLLELTSKLRKAE-ERHGNIEER 439
Cdd:TIGR00618 311 RIHTELQSKMRSRAKLLMKR----------AAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREIsCQQHTLTQH 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 440 LRQMEAQLEEKNQELQRARQR-EKMNEEHNKRLSDTVD---------------KLLSESNERLQLHLKERMAALEDKNSL 503
Cdd:TIGR00618 381 IHTLQQQKTTLTQKLQSLCKElDILQREQATIDTRTSAfrdlqgqlahakkqqELQQRYAELCAAAITCTAQCEKLEKIH 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 504 LREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRgpslHHGRPHLgsvpdfrFSVADGHVDAYSTSAVLRRPQKGR 583
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLE----LQEEPCP-------LCGSCIHPNPARQDIDNPGPLTRR 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 584 LAALRDEPSKVQT-----------LNEQDWERAQQASVLANVAQAFESDVDVSdgEDDRDTLLSSVDLLSPSGQADAQTL 652
Cdd:TIGR00618 530 MQRGEQTYAQLETseedvyhqltsERKQRASLKEQMQEIQQSFSILTQCDNRS--KEDIPNLQNITVRLQDLTEKLSEAE 607
|
490 500 510
....*....|....*....|....*....|....*...
gi 568952884 653 AMMLQE--------QLDAINKEIRLIQEEKENTEQRAE 682
Cdd:TIGR00618 608 DMLACEqhallrklQPEQDLQDVRLHLQQCSQELALKL 645
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
159-405 |
1.42e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 159 EVLKALKSLFEHHKALDEkVRERLRVALERCSLLEEeLGATHKELMILKEQNNQKKTLTDGLLDGNHEQESApstngkrs 238
Cdd:COG4913 222 DTFEAADALVEHFDDLER-AHEALEDAREQIELLEP-IRELAERYAAARERLAELEYLRAALRLWFAQRRLE-------- 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 239 sdgslshedlakvlELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDL--IKSEEMNTkLQREVREAMAQKED 316
Cdd:COG4913 292 --------------LLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrgNGGDRLEQ-LEREIERLERELEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 317 MEERITTLEKRylaaqreatsVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQ 396
Cdd:COG4913 357 RERRRARLEAL----------LAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
....*....
gi 568952884 397 RVAALSKSG 405
Cdd:COG4913 427 EIASLERRK 435
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
163-454 |
1.49e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.89 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 163 ALKSLFEhhkALDEKVR--ERLRVALER-CSLLEEELGATHKELMILKEQ-NNQKKTLTD---GLLD-GNHEQESAPSTN 234
Cdd:pfam10174 437 ALTTLEE---ALSEKERiiERLKEQREReDRERLEELESLKKENKDLKEKvSALQPELTEkesSLIDlKEHASSLASSGL 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 235 GKRSSDGSL-----SHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHaaeLEEDLDTARKDLIKSEEMNTKLQREVRE 309
Cdd:pfam10174 514 KKDSKLKSLeiaveQKKEECSKLENQLKKAHNAEEAVRTNPEINDRIRL---LEQEVARYKEESGKAQAEVERLLGILRE 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 310 AMAQKEDMEERITTLEKRYLAAQREATSvhdlndklenEIANKDSMhrQTEDKNRQLQErlelaeqkLQQTLRKAETLPE 389
Cdd:pfam10174 591 VENEKNDKDKKIAELESLTLRQMKEQNK----------KVANIKHG--QQEMKKKGAQL--------LEEARRREDNLAD 650
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952884 390 VEAE--LAQRVAALSKSgplssgsSAAKEAKLLELTSKLRKAEERHGNIE----ERLRQMEAQLEEKNQEL 454
Cdd:pfam10174 651 NSQQlqLEELMGALEKT-------RQELDATKARLSSTQQSLAEKDGHLTnlraERRKQLEEILEMKQEAL 714
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
246-484 |
1.68e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.61 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 246 EDLAKVLE-LQE-----VIDRQAREQSqmkERLASLSSHAAELEEDLDTARKDLiKSEEMNTKLQREVReamaqKEDMEE 319
Cdd:PRK05771 16 SYKDEVLEaLHElgvvhIEDLKEELSN---ERLRKLRSLLTKLSEALDKLRSYL-PKLNPLREEKKKVS-----VKSLEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 320 RITTLEKRYLAAQREAtsvhdlnDKLENEIANKDSMHRQTEDKNRQLQ--ERLELAEQKLQQT--------LRKAETLPE 389
Cdd:PRK05771 87 LIKDVEEELEKIEKEI-------KELEEEISELENEIKELEQEIERLEpwGNFDLDLSLLLGFkyvsvfvgTVPEDKLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 390 VEAELAQRVAALSKSGPLSSGSSAAKEAKLLELTSK-LRKAEER------HGNIEERLRQMEAQLEEKNQELQRARQR-E 461
Cdd:PRK05771 160 LKLESDVENVEYISTDKGYVYVVVVVLKELSDEVEEeLKKLGFErleleeEGTPSELIREIKEELEEIEKERESLLEElK 239
|
250 260
....*....|....*....|...
