|
Name |
Accession |
Description |
Interval |
E-value |
| 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 ... |
942-1012 |
5.51e-44 |
|
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.
Pssm-ID: 188961 Cd Length: 71 Bit Score: 153.49 E-value: 5.51e-44
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442626414 942 FALWNGPTIVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 1012
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 ... |
1114-1185 |
3.75e-42 |
|
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.
Pssm-ID: 188967 Cd Length: 72 Bit Score: 148.23 E-value: 3.75e-42
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626414 1114 DVLVWSNERVIRWVGSIGLKEYANNLLESGVHGGLMALDEGFDANAMGLALQIPTQNAQARQILDTEFNNLL 1185
Cdd:cd09568 1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
|
|
| 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 ... |
1029-1094 |
2.83e-40 |
|
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: 142.61 E-value: 2.83e-40
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442626414 1029 MNHEWIGNYWLPGLGLPQYRTTFMECLVDARMLDHLTKKDLRGQLKMVDSFHRTSLQYGISMLKRL 1094
Cdd:cd09565 1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
|
|
| SAM_liprin-kazrin_repeat1 |
cd09494 |
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
949-1007 |
1.48e-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: 1.48e-26
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 442626414 949 TIVAWLELWVGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 1007
Cdd:cd09494 1 RVCAWLEDFGLMP-MYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
|
|
| SAM_liprin-kazrin_repeat2 |
cd09495 |
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ... |
1033-1092 |
1.98e-25 |
|
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: 100.30 E-value: 1.98e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 1033 WIGNYWLPGLGLPQYRTTFMECLVDARMLDHLTKKDLRGQLKMVDSFHRTSLQYGISMLK 1092
Cdd:cd09495 1 WWVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLVHLKVTSQLHHLSLKCGIHVLH 60
|
|
| SAM_liprin-kazrin_repeat3 |
cd09496 |
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of ... |
1122-1183 |
2.69e-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: 96.84 E-value: 2.69e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626414 1122 RVIRWVGSIGLKEYANNLLESGVHGGLMALDEGFDANAMGLALQIPTQNAQARQILDTEFNN 1183
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 ... |
1114-1185 |
4.41e-24 |
|
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: 96.74 E-value: 4.41e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626414 1114 DVLVWSNERVIRWVGSIGLKEYANNLLESGVHGGLMALDEGFDANAMGLALQIPTQNAQARQILDTEFNNLL 1185
Cdd:cd09570 1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
255-526 |
1.35e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 85.37 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 255 YAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEK 334
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 335 RYLNAQRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKAQERHG 414
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 415 SAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESNERLQVH---LKERMHALDEKNALTQELEKAR 491
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALeeaAEEEAELEEEEEALLELLAELL 469
|
250 260 270
....*....|....*....|....*....|....*
gi 442626414 492 KVAEELHHEKSEIMKELSKTRLEIENFKRQLLQQE 526
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
261-533 |
3.46e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 84.34 E-value: 3.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 261 ELQTIIEKQTSELSQWQRRVSDLNNKISELEEnmsrvqkehckaqdQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQ 340
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEE--------------ELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 341 RESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKAQERHGSAEDRI 420
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 421 RGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKL---LSESNERLQVHLKERMHALDEKNALTQELEKARKVAEEL 497
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELeelIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
250 260 270
....*....|....*....|....*....|....*...
gi 442626414 498 HHEKSEIMKELSKTRLEIENFKRQL--LQQEIAYNIQQ 533
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLegLEVRIDNLQER 944
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
255-524 |
4.10e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 83.95 E-value: 4.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 255 YAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEK 334
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 335 RYLNAQRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKArmealtkAQERHG 414
Cdd:TIGR02168 310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE-------LEEQLE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 415 SAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESNErlqVHLKERMHALDEKNaltQELEKARKVA 494
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE---AELKELQAELEELE---EELEELQEEL 456
|
250 260 270
....*....|....*....|....*....|
gi 442626414 495 EELHHEKSEIMKELSKTRLEIENFKRQLLQ 524
Cdd:TIGR02168 457 ERLEEALEELREELEEAEQALDAAERELAQ 486
|
|
| SAM_liprin-beta1,2_repeat3 |
cd09569 |
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ... |
1114-1185 |
5.65e-16 |
|
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: 73.64 E-value: 5.65e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626414 1114 DVLVWSNERVIRWVGSIGLKEYANNLLESGVHGGLMALDEGFDANAMGLALQIPTQNAQARQILDTEFNNLL 1185
Cdd:cd09569 1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
|
|
| SAM_kazrin_repeat1 |
cd09564 |
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ... |
945-1007 |
1.44e-15 |
|
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: 72.48 E-value: 1.44e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442626414 945 WNGPTIVAWLELWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 1007
Cdd:cd09564 4 WKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
50-683 |
2.69e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.14 E-value: 2.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 50 REAQERLNETENKL-------RDVEKERDSLQRQinANLPQEFATLTKELT--QARETLLERDEeigeLKAERNNTRLLL 120
Cdd:COG1196 175 EEAERKLEATEENLerledilGELERQLEPLERQ--AEKAERYRELKEELKelEAELLLLKLRE----LEAELEELEAEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 121 EHLECLVSRHERSLRMTVVKRQAAAQSGVSSEVEVLKALKSLFEHHKALdEKVRERLRLSIEKNNMMEEELSSAKEELAQ 200
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL-ARLEQDIARLEERRRELEERLEELEEELAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 201 YKAgvvpagvgsgsgAGSAATTAGGGGAENGLKEKMAGVGGSGGVNGEANELNDYAAKTHELQTIIEKQTSELSQWQRRV 280
Cdd:COG1196 328 LEE------------ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 281 SDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQREstslhdlNEKLEQELRHK 360
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE-------EEALLELLAEL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 361 EAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQR 440
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAL 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 441 LKMNEEHNLRLSSTVDKLLSESNER---LQVHLKERMHALDEKNALTQELEKARKVAEELHHEKSEIMKELSKTRLEIEN 517
Cdd:COG1196 549 QNIVVEDDEVAAAAIEYLKAAKAGRatfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLV 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 518 FKRQLLQQEIAYNIQQTEALTRSLSPSSvvdpSGAFSRSNSHASFETHSLRRQSKQRLSEENALVRSMAEQEWEKLQQAA 597
Cdd:COG1196 629 AARLEAALRRAVTLAGRLREVTLEGEGG----SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEE 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 598 HAQQQAYELASAADCDDSDVLYAAATDMMspsgHTDAQTLAMMLQEQLDAINNEIRLIQEEKQSTEARAEELESRVGSLE 677
Cdd:COG1196 705 EERELAEAEEERLEEELEEEALEEQLEAE----REELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG 780
|
....*.
gi 442626414 678 HVNLLA 683
Cdd:COG1196 781 PVNLLA 786
|
|
| SAM_kazrin_repeat2 |
cd09567 |
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ... |
1028-1092 |
1.02e-14 |
|
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: 69.75 E-value: 1.02e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626414 1028 DMNHEWIGNYWLPGLGLPQYRTTFMECLVDARMLDHLTKKDLRGQLKMVDSFHRTSLQYGISMLK 1092
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 ... |
1028-1092 |
1.25e-14 |
|
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: 69.65 E-value: 1.25e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626414 1028 DMNHEWIGNyWLPGLGLPQYRTTFMECLVDARMLDHLTKKDLRgQLKMVDSFHRTSLQYGISMLK 1092
Cdd:cd09566 1 KLDTHWVLR-WLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDLL-HLKVTSALHHASIRRGIQVLR 63
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
249-529 |
1.67e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 78.95 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 249 ANELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEER 328
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 329 ITTLEKRYLNAQREstslhdlNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTK 408
Cdd:TIGR02168 784 IEELEAQIEQLKEE-------LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 409 AQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLkmnEEHNLRLSSTVDKLLSESNERLQvhLKERMHALDEK-NALTQEL 487
Cdd:TIGR02168 857 LAAEIEELEELIEELESELEALLNERASLEEAL---ALLRSELEELSEELRELESKRSE--LRRELEELREKlAQLELRL 931
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 442626414 488 EKAR--------KVAEELHHEKSEIMKELSKTRLEIENFKRQL--LQQEIAY 529
Cdd:TIGR02168 932 EGLEvridnlqeRLSEEYSLTLEEAEALENKIEDDEEEARRRLkrLENKIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
58-467 |
5.16e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 77.02 E-value: 5.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 58 ETENKLRDVEKERDSLQRQINAnlpqefatLTKELTQARETLLERDEEIGELKAERNNTRLLLEHLECLVSRHERslrmt 137
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAE--------LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA----- 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 138 vvKRQAAAQSGVSSEVEVLKAlkslfehhkaldEKVRERLRLSIEKNnmmEEELSSAKEELAQYKAGVvpagvgsgsgag 217
Cdd:TIGR02168 741 --EVEQLEERIAQLSKELTEL------------EAEIEELEERLEEA---EEELAEAEAEIEELEAQI------------ 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 218 saattaggggaENGLKEKMAGVGGSGGVNGEANELNDYAaktHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRV 297
Cdd:TIGR02168 792 -----------EQLKEELKALREALDELRAELTLLNEEA---ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 298 QKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQRE----STSLHDLNEKLeQELRHKEAQLKLHEEKI-- 371
Cdd:TIGR02168 858 AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEElrelESKRSELRREL-EELREKLAQLELRLEGLev 936
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 372 ------GAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKAQERHG----SAEDRIRGLETNLDEKTNEVVRLNQRL 441
Cdd:TIGR02168 937 ridnlqERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGpvnlAAIEEYEELKERYDFLTAQKEDLTEAK 1016
|
410 420
....*....|....*....|....*.
gi 442626414 442 KmneehnlRLSSTVDKLLSESNERLQ 467
Cdd:TIGR02168 1017 E-------TLEEAIEEIDREARERFK 1035
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
49-464 |
2.41e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.09 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 49 LREAQERLNETENKLRDVEKERDSLQRQinANLPQEFATLTKEL------------TQARETLLERDEEIGELKAERNNT 116
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKSLERQ--AEKAERYKELKAELrelelallvlrlEELREELEELQEELKEAEEELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 117 RLLLEHLECLVSRHErsLRMTVVKRQAAAQSGvssEVEVLKALKSLFEHHKALDEKVRERLRLSIEKNNMMEEELSSAKE 196
Cdd:TIGR02168 259 TAELQELEEKLEELR--LEVSELEEEIEELQK---ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 197 ELAQYKAGVVPAGVGSGSGAgsaattaggggaeNGLKEKMAGvggsggvngEANELNDYAAKTHELQTIIEKQTSELSQW 276
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEEL-------------ESLEAELEE---------LEAELEELESRLEELEEQLETLRSKVAQL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 277 QRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLREnvAQKEDQEERITTLEKrylnaqrestslhdLNEKLEQE 356
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEE--------------ELEELQEE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 357 LRHKEAQLKLHEEKIGAIEEKLELSEQKLAQhaklqpdmeeqLKARMEALTKAQERHGSAEDRIRGLETNLDEKTNEVVR 436
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQ-----------LQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGV 524
|
410 420 430
....*....|....*....|....*....|..
gi 442626414 437 LNQRLKMNEEH----NLRLSSTVDKLLSESNE 464
Cdd:TIGR02168 525 LSELISVDEGYeaaiEAALGGRLQAVVVENLN 556
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
1028-1092 |
3.39e-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: 65.37 E-value: 3.39e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626414 1028 DMNHEWIGNYWLPGLGLPQYRTTFMECLVDARMLDHLTKKDLRgQLKMVDSFHRTSLQYGISMLK 1092
Cdd:pfam00536 1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
43-530 |
1.92e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.02 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 43 DKLMDSLREAQERLNETENKLRDVEKERDSLQRQINanlpqEFATLTKELTQARETLLERDEEIGELKAERNNTRLLLEH 122
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREIN-----EISSELPELREELEKLEKEVKELEELKEEIEELEKELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 123 LECLVSRHERSLRMTvvkrqaaaQSGVSSEVEVLKALKSLFEHHKALDEKVRERLRLSIEKNNMmEEELSSAKEELAQYK 202
Cdd:PRK03918 250 LEGSKRKLEEKIREL--------EERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEY-LDELREIEKRLSRLE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 203 AGVVPAGVGSGSGAGSAATTAGGGGAENGLKEKMAGVGGSGGVNGEA----------------NELNDYAAKTHELQTII 266
Cdd:PRK03918 321 EEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAkakkeelerlkkrltgLTPEKLEKELEELEKAK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 267 EKQTSELSQWQRRVSDLNNKISELEENMSRVQKehckAQDQCAKLQRDLREnvaqkEDQEERITTLEKRYLNAQRESTSL 346
Cdd:PRK03918 401 EEIEEEISKITARIGELKKEIKELKKAIEELKK----AKGKCPVCGRELTE-----EHRKELLEEYTAELKRIEKELKEI 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 347 HDLNEKLEQELRHKEAQLKLHEE--KIGAIEEKLELSEQKLAQHAKlqpdmeEQLKARMEALTKAQERHGSAEDRIRGLE 424
Cdd:PRK03918 472 EEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNL------EELEKKAEEYEKLKEKLIKLKGEIKSLK 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 425 TNLDEKT---NEVVRLNQRLKMNEEHNLRLSSTVDKLLSESNERLQVHLKERMHALDEKNALT---QELEKARKVAEELH 498
Cdd:PRK03918 546 KELEKLEelkKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKdaeKELEREEKELKKLE 625
|
490 500 510
....*....|....*....|....*....|..
gi 442626414 499 HEKSEIMKELSKTRLEIENFKRQLLQQEIAYN 530
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEELEKKYS 657
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
40-528 |
6.24e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 6.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 40 DERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINANLpQEFATLTKELTQARETLLERDEEIGELKAERNNTRLL 119
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE-ERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 120 LEHLECLVSRHERSLRMTVVKRQAAAQSGVSSEVEVLKALKSLFEHHKALDEKVRERLRLSIEKNNMMEEELSSAKEELA 199
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 200 QYKAGVVPAGVGSGSGAGSAATTAGGGGAENGLKEKMAGVGGSGGVNGEANELNDYAAKTHELQTIIEKQTSELSQWQRR 279
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 280 VSDLNNK--ISELEENMSRVQKEHcKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRylNAQREStslhdlnekLEQEL 357
Cdd:COG1196 513 ALLLAGLrgLAGAVAVLIGVEAAY-EAALEAALAAALQNIVVEDDEVAAAAIEYLKAA--KAGRAT---------FLPLD 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 358 RHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARmealTKAQERHGSAEDRIRGLETNLDEKTNEVVRL 437
Cdd:COG1196 581 KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR----TLVAARLEAALRRAVTLAGRLREVTLEGEGG 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 438 NQRLKMNEEHNLRLSSTVDKLLSESNERLQVHLKERMHALDEKNALTQELEKARKVAEELHHEKSEIMKELSKTRLEIEN 517
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
490
....*....|.
gi 442626414 518 FKRQLLQQEIA 528
Cdd:COG1196 737 LLEELLEEEEL 747
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
157-514 |
2.07e-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: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 157 KALKSLFEHHKALDEKVRERLRLSIEKnnmmEEELSSAKEELAQYKAGVvpagvgsgsGAGSAATTAGGGGAENGLKEKM 236
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEEL----SRQISALRKDLARLEAEV---------EQLEERIAQLSKELTELEAEIE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 237 AGVGGSGGVNGEANELndyAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLR 316
Cdd:TIGR02168 765 ELEERLEEAEEELAEA---EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 317 ENVAQKEDQEERITTLEKrylnaqrESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDME 396
Cdd:TIGR02168 842 DLEEQIEELSEDIESLAA-------EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 397 EQLKARMEALTKAQERHGSAEDRIRGLETnldektnevvRLNQRLKMNEEHNLRLSSTVDKLLSESNERLQvHLKERMHA 476
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLEVRIDNLQE----------RLSEEYSLTLEEAEALENKIEDDEEEARRRLK-RLENKIKE 983
|
330 340 350
....*....|....*....|....*....|....*....
