|
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 ... |
835-905 |
2.44e-42 |
|
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.
Pssm-ID: 188961 Cd Length: 71 Bit Score: 148.87 E-value: 2.44e-42
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161016786 835 FAAWDGPTVVSWLELWVGMPAWYVAACRANVKSGAIMANLSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 905
Cdd:cd09562 1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
|
|
| SAM_liprin-alpha1,2,3,4_repeat2 |
cd09565 |
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ... |
952-1017 |
1.74e-39 |
|
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: 140.30 E-value: 1.74e-39
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161016786 952 MNHEWVGNDWLPSLGLPQYRSYFMESLVDARMLDHLNKKELRGQLKMVDSFHRVSLHYGIMCLKRL 1017
Cdd:cd09565 1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
|
|
| 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 ... |
1037-1108 |
1.95e-37 |
|
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: 134.75 E-value: 1.95e-37
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161016786 1037 DVMVWSNERVMGWVSGLGLKEFATNLTESGVHGALLALDETFDYSDLALLLQIPTQNAQARQLLEKEFSNLI 1108
Cdd:cd09568 1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
|
|
| SAM_liprin-kazrin_repeat2 |
cd09495 |
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ... |
956-1015 |
6.80e-27 |
|
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: 104.15 E-value: 6.80e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 956 WVGNDWLPSLGLPQYRSYFMESLVDARMLDHLNKKELRGQLKMVDSFHRVSLHYGIMCLK 1015
Cdd:cd09495 1 WWVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLVHLKVTSQLHHLSLKCGIHVLH 60
|
|
| SAM_liprin-kazrin_repeat1 |
cd09494 |
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
842-900 |
7.67e-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: 101.15 E-value: 7.67e-26
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 161016786 842 TVVSWLELWVGMPaWYVAACRANVKSGAIMANLSDTEIQREIGISNPLHRLKLRLAIQE 900
Cdd:cd09494 1 RVCAWLEDFGLMP-MYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
|
|
| SAM_kazrin_repeat3 |
cd09570 |
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin ... |
1037-1108 |
1.43e-19 |
|
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: 83.65 E-value: 1.43e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161016786 1037 DVMVWSNERVMGWVSGLGLKEFATNLTESGVHGALLALDETFDYSDLALLLQIPTQNAQARQLLEKEFSNLI 1108
Cdd:cd09570 1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
|
|
| SAM_liprin-kazrin_repeat3 |
cd09496 |
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of ... |
1045-1106 |
2.11e-19 |
|
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: 82.97 E-value: 2.11e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161016786 1045 RVMGWVSGLGLKEFATNLTESGVHGALLALDETFDYSDLALLLQIPTQNAQARQLLEKEFSN 1106
Cdd:cd09496 1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETEFNN 62
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
39-635 |
7.04e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.61 E-value: 7.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 39 RERLLETLREAQDGLATAQLRLRELGHEKDSLQRQLSIAlpQEFAALTKELNLcrEQLLEREEEIAELKAERNNTRLLLE 118
Cdd:COG1196 174 KEEAERKLEATEENLERLEDILGELERQLEPLERQAEKA--ERYRELKEELKE--LEAELLLLKLRELEAELEELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 119 HLEclvsRHERSLRMTVVKRQAQspggvssevevLKALKSLFEHHKALDEKVRERLRMALERVAVLEEELELSNQEALNL 198
Cdd:COG1196 250 ELE----AELEELEAELAELEAE-----------LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 199 RDQLSRRRSGLEEpgkdgdgqtlanglgpvgeSNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELG 278
Cdd:COG1196 315 EERLEELEEELAE-------------------LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 279 KAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAK 358
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 359 QKLQQTLQKAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQREKmnddhNKRLSETVDKLL 438
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG-----LRGLAGAVAVLI 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 439 SESnERLQLHLKERMGALEEkNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQLRGRPPSSYSRSLP--GSALEL 516
Cdd:COG1196 531 GVE-AAYEAALEAALAAALQ-NIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAvdLVASDL 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 517 RYSQAPTLPSGAPLDPYGAGSGRAGKRGRWS----GAKDESSKDWDRSAPAGSIPPPFPGELDGSDEEEAEGMFGAELLS 592
Cdd:COG1196 609 READARYYVLGDTLLGRTLVAARLEAALRRAvtlaGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERL 688
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 161016786 593 PSGQADVQTLAIMLQEQLEAINKEIKLIQEEKETTEQRAEELE 635
Cdd:COG1196 689 AEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLE 731
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
153-494 |
8.34e-17 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 86.26 E-value: 8.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 153 LKALKSLFEHHKALDEKVRERLRMALERVAVLEEELELSNQEALNLRDQLSRRRSGLEEPGKDGDGQTLAnglgpVGESN 232
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEER-----LEEAE 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 233 RRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRY 312
Cdd:TIGR02168 775 EELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 313 LSAQREATSLHDANDKLENELASKESLYRQSEEKSRQlaewLDDAKQKLQQTLQKAETlpeiEAQLAQRvaALNKAEERH 392
Cdd:TIGR02168 855 ESLAAEIEELEELIEELESELEALLNERASLEEALAL----LRSELEELSEELRELES----KRSELRR--ELEELREKL 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 393 GNFEERLRQLEAQLEEKnqeLQRARQREKMNDDHNKRLSETVDKLLSESNERLQLHLKER-------MGALEEKNSLSEE 465
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNL---QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIkelgpvnLAAIEEYEELKER 1001
|
330 340
....*....|....*....|....*....