gi 568952884 462 KMNEEHNKRLSDTVDKLLSESNE 484
Cdd:PRK05771 240 ELAKKYLEELLALYEYLEIELER 262
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
911-973 |
1.76e-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: 38.02 E-value: 1.76e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568952884 911 QWDGPTVVVWLElWVGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQ 973
Cdd:pfam00536 2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQ 61
|
|
| SAM_SARM1-like_repeat1 |
cd09501 |
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
1005-1052 |
1.77e-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: 1.77e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 568952884 1005 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSF 1052
Cdd:cd09501 11 TWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLRKRF 58
|
|
| SAM_Neurabin-like |
cd09512 |
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ... |
1081-1147 |
1.92e-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: 38.02 E-value: 1.92e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568952884 1081 RDVLVWSNDRVIRWILSIGLKEYANNLIESGVHG-ALLALDETfDFSALALllqiptQNTQARAVLER 1147
Cdd:cd09512 2 RPVSEWSVQQVCQWLMGLGLEQYIPEFTANNIDGqQLLQLDSS-KLKALGI------TSSSDRSLLKK 62
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
177-557 |
1.93e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.52 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 177 KVRERLRVALERCSLLEEELGATHKELmilkeqNNQKKTLTDglldgnheqeSAPSTNGKRSSDGSLSHEDLAKVLELQE 256
Cdd:pfam12128 608 KAEEALQSAREKQAAAEEQLVQANGEL------EKASREETF----------ARTALKNARLDLRRLFDEKQSEKDKKNK 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 257 VIdrqAREQSQMKERLASLSSHAAELEEDLDtARKDLIKSE--EMNTKLQREVREAMAQKEDMEERI-TTLEKRYLAAQR 333
Cdd:pfam12128 672 AL---AERKDSANERLNSLEAQLKQLDKKHQ-AWLEEQKEQkrEARTEKQAYWQVVEGALDAQLALLkAAIAARRSGAKA 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 334 EATSVHDLND--------------KLENEIANkdsMHRQTEDKNRQLQERLE----LAEQKLQQTLRKAETLPEVEaela 395
Cdd:pfam12128 748 ELKALETWYKrdlaslgvdpdviaKLKREIRT---LERKIERIAVRRQEVLRyfdwYQETWLQRRPRLATQLSNIE---- 820
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 396 qrvaalsksgplssgsSAAKEAKLlELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQR-EKMNEEHnkrlsdt 474
Cdd:pfam12128 821 ----------------RAISELQQ-QLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEmSKLATLK------- 876
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 475 vdklLSESNERLQLHLKERMAALED-KNSLLREVENAKKQLEE-----TQHDKDQLVVTIEALKAELEQMRLRGPSLHHG 548
Cdd:pfam12128 877 ----EDANSEQAQGSIGERLAQLEDlKLKRDYLSESVKKYVEHfknviADHSGSGLAETWESLREEDHYQNDKGIRLLDY 952
|
....*....