gi 442626414 477 LDEKN-ALTQELEKARKVAEELHHEKSEIMKelSKTRLE 514
Cdd:TIGR02168 984 LGPVNlAAIEEYEELKERYDFLTAQKEDLTE--AKETLE 1020
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
29-522 |
3.16e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.78 E-value: 3.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 29 ANFEQLMVSMLDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQinANLPQEFATLTKELTQARETLLERDEEIGE 108
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKEL--KEKAEEYIKLSEFYEEYLDELREIEKRLSR 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 109 LKAERNNTRLLLEHLECLVSRherslrmtvVKRQAAAQSGVSSEVEVLKALKSLFEHHKALD---EKVRERLR-LSIEKN 184
Cdd:PRK03918 319 LEEEINGIEERIKELEEKEER---------LEELKKKLKELEKRLEELEERHELYEEAKAKKeelERLKKRLTgLTPEKL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 185 NMMEEELSSAKEELaqykagvvpagvgsgsgagsaattaggGGAENGLKEKMAGVGGSGGVNGEA-NELNDYAAKT---- 259
Cdd:PRK03918 390 EKELEELEKAKEEI---------------------------EEEISKITARIGELKKEIKELKKAiEELKKAKGKCpvcg 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 260 -----HELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCK-----AQDQCAKLQRDLRE-----NVAQKED 324
Cdd:PRK03918 443 relteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKeseliKLKELAEQLKELEEklkkyNLEELEK 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 325 QEERITTLEKRYLNAQRESTSLHDLNEKLEqELRHKEAQLklhEEKIGAIEEKLELSEQKLAqhaKLQPDMEEQLKARME 404
Cdd:PRK03918 523 KAEEYEKLKEKLIKLKGEIKSLKKELEKLE-ELKKKLAEL---EKKLDELEEELAELLKELE---ELGFESVEELEERLK 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 405 ALTKAQERHGSA----------EDRIRGLETNLDEKTNEVVRLNQRLKMNEEhnlRLSSTVDKLLSESNERLQVHLKERM 474
Cdd:PRK03918 596 ELEPFYNEYLELkdaekelereEKELKKLEEELDKAFEELAETEKRLEELRK---ELEELEKKYSEEEYEELREEYLELS 672
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 442626414 475 HALDEKNALTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQL 522
Cdd:PRK03918 673 RELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKAL 720
|
|
| SAM_liprin-beta1,2_repeat1 |
cd09563 |
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
942-1006 |
5.14e-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: 59.16 E-value: 5.14e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442626414 942 FALWNGPTIVAWL-ELWVGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQ 1006
Cdd:cd09563 1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
37-408 |
5.74e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.40 E-value: 5.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 37 SMLDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINAnLPQEFATLTKELTQARETLLERDEEIGELKAErnnt 116
Cdd:TIGR02169 685 GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ-LEQEEEKLKERLEELEEDLSSLEQEIENVKSE---- 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 117 rllLEHLECLVSRHERSLrmtvVKRQAA--------AQSGVSsevEVLKALKSLFEHHKALDEKVRErLRLSIEKNNMME 188
Cdd:TIGR02169 760 ---LKELEARIEELEEDL----HKLEEAlndlearlSHSRIP---EIQAELSKLEEEVSRIEARLRE-IEQKLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 189 EELSSAKEELAQYKagvvpagvgsgsgagsaattaggggaeNGLKEKMAgvggsggvnGEANELNDYAAKTHELQTIIEK 268
Cdd:TIGR02169 829 EYLEKEIQELQEQR---------------------------IDLKEQIK---------SIEKEIENLNGKKEELEEELEE 872
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 269 QTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQRESTSLHD 348
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS 952
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626414 349 LnEKLEQELRHKEAQL-KLHEEKIGAIEE----KLELSEQKlAQHAKLQPDmEEQLKARMEALTK 408
Cdd:TIGR02169 953 L-EDVQAELQRVEEEIrALEPVNMLAIQEyeevLKRLDELK-EKRAKLEEE-RKAILERIEEYEK 1014
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
277-683 |
1.13e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.23 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 277 QRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQRESTSLHDLNEKLEQE 356
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 357 LRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKAQERH-------GSAEDRIRGLETNLDE 429
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtllneeaANLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 430 KTNEVVRLNQRLKMNEEHNLRLSSTVDKL---LSESNERLQVHLKERMHALDEKNALTQELEKARKVAEELHHEKSEIMK 506
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELeelIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 507 ELSKTRLEIENFKRQL--LQQEIAYNIQqtealtrslspssvvdpsgafsrsnshasfethslrrqskqRLSEEnalvrs 584
Cdd:TIGR02168 916 ELEELREKLAQLELRLegLEVRIDNLQE-----------------------------------------RLSEE------ 948
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 585 maeqeweklqqaahaqqqaYELAsaadcddsdvlyaaatdmmspsghtdaqtlammlqeqLDAINNEIRLIQEEKQSTEA 664
Cdd:TIGR02168 949 -------------------YSLT-------------------------------------LEEAEALENKIEDDEEEARR 972
|
410
....*....|....*....
gi 442626414 665 RAEELESRVGSLEHVNLLA 683
Cdd:TIGR02168 973 RLKRLENKIKELGPVNLAA 991
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
36-497 |
2.83e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.70 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 36 VSMLDERDKLMDSLREAQERLNETENKLRDVEKERdslqrqinanLPQEFATLTKELTQARETLLERDEEIGELKAERNN 115
Cdd:PRK03918 354 LEELEERHELYEEAKAKKEELERLKKRLTGLTPEK----------LEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 116 TRLLLEHLE-----CLVSRHERS--LRMTVVKRQAAAQSGVSSEVEVLKALKslfehhkaldEKVRERLRlSIEKNNMME 188
Cdd:PRK03918 424 LKKAIEELKkakgkCPVCGRELTeeHRKELLEEYTAELKRIEKELKEIEEKE----------RKLRKELR-ELEKVLKKE 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 189 EELSSAKEELAQYKAgvvpagvgsgsgagsaattaggggaengLKEKMagvggsggvngEANELNDYAAKTHELQTIIEK 268
Cdd:PRK03918 493 SELIKLKELAEQLKE----------------------------LEEKL-----------KKYNLEELEKKAEEYEKLKEK 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 269 qTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRE-NVAQKEDQEERITTLEKRYlnaqRESTSLH 347
Cdd:PRK03918 534 -LIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEElGFESVEELEERLKELEPFY----NEYLELK 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 348 DLneklEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLaqhaklqpdmeEQLKARMEALTKAqerhgSAEDRIRGLETNL 427
Cdd:PRK03918 609 DA----EKELEREEKELKKLEEELDKAFEELAETEKRL-----------EELRKELEELEKK-----YSEEEYEELREEY 668
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 428 DEKTNEVVRLNQRLKMNEEHNLRLSSTVDKllsesnerlqvhLKERMHALDEKNALTQELEKARKVAEEL 497
Cdd:PRK03918 669 LELSRELAGLRAELEELEKRREEIKKTLEK------------LKEELEEREKAKKELEKLEKALERVEEL 726
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
39-467 |
3.57e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.40 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 39 LDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINA-NLPQEFATLTKELTQARETLLERDEEIGELKAERNNTR 117
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKlEKLLQLLPLYQELEALEAELAELPERLEELEERLEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 118 LLLEHLECLVSRHERslrmtvvKRQAAAQSGVSSEVEVLKALKSLFEHHKALDEKVRErLRLSIEKNnmmEEELSSAKEE 197
Cdd:COG4717 160 ELEEELEELEAELAE-------LQEELEELLEQLSLATEEELQDLAEELEELQQRLAE-LEEELEEA---QEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 198 LAQYKAGVVPAGVGSGSGAGS--------------AATTAGGGGAENGLKEKMAGVGGSGGVNGEANELNDYAAKTHELQ 263
Cdd:COG4717 229 LEQLENELEAAALEERLKEARlllliaaallallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 264 TIIEKQTSELSQWQRRVSDL----NNKISELEENMSRVQkEHCKAQDQCAKLQRDLRENVAQKEDQE-------ERITTL 332
Cdd:COG4717 309 ALPALEELEEEELEELLAALglppDLSPEELLELLDRIE-ELQELLREAEELEEELQLEELEQEIAAllaeagvEDEEEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 333 EKRYLNAQREstslhdlnEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKlaqhAKLQpDMEEQLKARMEALTKAQER 412
Cdd:COG4717 388 RAALEQAEEY--------QELKEELEELEEQLEELLGELEELLEALDEEELE----EELE-ELEEELEELEEELEELREE 454
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 442626414 413 HGSAEDRIRGLETN--LDEKTNEVVRLNQRLKMNEEHNLRLsSTVDKLLSESNERLQ 467
Cdd:COG4717 455 LAELEAELEQLEEDgeLAELLQELEELKAELRELAEEWAAL-KLALELLEEAREEYR 510
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
40-536 |
4.71e-10 |
|
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: 63.89 E-value: 4.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 40 DERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINaNLPQEFATLTKELTQARETLLERDEEIGELKAERNNTRLL 119
Cdd:TIGR04523 124 VELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYN-DLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 120 LEHLECLVSRHeRSLRMTVVKrqaaAQSGVSSEVEVLKALKSLFEHHKALDEKVRERLRLSIEKNNMMEEELSSAKEELA 199
Cdd:TIGR04523 203 LSNLKKKIQKN-KSLESQISE----LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 200 QYKAgvvpagvgsgsgagsaattaGGGGAENGLKEkmagvggsggVNGEANELNDYAAK--THELQTIIEKQ-------T 270
Cdd:TIGR04523 278 QNNK--------------------KIKELEKQLNQ----------LKSEISDLNNQKEQdwNKELKSELKNQekkleeiQ 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 271 SELSQWQRRVSDLNNKISELEE-------NMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQRES 343
Cdd:TIGR04523 328 NQISQNNKIISQLNEQISQLKKeltnsesENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLN 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 344 TSLHDLNEKLEQELRHKEAQLKLHEEKIgaIEEKLELSEQKLAQHAKlqpdmeEQLKARMEALTKAQERHGSA-EDRIRG 422
Cdd:TIGR04523 408 QQKDEQIKKLQQEKELLEKEIERLKETI--IKNNSEIKDLTNQDSVK------ELIIKNLDNTRESLETQLKVlSRSINK 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 423 LETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESNErlqvhLKERMHALD-EKNALTQELE---------KARK 492
Cdd:TIGR04523 480 IKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS-----LKEKIEKLEsEKKEKESKISdledelnkdDFEL 554
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 442626414 493 VAEELHHEKSEIMKELSKTRLEIENFKRQllQQEIAYNIQQTEA 536
Cdd:TIGR04523 555 KKENLEKEIDEKNKEIEELKQTQKSLKKK--QEEKQELIDQKEK 596
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
248-524 |
5.65e-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: 5.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 248 EANELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQdQCAKLQRDLRE-----NVAQK 322
Cdd:TIGR02169 154 ERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREyegyeLLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 323 EDQEERITTLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQL--------KLHEEKIGAIEEKLELSEQKLAQHAKLQPD 394
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLeelnkkikDLGEEEQLRVKEKIGELEAEIASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 395 MEEQLKARMEALTKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLK-----MN------EEHNLRLSSTVDKL----- 458
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAelkeeLEdlraelEEVDKEFAETRDELkdyre 392
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442626414 459 -LSESNERLQVHLKERMHALDEKNALTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQLLQ 524
Cdd:TIGR02169 393 kLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ 459
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
312-556 |
1.31e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 312 QRDLRENVAQKEDQEERITTLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQhakL 391
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE---L 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 392 QPDMEEQlKARMEALTKAQERHGSAEdrirglETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKlLSESNERLQVHLK 471
Cdd:COG4942 96 RAELEAQ-KEELAELLRALYRLGRQP------PLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE-LRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 472 ERMHALDEKNALTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQLLQQEIAYNiQQTEALTRSLSPSSVVDPSG 551
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE-ALIARLEAEAAAAAERTPAA 246
|
....*
gi 442626414 552 AFSRS 556
Cdd:COG4942 247 GFAAL 251
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
250-542 |
3.87e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.19 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 250 NELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERI 329
Cdd:TIGR04523 61 KNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 330 TTLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAqhaklqpdmeeQLKARMEALTKA 409
Cdd:TIGR04523 141 DKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLL-----------KLELLLSNLKKK 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 410 QERHGSAEDRIRGLETNLDEKTNEVVRLNQRLkmnEEHNLRLSSTVDKL--LSESNERLQVHLKERMHALDEKNALTQEL 487
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEI---NEKTTEISNTQTQLnqLKDEQNKIKKQLSEKQKELEQNNKKIKEL 286
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626414 488 EKARKVA----EELHHEKSE-IMKELSKtrlEIENFKRQL--LQQEIAYNIQQTEALTRSLS 542
Cdd:TIGR04523 287 EKQLNQLkseiSDLNNQKEQdWNKELKS---ELKNQEKKLeeIQNQISQNNKIISQLNEQIS 345
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
249-446 |
3.94e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.16 E-value: 3.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 249 ANELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEER 328
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 329 ITTLEKRY-------------------------LNAQRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQ 383
Cdd:COG4942 99 LEAQKEELaellralyrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442626414 384 KLAQHAKLQPDMEEQLKARMEALTKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEE 446
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
40-528 |
4.26e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.82 E-value: 4.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 40 DERDKLMDSLREAQERLNETENK---LRDVEKERDSLQRQInANLPQEFATLTKELTQARETLLERDEEIGELKAERNNT 116
Cdd:PRK02224 227 EQREQARETRDEADEVLEEHEERreeLETLEAEIEDLRETI-AETEREREELAEEVRDLRERLEELEEERDDLLAEAGLD 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 117 RL----LLEHLECLVSRHErSLRMTVVKRQAAAQsgvssevEVLKALKSLFEHHKALDEKVRErLRlsiEKNNMMEEELS 192
Cdd:PRK02224 306 DAdaeaVEARREELEDRDE-ELRDRLEECRVAAQ-------AHNEEAESLREDADDLEERAEE-LR---EEAAELESELE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 193 SAKEELAQYkagvvpagvgsgsgagsaattaggggaenglKEKMAGVGGSGGVNGEAneLNDYAAKTHELQTIIEKQTSE 272
Cdd:PRK02224 374 EAREAVEDR-------------------------------REEIEELEEEIEELRER--FGDAPVDLGNAEDFLEELREE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 273 LSQWQRRVSDLNNKISELEENMSrvQKEHCKAQDQCAKLQRDLREN--VAQKEDQEERITTLEKRYLNAQRESTslhDLN 350
Cdd:PRK02224 421 RDELREREAELEATLRTARERVE--EAEALLEAGKCPECGQPVEGSphVETIEEDRERVEELEAELEDLEEEVE---EVE 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 351 EKLEQELRHKEAqlklhEEKIGAIEEKLELSEQKLAQH-AKLQPDME--EQLKARMEAL-TKAQERHGSAEDrirgLETN 426
Cdd:PRK02224 496 ERLERAEDLVEA-----EDRIERLEERREDLEELIAERrETIEEKREraEELRERAAELeAEAEEKREAAAE----AEEE 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 427 LDEKTNEVVRLNQRLKMNEE--HNLRLSSTVDKLLSESNERLQvHLKERMHALDEKNaltqelEKARKVAEELHHEKSEI 504
Cdd:PRK02224 567 AEEAREEVAELNSKLAELKEriESLERIRTLLAAIADAEDEIE-RLREKREALAELN------DERRERLAEKRERKREL 639
|
490 500
....*....|....*....|....
gi 442626414 505 MKELSKTRLEIENFKRQLLQQEIA 528
Cdd:PRK02224 640 EAEFDEARIEEAREDKERAEEYLE 663
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
49-542 |
4.75e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.82 E-value: 4.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 49 LREAQERLNETENKLRDVEKERDSLQRQINANLPQ-EFATLTKELTQARETLLERDEEIGELKAERNNTRLLLEHLECLV 127
Cdd:PRK02224 164 LEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEkEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 128 SRHERSLrmtvvkrqaaaqsgvsSEVEVLKALKSLFEHHKALDEKVRERLRLSIEKNNMMEEELSSAKEELAqykagvvp 207
Cdd:PRK02224 244 EEHEERR----------------EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLL-------- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 208 agvgsgsgagsaattaggggAENGLkekmagvggsggvngEANELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKI 287
Cdd:PRK02224 300 --------------------AEAGL---------------DDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEA 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 288 SELEENMSRVQKEHCKAQDQCAKLQ-------RDLRENVAQKEDQEERITTLEKRYLNAQRESTSLHDLNEKLEQELRHK 360
Cdd:PRK02224 345 ESLREDADDLEERAEELREEAAELEseleearEAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDEL 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 361 EAQLKLHEEKIGAIEEKLELSEQKLAQ--------------HAKLQPDMEEQLKARMEALTKAQERHGSAEDRIRGLETn 426
Cdd:PRK02224 425 REREAELEATLRTARERVEEAEALLEAgkcpecgqpvegspHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED- 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 427 LDEKTNEVVRLNQRLKmneehnlrlssTVDKLLSESNERLQvhlkERMHALDEKNALTQELEKArkvAEELHHEKSEIMK 506
Cdd:PRK02224 504 LVEAEDRIERLEERRE-----------DLEELIAERRETIE----EKRERAEELRERAAELEAE---AEEKREAAAEAEE 565
|
490 500 510
....*....|....*....|....*....|....*.