gi 161016786 466 IANMKKLQDELLLNKEQLLAEMERMQMEI 494
Cdd:TIGR02168 1002 YDFLTAQKEDLTEAKETLEEAIEEIDREA 1030
|
|
| SAM_kazrin_repeat2 |
cd09567 |
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ... |
951-1015 |
1.00e-15 |
|
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188966 Cd Length: 65 Bit Score: 72.83 E-value: 1.00e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161016786 951 DMNHEWVGNDWLPSLGLPQYRSYFMESLVDARMLDHLNKKELRGQLKMVDSFHRVSLHYGIMCLK 1015
Cdd:cd09567 1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
230-509 |
1.06e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 82.80 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 230 ESNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLE 309
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 310 KRYLSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQtLQKAETLPEIEAQLAQRvaALNKAE 389
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE-LRAELTLLNEEAANLRE--RLESLE 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 390 ERHGNFEERLRQLEAQLEEKNQELQR-ARQREKMNDDHNKRLSET--VDKLLSESNERLQLHLKERMGALEEKNSLSEEI 466
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESlAAEIEELEELIEELESELeaLLNERASLEEALALLRSELEELSEELRELESKR 910
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 161016786 467 ANMKKLQDELLLNKEQLLAEMERMQMEIDQLRGRPPSSYSRSL 509
Cdd:TIGR02168 911 SELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTL 953
|
|
| SAM_kazrin_repeat1 |
cd09564 |
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ... |
838-900 |
1.16e-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: 1.16e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161016786 838 WDGPTVVSWLELWVGMPAwYVAACRANVKSGAIMANLSDTEIQREIGISNPLHRLKLRLAIQE 900
Cdd:cd09564 4 WKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
233-498 |
1.40e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 82.41 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 233 RRTAELEEALERQRAEVCQLRERLAVLcrQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRY 312
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRELELALLVL--RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 313 LSAQREATSLHDANDKLENEL----ASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKA 388
Cdd:TIGR02168 284 EELQKELYALANEISRLEQQKqilrERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 389 EERHGNFEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVdKLLSESNERLQLHLKERMGALEE--KNSLSEEI 466
Cdd:TIGR02168 364 EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL-ERLEDRRERLQQEIEELLKKLEEaeLKELQAEL 442
|
250 260 270
....*....|....*....|....*....|..
gi 161016786 467 ANMKKLQDELLLNKEQLLAEMERMQMEIDQLR 498
Cdd:TIGR02168 443 EELEEELEELQEELERLEEALEELREELEEAE 474
|
|
| SAM_liprin-beta1,2_repeat2 |
cd09566 |
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ... |
951-1015 |
7.02e-15 |
|
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta potentially is able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.
Pssm-ID: 188965 Cd Length: 63 Bit Score: 70.03 E-value: 7.02e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161016786 951 DMNHEWVGNdWLPSLGLPQYRSYFMESLVDARMLDHLNKKELRgQLKMVDSFHRVSLHYGIMCLK 1015
Cdd:cd09566 1 KLDTHWVLR-WLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDLL-HLKVTSALHHASIRRGIQVLR 63
|
|
| SAM_liprin-beta1,2_repeat3 |
cd09569 |
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ... |
1037-1108 |
8.36e-15 |
|
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.
Pssm-ID: 188968 Cd Length: 72 Bit Score: 70.18 E-value: 8.36e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161016786 1037 DVMVWSNERVMGWVSGLGLKEFATNLTESGVHGALLALDETFDYSDLALLLQIPTQNAQARQLLEKEFSNLI 1108
Cdd:cd09569 1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
171-497 |
3.40e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 77.80 E-value: 3.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 171 RERLRMALERVAVLEEELELSNQE---ALNLRDQLSRRRSgleepgkdgdgqtlanglgpvgESNRRTAELEEALERQRA 247
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSElrrIENRLDELSQELS----------------------DASRKIGEIEKEIEQLEQ 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 248 EVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDL---KEALAQREDM--EERITTLEKRyLSAQREATS- 321
Cdd:TIGR02169 731 EEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLhklEEALNDLEARlsHSRIPEIQAE-LSKLEEEVSr 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 322 ----LHDANDKLENELASKESLYRQSEEKSRQLAEWlDDAKQKLQQTLQKAET-LPEIEAQLAQRVAALNKAEERHGNFE 396
Cdd:TIGR02169 810 iearLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL-KEQIKSIEKEIENLNGkKEELEEELEELEAALRDLESRLGDLK 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 397 ERLRQLEAQL---EEKNQELQRARQREKMND-----------DHNKRLSETVDKLLSESNERLQL--------HLKERMG 454
Cdd:TIGR02169 889 KERDELEAQLrelERKIEELEAQIEKKRKRLselkaklealeEELSEIEDPKGEDEEIPEEELSLedvqaelqRVEEEIR 968
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 161016786 455 ALEEKNSLS-EEIANMKKLQDELLLNKEQLLAEMERMQMEIDQL 497
Cdd:TIGR02169 969 ALEPVNMLAiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
39-422 |
1.03e-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: 76.25 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 39 RERLLET---LREAQDGLATAQLRLRELGHEKDSLQRQLSIAlpQEFAALTKELNlcREQLLEREEEIAELKAERNNTRL 115
Cdd:TIGR02168 171 KERRKETerkLERTRENLDRLEDILNELERQLKSLERQAEKA--ERYKELKAELR--ELELALLVLRLEELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 116 LLEHLECLVSRHERSLRMTvvkrqaqspggvSSEVEVLKALKSlfEHHKALDEkVRERLRMALERVAVLEEELELSNQEA 195
Cdd:TIGR02168 247 ELKEAEEELEELTAELQEL------------EEKLEELRLEVS--ELEEEIEE-LQKELYALANEISRLEQQKQILRERL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 196 LNLRDQLSRRrsgleepgkdgdgqtlanglgpvgesNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHR 275
Cdd:TIGR02168 312 ANLERQLEEL--------------------------EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 276 ELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLhdandklenelasKESLYRQSEEKSRQLAEWLD 355
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL-------------EDRRERLQQEIEELLKKLEE 432
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 161016786 356 DAKQKLQqtlqkaETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQREKM 422
Cdd:TIGR02168 433 AELKELQ------AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
172-497 |
4.94e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.94 E-value: 4.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 172 ERLRMALERVAVLEEELElSNQEALNLRDQLSRRRSGLEEPGKDGDGQTLANglgpvgesnrRTAELEEALERQRAEVCQ 251
Cdd:TIGR02168 182 ERTRENLDRLEDILNELE-RQLKSLERQAEKAERYKELKAELRELELALLVL----------RLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 252 LRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERIttlekRYLSAQREatSLHDANDKLEN 331
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK-----QILRERLA--NLERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 332 ELASKESlyrQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQ 411
Cdd:TIGR02168 324 QLEELES---KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 412 ELQRARQREKMNDDHNKRLSETVDKLLSESNE----RLQLHLKERMGALEEKNS-LSEEIANMKKLQDELLLNKEQL--- 483
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLQQEIEELLKKLEEaelkELQAELEELEEELEELQEeLERLEEALEELREELEEAEQALdaa 480
|
330 340
....*....|....*....|....