gi 568952884 549 RPHLGSVPD 557
Cdd:pfam12128 953 RKLVPYLEQ 961
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
45-452 |
2.06e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.63 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 45 EERDRLLD-------TLRETQETLALTQGKLHEVGHERDSLQRQlNTALPQEFAALTKELNVCREQLLER------EEEI 111
Cdd:COG3096 278 NERRELSEralelrrELFGARRQLAEEQYRLVEMARELEELSAR-ESDLEQDYQAASDHLNLVQTALRQQekieryQEDL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 112 AELkAERnntrlLLEHLECLVSRHERSLRmtvvkRQAQSPAgvsSEVEVlKALKS-LFEHHKALDE---------KVRER 181
Cdd:COG3096 357 EEL-TER-----LEEQEEVVEEAAEQLAE-----AEARLEA---AEEEV-DSLKSqLADYQQALDVqqtraiqyqQAVQA 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 182 LRVALERCSLLEEELGATHKELMILKEQNNQkktLTDGLLDGNHeqesapstngkRSSDGSLSHEDLAKVLELQEVID-- 259
Cdd:COG3096 422 LEKARALCGLPDLTPENAEDYLAAFRAKEQQ---ATEEVLELEQ-----------KLSVADAARRQFEKAYELVCKIAge 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 260 --------------RQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAmaqkEDMEERITTLE 325
Cdd:COG3096 488 versqawqtarellRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAA----EELEELLAELE 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 326 krylaAQREatsvhDLNDKLENEIANKDSMHRQTEdknrQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAalsksg 405
Cdd:COG3096 564 -----AQLE-----ELEEQAAEAVEQRSELRQQLE----QLRARIKELAARAPAWLAAQDALERLREQSGEALA------ 623
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 568952884 406 plssgSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQ 452
Cdd:COG3096 624 -----DSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQ 665
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
154-541 |
2.06e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 154 VSSEVEVLKALKSLFEHHKALDEKVRErLRVALERcslLEEELGATH------------------KELMILKEQNNQKKT 215
Cdd:pfam01576 670 VSSKDDVGKNVHELERSKRALEQQVEE-MKTQLEE---LEDELQATEdaklrlevnmqalkaqfeRDLQARDEQGEEKRR 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 216 LtdgLLDGNHEQESAPSTNGKRSSDGSLSHEDLA---KVLELQEVIDRQAREQS--QMKERLASLSSHAAELEEDLDTAR 290
Cdd:pfam01576 746 Q---LVKQVRELEAELEDERKQRAQAVAAKKKLEldlKELEAQIDAANKGREEAvkQLKKLQAQMKDLQRELEEARASRD 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 291 KDLIKSEEMNTKLQrevreamaqkeDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERL 370
Cdd:pfam01576 823 EILAQSKESEKKLK-----------NLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARI 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 371 ELAEQKLQQTLRKAETLPEVEAELAQRV----AALSKSGPLSSGSSAAKE----------AKLLELTSKLR-KAEERHGN 435
Cdd:pfam01576 892 AQLEEELEEEQSNTELLNDRLRKSTLQVeqltTELAAERSTSQKSESARQqlerqnkelkAKLQEMEGTVKsKFKSSIAA 971
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 436 IEERLRQMEAQLEEKNQELQRA----RQREK------MNEEHNKRLSDTVDKLLSESNERLQlHLKERMAALEDknsllr 505
Cdd:pfam01576 972 LEAKIAQLEEQLEQESRERQAAnklvRRTEKklkevlLQVEDERRHADQYKDQAEKGNSRMK-QLKRQLEEAEE------ 1044
|
410 420 430
....*....|....*....|....*....|....*.