gi 442626414 507 ELSKTRLEIENFKRQLlqQEIAYNIQQTEALTRSLS 542
Cdd:PRK02224 566 EAEEAREEVAELNSKL--AELKERIESLERIRTLLA 599
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
255-531 |
1.60e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.31 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 255 YAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERIttlek 334
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL----- 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 335 rylnaqrestslhdlnEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQ-HAKLQPDMEEQLKARMEALtkaQERH 413
Cdd:TIGR02169 747 ----------------SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlEARLSHSRIPEIQAELSKL---EEEV 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 414 GSAEDRIRGLETNLDEKTNEVVRLNQrlKMNEEHNLRLSSTVDKllsesnerlqVHLKERMHALD-EKNALTQELEKARK 492
Cdd:TIGR02169 808 SRIEARLREIEQKLNRLTLEKEYLEK--EIQELQEQRIDLKEQI----------KSIEKEIENLNgKKEELEEELEELEA 875
|
250 260 270
....*....|....*....|....*....|....*....
gi 442626414 493 VAEELHHEKSEIMKELSKTRLEIENFKRQLLQQEIAYNI 531
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEK 914
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
251-510 |
1.76e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 251 ELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERIT 330
Cdd:TIGR02168 268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 331 TLEKrylnaqrESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQpdmeEQLKARMEALTKAQ 410
Cdd:TIGR02168 348 ELKE-------ELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI----ERLEARLERLEDRR 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 411 ERhgsAEDRIRGLETNLDEKTNEVV--RLNQRLKMNEEHNLRLSSTVDKL--LSESNERLQVHLKERMHALDEKNALTQE 486
Cdd:TIGR02168 417 ER---LQQEIEELLKKLEEAELKELqaELEELEEELEELQEELERLEEALeeLREELEEAEQALDAAERELAQLQARLDS 493
|
250 260
....*....|....*....|....
gi 442626414 487 LEKARKVAEELHHEKSEIMKELSK 510
Cdd:TIGR02168 494 LERLQENLEGFSEGVKALLKNQSG 517
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
55-530 |
3.24e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 55 RLNETENKLRDVEkERDSLQRQI-------NA--NLpQEFATLTKELTQARETLLERDEEIGELKaeRNNTRLLLEHLec 125
Cdd:PRK03918 133 RQGEIDAILESDE-SREKVVRQIlglddyeNAykNL-GEVIKEIKRRIERLEKFIKRTENIEELI--KEKEKELEEVL-- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 126 lvsrHERSLRMTVVKRQAAAQSGVSSEVEVLKALKSLFEHHKALDEKVRERLRLSIEKNNMMEEELSSAKEELAQYKAGV 205
Cdd:PRK03918 207 ----REINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 206 vpagvgsgsgagsaattAGGGGAENGLKEKMAGVGGSGGVNGEANELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNN 285
Cdd:PRK03918 283 -----------------KELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKK 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 286 KISELEENMSRVQKEHckaqdqcaKLQRDLRENVAQKEDQEERIT-----TLEKRYLNAQRESTSLHDLNEKLEQ---EL 357
Cdd:PRK03918 346 KLKELEKRLEELEERH--------ELYEEAKAKKEELERLKKRLTgltpeKLEKELEELEKAKEEIEEEISKITArigEL 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 358 RHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLqpDMEEQLKARMEALTKAQERHGSAEDRIRGLETNLD---EKTNEV 434
Cdd:PRK03918 418 KKEIKELKKAIEELKKAKGKCPVCGRELTEEHRK--ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEkvlKKESEL 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 435 VRLNQRLKMNEEHNLRLSSTVDKLLSESNERLQvHLKERMHAL-----------DEKNALTQELEKARKVAEELHHEKSE 503
Cdd:PRK03918 496 IKLKELAEQLKELEEKLKKYNLEELEKKAEEYE-KLKEKLIKLkgeikslkkelEKLEELKKKLAELEKKLDELEEELAE 574
|
490 500
....*....|....*....|....*...
gi 442626414 504 IMKELSKTRLE-IENFKRQLLQQEIAYN 530
Cdd:PRK03918 575 LLKELEELGFEsVEELEERLKELEPFYN 602
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
326-473 |
4.18e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 55.32 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 326 EERITTLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKlqpdmEEQLKARMEA 405
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN-----NKEYEALQKE 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442626414 406 LTKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESNERLQVHLKER 473
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
30-663 |
6.70e-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: 57.05 E-value: 6.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 30 NFEQLMVSMLDERDKLMDSLREAQERLNETENKLRDVEKERDSlQRQINANLPQEFATltkELTQARETLLERDEEIGEL 109
Cdd:pfam15921 114 DLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEA-AKCLKEDMLEDSNT---QIEQLRKMMLSHEGVLQEI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 110 KA-----ERNNTRLLLEHlECLVSRHERSLRMTVVKrqaaaqsgvsseveVLKALKSLFEHHKALDEKVRERLR-LSIEK 183
Cdd:pfam15921 190 RSilvdfEEASGKKIYEH-DSMSTMHFRSLGSAISK--------------ILRELDTEISYLKGRIFPVEDQLEaLKSES 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 184 NNMMEEELSSAKEELAQYKAgvvpagVGSGSGAGSAATTAGGGGAENGLKEKMAGVGGSGGvngeaNELNDYAAKTHELQ 263
Cdd:pfam15921 255 QNKIELLLQQHQDRIEQLIS------EHEVEITGLTEKASSARSQANSIQSQLEIIQEQAR-----NQNSMYMRQLSDLE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 264 TIIEKQTSELSQWQRRVSDlnnKISELEENMSRVQKEHCKAQ--------------DQCAKLQRDLRENVAQKEDQEERI 329
Cdd:pfam15921 324 STVSQLRSELREAKRMYED---KIEELEKQLVLANSELTEARterdqfsqesgnldDQLQKLLADLHKREKELSLEKEQN 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 330 TTLEKRYLNaqrESTSLHDLNEKLEQ---ELRHKEAQLKL--------HEEKIGAIEEKLELSEQKLAQHAKLQpDMEEQ 398
Cdd:pfam15921 401 KRLWDRDTG---NSITIDHLRRELDDrnmEVQRLEALLKAmksecqgqMERQMAAIQGKNESLEKVSSLTAQLE-STKEM 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 399 LKARMEALTKAQERHGSAEDRIRGLETNLDEK------TN-EVVRLNQRLKMNEEHNLRLSSTVDKLLSESNE----RLQ 467
Cdd:pfam15921 477 LRKVVEELTAKKMTLESSERTVSDLTASLQEKeraieaTNaEITKLRSRVDLKLQELQHLKNEGDHLRNVQTEcealKLQ 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 468 VHLKERMHAL--DEKNALTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKrqLLQQEIAYNIQQTEALTRSLSPSS 545
Cdd:pfam15921 557 MAEKDKVIEIlrQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFK--ILKDKKDAKIRELEARVSDLELEK 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 546 V--VDPSGAFSRSNSHASFETHSLRRQSKQRLSEENALvrsmaEQEWEKLQQAAHAQQQAYE-----LASAADCDDSDVL 618
Cdd:pfam15921 635 VklVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSL-----SEDYEVLKRNFRNKSEEMEtttnkLKMQLKSAQSELE 709
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 442626414 619 YAAAT--DMMSPSGHtdAQTLAMMLQEQLDAINNEIRLIQEEKQSTE 663
Cdd:pfam15921 710 QTRNTlkSMEGSDGH--AMKVAMGMQKQITAKRGQIDALQSKIQFLE 754
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
257-677 |
6.78e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 6.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 257 AKTHELQTIIEkQTSELSQWQRRVSDLNNKISELEENMSRV---------QKEHCKAQDQCAKLQRDLREnvaQKEDQEE 327
Cdd:TIGR02168 152 AKPEERRAIFE-EAAGISKYKERRKETERKLERTRENLDRLedilnelerQLKSLERQAEKAERYKELKA---ELRELEL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 328 RITTLEkrylnaqrestsLHDLNEKLEQelrhKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLkarmealT 407
Cdd:TIGR02168 228 ALLVLR------------LEELREELEE----LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEI-------E 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 408 KAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKL---LSESNERLQVhLKERMHALDEKNAlt 484
Cdd:TIGR02168 285 ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELaeeLAELEEKLEE-LKEELESLEAELE-- 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 485 qELEKARKVAEELHHEKSEIMKELSKTRLEIENfKRQLLQQEIAYNIQQTEALTRSLspssvvdpsgafsrsnshasfet 564
Cdd:TIGR02168 362 -ELEAELEELESRLEELEEQLETLRSKVAQLEL-QIASLNNEIERLEARLERLEDRR----------------------- 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 565 hslrrqskQRLSEENALVRsMAEQEWEKLQQAAHAQQQAYELASAADCDDSdvlyaaatdmmspsghtdaqtlammLQEQ 644
Cdd:TIGR02168 417 --------ERLQQEIEELL-KKLEEAELKELQAELEELEEELEELQEELER-------------------------LEEA 462
|
410 420 430
....*....|....*....|....*....|...
gi 442626414 645 LDAINNEIRLIQEEKQSTEARAEELESRVGSLE 677
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQARLDSLE 495
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
19-427 |
9.76e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 9.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 19 QRSSQFSGEDANFEQLMVSMLDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINANLpQEFATLTKELTQARET 98
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE-EEEEALLELLAELLEE 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 99 LLERDEEIGELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAAAQSGVSSEVEVLKALKSLFEhhKALDEKVRERLR 178
Cdd:COG1196 472 AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYE--AALEAALAAALQ 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 179 LSIEKNnmmEEELSSAKEELAQYKAGVVpagvgsgsgagsAATTAGGGGAENGLKEKMAGVGGSGGVNGEANELNDYAAK 258
Cdd:COG1196 550 NIVVED---DEVAAAAIEYLKAAKAGRA------------TFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADAR 614
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 259 THELQTIIEKQTSE---LSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERittLEKR 335
Cdd:COG1196 615 YYVLGDTLLGRTLVaarLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAER---LAEE 691
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 336 YLNAQRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKAQERHGS 415
Cdd:COG1196 692 ELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER 771
|
410
....*....|...
gi 442626414 416 AEDRIRGLET-NL 427
Cdd:COG1196 772 LEREIEALGPvNL 784
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
44-678 |
1.24e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 56.13 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 44 KLMDSLREAQERLNETENKLRDVEK---ERDSLQRQINANLP--QEFATLTKELTQARETL------------LERDEEI 106
Cdd:TIGR00618 226 KELKHLREALQQTQQSHAYLTQKREaqeEQLKKQQLLKQLRAriEELRAQEAVLEETQERInrarkaaplaahIKAVTQI 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 107 gELKAERNNTRLllehleclvSRHERSLRMTVVKRQAAAQSGVSSEvEVLKALKSLFEHHkaldekvrERLRLSIEKNNM 186
Cdd:TIGR00618 306 -EQQAQRIHTEL---------QSKMRSRAKLLMKRAAHVKQQSSIE-EQRRLLQTLHSQE--------IHIRDAHEVATS 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 187 MEEELSSAKEELAQYKAgvvpagvgsgsgagSAATTAGGGGAENGLKEKMagvggsggvngeanelndyaAKTHELQTII 266
Cdd:TIGR00618 367 IREISCQQHTLTQHIHT--------------LQQQKTTLTQKLQSLCKEL--------------------DILQREQATI 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 267 EKQTSELSQWQRRVSDLNNKIsELEENMSRVQKEHCKAQDQCAKL----QRDLRENVAQKEDQEERITTLEKRYlnAQRE 342
Cdd:TIGR00618 413 DTRTSAFRDLQGQLAHAKKQQ-ELQQRYAELCAAAITCTAQCEKLekihLQESAQSLKEREQQLQTKEQIHLQE--TRKK 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 343 STSLHDLNEKLEQELRHKEAQLKLHEEKI-----GAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKAQERHGSAE 417
Cdd:TIGR00618 490 AVVLARLLELQEEPCPLCGSCIHPNPARQdidnpGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQ 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 418 D-------RIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESNERL---QVHLKERMHALDEKNALTQEL 487
Cdd:TIGR00618 570 QsfsiltqCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQdlqDVRLHLQQCSQELALKLTALH 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 488 EKARKVAEELHHEKSEIMKELSKTRLEIENFKRQLLQQEIAYNIQQTEALTRSLS-PSSVVDPSGAFSRSNSHASFETHS 566
Cdd:TIGR00618 650 ALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTlLRELETHIEEYDREFNEIENASSS 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 567 LRRQSKQRLSEENALVRSMAEQEWEKLQQAAHAQQQAYELASAADCDDSDVLYAAAT-----DMMSPSGHTDAQTLAMML 641
Cdd:TIGR00618 730 LGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEiqffnRLREEDTHLLKTLEAEIG 809
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 442626414 642 Q---EQLDAINNEIRLIQEEKQSTEARAEELESRVGSLEH 678
Cdd:TIGR00618 810 QeipSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITH 849
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
248-440 |
1.75e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 248 EANELNDYAAKTHELQTIIEKQTSELSQW--QRRVSDLNNKISELEEnmsrvqkehckaqdQCAKLQRDLRENVAQKEDQ 325
Cdd:COG4913 256 PIRELAERYAAARERLAELEYLRAALRLWfaQRRLELLEAELEELRA--------------ELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 326 EERITTLEKRYLNAQ-RESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARME 404
Cdd:COG4913 322 REELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELE 401
|
170 180 190
....*....|....*....|....*....|....*.