gi 161016786 484 ----------LAEMERMQMEIDQL 497
Cdd:TIGR02168 481 erelaqlqarLDSLERLQENLEGF 504
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
37-500 |
1.19e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 37 TERERLLETLREAQDGLATAQLRLRELGHEKDSLQRQLSIALpQEFAALTKELNLCREQLLEREEEIAELKAERNNTRLL 116
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL-AELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 117 LEHLECLVSRHERSLRMTVVKRQAqspggvsSEVEVLKALKSLFEHHKALDEKVRERLRMALERVAVLEEELELSNQEAl 196
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEE-------AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 197 nlrdQLSRRRSGLEepgkdgdgQTLANGLGPVGESNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRE 276
Cdd:COG1196 404 ----ELEEAEEALL--------ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 277 LGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATS------------LHDANDKLENELASKESLYRQ-- 342
Cdd:COG1196 472 AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLaglrglagavavLIGVEAAYEAALEAALAAALQni 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 343 ---SEEKSRQLAEWLDDAKQK----LQQTLQKAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQR 415
Cdd:COG1196 552 vveDDEVAAAAIEYLKAAKAGratfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAR 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 416 ARQREKMNDDHNKRLSETV--DKLLSESNERLQLHLKERMGALEEKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQME 493
Cdd:COG1196 632 LEAALRRAVTLAGRLREVTleGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711
|
....*..
gi 161016786 494 IDQLRGR 500
Cdd:COG1196 712 AEEERLE 718
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
235-500 |
1.77e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 72.02 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 235 TAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANsKLQRDLKEA-----LAQREDMEERITTLE 309
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQ-ALLKEKREYegyelLKEKEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 310 KRYLSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEwlddakqklQQTLQKAETLPEIEAQLAQRVAALNKAE 389
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE---------EEQLRVKEKIGELEAEIASLERSIAEKE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 390 ERHGNFEERLRQLEAQLEEKNQEL--------QRARQREKMNDDHNKRLSETVDKL--LSESNERLQLHLKERMGALEEK 459
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIeelereieEERKRRDKLTEEYAELKEELEDLRaeLEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 161016786 460 NSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQLRGR 500
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
225-419 |
2.25e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.87 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 225 LGPVGESNRRTAELEEALERQRAevcqLRERLAVLcrqmsQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEER 304
Cdd:COG4913 254 LEPIRELAERYAAARERLAELEY----LRAALRLW-----FAQRRLELLEAELEELRAELARLEAELERLEARLDALREE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 305 ITTLEKRYLSAQreatslHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQK-AETLPEIEAQLAQRVA 383
Cdd:COG4913 325 LDELEAQIRGNG------GDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEfAALRAEAAALLEALEE 398
|
170 180 190
....*....|....*....|....*....|....*.
gi 161016786 384 ALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQR 419
Cdd:COG4913 399 ELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
951-1015 |
8.54e-12 |
|
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: 61.52 E-value: 8.54e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161016786 951 DMNHEWVGNDWLPSLGLPQYRSYFMESLVDARMLDHLNKKELRgQLKMVDSFHRVSLHYGIMCLK 1015
Cdd:pfam00536 1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
187-498 |
9.68e-12 |
|
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: 69.28 E-value: 9.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 187 ELELSNQEALNLRDQLSRRRSGLEEpgkdgdgqtlangLGPVGESNRrTAELEEALERQRAEVCQLRERLAVLCRQMSQL 266
Cdd:TIGR04523 275 ELEQNNKKIKELEKQLNQLKSEISD-------------LNNQKEQDW-NKELKSELKNQEKKLEEIQNQISQNNKIISQL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 267 EEELGTAHRELGKAEEANSKLQRDLKEALAQredmeerITTLEKRYLSAQREATSLHDANDKLENELASKESLYRQSEEK 346
Cdd:TIGR04523 341 NEQISQLKKELTNSESENSEKQRELEEKQNE-------IEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQ 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 347 SRQLA---EWLDDAKQKL-QQTLQKAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQ-------LEEKNQELQR 415
Cdd:TIGR04523 414 IKKLQqekELLEKEIERLkETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSinkikqnLEQKQKELKS 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 416 ARQREKMNDDHNKRLSETVDKLLSESNErlqlhLKERMGALE-EKNSLSEEIANMKK--LQDELLLNKEQLLAEMERMQM 492
Cdd:TIGR04523 494 KEKELKKLNEEKKELEEKVKDLTKKISS-----LKEKIEKLEsEKKEKESKISDLEDelNKDDFELKKENLEKEIDEKNK 568
|
....*.