gi 568952884 506 EVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLR 541
Cdd:pfam01576 1045 EASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
238-510 |
2.09e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.58 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 238 SSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEED-LDTARKDLIKSEEMntklQREVREAMAQKED 316
Cdd:PRK01156 475 NEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNkIESARADLEDIKIK----INELKDKHDKYEE 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 317 MEERITTLEKRYLAAQRE----ATSVHDLNDkLENEIANKDSMHRQTEDKNRQLQE---RLELAEQKLQQTLRKAET--- 386
Cdd:PRK01156 551 IKNRYKSLKLEDLDSKRTswlnALAVISLID-IETNRSRSNEIKKQLNDLESRLQEieiGFPDDKSYIDKSIREIENean 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 387 -----LPEVEAELAQRVAALSKSGPLSSGSSAAK--EAKLLELTSKLRKaeerhgnIEERLRQMEAQLEEKNQELQRARQ 459
Cdd:PRK01156 630 nlnnkYNEIQENKILIEKLRGKIDNYKKQIAEIDsiIPDLKEITSRIND-------IEDNLKKSRKALDDAKANRARLES 702
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 568952884 460 REKMNEEHNKRLSDTVdkllSESNERLqlhlkERMAALEDKNSLLREVENA 510
Cdd:PRK01156 703 TIEILRTRINELSDRI----NDINETL-----ESMKKIKKAIGDLKRLREA 744
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
44-688 |
2.76e-03 |
|
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: 41.98 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 44 LEERDRLLDTLRETQETLALTQGKLHE-----VGHERDSLQRQLN------TALPQEFAALTKELN--------VCREQL 104
Cdd:TIGR02169 210 AERYQALLKEKREYEGYELLKEKEALErqkeaIERQLASLEEELEklteeiSELEKRLEEIEQLLEelnkkikdLGEEEQ 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 105 LEREEEIAELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSP--AGVSSEVEVLKALKSLFEHHKALDEKVRERL 182
Cdd:TIGR02169 290 LRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAeiEELEREIEEERKRRDKLTEEYAELKEELEDL 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 183 RVALERcslLEEELGATHKELMILKEQnnqKKTLTDGLLDGNHEQESAPSTNGKRSSDGSLSHEDLA----KVLELQEVI 258
Cdd:TIGR02169 370 RAELEE---VDKEFAETRDELKDYREK---LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAgieaKINELEEEK 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 259 DRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERIT---------------- 322
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRggraveevlkasiqgv 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 323 --------TLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDK---------NRQLQERLELAEQKLQQTLRKAE 385
Cdd:TIGR02169 524 hgtvaqlgSVGERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKagratflplNKMRDERRDLSILSEDGVIGFAV 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 386 TLPEVEAELAQRVAALSKSGPLSSGSSAAK-----------EAKLLE----LTSKLRKAEERHGN---IEERLRQMEAQL 447
Cdd:TIGR02169 604 DLVEFDPKYEPAFKYVFGDTLVVEDIEAARrlmgkyrmvtlEGELFEksgaMTGGSRAPRGGILFsrsEPAELQRLRERL 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 448 EEKNQELQRARQREkmneEHNKRLSDTVDKLLSESNERLQLHLKERmaaledkNSLLREVENAKKQLEETQHDKDQLVVT 527
Cdd:TIGR02169 684 EGLKRELSSLQSEL----RRIENRLDELSQELSDASRKIGEIEKEI-------EQLEQEEEKLKERLEELEEDLSSLEQE 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 528 IEALKAELEQMRLRgpslhhgrphlgsvpdfrfsvadghVDAYSTSAVLRRPQKGRLAAlRDEPSKVQTLNEQdwERAQQ 607
Cdd:TIGR02169 753 IENVKSELKELEAR-------------------------IEELEEDLHKLEEALNDLEA-RLSHSRIPEIQAE--LSKLE 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 608 ASVLANVAQAFESDVDVSDGEDDRDTLLSSVdllspsgqADAQTLAMMLQEQLDAINKEIRLIQEEKENTEQRAEEIESR 687
Cdd:TIGR02169 805 EEVSRIEARLREIEQKLNRLTLEKEYLEKEI--------QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA 876
|
.
gi 568952884 688 V 688
Cdd:TIGR02169 877 L 877
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
388-527 |
3.27e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 41.19 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 388 PEVEAELAQRVAALsksgplssgssAAKEAKLLELTSKLRKAEERHGnIEERLRQMEAQLEEKNQELQRARQ-------- 459
Cdd:COG1566 79 TDLQAALAQAEAQL-----------AAAEAQLARLEAELGAEAEIAA-AEAQLAAAQAQLDLAQRELERYQAlykkgavs 146
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568952884 460 REKMNEEHNKRlsDTVDKLLSESNERLQLhLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVT 527
Cdd:COG1566 147 QQELDEARAAL--DAAQAQLEAAQAQLAQ-AQAGLREEEELAAAQAQVAQAEAALAQAELNLARTTIR 211
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
45-276 |
3.58e-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: 41.29 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNtALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLL 124
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA-ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 125 LEHLECLVSRHERSLRMTVVKRQAQ---SPAGVSSEVEVLKALKSLFEHhkalDEKVRERLRVALERCSLLEEELGATHK 201
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPA----RREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568952884 202 ELMILKEQNNQKKTLTDGLLDGnhEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASLS 276
Cdd:COG4942 175 ELEALLAELEEERAALEALKAE--RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
250-396 |
3.59e-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: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 250 KVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQR--EVREAMAQKEDMEERITTLEKR 327
Cdd:COG3206 206 GLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSAR 285
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 328 YLAAQREATSVHDLNDKLENEIAN-KDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQ 396
Cdd:COG3206 286 YTPNHPDVIALRAQIAALRAQLQQeAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
|
|
| Stathmin |
pfam00836 |
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ... |
404-523 |
3.62e-03 |
|
Stathmin family; The Stathmin family of proteins play an important role in the regulation of the microtubule cytoskeleton. They regulate microtubule dynamics by promoting depolymerization of microtubules and/or preventing polymerization of tubulin heterodimers.