gi 442626414 405 ALtkaQERHGSAEDRIRGLETNLDEKTNEVVRLNQR 440
Cdd:COG4913 402 AL---EEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
942-1008 |
2.74e-07 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 48.83 E-value: 2.74e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442626414 942 FALWNGPTIVAWLELWvGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 1008
Cdd:smart00454 1 VSQWSPESVADWLESI-GLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
37-474 |
2.76e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.05 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 37 SMLDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQI------NANLPQEFATLTKELTQARETLLER-------D 103
Cdd:PRK02224 311 AVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDAddleerAEELREEAAELESELEEAREAVEDRreeieelE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 104 EEIGELKAERNNTRLLLE----HLECLVSRHERslrmtVVKRQAAAQSGVSSEVEVLKALKSLFE--------------- 164
Cdd:PRK02224 391 EEIEELRERFGDAPVDLGnaedFLEELREERDE-----LREREAELEATLRTARERVEEAEALLEagkcpecgqpvegsp 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 165 HHKALDEKVRERLRLSIEKNNmMEEELSSAKEELAQYKAGVVPAGVGSGSGAGSAATTAGGGGAENGLKEKmagVGGSGG 244
Cdd:PRK02224 466 HVETIEEDRERVEELEAELED-LEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEK---RERAEE 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 245 VNGEANELNDYAAKTHELQTiieKQTSELSQWQRRVSDLNNKISELEENMSRVqkehckaqdqcaklqRDLRENVAQKED 324
Cdd:PRK02224 542 LRERAAELEAEAEEKREAAA---EAEEEAEEAREEVAELNSKLAELKERIESL---------------ERIRTLLAAIAD 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 325 QEERITTL-EKRYLNAQRESTSLHDLNEKLEqelRHKEAQLKLHEEKIGAIEEKLELSEQKLAQhaklqpdMEEQLKARM 403
Cdd:PRK02224 604 AEDEIERLrEKREALAELNDERRERLAEKRE---RKRELEAEFDEARIEEAREDKERAEEYLEQ-------VEEKLDELR 673
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442626414 404 EALTKAQERHGSAEDRIRGLEtNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESNERlQVHLKERM 474
Cdd:PRK02224 674 EERDDLQAEIGAVENELEELE-ELRERREALENRVEALEALYDEAEELESMYGDLRAELRQR-NVETLERM 742
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
41-492 |
3.23e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 41 ERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINANLpQEFATLTKELTQARETLLERDEEIGELKAERNNTRLLL 120
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE-EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 121 EHLEclvsRHERSLRMTVVKRQAAAQSGVSSEVEVLKALKSLFEHHKALDEKVRERLRLSIEKNNMMEEELSSAKEELAQ 200
Cdd:COG1196 403 EELE----EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 201 YKAGVVPAGVGSGSGAGSAATTAGGGGAENGLKEKMAGVGGSGGVNGEANELND-----YAAKTHELQTIIEKQTSELSQ 275
Cdd:COG1196 479 LAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVeaayeAALEAALAAALQNIVVEDDEV 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 276 WQRRVSDLNNK----ISELEENMSRVQKEHCKAQDQCAKLQRdlRENVAQKEDQEERITTLEKRYLNAQRESTSLHDLNE 351
Cdd:COG1196 559 AAAAIEYLKAAkagrATFLPLDKIRARAALAAALARGAIGAA--VDLVASDLREADARYYVLGDTLLGRTLVAARLEAAL 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 352 KLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKAQERhgsAEDRIRGLETNLDEKT 431
Cdd:COG1196 637 RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEE---ALLAEEEEERELAEAE 713
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442626414 432 NEVVRLNQRLKMNEEHNLRLSSTVDKLLSESNERLQVHLKERMHALDEKNALTQELEKARK 492
Cdd:COG1196 714 EERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER 774
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
1115-1185 |
3.32e-07 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 48.42 E-value: 3.32e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442626414 1115 VLVWSNERVIRWVGSIGLKEYANNLLESGVHGGLMALdeGFDANAMGlalQIPTQNAQARQILDTEFNNLL 1185
Cdd:pfam07647 1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK---RLGITSVGHRRKILKKIQELK 66
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
287-515 |
5.36e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 5.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 287 ISELEENM---SRVQKEHCKAQDQCAKLQ------RDLRENVAQKEDQEERITTLekRYLNAQRESTSLHDLNEKLEQEL 357
Cdd:COG4913 227 ADALVEHFddlERAHEALEDAREQIELLEpirelaERYAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 358 RHKEAQLKLHEEKIGAIEEKLELSEQKLAQH--AKLQpDMEEQLKARMEALTKAQERHGSAEDRIRGLETNLDEKTNEVV 435
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQIRGNggDRLE-QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 436 RLNQRLKmneehnlRLSSTVDKLLSESNERLQVHLKERMHALDEKNALTQELE--KARK--VAEELHHEKSEIMKELSKT 511
Cdd:COG4913 384 ALRAEAA-------ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAslERRKsnIPARLLALRDALAEALGLD 456
|
....
gi 442626414 512 RLEI 515
Cdd:COG4913 457 EAEL 460
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
93-424 |
5.66e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 5.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 93 TQARETLLERDEEIGELKAERNNTRLLLEHLECLVsrHERSLRMTVVKRQAAAqsgVSSEVEVLKAlkslfEHhkaldEK 172
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRL--DELSQELSDASRKIGE---IEKEIEQLEQ-----EE-----EK 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 173 VRERLRLSIEKNNMMEEELSSAKEELAQYkAGVVPAGVGSGSGAGSAATTAGGGGAENGLKEKMAgvggsggvngEANEL 252
Cdd:TIGR02169 735 LKERLEELEEDLSSLEQEIENVKSELKEL-EARIEELEEDLHKLEEALNDLEARLSHSRIPEIQA----------ELSKL 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 253 NDYAAK----THELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEER 328
Cdd:TIGR02169 804 EEEVSRiearLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 329 ITTLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQhakLQPDMEEQLKARmealtK 408
Cdd:TIGR02169 884 LGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE---DEEIPEEELSLE-----D 955
|
330
....*....|....*.
gi 442626414 409 AQERHGSAEDRIRGLE 424
Cdd:TIGR02169 956 VQAELQRVEEEIRALE 971
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
261-421 |
6.19e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.85 E-value: 6.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 261 ELQTIIEKQT--SELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKR--- 335
Cdd:COG1579 5 DLRALLDLQEldSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgn 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 336 ------YLNAQRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQH--------AKLQPDMEEQLKA 401
Cdd:COG1579 85 vrnnkeYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKkaeldeelAELEAELEELEAE 164
|
170 180
....*....|....*....|
gi 442626414 402 RMEALTKAQERHGSAEDRIR 421
Cdd:COG1579 165 REELAAKIPPELLALYERIR 184
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
19-522 |
9.09e-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: 53.49 E-value: 9.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 19 QRSSQFSGEDANFEQLMVSMLDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINANlpqefatlTKELTQARET 98
Cdd:TIGR04523 211 QKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK--------QKELEQNNKK 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 99 LLERDEEIGELKAErnntrllLEHLeclvsrherslrmtvvKRQAAAqsgvssevEVLKALKSLFEHHKaldEKVRErLR 178
Cdd:TIGR04523 283 IKELEKQLNQLKSE-------ISDL----------------NNQKEQ--------DWNKELKSELKNQE---KKLEE-IQ 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 179 LSIEKNNmmeEELSSAKEELAQYKagvvpagvgsgsgagsaattaggggaenglKEKMAGVGGSGGVNGEANElndyaaK 258
Cdd:TIGR04523 328 NQISQNN---KIISQLNEQISQLK------------------------------KELTNSESENSEKQRELEE------K 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 259 THELQTIIEKQTS---ELSQWQRRVSDLNNKIS-------ELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEER 328
Cdd:TIGR04523 369 QNEIEKLKKENQSykqEIKNLESQINDLESKIQnqeklnqQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQ 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 329 ITTLEKRY--LNAQRES--TSLHDLN---EKLEQELRHKEAQLKLHEEKIGAI-EEKLELSEQ--KLAQHAKLQPDMEEQ 398
Cdd:TIGR04523 449 DSVKELIIknLDNTRESleTQLKVLSrsiNKIKQNLEQKQKELKSKEKELKKLnEEKKELEEKvkDLTKKISSLKEKIEK 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 399 LKArmEALTKAQERhGSAEDRI---------RGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESNErlqvh 469
Cdd:TIGR04523 529 LES--EKKEKESKI-SDLEDELnkddfelkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKD----- 600
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 442626414 470 LKERMHALDEKNA-LTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQL 522
Cdd:TIGR04523 601 LIKEIEEKEKKISsLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETI 654
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
40-507 |
1.11e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 40 DERDKLMDSLREAQE--RLNETENKLRDVEKERDSLQRQinANLPQEFATLTKELTQARETLLERDEEigELKAERNNTR 117
Cdd:PTZ00121 1299 EEKKKADEAKKKAEEakKADEAKKKAEEAKKKADAAKKK--AEEAKKAAEAAKAEAEAAADEAEAAEE--KAEAAEKKKE 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 118 LLLEHLECLVSRHERSLRMTVVKRQAAAQSGVSSEVEVLKALKSLFEHHKALDEKVR--ERLRLSIEKNNMMEEELSSAK 195
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKkaDEAKKKAEEAKKADEAKKKAE 1454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 196 E----ELAQYKAGVVPAGVGSGSGAGSAATTAGGGGAENGLKEKMAGVGGSGGVNGEANELN--DYAAKTHELQTIIEKQ 269
Cdd:PTZ00121 1455 EakkaEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKkaEEAKKADEAKKAEEAK 1534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 270 TSElsqwQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRD----LRENVAQKEDQEERITTLEKRYlnaqRESTS 345
Cdd:PTZ00121 1535 KAD----EAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDknmaLRKAEEAKKAEEARIEEVMKLY----EEEKK 1606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 346 LHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDmEEQLKARMEALTKAQERHG-------SAED 418
Cdd:PTZ00121 1607 MKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA-EEENKIKAAEEAKKAEEDKkkaeeakKAEE 1685
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 419 RIRGLETNLDEKTNEVVRLNQRLKMNEE-----HNLRLSSTVDKLLSESNERLQVHLKERMHAL----DEKNALTQELEK 489
Cdd:PTZ00121 1686 DEKKAAEALKKEAEEAKKAEELKKKEAEekkkaEELKKAEEENKIKAEEAKKEAEEDKKKAEEAkkdeEEKKKIAHLKKE 1765
|
490
....*....|....*...
gi 442626414 490 ARKVAEELHHEKSEIMKE 507
Cdd:PTZ00121 1766 EEKKAEEIRKEKEAVIEE 1783
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
256-593 |
1.39e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 53.05 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 256 AAKTHELQTIIEKQTSELSQWQRRVSDLNNKIselEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKR 335
Cdd:pfam02463 148 AMMKPERRLEIEEEAAGSRLKRKKKEALKKLI---EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 336 YLNAQRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKAQERHGS 415
Cdd:pfam02463 225 YLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 416 AEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSstvdKLLSESNERLQVHLKERMHALDEKNALTQELEKARKVAE 495
Cdd:pfam02463 305 LERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELE----KELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 496 ELHHEKSEIMKELSKTRLEIENFKRQLLQQEIAYNIQQTEALTRSLSPSSVVDPSGAFSRSNS-HASFETHSLRRQSKQR 574
Cdd:pfam02463 381 LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQgKLTEEKEELEKQELKL 460
|
330
....*....|....*....
gi 442626414 575 LSEENALVRSMAEQEWEKL 593
Cdd:pfam02463 461 LKDELELKKSEDLLKETQL 479
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
17-592 |
1.92e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 52.36 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 17 ISQRSSQFSGEDANFeQLMVSMLDERDKLMDSLREAQERLNETENKLRD--VEKERDSLQRQINANLPQEFATLTKELTQ 94
Cdd:TIGR00606 338 LNQEKTELLVEQGRL-QLQADRHQEHIRARDSLIQSLATRLELDGFERGpfSERQIKNFHTLVIERQEDEAKTAAQLCAD 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 95 ARETLLERDEEIGELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAAAQSgvssevevlkaLKSLFEHHKALDEKVR 174
Cdd:TIGR00606 417 LQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGS-----------SDRILELDQELRKAER 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 175 ErlrLSIEKNNMMEEELSSAKEELAQYKAGVVPAGVGSGSGAGSAATTAGGGGAENGLKEKMAGVGGS-----GGVNGEA 249
Cdd:TIGR00606 486 E---LSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQirkikSRHSDEL 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 250 NELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLREnVAQKEDQEERI 329
Cdd:TIGR00606 563 TSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFD-VCGSQDEESDL 641
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 330 TTLEKRYLNAQRESTSLH---DLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEAL 406
Cdd:TIGR00606 642 ERLKEEIEKSSKQRAMLAgatAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKK 721
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 407 TKAQER-------HGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESN---------ERLQVHL 470
Cdd:TIGR00606 722 EKRRDEmlglapgRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKvcltdvtimERFQMEL 801
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 471 KERMHALDEKNALTQELEKARKVaEELHHEKSEIMKELSKTRLEIE-NFKRQLLQQEIAYNIQQT--EALTRSLSPSSVV 547
Cdd:TIGR00606 802 KDVERKIAQQAAKLQGSDLDRTV-QQVNQEKQEKQHELDTVVSKIElNRKLIQDQQEQIQHLKSKtnELKSEKLQIGTNL 880
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 442626414 548 DPSGAFSRSNSHASFETHSLRRQSKQRLSEENALVRSMAEQEWEK 592
Cdd:TIGR00606 881 QRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEK 925
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
262-677 |
2.31e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.04 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 262 LQTIIEKQTSELSQwqrRVSDLNNKISELEENMSRVQKEhckAQDQCAKLQRDLRENVAQK-EDQEERITTLEKRYLNAQ 340
Cdd:pfam15921 218 LGSAISKILRELDT---EISYLKGRIFPVEDQLEALKSE---SQNKIELLLQQHQDRIEQLiSEHEVEITGLTEKASSAR 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 341 RESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKL--ELSEQKLAQHAKLQpDMEEQLKARMEALTKAQ-------E 411
Cdd:pfam15921 292 SQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLrsELREAKRMYEDKIE-ELEKQLVLANSELTEARterdqfsQ 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 412 RHGSAEDRIRGLETNLDEKTNEvvrlnqrLKMNEEHNLRL-------SSTVDKLLSESNER-----------------LQ 467
Cdd:pfam15921 371 ESGNLDDQLQKLLADLHKREKE-------LSLEKEQNKRLwdrdtgnSITIDHLRRELDDRnmevqrleallkamkseCQ 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 468 VHLKERMHALDEKNaltQELEKARKVAEELHHEKS---EIMKELSKTRLEIENFKRQLlqQEIAYNIQQTEaltRSLSPS 544
Cdd:pfam15921 444 GQMERQMAAIQGKN---ESLEKVSSLTAQLESTKEmlrKVVEELTAKKMTLESSERTV--SDLTASLQEKE---RAIEAT 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 545 SVvDPSGAFSRSNshasfethsLRRQSKQRLSEENALVRSmAEQEWEKLQQAAHAQQQAYElasaadcddsdVLYAAATD 624
Cdd:pfam15921 516 NA-EITKLRSRVD---------LKLQELQHLKNEGDHLRN-VQTECEALKLQMAEKDKVIE-----------ILRQQIEN 573
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 442626414 625 MMSPSGHTDAQTLAMMLQE-QLDAINNEIRLIQEE----KQSTEARAEELESRVGSLE 677
Cdd:pfam15921 574 MTQLVGQHGRTAGAMQVEKaQLEKEINDRRLELQEfkilKDKKDAKIRELEARVSDLE 631
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
287-534 |
2.49e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.06 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 287 ISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQREStslhdlnEKLEQELRHKEAQLKL 366
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL-------EELNEQLQAAQAELAQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 367 HEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEE 446
Cdd:COG4372 99 AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 447 HNLRlsSTVDKLLSESNERLQVH--LKERMHALDEKNALTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQLLQ 524
Cdd:COG4372 179 AEAE--QALDELLKEANRNAEKEeeLAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
250
....*....|
gi 442626414 525 QEIAYNIQQT 534
Cdd:COG4372 257 LKEIEELELA 266
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
32-489 |
2.53e-06 |
|
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: 51.75 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 32 EQLMVSMLDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINaNLPQ-------EFATLTKELTQARETLLERDE 104
Cdd:pfam10174 337 EQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIR-DLKDmldvkerKINVLQKKIENLQEQLRDKDK 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 105 EIGELK-------AERNNTRLLLEHLECLVSRHERslrmtvvkrqaaaqsgvsseveVLKALKslfEHHKALDEKVRERL 177
Cdd:pfam10174 416 QLAGLKervkslqTDSSNTDTALTTLEEALSEKER----------------------IIERLK---EQREREDRERLEEL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 178 RLSIEKNNMMEEELSSAKEELAQYKAGVVPAGVGSGSGAGSAATTAGGGGAENGLKEKmagvggsggVNGEANELNDYAA 257
Cdd:pfam10174 471 ESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQ---------KKEECSKLENQLK 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 258 KTHELQTIiekqtselsqwQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYL 337
Cdd:pfam10174 542 KAHNAEEA-----------VRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTL 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 338 NAQRESTSLHDLNEKLEQELRHKEAQLklheekigaIEEKLELSEQKLAQHAKLQpdMEEQlkarMEALTKAQERHGSAE 417
Cdd:pfam10174 611 RQMKEQNKKVANIKHGQQEMKKKGAQL---------LEEARRREDNLADNSQQLQ--LEEL----MGALEKTRQELDATK 675
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 418 DRIRGLETNLDEKTNEVVRLNQ--------RLKMNEEHNLRLSSTVDK---LLSESNERLQVHLKERMHALDEKNALTQE 486
Cdd:pfam10174 676 ARLSSTQQSLAEKDGHLTNLRAerrkqleeILEMKQEALLAAISEKDAniaLLELSSSKKKKTQEEVMALKREKDRLVHQ 755
|
...