gi 161016786 493 EIDQLR 498
Cdd:TIGR04523 569 EIEELK 574
|
|
| SAM_liprin-beta1,2_repeat1 |
cd09563 |
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
835-899 |
1.04e-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: 61.09 E-value: 1.04e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161016786 835 FAAWDGPTVVSWL-ELWVGMpawYVAACRANVKSGAIMANLSDTEIQREIGISNPLHRLKLRLAIQ 899
Cdd:cd09563 1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
65-498 |
2.26e-11 |
|
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: 68.61 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 65 HEKDSLQ----RQLSIALPQEFAALTKELNLCREQLLEREEEIAELKAE-RNNTRLLLEH----LECLVSRHERSL---- 131
Cdd:pfam15921 205 YEHDSMStmhfRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSEsQNKIELLLQQhqdrIEQLISEHEVEItglt 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 132 -RMTVVKRQAQSpggVSSEVEV------------LKALKSLFEHHKALDEKVRERLRMALERVAVLEEELELSN------ 192
Cdd:pfam15921 285 eKASSARSQANS---IQSQLEIiqeqarnqnsmyMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANseltea 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 193 --------QEALNLRDQLSRRRSGLEEPGKD----------------GDGQTLANGLGPVGESNRRTAELEEAL------ 242
Cdd:pfam15921 362 rterdqfsQESGNLDDQLQKLLADLHKREKElslekeqnkrlwdrdtGNSITIDHLRRELDDRNMEVQRLEALLkamkse 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 243 -----ERQRAEVCQLRERLAVLCRQMSQLE----------EELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITT 307
Cdd:pfam15921 442 cqgqmERQMAAIQGKNESLEKVSSLTAQLEstkemlrkvvEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITK 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 308 LEKRYLSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNK 387
Cdd:pfam15921 522 LRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEIND 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 388 AEERHGNF-------EERLRQLEAQLEEknQELQRArqreKMNDDHNKRLSETVDKllseSNERLQLhLKERMGALEEKN 460
Cdd:pfam15921 602 RRLELQEFkilkdkkDAKIRELEARVSD--LELEKV----KLVNAGSERLRAVKDI----KQERDQL-LNEVKTSRNELN 670
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 161016786 461 SLSEEIA----NMKKLQDELLLNKEQLLAEMERMQMEIDQLR 498
Cdd:pfam15921 671 SLSEDYEvlkrNFRNKSEEMETTTNKLKMQLKSAQSELEQTR 712
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
234-497 |
4.54e-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: 4.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 234 RTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYL 313
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 314 SAQREATSLHDANDKLENELASKeslyrqsEEKSRQLAEWLDDAKQKL--QQTLQKAETLPEIEAQLAQRVAALNKAEER 391
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEEL-------EEDLHKLEEALNDLEARLshSRIPEIQAELSKLEEEVSRIEARLREIEQK 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 392 hgnfEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKLLSESNERLQLHLKERMGALEEKNSLSEEIANMKK 471
Cdd:TIGR02169 821 ----LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA 896
|
250 260
....*....|....*....|....*.
gi 161016786 472 LQDELLLNKEQLLAEMERMQMEIDQL 497
Cdd:TIGR02169 897 QLRELERKIEELEAQIEKKRKRLSEL 922
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
26-387 |
5.34e-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: 5.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 26 GELERLMVTMLTERERLLETLREAQDGLATAQLRLRELGHEKDSLQRQLSiALPQEFAALTKELNLCREQllereeeIAE 105
Cdd:TIGR02169 684 EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE-KLKERLEELEEDLSSLEQE-------IEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 106 LKAE--RNNTRL-----LLEHLECLVSRHERSLRMTVVKrqaqspggvssevEVLKALKSLFEHHKALDEKVRErLRMAL 178
Cdd:TIGR02169 756 VKSElkELEARIeeleeDLHKLEEALNDLEARLSHSRIP-------------EIQAELSKLEEEVSRIEARLRE-IEQKL 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 179 ERVAVLEEELELSNQEALNLRDQLSRRRSGLEEpgkdgdgqtlanglgPVGESNRRTAELEEALERQRAEVCQLRERLAV 258
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK---------------EIENLNGKKEELEEELEELEAALRDLESRLGD 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 259 LCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHDAND------KLENE 332
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDvqaelqRVEEE 966
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 161016786 333 LASKESLYRQSEEKSRQLAEWLDDAKQKLqqtlqkaETLPEIEAQLAQRVAALNK 387
Cdd:TIGR02169 967 IRALEPVNMLAIQEYEEVLKRLDELKEKR-------AKLEEERKAILERIEEYEK 1014
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
168-498 |
7.35e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.60 E-value: 7.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 168 EKVRERLRMALERVAVLEEELELSNQEALNLRDQLSRRRSGLEEPGKDGDGQTLANGLGPV--GESNRRTAELEEALERQ 245
Cdd:PRK02224 345 ESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVdlGNAEDFLEELREERDEL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 246 RAEVCQLRERLAVLCRQMSQLEEEL-------------GTAHRE-LGKAEEANSKLQRDLKEALAQREDMEERITTLEKr 311
Cdd:PRK02224 425 REREAELEATLRTARERVEEAEALLeagkcpecgqpveGSPHVEtIEEDRERVEELEAELEDLEEEVEEVEERLERAED- 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 312 YLSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEER 391
Cdd:PRK02224 504 LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAE 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 392 HGNFEERLRQLEAQL---EEKNQELQRARQREK----MNDDHNKRLS---ETVDKLLSESNE-RLQlhlkermGALEEKN 460
Cdd:PRK02224 584 LKERIESLERIRTLLaaiADAEDEIERLREKREalaeLNDERRERLAekrERKRELEAEFDEaRIE-------EAREDKE 656
|
330 340 350
....*....|....*....|....*....|....*...