Pssm-ID: 459956 [Multi-domain] Cd Length: 136 Bit Score: 38.87 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 404 SGPLSSGSSAAKEAKLLELTSKLRKAEERHGNIEErlrQMEAQLEEKNQELQRARQreKMNEEHNKRLSDTVDKLlsesN 483
Cdd:pfam00836 29 APPKLSLSPKKKDSSLEEIQKKLEAAEERRKSLEA---QKLKQLAEKREKEEEALQ--KADEENNNFSKMAEEKL----K 99
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 568952884 484 ERLQLHLKERMAALEDKNSLLREVEnakKQLEETQHDKDQ 523
Cdd:pfam00836 100 QKMEAYKENREAQIAALKEKLKEKE---KHVEEVRKNKEQ 136
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
344-535 |
3.78e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.19 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 344 KLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETlpeveaELAqRVAALSKsgplssgssAAKEAKLLELT 423
Cdd:COG1842 41 EARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKGRE------DLA-REALERK---------AELEAQAEALE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 424 SKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNeEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSL 503
Cdd:COG1842 105 AQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAA-KAQEKVNEALSGIDSDDATSALERMEEKIEEMEARAEA 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 568952884 504 LREVENAK---KQLEETQHDK---DQLvvtiEALKAEL 535
Cdd:COG1842 184 AAELAAGDsldDELAELEADSeveDEL----AALKAKM 217
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
281-532 |
4.14e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 281 ELEEDLDT--ARKDLIKSE-EMNTKLQREVREAMAQkedmeeRITTLEKRYLAAQREATSVHDLNDKLENEIANKD-SMH 356
Cdd:PHA02562 178 ELNQQIQTldMKIDHIQQQiKTYNKNIEEQRKKNGE------NIARKQNKYDELVEEAKTIKAEIEELTDELLNLVmDIE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 357 RQTEDKNRQLQERLELAEQ-----KLQQTLRKAETLPEVEAELAQRVAALSKSgplssgssaakEAKLLELTSKLRKAEE 431
Cdd:PHA02562 252 DPSAALNKLNTAAAKIKSKieqfqKVIKMYEKGGVCPTCTQQISEGPDRITKI-----------KDKLKELQHSLEKLDT 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 432 RHGNIEER----------LRQMEAQLEEKNQELQRARQRekmneehNKRLSDTVDKLLSESNERlqlhlKERMAALEDKn 501
Cdd:PHA02562 321 AIDELEEImdefneqskkLLELKNKISTNKQSLITLVDK-------AKKVKAAIEELQAEFVDN-----AEELAKLQDE- 387
|
250 260 270
....*....|....*....|....*....|.