gi 442626414 487 LEK 489
Cdd:pfam10174 756 LKQ 758
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
251-464 |
3.32e-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: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 251 ELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERIT 330
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 331 TLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQhaklqpdMEEQLKARMEALTKAQ 410
Cdd:TIGR02169 396 KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKK-------QEWKLEQLAADLSKYE 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 442626414 411 ERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNlRLSSTVDKLLSESNE 464
Cdd:TIGR02169 469 QELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV-RGGRAVEEVLKASIQ 521
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
251-406 |
3.55e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.54 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 251 ELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEhckaQDQcAKLQRDLRENVAQKEDQEERIT 330
Cdd:COG1579 32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ----LGN-VRNNKEYEALQKEIESLKRRIS 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442626414 331 TLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKL-AQHAKLQPDMEEQLKARMEAL 406
Cdd:COG1579 107 DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELeAEREELAAKIPPELLALYERI 183
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
1038-1092 |
3.64e-06 |
|
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: 45.75 E-value: 3.64e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 442626414 1038 WLPGLGLPQYRTTFMECLVDARMLDHLTKKDLRGQLKMVDSFHRTSLQYGISMLK 1092
Cdd:smart00454 12 WLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
42-536 |
3.83e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 42 RDKLMDSLREAQERL-NETENKLRDVEKERDSLQRQInanlpQEFATLTKELTQARETLLERDEEIGELKAERNNTRLLL 120
Cdd:COG4717 44 RAMLLERLEKEADELfKPQGRKPELNLKELKELEEEL-----KEAEEKEEEYAELQEELEELEEELEELEAELEELREEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 121 EHLECLVSRHERSLRMTVVKRQaaaqsgvssevevlkaLKSLFEHHKALDEKVRERLRLsieknnmmEEELSSAKEELAQ 200
Cdd:COG4717 119 EKLEKLLQLLPLYQELEALEAE----------------LAELPERLEELEERLEELREL--------EEELEELEAELAE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 201 ykagvvpagvgsgsgagsaattaggggaengLKEKMAGVGGSGGVNGEaNELNDYAAKTHELQTIIEKQTSELSQWQRRV 280
Cdd:COG4717 175 -------------------------------LQEELEELLEQLSLATE-EELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 281 SDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDqeeRITTLEKRYLNAQRESTSL-----------HDL 349
Cdd:COG4717 223 EELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGG---SLLSLILTIAGVLFLVLGLlallflllareKAS 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 350 NEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKAQERH--GSAEDRIRGLETNL 427
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELqlEELEQEIAALLAEA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 428 DEKTNEvvRLNQRLKMNEE-HNLRlsstvdKLLSESNERLQVHLKERMHALD--EKNALTQELEKARKVAEELHHEKSEI 504
Cdd:COG4717 380 GVEDEE--ELRAALEQAEEyQELK------EELEELEEQLEELLGELEELLEalDEEELEEELEELEEELEELEEELEEL 451
|
490 500 510
....*....|....*....|....*....|..
gi 442626414 505 MKELSKTRLEIENFKRQLLQQEIAYNIQQTEA 536
Cdd:COG4717 452 REELAELEAELEQLEEDGELAELLQELEELKA 483
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
263-439 |
5.22e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 5.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 263 QTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKR------- 335
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElgerara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 336 ---------YLNAQRESTSLHDLNEKLE----------QELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDME 396
Cdd:COG3883 95 lyrsggsvsYLDVLLGSESFSDFLDRLSalskiadadaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 442626414 397 EQLKARMEALTKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQ 439
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
229-522 |
5.71e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.88 E-value: 5.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 229 ENGLKEKMAGVGGSGGVNGEANELNDYAAKTHELQTIIEKQTSELSQwqrRVSDLNNKISELEENMS--RVQKE------ 300
Cdd:pfam05483 137 EEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQ---VYMDLNNNIEKMILAFEelRVQAEnarlem 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 301 HCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEK--- 377
Cdd:pfam05483 214 HFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKkdh 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 378 ----LELSEQKLAQHAKLQPDMEEQLK--------------ARMEALTKAQERHGSAEDRIRGLETNLDE--KTNEvvrl 437
Cdd:pfam05483 294 ltkeLEDIKMSLQRSMSTQKALEEDLQiatkticqlteekeAQMEELNKAKAAHSFVVTEFEATTCSLEEllRTEQ---- 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 438 nQRLKMNEEHNLRLSSTVDKLLSESNERL------QVHLKERMHALDEKNALTQELEKARKVAEELHHEKSEIMKELSKT 511
Cdd:pfam05483 370 -QRLEKNEDQLKIITMELQKKSSELEEMTkfknnkEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAR 448
|
330
....*....|.
gi 442626414 512 RLEIENFKRQL 522
Cdd:pfam05483 449 EKEIHDLEIQL 459
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
272-536 |
5.98e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.72 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 272 ELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRE-NVAQKEDQEERITTLEKRYLNAQrestslhdln 350
Cdd:COG3096 837 ELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQaNLLADETLADRLEELREELDAAQ---------- 906
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 351 ekleqelrhkEAQ--LKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEE------QLKARMEALTKAQER--HGSAEDRI 420
Cdd:COG3096 907 ----------EAQafIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQakeqqrRLKQQIFALSEVVQRrpHFSYEDAV 976
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 421 RGLETNLDekTNEvvRLNQRLKMNEEHNLRLSSTVDKLLSESNERLQV--HLKERMHA-LDEKNALTQEL---------- 487
Cdd:COG3096 977 GLLGENSD--LNE--KLRARLEQAEEARREAREQLRQAQAQYSQYNQVlaSLKSSRDAkQQTLQELEQELeelgvqadae 1052
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 442626414 488 --EKARKVAEELHHE-------KSEIMKELSKTRLEIENFKRQLLQQEIAYNIQQTEA 536
Cdd:COG3096 1053 aeERARIRRDELHEElsqnrsrRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQV 1110
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
12-516 |
8.85e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.22 E-value: 8.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 12 ISEDSISQRSSQFSGEDANF----EQLMVSMLDERDKLmDSLREAQERLNETENKLRDVEKERDSLQRQInANLPQEFAT 87
Cdd:pfam12128 206 LEDDGVVPPKSRLNRQQVEHwirdIQAIAGIMKIRPEF-TKLQQEFNTLESAELRLSHLHFGYKSDETLI-ASRQEERQE 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 88 LTKELTQARETLLE-----RDEEIGELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAAAQS--GVSSEVEVL-KAL 159
Cdd:pfam12128 284 TSAELNQLLRTLDDqwkekRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQlpSWQSELENLeERL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 160 KSLFEHHKALDEKVRERLRLSIEKNNmmeEELSSAKEELAQYKAGVVpagvgsgsgAGSAATTAGGGGAENGLKEKMAGV 239
Cdd:pfam12128 364 KALTGKHQDVTAKYNRRRSKIKEQNN---RDIAGIKDKLAKIREARD---------RQLAVAEDDLQALESELREQLEAG 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 240 GGSGGVNGEANELNDYAAKTHELQTIIEKQTselsqwqrrVSDLNNKISELEenmsRVQKEHCKAQDQCAKLQRDLRENV 319
Cdd:pfam12128 432 KLEFNEEEYRLKSRLGELKLRLNQATATPEL---------LLQLENFDERIE----RAREEQEAANAEVERLQSELRQAR 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 320 AQKEDQEERITTLEKRYLNAQRESTSLHDLNEKLEQELRH---KEAQL-----------------KLHEEKIGA-IEEKL 378
Cdd:pfam12128 499 KRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHflrKEAPDweqsigkvispellhrtDLDPEVWDGsVGGEL 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 379 ELSEQKLAQHAKLQPD---MEEQLKARM----EALTKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRL 451
Cdd:pfam12128 579 NLYGVKLDLKRIDVPEwaaSEEELRERLdkaeEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRL 658
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442626414 452 SSTVDKLLSESNERLQVHLK---ERMHALD-EKNALTQELEKARkvaEELHHEKSEIMKELSKTRLEIE 516
Cdd:pfam12128 659 FDEKQSEKDKKNKALAERKDsanERLNSLEaQLKQLDKKHQAWL---EEQKEQKREARTEKQAYWQVVE 724
|
|
| SAM_superfamily |
cd09487 |
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
1038-1088 |
9.93e-06 |
|
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.
Pssm-ID: 188886 [Multi-domain] Cd Length: 56 Bit Score: 44.15 E-value: 9.93e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 442626414 1038 WLPGLGLPQYRTTFMECLVDARMLDHLTKKDLRgQLKMVDSFHRTSLQYGI 1088
Cdd:cd09487 5 WLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
151-535 |
1.04e-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: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 151 SEVEVLKALKSLFEHHKALDEKVRErlrlsiEKNNMMEEE-LSSAKEELAQykagvvpagvgsgsgagsaaTTAGGGGAE 229
Cdd:pfam17380 266 TENEFLNQLLHIVQHQKAVSERQQQ------EKFEKMEQErLRQEKEEKAR--------------------EVERRRKLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 230 NGLKEKMAGVGGSGGVNGEANELNdyAAKTHELQTI-IEKQTSELSQWqrRVSDLNNKISELEEnMSRVQKEHckaQDQC 308
Cdd:pfam17380 320 EAEKARQAEMDRQAAIYAEQERMA--MERERELERIrQEERKRELERI--RQEEIAMEISRMRE-LERLQMER---QQKN 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 309 AKLQRDLRENVAQKEDQEERittlEKRYLNAQRESTSLhdlneKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQH 388
Cdd:pfam17380 392 ERVRQELEAARKVKILEEER----QRKIQQQKVEMEQI-----RAEQEEARQREVRRLEEERAREMERVRLEEQERQQQV 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 389 AKLQPDMEEQLKARMEALTKAQERHGSAEDRIRGLETNLDEKtnevvrlnqRLKMNEEHNLRlsstvdKLLSESNERLQ- 467
Cdd:pfam17380 463 ERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEER---------KQAMIEEERKR------KLLEKEMEERQk 527
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442626414 468 -VHLKERMHALDEKNALTQELEKARKVAEELHHEKSEimkelsKTRLEIENFKRQLLQQEIAYNIQQTE 535
Cdd:pfam17380 528 aIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEE------RSRLEAMEREREMMRQIVESEKARAE 590
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
251-433 |
1.17e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 251 ELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLREnvaQKEDQEERIT 330
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE---RREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 331 TLEKR-----YLNAQRESTSLHDLNEK---LEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKAR 402
Cdd:COG3883 94 ALYRSggsvsYLDVLLGSESFSDFLDRlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190
....*....|....*....|....*....|.
gi 442626414 403 MEALTKAQERHGSAEDRIRGLETNLDEKTNE 433
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAE 204
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
49-539 |
1.53e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 49 LREAQErLNETENKLRDVEKERDSLQRQINANLPQEFATLTKELTQARETLlERDEEIGELKAERNNTRLLLEHLECLVS 128
Cdd:PTZ00121 1187 VRKAEE-LRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAK-KDAEEAKKAEEERNNEEIRKFEEARMAH 1264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 129 RHERSLRMTVVKRQAAAQSGVSSEVEVLKALKSLFEHHKALDEKVR-ERLRLSIEKNNMMEEelSSAKEELAQYKAgvvp 207
Cdd:PTZ00121 1265 FARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKaEEAKKADEAKKKAEE--AKKKADAAKKKA---- 1338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 208 AGVGSGSGAGSAATTAGGGGAENGLKEKMAGVGGSGGVNGEANELNDYAA---KTHELQTIIEKQTSELSQWQRRVSDlN 284
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEekkKADEAKKKAEEDKKKADELKKAAAA-K 1417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 285 NKISELEENMSRVQK--------EHCKAQDQCAKLQRDLR--ENVAQKEDQEERITTLEKRYLNAQR--ESTSLHDLNEK 352
Cdd:PTZ00121 1418 KKADEAKKKAEEKKKadeakkkaEEAKKADEAKKKAEEAKkaEEAKKKAEEAKKADEAKKKAEEAKKadEAKKKAEEAKK 1497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 353 LEQELRHKEAQLKLHEEKIGAiEEKLELSEQKLAQHAKLQPDM---EEQLKA----------RMEALTKAQERHGSAEDR 419
Cdd:PTZ00121 1498 KADEAKKAAEAKKKADEAKKA-EEAKKADEAKKAEEAKKADEAkkaEEKKKAdelkkaeelkKAEEKKKAEEAKKAEEDK 1576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 420 IRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESN--ERLQVHLKERMHALDEKNALTQELEKARKVAEEl 497
Cdd:PTZ00121 1577 NMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIkaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA- 1655
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 442626414 498 hHEKSEIMKELSKTRLEIENFKRQLLQQEIAYNIQQTEALTR 539
Cdd:PTZ00121 1656 -EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
365-535 |
3.00e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 365 KLHEEKIGAIEEKLElseqKLAQHAKLQpdMEEQLKarmEALTKAQERhgsAEDRIRGLETNLDEKTNEVVRLNQRLKMN 444
Cdd:PRK12704 27 KIAEAKIKEAEEEAK----RILEEAKKE--AEAIKK---EALLEAKEE---IHKLRNEFEKELRERRNELQKLEKRLLQK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 445 EEhnlrlssTVDKLLsESNERLQVHLKERMHALDEKnalTQELEKARKVAEELHHEKSEIMKELSKtrLEIENFKRQLLQ 524
Cdd:PRK12704 95 EE-------NLDRKL-ELLEKREEELEKKEKELEQK---QQELEKKEEELEELIEEQLQELERISG--LTAEEAKEILLE 161
|
170
....*....|....*...
gi 442626414 525 Q-------EIAYNIQQTE 535
Cdd:PRK12704 162 KveeearhEAAVLIKEIE 179
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
50-203 |
3.05e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 50 REAQERLNEtenkLRDVEKERDSLQRQInANLPQEFATLTKELTQARETLLERDEEIGELKAERNNTRLLLEHLECLVSR 129
Cdd:COG1579 3 PEDLRALLD----LQELDSELDRLEHRL-KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626414 130 HERSLRMTVVKRQAAAqsgVSSEVEVLKALKSLFEHH-KALDEKVrERLRLSIEKnnmMEEELSSAKEELAQYKA 203
Cdd:COG1579 78 YEEQLGNVRNNKEYEA---LQKEIESLKRRISDLEDEiLELMERI-EELEEELAE---LEAELAELEAELEEKKA 145
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
174-489 |
3.11e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.43 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 174 RERLRLSIEKNNMMEEELSSAKEELAQYKAGVVPAGVGSGSGAGSAATTAGGGGAENGL------KEKMAGVGGSGGVNG 247
Cdd:pfam02463 197 LQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESskqeieKEEEKLAQVLKENKE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 248 EANELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEE 327
Cdd:pfam02463 277 EEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 328 RITTLEKRYLNA----QRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKlaqhaklqpdmEEQLKARM 403
Cdd:pfam02463 357 EEEELEKLQEKLeqleEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQL-----------EDLLKEEK 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 404 EALTKAQErhgSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSstvDKLLSESNERLQVHLKERMHALDEKNAL 483
Cdd:pfam02463 426 KEELEILE---EEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSE---DLLKETQLVKLQEQLELLLSRQKLEERS 499
|
....*.
gi 442626414 484 TQELEK 489
Cdd:pfam02463 500 QKESKA 505
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
284-526 |
4.40e-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: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 284 NNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQ 363
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 364 LKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKM 443
Cdd:TIGR04523 112 IKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 444 --NEEHNLRLSSTVDKLLSESNERLQ---VHLKERMHAL--------DEKNALTQELEKARKVAEELHHEKSEIMKELSK 510
Cdd:TIGR04523 192 ikNKLLKLELLLSNLKKKIQKNKSLEsqiSELKKQNNQLkdniekkqQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSE 271
|
250
....*....|....*.