gi 161016786 461 SLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQLR 498
Cdd:PRK02224 657 RAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELE 694
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
27-500 |
7.67e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 7.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 27 ELERLMVTMLTERERLLETLREAQDGLATAQLRLRELGHEKDSLQRQLSIALPQEFAALTKELNLCREQLLEREEEIAEL 106
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 107 KAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPggVSSEVEVLKALKSLFEHHKALDEKVRERLRMALERVAVLEE 186
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEA--LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 187 ELELSNQEALNLRDQLSRRRS--GLEEPGKDGDGQTLANGLGPVGESNRRTAELEEALERQRAEVCQ--LRERLAVLCRQ 262
Cdd:COG1196 471 EAALLEAALAELLEELAEAAArlLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEaaLEAALAAALQN 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 263 msqleeelgtahrELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELASKESLYRQ 342
Cdd:COG1196 551 -------------IVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYV 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 343 SEEKSRQLAEWLDDAKQKLQQTLQKAETLpeIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQREKM 422
Cdd:COG1196 618 LGDTLLGRTLVAARLEAALRRAVTLAGRL--REVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELEL 695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 423 NDDHNKRLSETVDKLLSESNERLQLHLKERM--GALEEKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQLRGR 500
Cdd:COG1196 696 EEALLAEEEEERELAEAEEERLEEELEEEALeeQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
171-419 |
9.90e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.48 E-value: 9.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 171 RERLRMALERVAVLEEELELSNQEALNLRDQLSRRRSGLEepgkdgdgqtLANGLGPVGESNRRTAELEEALERQRAEVC 250
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERRE----------ALQRLAEYSWDEIDVASAEREIAELEAELE 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 251 QLRE---RLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREatslhDAND 327
Cdd:COG4913 679 RLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA-----LLEE 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 328 KLENELAskeslyrqsEEKSRQLAEWLDDAKQKLQQTLQKAETlpEIEAQLAQ-------RVAALNKAEERHGNFEERLR 400
Cdd:COG4913 754 RFAAALG---------DAVERELRENLEERIDALRARLNRAEE--ELERAMRAfnrewpaETADLDADLESLPEYLALLD 822
|
250 260
....*....|....*....|
gi 161016786 401 QLEAQ-LEEKNQELQRARQR 419
Cdd:COG4913 823 RLEEDgLPEYEERFKELLNE 842
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
153-497 |
1.05e-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: 66.20 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 153 LKALKSLFEHHKALDEKVRErlrmaLER-VAVLEEELELSNQEALNLRDQLSRRRSGLeepgkdgdgQTLANglgpvgES 231
Cdd:TIGR04523 203 LSNLKKKIQKNKSLESQISE-----LKKqNNQLKDNIEKKQQEINEKTTEISNTQTQL---------NQLKD------EQ 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 232 NrrtaELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRElgKAEEANSKLQRDLKEALAQREDMEERITTLEKR 311
Cdd:TIGR04523 263 N----KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ--KEQDWNKELKSELKNQEKKLEEIQNQISQNNKI 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 312 YlsaqreaTSLHDANDKLENELASKESlyrQSEEKSRQLAEwlddaKQKLQQTL--QKAETLPEIEaQLAQRVAALN--- 386
Cdd:TIGR04523 337 I-------SQLNEQISQLKKELTNSES---ENSEKQRELEE-----KQNEIEKLkkENQSYKQEIK-NLESQINDLEski 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 387 -KAEERHGNFEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSE--TVDKLLSESNERLQLHLKERMGALE------ 457
Cdd:TIGR04523 401 qNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNqdSVKELIIKNLDNTRESLETQLKVLSrsinki 480
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161016786 458 -----------------------EKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQL 497
Cdd:TIGR04523 481 kqnleqkqkelkskekelkklneEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
38-419 |
1.50e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.56 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 38 ERERLLETLREAQDGLATAQLRLRELGHEKDSLQRQLSIA-LPQEFAALTKELNLCREQLLEREEEIAELKAERNNTRLL 116
Cdd:COG4717 89 EYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLpLYQELEALEAELAELPERLEELEERLEELRELEEELEEL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 117 LEHLEclvsRHERSLRMTVVKRQAQSPGGVSSEVEVLKALKSLFEHHKALDEKVRERLRMALERVAVLEEELElsnqeAL 196
Cdd:COG4717 169 EAELA----ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE-----AA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 197 NLRDQLSRRRSGLEEPGK----DGDGQTLANGLGPVGESNRRTAEL----EEALERQRAEVCQLRERLAVLCRQMSQLEE 268
Cdd:COG4717 240 ALEERLKEARLLLLIAAAllalLGLGGSLLSLILTIAGVLFLVLGLlallFLLLAREKASLGKEAEELQALPALEELEEE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 269 ELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATS---LHDANDKLENELASKESLYRQSEE 345
Cdd:COG4717 320 ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIaalLAEAGVEDEEELRAALEQAEEYQE 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 346 KSRQLAEWLD--DAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEERH-------GNFEERLRQLEAQ--LEEKNQELQ 414
Cdd:COG4717 400 LKEELEELEEqlEELLGELEELLEALDEEELEEELEELEEELEELEEELeelreelAELEAELEQLEEDgeLAELLQELE 479
|
....*
gi 161016786 415 RARQR 419
Cdd:COG4717 480 ELKAE 484
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
27-497 |
1.66e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.47 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 27 ELERLMVTMLTERERLLETLREAQDGLATAQLRLRELgheKDSLQRQLSI-ALPQEFAALTKELNLCREQLLEREEEIAE 105
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL---EEKVKELKELkEKAEEYIKLSEFYEEYLDELREIEKRLSR 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 106 LKAERNNTRLLLEHLECLVSR-HERSLRMTVVKRQAQSPGGVSSEVEVLKALKSLFEHHKALD-----EKVRERLRMALE 179
Cdd:PRK03918 319 LEEEINGIEERIKELEEKEERlEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLtgltpEKLEKELEELEK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 180 RVAVLEEELELSNQEALNLRDQLSRRRSGLEEPGKdgdgqtlANGLGPVGESNRRTAELEEALERQRAEVCQLRERLAVL 259
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKKEIKELKKAIEELKK-------AKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEI 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 260 CRQMSQLEEELgtahRELGKAEEANSKLQRdLKEALAQREDMEERITTLEKRYLSAQ-REATSLHDANDKLENELAS-KE 337