gi 568952884 502 slLREVENAKKQLEEtqhDKDQLVVTIEALK 532
Cdd:PHA02562 388 --LDKIVKTKSELVK---EKYHRGIVTDLLK 413
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
342-471 |
4.19e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 342 NDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRvaalsksgplssgssAAKEAKlle 421
Cdd:PRK00409 515 KEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEE---------------AEKEAQ--- 576
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 568952884 422 ltSKLRKAEERHGNIEERLRQMEAQL--EEKNQELQRARQR-EKMNEEHNKRL 471
Cdd:PRK00409 577 --QAIKEAKKEADEIIKELRQLQKGGyaSVKAHELIEARKRlNKANEKKEKKK 627
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
284-539 |
4.67e-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: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 284 EDLDTARKDLIKSEEMN----TKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQT 359
Cdd:TIGR04523 78 KILEQQIKDLNDKLKKNkdkiNKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 360 EDKNRQLQERLELAEQKL----QQTLRKAETLPEVEAELAQRVAALSKsgplssgsSAAKEAKLLELTSKLRKAEERHGN 435
Cdd:TIGR04523 158 NNKYNDLKKQKEELENELnlleKEKLNIQKNIDKIKNKLLKLELLLSN--------LKKKIQKNKSLESQISELKKQNNQ 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 436 IEERLRQMEAQLEEKNQELQRARQREK----MNEEHNKRLSD------TVDKLLSESNERLQlHLKERMAALEDK----- 500
Cdd:TIGR04523 230 LKDNIEKKQQEINEKTTEISNTQTQLNqlkdEQNKIKKQLSEkqkeleQNNKKIKELEKQLN-QLKSEISDLNNQkeqdw 308
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 568952884 501 -NSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMR 539
Cdd:TIGR04523 309 nKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLK 348
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
281-456 |
5.59e-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: 39.66 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 281 ELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERIT-TLEKRYLAAQREATSVhdlNDKLENEIANKDSMHRQT 359
Cdd:pfam04012 33 DMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQaALTKGNEELAREALAE---KKSLEKQAEALETQLAQQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 360 EDKNRQLQERLELAEQKLQQTLRKAETLpEVEAELAQRVAALSKS-GPLSSGSSAAK----EAKLLELTSKLRKAEERHG 434
Cdd:pfam04012 110 RSAVEQLRKQLAALETKIQQLKAKKNLL-KARLKAAKAQEAVQTSlGSLSTSSATDSferiEEKIEEREARADAAAELAS 188
|
170 180
....*....|....*....|....
gi 568952884 435 --NIEERLRQMEAQLEEKNQELQR 456
Cdd:pfam04012 189 avDLDAKLEQAGIQMEVSEDVLAR 212
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
257-537 |
6.28e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 257 VIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITT-------LEKRYL 329
Cdd:TIGR04523 27 IANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKnkdkinkLNSDLS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 330 AAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKsgplss 409
Cdd:TIGR04523 107 KINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEK------ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 410 gSSAAKEAKLLELTSKLRKAEERHGNIE---ERLRQMEAQLEE-KNQELQRARQREKMNEEHNKR---LSDTVDKLLSES 482
Cdd:TIGR04523 181 -EKLNIQKNIDKIKNKLLKLELLLSNLKkkiQKNKSLESQISElKKQNNQLKDNIEKKQQEINEKtteISNTQTQLNQLK 259
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 568952884 483 NErlQLHLKERmaaLEDKNSllrEVENAKKQLEETQHDKDQLVVTIEALKAELEQ 537
Cdd:TIGR04523 260 DE--QNKIKKQ---LSEKQK---ELEQNNKKIKELEKQLNQLKSEISDLNNQKEQ 306
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
176-542 |
6.36e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.88 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 176 EKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGLldGNHEQESAPSTNgkrssdgslSHEDLAKVLELQ 255
Cdd:pfam05557 135 EELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEI--QSQEQDSEIVKN---------SKSELARIPELE 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 256 EVIDRQAREQSQ---MKERLASLSSHAAELEEDLDT---ARKDLIKSEEMNTKLQREVRE----------AMAQKEDMEE 319
Cdd:pfam05557 204 KELERLREHNKHlneNIENKLLLKEEVEDLKRKLEReekYREEAATLELEKEKLEQELQSwvklaqdtglNLRSPEDLSR 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 320 RITTLEKRYLAAQREATSVhdlndkleneiankDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVA 399
Cdd:pfam05557 284 RIEQLQQREIVLKEENSSL--------------TSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVL 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 400 ALSKSGPL------SSGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEehnkrlsd 473
Cdd:pfam05557 350 LLTKERDGyraileSYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLE-------- 421
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568952884 474 tvdkllsesnerLQLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRG 542