gi 442626414 511 TRLEIENFKRQLLQQE 526
Cdd:TIGR04523 272 KQKELEQNNKKIKELE 287
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
266-542 |
4.43e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 266 IEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQR---- 341
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEelee 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 342 ---ESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQ-HAKLQPDMEEQLKARMEALTK-AQERHGSA 416
Cdd:COG4372 120 lqkERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAlEQELQALSEAEAEQALDELLKeANRNAEKE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 417 EDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESNERLQVHLKERMH--------ALDEKNALTQELE 488
Cdd:COG4372 200 EELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKeieelelaILVEKDTEEEELE 279
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 442626414 489 KARKVAEELHHEKSEIMKELSKTRLEIENFKRQLLQQEIAYNIQQTEALTRSLS 542
Cdd:COG4372 280 IAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALA 333
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
261-477 |
4.80e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.98 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 261 ELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLREN-VAQKEDQEERITTL--EKRYL 337
Cdd:PRK11281 125 QLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGkVGGKALRPSQRVLLqaEQALL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 338 NAQRE--------STSLHDLNEKLEQELRHKEAQLKLHEEKI-GAIEEK-LELSEQKLAQHAKLQpdmeEQLKARMEALT 407
Cdd:PRK11281 205 NAQNDlqrkslegNTQLQDLLQKQRDYLTARIQRLEHQLQLLqEAINSKrLTLSEKTVQEAQSQD----EAARIQANPLV 280
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442626414 408 KAQerhgsaedrirgLETNLdektnevvRLNQRL-----KMNE--EHNLRLSSTVDKLL-SESNerlqvhLKERMHAL 477
Cdd:PRK11281 281 AQE------------LEINL--------QLSQRLlkateKLNTltQQNLRVKNWLDRLTqSERN------IKEQISVL 332
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
324-491 |
4.85e-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: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 324 DQEERITTLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQLKLH---------EEKIGAIEEKLELSEQKLAQHAKLQPD 394
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALqrlaeyswdEIDVASAEREIAELEAELERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 395 ---MEEQLKARMEALTKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRL-----KMNEEHNLRLSSTVDKLLSESNER- 465
Cdd:COG4913 687 laaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLeaaedLARLELRALLEERFAAALGDAVERe 766
|
170 180
....*....|....*....|....*..
gi 442626414 466 LQVHLKERMHALDEK-NALTQELEKAR 491
Cdd:COG4913 767 LRENLEERIDALRARlNRAEEELERAM 793
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
64-537 |
5.02e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.66 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 64 RDVEKERDSLQRQINANLPQEF----ATLTKELTQARETLLERDEEIGELKAERN--NTRLLLEHLECLVSRHERSLRmT 137
Cdd:TIGR00618 196 AELLTLRSQLLTLCTPCMPDTYherkQVLEKELKHLREALQQTQQSHAYLTQKREaqEEQLKKQQLLKQLRARIEELR-A 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 138 VVKRQAAAQSGVSSEVEVLKalksLFEHHKALDEKVRERLRLSieknnmmeEELSSAKEELAQYKAGVVPAGVGSGSGAG 217
Cdd:TIGR00618 275 QEAVLEETQERINRARKAAP----LAAHIKAVTQIEQQAQRIH--------TELQSKMRSRAKLLMKRAAHVKQQSSIEE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 218 SAATTAGGGGAENGLKEKMAGVGGSGGVNGEANELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKIS--ELEENMS 295
Cdd:TIGR00618 343 QRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDtrTSAFRDL 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 296 RVQKEHCKAQDQCAKLQRDLRENVAQKEDQEEritTLEKRYLNaqrestslhdlneKLEQELRHKEAQLKLHEEKIGAIE 375
Cdd:TIGR00618 423 QGQLAHAKKQQELQQRYAELCAAAITCTAQCE---KLEKIHLQ-------------ESAQSLKEREQQLQTKEQIHLQET 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 376 EKLELSEQKLAQHAKLQPDMEEQLKARMEALTKA------QERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNL 449
Cdd:TIGR00618 487 RKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIdnpgplTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQ 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 450 RLSSTVDKLLSESNErlqvhLKERMhaldekNALTQELEKARKVAEELhhEKSEIMKELSKTRLEIENFKRQLLQQEIAY 529
Cdd:TIGR00618 567 EIQQSFSILTQCDNR-----SKEDI------PNLQNITVRLQDLTEKL--SEAEDMLACEQHALLRKLQPEQDLQDVRLH 633
|
490
....*....|
gi 442626414 530 --NIQQTEAL 537
Cdd:TIGR00618 634 lqQCSQELAL 643
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
272-548 |
6.35e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 6.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 272 ELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDL-RENVAQKEDQEERITTLE---KRYLNAQRESTSLH 347
Cdd:PRK04863 838 ELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLpRLNLLADETLADRVEEIReqlDEAEEAKRFVQQHG 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 348 DLNEKLEQELrhkeAQLKLHEEKIGAIEEKLELSEQKLaqhaklqpdmeEQLKARMEALTKAQER--HGSAEDRIRGLET 425
Cdd:PRK04863 918 NALAQLEPIV----SVLQSDPEQFEQLKQDYQQAQQTQ-----------RDAKQQAFALTEVVQRraHFSYEDAAEMLAK 982
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 426 NLDekTNEvvRLNQRLKMNEEHNLRLSSTVDKLLSESNERLQVH--LKERMHAL-DEKNALTQEL------------EKA 490
Cdd:PRK04863 983 NSD--LNE--KLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLasLKSSYDAKrQMLQELKQELqdlgvpadsgaeERA 1058
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626414 491 RKVAEELHHE-------KSEIMKELSKTRLEIENFKRQLLQQEIAYNIQQTEALTRSLSPSSVVD 548
Cdd:PRK04863 1059 RARRDELHARlsanrsrRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLR 1123
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
22-162 |
7.75e-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: 44.89 E-value: 7.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 22 SQFSGEDANFEQLMVSMLDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINA--------NLPqEFATLTKELT 93
Cdd:pfam15619 49 GKYEGTESELPQLIARHNEEVRVLRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRleklsedkNLA-EREELQKKLE 127
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442626414 94 QARETLLERDEEIGELkaERnntrllleHLECLVSRHERSLRMTVVKrQAAAQSGVSSEVEVLKALKSL 162
Cdd:pfam15619 128 QLEAKLEDKDEKIQDL--ER--------KLELENKSFRRQLAAEKKK-HKEAQEEVKILQEEIERLQQK 185
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
304-521 |
7.93e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 7.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 304 AQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQlklheEKIGAIEEKLElseq 383
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE-----REIAELEAELE---- 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 384 klaqhaklqpdmeeQLKARMEALTKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESN 463
Cdd:COG4913 679 --------------RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR 744
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626414 464 ERLQVHLKERMHALDEKNAltqelekARKVAEELHHEKSEIMKELSKTRLEIEN----FKRQ 521
Cdd:COG4913 745 LELRALLEERFAAALGDAV-------ERELRENLEERIDALRARLNRAEEELERamraFNRE 799
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
266-581 |
9.93e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.99 E-value: 9.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 266 IEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEhckaqdqcakLQRDLRENVaqkEDQEERITTLEKRYLNAQ----- 340
Cdd:COG5022 880 AERQLQELKIDVKSISSLKLVNLELESEIIELKKS----------LSSDLIENL---EFKTELIARLKKLLNNIDleegp 946
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 341 -------RESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAI---EEKLELSEQKLAQHAKLQPDMEEQLKaRMEALTKAQ 410
Cdd:COG5022 947 sieyvklPELNKLHEVESKLKETSEEYEDLLKKSTILVREGnkaNSELKNFKKELAELSKQYGALQESTK-QLKELPVEV 1025
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 411 ERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLsstvdKLLSESNERLQVHLKERMHALDEKNALTQELEKA 490
Cdd:COG5022 1026 AELQSASKIISSESTELSILKPLQKLKGLLLLENNQLQARY-----KALKLRRENSLLDDKQLYQLESTENLLKTINVKD 1100
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 491 RKVAEElHHEKSE-----IMKELSKTRL--EIENFKRQLLqqeiaYNIQQTEALTRSLSPssvvDPSGAFSRSNSHASFE 563
Cdd:COG5022 1101 LEVTNR-NLVKPAnvlqfIVAQMIKLNLlqEISKFLSQLV-----NTLEPVFQKLSVLQL----ELDGLFWEANLEALPS 1170
|
330
....*....|....*...
gi 442626414 564 THSLRRQSKQRLSEENAL 581
Cdd:COG5022 1171 PPPFAALSEKRLYQSALY 1188
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
36-522 |
1.14e-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: 46.64 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 36 VSMLDERDKLMD-SLREAQERLNETENKLRDVEKerdSLQRQINAN--LPQEFATLTKELTQAREtllERDEEIGELKAE 112
Cdd:pfam05483 270 ANQLEEKTKLQDeNLKELIEKKDHLTKELEDIKM---SLQRSMSTQkaLEEDLQIATKTICQLTE---EKEAQMEELNKA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 113 RNNTRLLLEHLECLVSRHERSLRmtvvkrqaAAQSGVSSEVEVLKALKslfehhKALDEKVRERLRLSIEKNNMmEEELS 192
Cdd:pfam05483 344 KAAHSFVVTEFEATTCSLEELLR--------TEQQRLEKNEDQLKIIT------MELQKKSSELEEMTKFKNNK-EVELE 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 193 SAKEELAQyKAGVVPAGVGSGSGAGSAATTAGGGGAENGLKEKMAGVGGSGGVNGEANElNDYAAKTHELQTIIEKQ--- 269
Cdd:pfam05483 409 ELKKILAE-DEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSE-EHYLKEVEDLKTELEKEklk 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 270 TSELSQWQRRVSDLNNKISELEENMSRVQKEHckaqdqcaklQRDLRENVAQKEDQEERITTLEKRYLNAQREstsLHDL 349
Cdd:pfam05483 487 NIELTAHCDKLLLENKELTQEASDMTLELKKH----------QEDIINCKKQEERMLKQIENLEEKEMNLRDE---LESV 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 350 NEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKAR------MEALTKAQERHGSAED----- 418
Cdd:pfam05483 554 REEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKnknieeLHQENKALKKKGSAENkqlna 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 419 ---RIRGLETNLD---EKTNEVVRLNQR----LKMNEEHNL----RLSSTVD---KLLSESNERLQVHLKErMHALDEKN 481
Cdd:pfam05483 634 yeiKVNKLELELAsakQKFEEIIDNYQKeiedKKISEEKLLeeveKAKAIADeavKLQKEIDKRCQHKIAE-MVALMEKH 712
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 442626414 482 A---------LTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQL 522
Cdd:pfam05483 713 KhqydkiieeRDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQL 762
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
1115-1186 |
1.21e-04 |
|
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: 41.51 E-value: 1.21e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626414 1115 VLVWSNERVIRWVGSIGLKEYANNLLESGVHGGLMALDEGFDanamgLALQIPTQNAQARQILDTEFNNLLQ 1186
Cdd:smart00454 1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEE-----DLKELGITKLGHRKKILKAIQKLKE 67
|
|
| SAM_STIM-1,2-like |
cd09504 |
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ... |
945-1003 |
1.27e-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: 41.55 E-value: 1.27e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626414 945 WNGPTIVAWLELWVGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNPLHRLKLRL 1003
Cdd:cd09504 5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
248-489 |
1.63e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.19 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 248 EANEL-NDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRE---NVAQKE 323
Cdd:TIGR00606 692 ELQEFiSDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRlknDIEEQE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 324 DQEERITTLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQLKLHE------------EKIGAIEEKLELSEQKLAQHAKL 391
Cdd:TIGR00606 772 TLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQgsdldrtvqqvnQEKQEKQHELDTVVSKIELNRKL 851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 392 QPDMEEQ---LKARMEALTKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESNERLQV 468
Cdd:TIGR00606 852 IQDQQEQiqhLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISS 931
|
250 260
....*....|....*....|.
gi 442626414 469 HLKERMHALDEKNALTQELEK 489
Cdd:TIGR00606 932 KETSNKKAQDKVNDIKEKVKN 952
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
320-507 |
1.67e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 320 AQKEDQEERittlEKRYLNAQREstsLHDLNEKLEQELRHKEAQLKLHEEKIgaieeklelsEQKlaqhaklqpdmEEQL 399
Cdd:PRK12704 47 AKKEAEAIK----KEALLEAKEE---IHKLRNEFEKELRERRNELQKLEKRL----------LQK-----------EENL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 400 KARMEALTKAQERhgsaedrirgletnLDEKTNEVVRLNQRLKMNEEhnlrlssTVDKLLSESNERLqvhlkERMHALDE 479
Cdd:PRK12704 99 DRKLELLEKREEE--------------LEKKEKELEQKQQELEKKEE-------ELEELIEEQLQEL-----ERISGLTA 152
|
170 180
....*....|....*....|....*...
gi 442626414 480 KNALTQELEKARkvaEELHHEKSEIMKE 507
Cdd:PRK12704 153 EEAKEILLEKVE---EEARHEAAVLIKE 177
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
38-593 |
1.71e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 38 MLDERDkLMDSLREAQE---RLNETENKLRDVEKERDSLQrQINAnLPQEFATLTKELTQARE-----TLLERDEEIGEL 109
Cdd:COG4913 217 MLEEPD-TFEAADALVEhfdDLERAHEALEDAREQIELLE-PIRE-LAERYAAARERLAELEYlraalRLWFAQRRLELL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 110 KAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAAAQSGVSSEVEVLKALKSLFEHH-KALDEKVRERLRLSiEKNNMME 188
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLeRELEERERRRARLE-ALLAALG 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 189 EELSSAKEELAQYKAGVvpagvgsgsgagsaattaggggaenglkekmagvggsggvngeANELNDYAAKTHELQTIIEK 268
Cdd:COG4913 373 LPLPASAEEFAALRAEA-------------------------------------------AALLEALEEELEALEEALAE 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 269 QTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQ-CAKL---QRDLR---ENVAQKEDQEERITTLEkRYLNAQR 341
Cdd:COG4913 410 AEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAlAEALgldEAELPfvgELIEVRPEEERWRGAIE-RVLGGFA 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 342 esTSL----------------HDLNEKLE-QELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAK---------LQPDM 395
Cdd:COG4913 489 --LTLlvppehyaaalrwvnrLHLRGRLVyERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEaelgrrfdyVCVDS 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 396 EEQLKARMEALTKA------QERH---------------GSAEDRIRGLETNLDEKTNEVVRLNQRL-KMNEEHN----- 448
Cdd:COG4913 567 PEELRRHPRAITRAgqvkgnGTRHekddrrrirsryvlgFDNRAKLAALEAELAELEEELAEAEERLeALEAELDalqer 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 449 LRLSSTVDKLLSESNERLQVH-----LKERMHALDEKN----ALTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFK 519
Cdd:COG4913 647 REALQRLAEYSWDEIDVASAEreiaeLEAELERLDASSddlaALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE 726
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442626414 520 RQllqqeiaynIQQTEALTRSLSPSSVVDPSGAFSRSNSHASFETHslRRQSKQRLSEENALVRSMAEQEWEKL 593
Cdd:COG4913 727 EE---------LDELQDRLEAAEDLARLELRALLEERFAAALGDAV--ERELRENLEERIDALRARLNRAEEEL 789
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
256-437 |
1.83e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 256 AAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEE---------NMSRVQKEHCKAQDQCAKLQ---RDLRENVAQKE 323
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQErrealqrlaEYSWDEIDVASAEREIAELEaelERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 324 DQEERITTLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEklelsEQKLAQHAKLQPDMEEQLKARM 403
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED-----LARLELRALLEERFAAALGDAV 763
|
170 180 190
....*....|....*....|....*....|....