Cdd:PRK03918 472 EEKERKLRKEL----RELEKVLKKESELIK-LKELAEQLKELEEKLKKYNLEELEKKaEEYEKLKEKLIKLKGEIKSlKK 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 338 SLYRQSE--EKSRQLAEWLDDAKQKLQQTLQKAETLP-EIEAQLAQRVAALNKAEERH---GNFEERLRQLEAQLEEKNQ 411
Cdd:PRK03918 547 ELEKLEElkKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYlelKDAEKELEREEKELKKLEE 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 412 ELQRARQREKMNDDHNKRLSETVDKLLSESNERLQLHLKERMGALE-EKNSLSEEIANMKKLQDELLLNKEQL---LAEM 487
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSrELAGLRAELEELEKRREEIKKTLEKLkeeLEER 706
|
490
....*....|
gi 161016786 488 ERMQMEIDQL 497
Cdd:PRK03918 707 EKAKKELEKL 716
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
144-494 |
2.84e-10 |
|
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: 64.76 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 144 GGVSSEVEVLKALKSLFEHHKALDEKVRERL--RMALERVavleeelelsNQEALNLRDQLSRRRSgLEEPGKDGDGQtL 221
Cdd:pfam17380 262 GQTMTENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERL----------RQEKEEKAREVERRRK-LEEAEKARQAE-M 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 222 ANGLGPVGESNRRTAELEEALER-----QRAEVCQLR-ERLAVLCRQMSQLEeelgtahRELGKAEEANSKLQRDLKEAL 295
Cdd:pfam17380 330 DRQAAIYAEQERMAMERERELERirqeeRKRELERIRqEEIAMEISRMRELE-------RLQMERQQKNERVRQELEAAR 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 296 AQREDMEERittlEKRYLSAQREATSLhdandKLENELASKESLYRQSEEKSRQLaewlDDAKQKLQQTLQKAETLPEIE 375
Cdd:pfam17380 403 KVKILEEER----QRKIQQQKVEMEQI-----RAEQEEARQREVRRLEEERAREM----ERVRLEEQERQQQVERLRQQE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 376 AQLAQRVAALNKAEERHGNFEERLRQ-LEAQLEEKNQE-LQRARQR---EKMNDDHNKRLSETVDKLLSESNERLQLHLK 450
Cdd:pfam17380 470 EERKRKKLELEKEKRDRKRAEEQRRKiLEKELEERKQAmIEEERKRkllEKEMEERQKAIYEEERRREAEEERRKQQEME 549
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 161016786 451 ERMGALEEKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEI 494
Cdd:pfam17380 550 ERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEA 593
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
42-422 |
2.87e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.40 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 42 LLETLREAQDGLATAQLRLRELGHEK-DSLQRQLSIA--LPQEFAALTKELNLCREQLLEREEEIAELKAERNNTRLLLE 118
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKElKELEEELKEAeeKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 119 HLECLVSRHE------------RSLRMTVVKRQAQSPGGVSSEVEVLKALKSLFEHHKALDEKVRERLRMALERVAVLEE 186
Cdd:COG4717 127 LLPLYQELEAleaelaelperlEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 187 ELELSNQEALNLRDQLSRRRSGLEEPGKDGDGQTLAN-------------------GLGPVGESNRRT------------ 235
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEErlkearlllliaaallallGLGGSLLSLILTiagvlflvlgll 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 236 AELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSA 315
Cdd:COG4717 287 ALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 316 QREATS---LHDANDKLENELASKESLYRQSEEKSRQLAEWLD--DAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEE 390
Cdd:COG4717 367 ELEQEIaalLAEAGVEDEEELRAALEQAEEYQELKEELEELEEqlEELLGELEELLEALDEEELEEELEELEEELEELEE 446
|
410 420 430
....*....|....*....|....*....|....
gi 161016786 391 RHGNFEERLRQLEAQLE--EKNQELQRARQREKM 422
Cdd:COG4717 447 ELEELREELAELEAELEqlEEDGELAELLQELEE 480
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
38-439 |
4.01e-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: 64.32 E-value: 4.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 38 ERERLLETLREAQDGLATAQLRLRELGHEKDSLQRQLSIALpqEFAALTKELnlcreqlleREEEIAELKAERNNTRLLL 117
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE--RYQALLKEK---------REYEGYELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 118 EHLECLVSRHERSLRMTVVKRQAQspggvssEVEVLKALKSLFEHHKALDEKVRERLRMALERVAVLEEELElsnqealn 197
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISEL-------EKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIA-------- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 198 lrdQLSRRRSGLEEPGKDGDGQtLANGLGPVGESNRRTAELEEALERQRAEVCQLRERLAvlcrqmsQLEEELGTAHREL 277
Cdd:TIGR02169 305 ---SLERSIAEKERELEDAEER-LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYA-------ELKEELEDLRAEL 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 278 GKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDA 357
Cdd:TIGR02169 374 EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 358 KQKLQQTlqkAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKL 437
Cdd:TIGR02169 454 EWKLEQL---AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQL 530
|
..
gi 161016786 438 LS 439
Cdd:TIGR02169 531 GS 532
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
230-418 |
5.73e-10 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 62.54 E-value: 5.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 230 ESNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEalaQREDMEERITTLE 309
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE---RREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 310 KR-----YLSAQREATSLHDANDKLE--NELASKE----SLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAET-LPEIEAQ 377
Cdd:COG3883 97 RSggsvsYLDVLLGSESFSDFLDRLSalSKIADADadllEELKADKAELEAKKAELEAKLAELEALKAELEAaKAELEAQ 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 161016786 378 LAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQ 418
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
32-517 |
5.90e-10 |
|
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: 63.83 E-value: 5.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 32 MVTMLTERERLLE-TLREAQDGLATAQL------RLRELGHEKDSLQRQLSIALPQEFAALTKElnlcreqllereEEIA 104
Cdd:TIGR00618 213 MPDTYHERKQVLEkELKHLREALQQTQQshayltQKREAQEEQLKKQQLLKQLRARIEELRAQE------------AVLE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 105 ELKAERNNTRllleHLECLVsrhERSLRMTVVKRQAQSpggVSSEVEVLKA-LKSLFEHHKAL--DEKVRERLRMALERV 181
Cdd:TIGR00618 281 ETQERINRAR----KAAPLA---AHIKAVTQIEQQAQR---IHTELQSKMRsRAKLLMKRAAHvkQQSSIEEQRRLLQTL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 182 AVLEEELELSNQEALNLRDQLSRRRsgleepgkdgdgqtlanglgpvgesnrrtaELEEALERQRAEVCQLRERLAVLCR 261
Cdd:TIGR00618 351 HSQEIHIRDAHEVATSIREISCQQH------------------------------TLTQHIHTLQQQKTTLTQKLQSLCK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 262 QMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLS---AQREATSLHDANDKLENELASKES 338