Cdd:pfam05557 422 ------------RELQALRQQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQG 478
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
255-471 |
6.37e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 40.41 E-value: 6.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 255 QEVIDRQAREQSQMKERLASLSShaaELEEDLDTARKDLIKSEEmNTKLQREVREAMAQkEDMEErittleKRYLAAQRE 334
Cdd:pfam15558 54 LLLQQSQEQWQAEKEQRKARLGR---EERRRADRREKQVIEKES-RWREQAEDQENQRQ-EKLER------ARQEAEQRK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 335 ATSVHDLNDKLENEiankdsmHRQTEDKNRQLQERLELAEQKLQqtLRKAETLPEVEAE-LAQRVAALSKSGPLSSGSSA 413
Cdd:pfam15558 123 QCQEQRLKEKEEEL-------QALREQNSLQLQERLEEACHKRQ--LKEREEQKKVQENnLSELLNHQARKVLVDCQAKA 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 414 AKEAKLLELTSKLRKAEERH-GNIEERLRQMEAQLEEKNQELQRARQR-EKMNEEHNKRL 471
Cdd:pfam15558 194 EELLRRLSLEQSLQRSQENYeQLVEERHRELREKAQKEEEQFQRAKWRaEEKEEERQEHK 253
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
250-541 |
6.38e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 6.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 250 KVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKR-- 327
Cdd:COG4372 11 ARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQlq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 328 -----YLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALS 402
Cdd:COG4372 91 aaqaeLAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 403 KSgplssgSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSES 482
Cdd:COG4372 171 QE------LQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 568952884 483 NERLQLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLR 541
Cdd:COG4372 245 EEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLN 303
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
134-483 |
7.14e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 40.62 E-value: 7.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 134 RHERSLRMTVvkRQAQSPAGVSSEVEVLKAlKSLFEHHKALDEKVRERLRvalERCSLLEEELGATHKELMILKEQNNQK 213
Cdd:pfam02029 13 RRAREERRRQ--KEEEEPSGQVTESVEPNE-HNSYEEDSELKPSGQGGLD---EEEAFLDRTAKREERRQKRLQEALERQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 214 KTLTDGLLDG--------NHEQESAPSTNGKRSSDGSlshEDLAKVLELQEVIDRQAREQ--SQMKERLASLSSHAAELE 283
Cdd:pfam02029 87 KEFDPTIADEkesvaerkENNEEEENSSWEKEEKRDS---RLGRYKEEETEIREKEYQENkwSTEVRQAEEEGEEEEDKS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 284 EDLDTARKDLIKSEEM---NTKLQREVREAMAQKEDMEERITTLekrylAAQREATSVHDLNDKLENEIANKDSMHRQTE 360
Cdd:pfam02029 164 EEAEEVPTENFAKEEVkdeKIKKEKKVKYESKVFLDQKRGHPEV-----KSQNGEEEVTKLKVTTKRRQGGLSQSQEREE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 361 DKNRQLQerlelAEQKLQQTLRKAETLPEVEAE-LAQRVAalsksgplssgssaakEAKLlELTSKLRKAEERHGNIEER 439
Cdd:pfam02029 239 EAEVFLE-----AEQKLEELRRRRQEKESEEFEkLRQKQQ----------------EAEL-ELEELKKKREERRKLLEEE 296
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 568952884 440 LRQMEAqlEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESN 483
Cdd:pfam02029 297 EQRRKQ--EEAERKLREEEEKRRMKEEIERRRAEAAEKRQKLPE 338
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
255-403 |
7.47e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.95 E-value: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 255 QEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRyLAAQRe 334
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQE-LDSEK- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 335 ATSVHDLndkleneiankdsmhRQTEDKNRQ----------LQERLELAEQKLQQTLRKAETL-PEVEAELAQRVAALSK 403
Cdd:PRK09039 130 QVSARAL---------------AQVELLNQQiaalrrqlaaLEAALDASEKRDRESQAKIADLgRRLNVALAQRVQELNR 194
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
295-534 |
7.50e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 40.55 E-value: 7.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 295 KSEEMNTKLQ------REVREAMAQKEDMEERITTLEKRYLAAqreatsvHDLNDKLENEIAN-KDSMHRQTEDKN--RQ 365
Cdd:PRK10246 312 QIEEVNTRLQstmalrARIRHHAAKQSAELQAQQQSLNTWLAE-------HDRFRQWNNELAGwRAQFSQQTSDREqlRQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 366 LQERLELAEQKLQQTLRKAETL-PEveaELAQRVAALSKSGPLSS------GSSAAKEAKLLELTSKLRKAEERHGNIEE 438
Cdd:PRK10246 385 WQQQLTHAEQKLNALPAITLTLtAD---EVAAALAQHAEQRPLRQrlvalhGQIVPQQKRLAQLQVAIQNVTQEQTQRNA 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 439 RLRQMEAQLEEKNQELQRAR------QREKMNEEHNKRLS----------------DTVDKLLSESNERLQLHLKERMAA 496
Cdd:PRK10246 462 ALNEMRQRYKEKTQQLADVKticeqeARIKDLEAQRAQLQagqpcplcgstshpavEAYQALEPGVNQSRLDALEKEVKK 541
|
250 260 270
....*....|....*....|....*....|....*....