gi 442626414 404 EALTKAQerhgsAEDRIRGLETNLDEKTNEVVRL 437
Cdd:COG4913 764 ERELREN-----LEERIDALRARLNRAEEELERA 792
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
41-203 |
2.06e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 41 ERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINAnlpqefatLTKELTQARETLLERDEEIGEL-----KAERNN 115
Cdd:COG4942 49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAE--------LEKEIAELRAELEAQKEELAELlralyRLGRQP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 116 TRLLLEHLEcLVSRHERSLRM--TVVKRQAAAQSGVSSEVEVLKALKSLFEHHKA-----LDEKVRERLRLSIEKNNmME 188
Cdd:COG4942 121 PLALLLSPE-DFLDAVRRLQYlkYLAPARREQAEELRADLAELAALRAELEAERAelealLAELEEERAALEALKAE-RQ 198
|
170
....*....|....*
gi 442626414 189 EELSSAKEELAQYKA 203
Cdd:COG4942 199 KLLARLEKELAELAA 213
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
249-410 |
2.82e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 44.28 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 249 ANELNDYAAKThelQTIIEKQTSELSQWQRRVSDLNNKiSELEENMSRVQ-------KEHCKAQDQCAKLQRDLRENVAQ 321
Cdd:cd22656 75 AGDIYNYAQNA---GGTIDSYYAEILELIDDLADATDD-EELEEAKKTIKallddllKEAKKYQDKAAKVVDKLTDFENQ 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 322 KEDQEERITTLEKRY------LNAQRESTSLHDLNEKLEQELRHKEAQLKlheEKIGAIEEKLELSEQKLAQHAKLQ--- 392
Cdd:cd22656 151 TEKDQTALETLEKALkdlltdEGGAIARKEIKDLQKELEKLNEEYAAKLK---AKIDELKALIADDEAKLAAALRLIadl 227
|
170 180
....*....|....*....|....*
gi 442626414 393 -------PDMEEQLKARMEALTKAQ 410
Cdd:cd22656 228 taadtdlDNLLALIGPAIPALEKLQ 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
267-677 |
4.43e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 267 EKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQR--DLRENVAQKEDQEERITTLEKRYLNAQREST 344
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEERLE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 345 SLHDLneklEQELRHKEAQLKLHEEKIGAIEEKLELS-EQKLAQHAKLQPDMEEQLKARMEALTKAQERHGSAEDRIRGL 423
Cdd:COG4717 157 ELREL----EEELEELEAELAELQEELEELLEQLSLAtEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 424 ETNLdektnEVVRLNQRLKMNEEHnLRLSSTVDKLLSESNERLQVHLKERMHALDEKNALTQELEKARKVAEELHHEKSE 503
Cdd:COG4717 233 ENEL-----EAAALEERLKEARLL-LLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 504 IMKELSKTRLEIENFKRQLLQQEIAYNIQQTEALTRSLSPSSVVDPSGAFSRSNSHASFETHSLRRQSKQRL----SEEN 579
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEagveDEEE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 580 ALVRSMAEQEWEKLQQAAHAQQQayELASAADCDDSDVLYAAATDMMSPSGHTDAQTLAM-----MLQEQLDAINNEIRL 654
Cdd:COG4717 387 LRAALEQAEEYQELKEELEELEE--QLEELLGELEELLEALDEEELEEELEELEEELEELeeeleELREELAELEAELEQ 464
|
410 420
....*....|....*....|....*
gi 442626414 655 IQEEKQSTEARA--EELESRVGSLE 677
Cdd:COG4717 465 LEEDGELAELLQelEELKAELRELA 489
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
375-542 |
4.92e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 375 EEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEE-------- 446
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREelgerara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 447 --HNLRLSSTVDKLL-SESNERL--QVHLKERMHALDekNALTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQ 521
Cdd:COG3883 95 lyRSGGSVSYLDVLLgSESFSDFldRLSALSKIADAD--ADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180
....*....|....*....|.
gi 442626414 522 LLQQeiaynIQQTEALTRSLS 542
Cdd:COG3883 173 LEAQ-----QAEQEALLAQLS 188
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
307-589 |
5.47e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 44.30 E-value: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 307 QCAKLQRDLRENVAQKEdqEERITTLEKR-----YLNA----QRESTSLHDLNEKLEQELRHKEAQLKlheekigaieEK 377
Cdd:COG5022 783 LRRLVDYELKWRLFIKL--QPLLSLLGSRkeyrsYLACiiklQKTIKREKKLRETEEVEFSLKAEVLI----------QK 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 378 LELSEQKLAQHAKLQPD-MEEQLKARME-ALTKAQERHGSAEDRirgleTNLDEKTNEVVRLNQRLKMNEEHNLRLSStv 455
Cdd:COG5022 851 FGRSLKAKKRFSLLKKEtIYLQSAQRVElAERQLQELKIDVKSI-----SSLKLVNLELESEIIELKKSLSSDLIENL-- 923
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 456 dKLLSESNERLQVHLKER---------MHALDEKNALTQELEKARKVAEELHH--EKSEI-MKELSKTRLEIENFKRQLL 523
Cdd:COG5022 924 -EFKTELIARLKKLLNNIdleegpsieYVKLPELNKLHEVESKLKETSEEYEDllKKSTIlVREGNKANSELKNFKKELA 1002
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442626414 524 QQEIAYniqqtEALTRSLSPSSVVDPSGAFSRSNSHASFETHSlrrqSKQRLSEENALVRSMAEQE 589
Cdd:COG5022 1003 ELSKQY-----GALQESTKQLKELPVEVAELQSASKIISSEST----ELSILKPLQKLKGLLLLEN 1059
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
275-536 |
9.90e-04 |
|
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: 43.35 E-value: 9.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 275 QWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLREN-------VAQKEDQEERITTLEKRYLN-AQRESTSL 346
Cdd:pfam07888 70 QWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELseekdalLAQRAAHEARIRELEEDIKTlTQRVLERE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 347 HDLnEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAK-------LQPDMEEQLKARMEALTKAQERHGSAEDR 419
Cdd:pfam07888 150 TEL-ERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKefqelrnSLAQRDTQVLQLQDTITTLTQKLTTAHRK 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 420 IRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTV---DKLLSESNE-RLQV------------HLKE-RMHALDEKNA 482
Cdd:pfam07888 229 EAENEALLEELRSLQERLNASERKVEGLGEELSSMAaqrDRTQAELHQaRLQAaqltlqladaslALREgRARWAQERET 308
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 442626414 483 LTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQLLQQEIAYNIQQTEA 536
Cdd:pfam07888 309 LQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSES 362
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
359-536 |
1.03e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 359 HKEAQLKLHEEKIGAIEEKLELSEQKLAQ-HAKLQPDMEEQLKARmEALTKAQERHGSAEDRIRGLETNLDEKTNEVVRL 437
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDAlQAELEELNEEYNELQ-AELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 438 NQRLKMNEEHNLRLS---------------STVDKLLSESNERLQVHLKERmhalDEKNALTQELEKARKVAEELHHEKS 502
Cdd:COG3883 92 ARALYRSGGSVSYLDvllgsesfsdfldrlSALSKIADADADLLEELKADK----AELEAKKAELEAKLAELEALKAELE 167
|
170 180 190
....*....|....*....|....*....|....
gi 442626414 503 EIMKELSKTRLEIENFKRQLLQQEIAYNIQQTEA 536
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAEL 201
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
355-475 |
1.12e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.15 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 355 QELRHKEAQLKlhEEKIGAIEEKLELSEQKLAqhaKLQpDMEEQLKARMEALTKAQERHGSAEDRIRGLETNLDEKTNEV 434
Cdd:COG0542 414 DELERRLEQLE--IEKEALKKEQDEASFERLA---ELR-DELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKI 487
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626414 435 VRLNQRLKMNEE----HNLRLSSTVD-----------------KLLSESNERLQvHLKERMH 475
Cdd:COG0542 488 PELEKELAELEEelaeLAPLLREEVTeediaevvsrwtgipvgKLLEGEREKLL-NLEEELH 548
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
378-543 |
1.19e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 378 LELSE--QKLAQHAKLQPDMEEQLKARMEALTKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEhnlRLSST- 454
Cdd:COG1579 10 LDLQEldSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE---QLGNVr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 455 ----VDKLLSE--SNERLQVHLKERMHALDEknaltqELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQlLQQEIA 528
Cdd:COG1579 87 nnkeYEALQKEieSLKRRISDLEDEILELME------RIEELEEELAELEAELAELEAELEEKKAELDEELAE-LEAELE 159
|
170
....*....|....*
gi 442626414 529 YNIQQTEALTRSLSP 543
Cdd:COG1579 160 ELEAEREELAAKIPP 174
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
53-423 |
1.21e-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: 43.42 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 53 QERLNETENKLRDVEKERDSLQRQINANLPQeFATLTKELTQARETLLERDEEIGELKAERNNTRLLLEHLECLV---SR 129
Cdd:TIGR00618 527 TRRMQRGEQTYAQLETSEEDVYHQLTSERKQ-RASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTeklSE 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 130 HERSLRmtvvkrqaaaqsgvssevEVLKALKSLFEHHKALdekvrerLRLSIEKNNMmEEELSSAKEELAQYKAGVVPAG 209
Cdd:TIGR00618 606 AEDMLA------------------CEQHALLRKLQPEQDL-------QDVRLHLQQC-SQELALKLTALHALQLTLTQER 659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 210 VGSGSGAGSAATTAGGGGAENGLKEKMAGVGGSGGVNGEANELNdyaAKTHELQTIIEKQTSELSQWQR----RVSDLNN 285
Cdd:TIGR00618 660 VREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQ---TLLRELETHIEEYDREFNEIENasssLGSDLAA 736
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 286 KISELEENMS---RVQKEHCKAQDQcAKLQRDLRENVAQKEDQEER--ITTLEKRYLNAQRESTSLHDLNEKLEQELRHK 360
Cdd:TIGR00618 737 REDALNQSLKelmHQARTVLKARTE-AHFNNNEEVTAALQTGAELShlAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSD 815
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442626414 361 EAQLKLHEEKIGAIEE----KLELSEQKLAQHAKLQPDMEEQLKaRMEALTKAQERHGSAEDRIRGL 423
Cdd:TIGR00618 816 EDILNLQCETLVQEEEqflsRLEEKSATLGEITHQLLKYEECSK-QLAQLTQEQAKIIQLSDKLNGI 881
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
248-520 |
1.25e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.11 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 248 EANELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRV---------------QKEHCKAQDQCAKLQ 312
Cdd:TIGR00606 246 ELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVfqgtdeqlndlyhnhQRTVREKERELVDCQ 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 313 RDLRENVAQKEDQEERITTLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGA---------IEEKLELSEQ 383
Cdd:TIGR00606 326 RELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPfserqiknfHTLVIERQED 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 384 KLAQHAKLQPDMEEQLKARMEALTKAQERHGSAEDRIRGLETNLDEKTNE---VVRLNQRLKMNEEHNLRLSSTVDKLLS 460
Cdd:TIGR00606 406 EAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEElkfVIKELQQLEGSSDRILELDQELRKAER 485
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626414 461 E-----SNERLQVHLKERMHALDEKNALTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKR 520
Cdd:TIGR00606 486 ElskaeKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQ 550
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
248-526 |
1.34e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 248 EANELNDYAAKTHELQTIIEKQTSELSQwQRRvsDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEE 327
Cdd:COG1340 16 KIEELREEIEELKEKRDELNEELKELAE-KRD--ELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELRE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 328 RITTLEKRYLNAQRESTSLHDLNEKLEQ-ELRHKEAQLKLHEE-----KIGAIEEKLELSEQKLAQHAKLQpDMEEQLKA 401
Cdd:COG1340 93 ELDELRKELAELNKAGGSIDKLRKEIERlEWRQQTEVLSPEEEkelveKIKELEKELEKAKKALEKNEKLK-ELRAELKE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 402 RMEALTKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKlLSESNERLQVHLKERMHALDEKN 481
Cdd:COG1340 172 LRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADE-LHEEIIELQKELRELRKELKKLR 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 442626414 482 ALTQELEKaRKVAEELHHEKSEIMKELSKT-RLEIENFKrqLLQQE 526
Cdd:COG1340 251 KKQRALKR-EKEKEELEEKAEEIFEKLKKGeKLTTEELK--LLQKS 293
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
86-365 |
1.51e-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: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 86 ATLTKELTQARETLLERDEEIGELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAAAQSGVSSEVE----VLKALKS 161
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDassdDLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 162 LFEHHKALDEKVRERLRLSIEKNNMMEEELSSAKEELAQykagvvpagvgsgsgagsaattaggggaenglkekmAGVGG 241
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE------------------------------------LQDRL 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 242 SGGVNGEANELNDYAAKTHElQTIIEKQTSELSQW-QRRVSDLNNKISELEENMSRVQKEHCKAQDQCAklqRDLRENVA 320
Cdd:COG4913 737 EAAEDLARLELRALLEERFA-AALGDAVERELRENlEERIDALRARLNRAEEELERAMRAFNREWPAET---ADLDADLE 812
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 442626414 321 QKEDQEERITTLE-----------KRYLNAQrESTSLHDLNEKLEQELRHKEAQLK 365
Cdd:COG4913 813 SLPEYLALLDRLEedglpeyeerfKELLNEN-SIEFVADLLSKLRRAIREIKERID 867
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
261-522 |
2.03e-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: 42.50 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 261 ELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAq 340
Cdd:pfam10174 356 EKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNT- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 341 reSTSLHDLNEKLEQELRHKEAqlkLHEEKIGAIEEKLELSEQ--KLAQHAK-----LQPDMEEQLKARMEALTKAQERH 413
Cdd:pfam10174 435 --DTALTTLEEALSEKERIIER---LKEQREREDRERLEELESlkKENKDLKekvsaLQPELTEKESSLIDLKEHASSLA 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 414 GSA---EDRIRGLETNLDEKTNEVVRLNQRLK----------MNEEHNLRLS-----------------STVDKLL---- 459
Cdd:pfam10174 510 SSGlkkDSKLKSLEIAVEQKKEECSKLENQLKkahnaeeavrTNPEINDRIRlleqevarykeesgkaqAEVERLLgilr 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 460 -------------SESNERLQVHLKE--------RMHALDEKNALTQELEKARKVAEEL-----HHEKSEIMKELSKTRL 513
Cdd:pfam10174 590 evenekndkdkkiAELESLTLRQMKEqnkkvaniKHGQQEMKKKGAQLLEEARRREDNLadnsqQLQLEELMGALEKTRQ 669
|
....*....
gi 442626414 514 EIENFKRQL 522
Cdd:pfam10174 670 ELDATKARL 678
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
32-179 |
2.20e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 32 EQLMVSMLDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQIN---------------ANLPQEFATLTKELTQAR 96
Cdd:COG3206 204 KNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGsgpdalpellqspviQQLRAQLAELEAELAELS 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 97 ETLLERDEEIGELKAERNNTRLLLehleclvsrhERSLRMTVVKRQAAAQSGVSSEVEVLKALKSLFEHHKALDEKVRER 176
Cdd:COG3206 284 ARYTPNHPDVIALRAQIAALRAQL----------QQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAEL 353
|
...
gi 442626414 177 LRL 179
Cdd:COG3206 354 RRL 356
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
49-183 |
2.34e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 49 LREAQERLNETENKLRDVEKERDSLQRqinanLPQEFATLTKELTQARETLLERDEEIGELKAERNNTRLLLEHLECLVS 128
Cdd:COG4913 663 VASAEREIAELEAELERLDASSDDLAA-----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 129 RHERSLRMTVV-----KRQAAAQSGVSSEVEvlkalKSLFEHHKALDEKvRERLRLSIEK 183
Cdd:COG4913 738 AAEDLARLELRalleeRFAAALGDAVERELR-----ENLEERIDALRAR-LNRAEEELER 791
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
280-513 |
2.50e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 41.76 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 280 VSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQ---------EERITTLEKRYLNAQRESTSLH--- 347
Cdd:pfam06160 181 LEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYREMEEEgyalehlnvDKEIQQLEEQLEENLALLENLElde 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 348 --DLNEKLEQELRHKEAQLklhEEKIGA---IEEKLELSEQKLaQHAKlqpDMEEQLKARMEALTKAQERHGSAEDRIRG 422
Cdd:pfam06160 261 aeEALEEIEERIDQLYDLL---EKEVDAkkyVEKNLPEIEDYL-EHAE---EQNKELKEELERVQQSYTLNENELERVRG 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 423 LETNLDEKTNEVVRLNQRLkmnEEHNLRLSSTVDKLLsESNERLQVHLKERMHALDEKNALTQELEKARKVAEELHHEKS 502
Cdd:pfam06160 334 LEKQLEELEKRYDEIVERL---EEKEVAYSELQEELE-EILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELR 409
|
250
....*....|.
gi 442626414 503 EIMKELSKTRL 513
Cdd:pfam06160 410 EIKRLVEKSNL 420
|
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
252-519 |
2.75e-03 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 42.03 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 252 LNDYAAKTHELQTIIEKQTS----ELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEE 327
Cdd:COG5192 418 IAEETSREDELSFDDSDVSTsdenEDVDFTGKKGAINNEDESDNEEVAFDSDSQFDESEGNLRWKEGLASKLAYSQSGKR 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 328 RITTLEKRYLnaqrESTSLHDLNEKLEQE-LRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEAL 406
Cdd:COG5192 498 GRNIQKIFYD----ESLSPEECIEEYKGEsAKSSESDLVVQDEPEDFFDVSKVANESISSNHEKLMESEFEELKKKWSSL 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 407 TKAQERH--GSAEDRIRGLE-----------------TNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDK-LLSESNERL 466
Cdd:COG5192 574 AQLKSRFqkDATLDSIEGEEeliqddekgnfedledeENSSDNEMEESRGSSVTAENEESADEVDYETEReENARKKEEL 653
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 442626414 467 QVHLKERMHALDEKNALTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFK 519
Cdd:COG5192 654 RGNFELEERGDPEKKDVDWYTEEKRKIEEQLKINRSEFETMVPESRVVIEGYR 706
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
251-489 |
2.99e-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: 41.65 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 251 ELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERIT 330
Cdd:pfam05557 28 ARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 331 TLEKRYLNAQREStslhdlnEKLEQELRHKEAQLKlheekigAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKAQ 410
Cdd:pfam05557 108 CLKNELSELRRQI-------QRAELELQSTNSELE-------ELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 411 --ERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDK--LLSESNERLQVHLKERMHALDEKNALTQE 486
Cdd:pfam05557 174 elEFEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNENIENklLLKEEVEDLKRKLEREEKYREEAATLELE 253
|
...
gi 442626414 487 LEK 489
Cdd:pfam05557 254 KEK 256
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
945-1008 |
3.00e-03 |
|
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.