Cdd:TIGR00618 401 ELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCeklEKIHLQESAQSLKEREQQLQTKEQ 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 339 LYRQSEEKSRQLAEWLDDaKQKLQQTLQKAETLPEIEAQLA--------------QRVAALNKAEE--RHGNFEER--LR 400
Cdd:TIGR00618 481 IHLQETRKKAVVLARLLE-LQEEPCPLCGSCIHPNPARQDIdnpgpltrrmqrgeQTYAQLETSEEdvYHQLTSERkqRA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 401 QLEAQLEEKNQELQR-ARQREKMNDDHNKRLSETVDkLLSESNERLQLHLKERMGALEEKNSLSEEIANMKKLQDELLLN 479
Cdd:TIGR00618 560 SLKEQMQEIQQSFSIlTQCDNRSKEDIPNLQNITVR-LQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCS 638
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 161016786 480 KEQ--LLAEMERMQMEIDQLRGRPPSSYSRSLPGSALELR 517
Cdd:TIGR00618 639 QELalKLTALHALQLTLTQERVREHALSIRVLPKELLASR 678
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
81-500 |
8.65e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.14 E-value: 8.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 81 EFAALTKELNLCREQLLEREEEIAELKAERNNTRLLLEHLECLVSRHERSL-RMTVVKrqaqspggvsSEVEVLKALKSL 159
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERReELETLE----------AEIEDLRETIAE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 160 FEHHK-ALDEKVRERLRMALERVAVLEE-----ELELSNQEALNLR-DQLSRRRSGLEEPGKD-----GDGQTLANGL-- 225
Cdd:PRK02224 270 TEREReELAEEVRDLRERLEELEEERDDllaeaGLDDADAEAVEARrEELEDRDEELRDRLEEcrvaaQAHNEEAESLre 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 226 ------GPVGESNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQRE 299
Cdd:PRK02224 350 daddleERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 300 DMEERITTLEKRYlsaqREATSLHDANDKLENELASKESLY----RQSEEKSRQLAEWLDDAK---QKLQQTLQKAETLP 372
Cdd:PRK02224 430 ELEATLRTARERV----EEAEALLEAGKCPECGQPVEGSPHvetiEEDRERVEELEAELEDLEeevEEVEERLERAEDLV 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 373 EIEAQlaqrvaaLNKAEERHGNFEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKLLSESNERLqlhlkER 452
Cdd:PRK02224 506 EAEDR-------IERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAR-----EE 573
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 161016786 453 MGALEEKNS-LSEEIANMKKLQDelllnkeqLLAEMERMQMEIDQLRGR 500
Cdd:PRK02224 574 VAELNSKLAeLKERIESLERIRT--------LLAAIADAEDEIERLREK 614
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
234-476 |
1.09e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.77 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 234 RTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSK---LQRDLKEALAQREDMEERITTLEK 310
Cdd:PRK03918 187 RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEieeLEKELESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 311 RYLSAQREATSLHDANDKLEnELASKESLYRQseeksrqLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEE 390
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELK-ELKEKAEEYIK-------LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 391 RHGNFEERLRQLE---AQLEEKNQELQRARQREKMNDDHNKRLS----ETVDKLLSESNERLQLHLKERMGALEEKNSLS 463
Cdd:PRK03918 339 RLEELKKKLKELEkrlEELEERHELYEEAKAKKEELERLKKRLTgltpEKLEKELEELEKAKEEIEEEISKITARIGELK 418
|
250
....*....|...
gi 161016786 464 EEIANMKKLQDEL 476
Cdd:PRK03918 419 KEIKELKKAIEEL 431
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
289-517 |
1.12e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.01 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 289 RDLKEALAQREDMEERITTLE------KRYLSAQREATSLHDANDKLEnelaskeslYRQSEEKSRQLAEWLDDAKQKLQ 362
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEpirelaERYAAARERLAELEYLRAALR---------LWFAQRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 363 QTLQKAETLPEIEAQLAQRVAALNKAEERHGNfeERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDklLSESN 442
Cdd:COG4913 306 RLEAELERLEARLDALREELDELEAQIRGNGG--DRLEQLEREIERLERELEERERRRARLEALLAALGLPLP--ASAEE 381
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161016786 443 -ERLQLHLKERmgaleeKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQLRGRPpssysRSLPGSALELR 517
Cdd:COG4913 382 fAALRAEAAAL------LEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK-----SNIPARLLALR 446
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
231-498 |
1.94e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 61.07 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 231 SNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEK 310
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 311 RYLSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQL--AQRVAALNKA 388
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALseAEAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 389 EERHGNFEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKLLSESNERLQLHLKERMGALEEKNSLSEEIAN 468
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260 270
....*....|....*....|....*....|
gi 161016786 469 MKKLQDELLLNKEQLLAEMERMQMEIDQLR 498
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLL 298
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
46-493 |
1.99e-09 |
|
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: 62.16 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 46 LREAQDGLATAQLRLRELGHEKDSLQRQLSiALPQEFAALTKELNLcreQLLEREEEIAELKAERNNTRLLL-------- 117
Cdd:pfam12128 246 LQQEFNTLESAELRLSHLHFGYKSDETLIA-SRQEERQETSAELNQ---LLRTLDDQWKEKRDELNGELSAAdaavakdr 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 118 EHLECLVSRHERSLRMTVVKR---QAQSPGgVSSEVEVL-KALKSLFEHHKALDEKVRERLRMALERvavLEEELELSNQ 193
Cdd:pfam12128 322 SELEALEDQHGAFLDADIETAaadQEQLPS-WQSELENLeERLKALTGKHQDVTAKYNRRRSKIKEQ---NNRDIAGIKD 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 194 EALNLRDQLSRRRSGLEepgkdGDGQTLANGLGPVGESNRRTAELEEALERQRAEVCQLRERLAV----LCRQMSQLEEE 269
Cdd:pfam12128 398 KLAKIREARDRQLAVAE-----DDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATatpeLLLQLENFDER 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 270 LGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHD----ANDKLENELASKESLYRQSEE 345
Cdd:pfam12128 473 IERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELqlfpQAGTLLHFLRKEAPDWEQSIG 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 346 K--SRQ------LAEWLDDAKQKLQQTL-------------QKAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEA 404
Cdd:pfam12128 553 KviSPEllhrtdLDPEVWDGSVGGELNLygvkldlkridvpEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANG 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 405 QLEEKNQELQRARQREKMNDDHNKRLsetvdkllseSNERLQLHLKERMGALEEKNSLSEEIANMKKLQDELLLNKEQLL 484
Cdd:pfam12128 633 ELEKASREETFARTALKNARLDLRRL----------FDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWL 702
|
....*....