gi 568952884 497 LEDKNSLLR-EVENAKKQLEETQHDKDQLVVTIEALKAE 534
Cdd:PRK10246 542 LGEEGAALRgQLDALTKQLQRDESEAQSLRQEEQALTQQ 580
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
264-401 |
8.27e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 39.12 E-value: 8.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 264 EQSQMKERLASLSSHAAELEEDLDTARKD---LIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAA-QREATSVH 339
Cdd:pfam13851 55 ENKRLTEPLQKAQEEVEELRKQLENYEKDkqsLKNLKARLKVLEKELKDLKWEHEVLEQRFEKVERERDELyDKFEAAIQ 134
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568952884 340 DLNDK-------LENEIANkdsMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAAL 401
Cdd:pfam13851 135 DVQQKtglknllLEKKLQA---LGETLEKKEAQLNEVLAAANLDPDALQAVTEKLEDVLESKNQLIKDL 200
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
281-537 |
8.81e-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: 40.22 E-value: 8.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 281 ELEEDLDTARKDLIKSEEMNTKLqrEVREAMAQKEDMEERITTL----EKRYLAAQreatSVHDLNDKLENEIANKDSMH 356
Cdd:pfam06160 234 NVDKEIQQLEEQLEENLALLENL--ELDEAEEALEEIEERIDQLydllEKEVDAKK----YVEKNLPEIEDYLEHAEEQN 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 357 RQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALsksgplssgssAAKEAKLLELTSKLRKaeerhgnI 436
Cdd:pfam06160 308 KELKEELERVQQSYTLNENELERVRGLEKQLEELEKRYDEIVERL-----------EEKEVAYSELQEELEE-------I 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 437 EERLRQMEAQLEEKNQELQRARQREKmneEHNKRLsDTVDKLLSESNERLQlhlKERMAAL-EDKNSLLREVENakkQLE 515
Cdd:pfam06160 370 LEQLEEIEEEQEEFKESLQSLRKDEL---EAREKL-DEFKLELREIKRLVE---KSNLPGLpESYLDYFFDVSD---EIE 439
|
250 260
....*....|....*....|..
gi 568952884 516 ETQHDKDQLVVTIEALKAELEQ 537
Cdd:pfam06160 440 DLADELNEVPLNMDEVNRLLDE 461
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
253-473 |
9.63e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 39.24 E-value: 9.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 253 ELQEVIDRQAREQSQMKE---RLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRyl 329
Cdd:pfam00261 9 ELDEAEERLKEAMKKLEEaekRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGRKVLENR-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 330 aAQREATSVHDLNDKLeneianKDSMHRQ--TEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQR---VAALSKS 404
Cdd:pfam00261 87 -ALKDEEKMEILEAQL------KEAKEIAeeADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEElkvVGNNLKS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568952884 405 GPLSSGSSAAKE----AKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRAR-QREKMNEEHNKRLSD 473
Cdd:pfam00261 160 LEASEEKASEREdkyeEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKeKYKAISEELDQTLAE 233
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
416-530 |
9.80e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 38.71 E-value: 9.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 416 EAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLqlhlkERMA 495
Cdd:pfam12072 70 ERELKERRNELQRQERRLLQKEETLDRKDESLEKKEESLEKKEKELEAQQQQLEEKEEELEELIEEQRQEL-----ERIS 144
|
90 100 110
....*....|....*....|....*....|....*...
gi 568952884 496 AL---EDKNSLLREVEnakkqlEETQHDKDQLVVTIEA 530
Cdd:pfam12072 145 GLtseEAKEILLDEVE------EELRHEAAVMIKEIEE 176
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
280-396 |
9.81e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.04 E-value: 9.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952884 280 AELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQ---REATSVHDLNDklENEIANKDSMH 356
Cdd:COG1842 94 AELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKaqeKVNEALSGIDS--DDATSALERME 171
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 568952884 357 RQTEDKNRQLQERLELAEQK-LQQTLRKAETLPEVEAELAQ 396
Cdd:COG1842 172 EKIEEMEARAEAAAELAAGDsLDDELAELEADSEVEDELAA 212
|
|
| |