Pssm-ID: 425739 Cd Length: 64 Bit Score: 37.25 E-value: 3.00e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442626414 945 WNGPTIVAWLElWVGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQEM 1008
Cdd:pfam00536 3 WSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
47-203 |
3.09e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 47 DSLREAQERLNETENKLRDVEKERDSLQRQINA-------------NLPQEFATLTKELTQARETLLERDEEIGELKAER 113
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEElneeynelqaeleALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 114 NNTRLLLEHLECLVSrhERSL-----RMTVVKRQAAAQsgvSSEVEVLKALKSLFEHHKALDEKVRERLRLSIEKNNMME 188
Cdd:COG3883 96 YRSGGSVSYLDVLLG--SESFsdfldRLSALSKIADAD---ADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170
....*....|....*
gi 442626414 189 EELSSAKEELAQYKA 203
Cdd:COG3883 171 AELEAQQAEQEALLA 185
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
154-342 |
3.17e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 154 EVLKALKSLFEHHKALD--EKVRERLRLSIEKnnmMEEELSSAKEELAQYKAGVvpagvgsgsgagsAATTAGGGGAENG 231
Cdd:COG1579 4 EDLRALLDLQELDSELDrlEHRLKELPAELAE---LEDELAALEARLEAAKTEL-------------EDLEKEIKRLELE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 232 LKEKMAGVGGSGGVNGEANELNDYAAKTHELQTIiekqtselsqwQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKL 311
Cdd:COG1579 68 IEEVEARIKKYEEQLGNVRNNKEYEALQKEIESL-----------KRRISDLEDEILELMERIEELEEELAELEAELAEL 136
|
170 180 190
....*....|....*....|....*....|.
gi 442626414 312 QRDLRENVAQKEDQEERITTLEKRyLNAQRE 342
Cdd:COG1579 137 EAELEEKKAELDEELAELEAELEE-LEAERE 166
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
37-376 |
3.65e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 37 SMLDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINAnLPQEFATLTKELTQARETLLERDEEIGELKAERNNT 116
Cdd:COG4372 35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQ-LEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 117 RLLLEHLECLVSRHERSlRMTVVKRQAAAQSGVSSEVEVLKALKSlfehhkALDEKVRERLRLSIEKNNMMEEELSSAKE 196
Cdd:COG4372 114 QEELEELQKERQDLEQQ-RKQLEAQIAELQSEIAEREEELKELEE------QLESLQEELAALEQELQALSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 197 ELAQYKAGVVPAGVGSGSGAGSAATTAGGGGAENGLKEKMAGVGGSGGVNGEANELNDYAAKTHELQTIIEKQTSELSQW 276
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 277 QRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQRESTSLHDLNEKLEQE 356
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLL 346
|
330 340
....*....|....*....|
gi 442626414 357 LRHKEAQLKLHEEKIGAIEE 376
Cdd:COG4372 347 LVGLLDNDVLELLSKGAEAG 366
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
41-588 |
4.23e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 41 ERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQinanlpQEFATLTKELTQARETLLERDEEIGELKAERNNTRLLL 120
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK------AEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAK 1424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 121 EHLEcLVSRHERSLRMTVVKRQAAAQSGVSSEVEVLKALKSLFEHHKALDE--------KVRERLRLSIEKNNMMEEELS 192
Cdd:PTZ00121 1425 KKAE-EKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEakkkaeeaKKADEAKKKAEEAKKKADEAK 1503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 193 SAKEELAQYKAGVVPAGVGSGSGAGSAATTAGGGGAENGLKEKMAGVGGSGGVNGEANELN--DYAAKTHELQTIIEKQT 270
Cdd:PTZ00121 1504 KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKkaEEAKKAEEDKNMALRKA 1583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 271 SELSQWQRRVSDLNNKISELEENM----------SRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQ 340
Cdd:PTZ00121 1584 EEAKKAEEARIEEVMKLYEEEKKMkaeeakkaeeAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKA 1663
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 341 RESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKAQE-RHGSAEDR 419
Cdd:PTZ00121 1664 AEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEaKKEAEEDK 1743
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 420 IRGLETNLDEKTNEVVrlnQRLKMNEEhnlrlsstvdKLLSESNERLQVHLKERMHALDEKNALTQElekaRKVAEELhh 499
Cdd:PTZ00121 1744 KKAEEAKKDEEEKKKI---AHLKKEEE----------KKAEEIRKEKEAVIEEELDEEDEKRRMEVD----KKIKDIF-- 1804
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 500 EKSEIMKELSKTRLEIENFKRQLLQQEI-----AYNIQQTEALTRSLSPSSVVDPSGAFSRSNSHASFETHSLRRqskqr 574
Cdd:PTZ00121 1805 DNFANIIEGGKEGNLVINDSKEMEDSAIkevadSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKED----- 1879
|
570
....*....|....
gi 442626414 575 lSEENALVRSMAEQ 588
Cdd:PTZ00121 1880 -DEEEIEEADEIEK 1892
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
266-504 |
4.30e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 266 IEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEhckaQDQCAKLQRDLRENVAQKEDQEERITTL----EKR----YL 337
Cdd:PRK04863 899 IREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSD----PEQFEQLKQDYQQAQQTQRDAKQQAFALtevvQRRahfsYE 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 338 NAQRESTSLHDLNEKLEQELRHKEAQlklheekigaieekleLSEQKlaqhaklqpdmeEQLKARMEALTKAQERHGSAE 417
Cdd:PRK04863 975 DAAEMLAKNSDLNEKLRQRLEQAEQE----------------RTRAR------------EQLRQAQAQLAQYNQVLASLK 1026
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 418 DRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRL-SSTVDKLLSESNERLQVHLKERMHALDEKNALTQeleKARKVAEE 496
Cdd:PRK04863 1027 SSYDAKRQMLQELKQELQDLGVPADSGAEERARArRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTK---KLRKLERD 1103
|
....*...
gi 442626414 497 LHHEKSEI 504
Cdd:PRK04863 1104 YHEMREQV 1111
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
250-429 |
5.45e-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: 40.01 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 250 NELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRvqkehckAQDQCAKLQRDLRENVAQKEDQEERI 329
Cdd:pfam00261 8 EELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELER-------TEERLAEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 330 TTLEKRylnAQRESTSLHDLNEKLEQ-ELRHKEAQLKLHE--EKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEAL 406
Cdd:pfam00261 81 KVLENR---ALKDEEKMEILEAQLKEaKEIAEEADRKYEEvaRKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNL 157
|
170 180 190
....*....|....*....|....*....|
gi 442626414 407 -------TKAQERHGSAEDRIRGLETNLDE 429
Cdd:pfam00261 158 ksleaseEKASEREDKYEEQIRFLTEKLKE 187
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
40-203 |
5.60e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 40 DERDKLMDS---LREAQERLNETENKLRDVEKERDSLQRQINAnLPQEFATLTKELTQARETLLERDEEIGELKAERNNT 116
Cdd:COG4913 675 AELERLDASsddLAALEEQLEELEAELEELEEELDELKGEIGR-LEKELEQAEEELDELQDRLEAAEDLARLELRALLEE 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 117 RLLLEHLECLVSRHERSLRmtvvKRQAAAQSGVSSEVEvlkALKSLFEHHKALDEKVRERLRLSIEKNNMMEEELSS-AK 195
Cdd:COG4913 754 RFAAALGDAVERELRENLE----ERIDALRARLNRAEE---ELERAMRAFNREWPAETADLDADLESLPEYLALLDRlEE 826
|
....*...
gi 442626414 196 EELAQYKA 203
Cdd:COG4913 827 DGLPEYEE 834
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
396-507 |
5.91e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 39.48 E-value: 5.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 396 EEQLKARMEALTKAQERHG---SAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESNERLQvhlkE 472
Cdd:pfam12072 60 EEIHKLRAEAERELKERRNelqRQERRLLQKEETLDRKDESLEKKEESLEKKEKELEAQQQQLEEKEEELEELIE----E 135
|
90 100 110
....*....|....*....|....*....|....*...
gi 442626414 473 RMHALDEKNALTQELEKAR---KVAEELHHEKSEIMKE 507
Cdd:pfam12072 136 QRQELERISGLTSEEAKEIlldEVEEELRHEAAVMIKE 173
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
250-472 |
6.58e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 250 NELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERI 329
Cdd:COG4372 80 EELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 330 TTLEKRY--LNAQRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALT 407
Cdd:COG4372 160 ESLQEELaaLEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALL 239
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626414 408 KAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESNERLQVHLKE 472
Cdd:COG4372 240 DALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNL 304
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
345-539 |
6.99e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 6.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 345 SLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQhaklqpdMEEQLKARMEALTKAQERHGSAEDRIRGLE 424
Cdd:COG4372 14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQ-------AREELEQLEEELEQARSELEQLEEELEELN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 425 TNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSEsNERLQvhlkermhalDEKNALTQELEKARKVAEELHHEKSEI 504
Cdd:COG4372 87 EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE-RQDLE----------QQRKQLEAQIAELQSEIAEREEELKEL 155
|
170 180 190
....*....|....*....|....*....|....*
gi 442626414 505 MKELSKTRLEIENFKRQLLQQEIAYNIQQTEALTR 539
Cdd:COG4372 156 EEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
39-193 |
7.17e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 7.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 39 LDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINanlPQEFATLTKELTQARETLLERDEEIGELKAERNNTRL 118
Cdd:PRK03918 618 EKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS---EEEYEELREEYLELSRELAGLRAELEELEKRREEIKK 694
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442626414 119 LLEHLeclvsrherslrmtvvKRQAAAQSGVSSEVEVL-KALKSLfehhKALDEKVReRLRLSIEKNNMME-EELSS 193
Cdd:PRK03918 695 TLEKL----------------KEELEEREKAKKELEKLeKALERV----EELREKVK-KYKALLKERALSKvGEIAS 750
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
291-526 |
7.69e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 7.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 291 EENMSRVQKEHCKAQDQCAKLQRDLREnVAQKEDQ--EERITTLEKR------YLNAQRESTSLHDLNEKLEQELRHKEA 362
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKE-LEKKHQQlcEEKNALQEQLqaetelCAEAEEMRARLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 363 QLKLHEEKigaiEEKLELSEQKLAQHAKlqpDMEEQLKARMEALTKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLK 442
Cdd:pfam01576 83 RLEEEEER----SQQLQNEKKKMQQHIQ---DLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 443 MNEEHNLRLSSTV------DKLLSESNERLQVHLKERMHALDEKNALTQELEKARKvaeELHHEKSEIMKELSKTRLEIE 516
Cdd:pfam01576 156 LLEERISEFTSNLaeeeekAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKR---KLEGESTDLQEQIAELQAQIA 232
|
250
....*....|
gi 442626414 517 NFKRQLLQQE 526
Cdd:pfam01576 233 ELRAQLAKKE 242
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
270-539 |
7.77e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 270 TSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQ-KEDQEERITTLEK-RYLNAQREST--S 345
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEaQELREKRDELNEKvKELKEERDELneK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 346 LHDLNEKLEqELRHKEAQLKLHEEKIGAIEEKLELSEQKLaQHAKLQPDMEEQLKARMEALTKAQErhgsAEDRIRGLET 425
Cdd:COG1340 87 LNELREELD-ELRKELAELNKAGGSIDKLRKEIERLEWRQ-QTEVLSPEEEKELVEKIKELEKELE----KAKKALEKNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 426 NLDEKTNEVVRLnqRLKMNEEHnlrlsstvdKLLSESNERLQVHLKERmhaldekNALTQELEKARKVAEELHHEKSEIM 505
Cdd:COG1340 161 KLKELRAELKEL--RKEAEEIH---------KKIKELAEEAQELHEEM-------IELYKEADELRKEADELHKEIVEAQ 222
|
250 260 270
....*....|....*....|....*....|....*.
gi 442626414 506 KELSKTRLEIENFKRQL--LQQEIAYNIQQTEALTR 539
Cdd:COG1340 223 EKADELHEEIIELQKELreLRKELKKLRKKQRALKR 258
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
275-409 |
8.16e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.17 E-value: 8.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 275 QWQRRVSDLNNKISELEENMSRVQKEHCKAQDQcAKLQRDLRENVAQKEDQ--EERITTLEKRYLNAQRESTSLHDLNEK 352
Cdd:PRK09510 84 KEQQQAEELQQKQAAEQERLKQLEKERLAAQEQ-KKQAEEAAKQAALKQKQaeEAAAKAAAAAKAKAEAEAKRAAAAAKK 162
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 442626414 353 LEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKA 409
Cdd:PRK09510 163 AAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKA 219
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
353-522 |
8.31e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 353 LEQELRHKEAQLKLHEEKIGAIEEK----LELSEQKLAQHAKLQPDMEEQLKARMEALTKAQERHGSAEDRIRGLETNLD 428
Cdd:PHA02562 186 LDMKIDHIQQQIKTYNKNIEEQRKKngenIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAA 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 429 EKTNEVVRLNQRLKMNEEHNLrlSSTVDKLLSESNERLQvHLKERMHALDEKnalTQELEKARKVAEELHHEKSEIMKEL 508
Cdd:PHA02562 266 KIKSKIEQFQKVIKMYEKGGV--CPTCTQQISEGPDRIT-KIKDKLKELQHS---LEKLDTAIDELEEIMDEFNEQSKKL 339
|
170
....*....|....
gi 442626414 509 SKTRLEIENFKRQL 522
Cdd:PHA02562 340 LELKNKISTNKQSL 353
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
45-527 |
8.32e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.49 E-value: 8.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 45 LMDSLREAQERLNETENKLRDvEKERDSLQRQINANLPQEFATLTKELTQARETLLERDEEIGELKAERNNTRLLLEHLE 124
Cdd:pfam05557 53 LQKRIRLLEKREAEAEEALRE-QAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTN 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 125 CLVSRHERSLRMTVVKRQAAAQSGVSSEvevlKALKSLFEHhkalDEKVRErLRLSIEKNNMMEEELSSAKEELAQykag 204
Cdd:pfam05557 132 SELEELQERLDLLKAKASEAEQLRQNLE----KQQSSLAEA----EQRIKE-LEFEIQSQEQDSEIVKNSKSELAR---- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 205 vVPAGVGSGSGAGSAATTAGGGGAENGLKEKMAGVGGSGGVNGEanelnDYAAKTHELQTIIEKQTSELSQWQRrvsdln 284
Cdd:pfam05557 199 -IPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREE-----KYREEAATLELEKEKLEQELQSWVK------ 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 285 nkiseleenmsrvqkehcKAQDQCAKLQRdlrenvaqKEDQEERITTLEKRYLNAQRESTSlhdlnekLEQELRHKEAQL 364
Cdd:pfam05557 267 ------------------LAQDTGLNLRS--------PEDLSRRIEQLQQREIVLKEENSS-------LTSSARQLEKAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 365 KLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLkarmeaLTKAQERhgsaeDRIRGLETNLDEK---TNEVVRLNQRL 441
Cdd:pfam05557 314 RELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRV------LLLTKER-----DGYRAILESYDKEltmSNYSPQLLERI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 442 KMNEEhnlrLSSTVDKLLSESNERLQVHLKERMHALDEKNALTQELEKARKvaEELHHEKSEIMKELSKTRLEIEN--FK 519
Cdd:pfam05557 383 EEAED----MTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQ--QESLADPSYSKEEVDSLRRKLETleLE 456
|
....*...
gi 442626414 520 RQLLQQEI 527
Cdd:pfam05557 457 RQRLREQK 464
|
|
|