gi 161016786 485 AEMERMQME 493
Cdd:pfam12128 703 EEQKEQKRE 711
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
171-507 |
2.18e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 62.28 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 171 RERLRMALERVAVLE-------EELELSNQEALNLR---DQLSRRRSGLEEpgkdgDGQTLANGLGPVGESNRRT----- 235
Cdd:PRK04863 278 ANERRVHLEEALELRrelytsrRQLAAEQYRLVEMArelAELNEAESDLEQ-----DYQAASDHLNLVQTALRQQekier 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 236 -----AELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRD----------LKEALAQRED 300
Cdd:PRK04863 353 yqadlEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRaiqyqqavqaLERAKQLCGL 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 301 MEERITTLEKRYLSAQREATSLHDANDKLENELASKESLYRQSEEKS---RQLAEWLD--DAKQKLQQTLQKAETLPEIE 375
Cdd:PRK04863 433 PDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYqlvRKIAGEVSrsEAWDVARELLRRLREQRHLA 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 376 AQLAQRVAALNKAEERHGN------------------------FEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLS 431
Cdd:PRK04863 513 EQLQQLRMRLSELEQRLRQqqraerllaefckrlgknlddedeLEQLQEELEARLESLSESVSEARERRMALRQQLEQLQ 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 432 ETVDKLLSESNERLQLH-----LKERMG-ALEEKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQLRGRPPSSY 505
Cdd:PRK04863 593 ARIQRLAARAPAWLAAQdalarLREQSGeEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSQPGGSED 672
|
..
gi 161016786 506 SR 507
Cdd:PRK04863 673 PR 674
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
36-408 |
2.53e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 36 LTERERLLETLREAQDGLATAQLRLRELGHEKDSLQRQLSIALPQEFAALTKELNLCREQLLEREEEIAELKAERNNTRL 115
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 116 LLEHLECLVSRHERSLRMtvVKRQAQSPGGVSSEVEVLKALKSLFEHHKALDEKVRERLRMALERVAVLEEELELSNQEA 195
Cdd:COG1196 482 LLEELAEAAARLLLLLEA--EADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVA 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 196 LNLRDQLSRRRSG------LEEPGKDGDGQTLANGLGPVGESNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEE 269
Cdd:COG1196 560 AAAIEYLKAAKAGratflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRA 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 270 LGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELASKESLYRQSEEKSRQ 349
Cdd:COG1196 640 VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEE 719
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 161016786 350 LAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEE 408
Cdd:COG1196 720 ELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
272-566 |
2.66e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 60.61 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 272 TAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELASKEslyRQSEEKSRQLA 351
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE---AEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 352 EWLDDAkQKLQQTLQKAETLPEIE--AQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQREKMNDDHNKR 429
Cdd:COG3883 90 ERARAL-YRSGGSVSYLDVLLGSEsfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 430 LSETVDKLLSESNERLQLHLKERMGALEEKNSLSEEIAnmKKLQDELLLNKEQLLAEMERMQMEIDQLRGRPPSSYSRSL 509
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA--AAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 161016786 510 PGSALELRYSQAPTLPSGAPLDPYGAGSGRAGKRGRWSGAKDESSKDWDRSAPAGSI 566
Cdd:COG3883 247 AGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGS 303
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
233-520 |
3.76e-09 |
|
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: 61.14 E-value: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 233 RRTAELEEALERQRA--EVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEK 310
Cdd:pfam02463 214 QLKEKLELEEEYLLYldYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAK 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 311 RYLSAQREATSL-HDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAE 389
Cdd:pfam02463 294 EEEELKSELLKLeRRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 390 ERHGNFEERLRQLEAQLEEKNQEL----------QRARQREKMNDDHNKRLSETVDKLLSESNERL---QLHLKERMGAL 456
Cdd:pfam02463 374 ELLAKKKLESERLSSAAKLKEEELelkseeekeaQLLLELARQLEDLLKEEKKEELEILEEEEESIelkQGKLTEEKEEL 453
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161016786 457 EEKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQLRGRPPSSYSRSLPGSALELRYSQ 520
Cdd:pfam02463 454 EKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIK 517
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
251-425 |
4.55e-09 |
|
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: 58.40 E-value: 4.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 251 QLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRylsaQREATSLHDANDkLE 330
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ----LGNVRNNKEYEA-LQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 331 NELASKESLYRQSEEKSRQLAEWLDDAKQKLQqtlqkaetlpEIEAQLAQRVAALNKAEERhgnFEERLRQLEAQLEEKN 410
Cdd:COG1579 96 KEIESLKRRISDLEDEILELMERIEELEEELA----------ELEAELAELEAELEEKKAE---LDEELAELEAELEELE 162
|
170
....*....|....*
gi 161016786 411 QElqRARQREKMNDD 425
Cdd:COG1579 163 AE--REELAAKIPPE 175
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
838-901 |
5.37e-09 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 53.45 E-value: 5.37e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161016786 838 WDGPTVVSWLELWvGMPAwYVAACRANVKSGAIMANLSDTEIQREIGISNPLHRLKLRLAIQEM 901
Cdd:smart00454 4 WSPESVADWLESI-GLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
232-433 |
5.88e-09 |
|
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: 60.74 E-value: 5.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 232 NRRTAELEEALERQRAEVCQLRERLAVLCRQMSQL---------------EEELGTAHRELGKAEEA------------- 283
Cdd:COG3096 842 RQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLnkllpqanlladetlADRLEELREELDAAQEAqafiqqhgkalaq 921
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 284 --------------NSKLQRDLKEALAQREDMEERITTLEkrYLSAQREATSLHDA----------NDKLENELASKESL 339
Cdd:COG3096 922 leplvavlqsdpeqFEQLQADYLQAKEQQRRLKQQIFALS--EVVQRRPHFSYEDAvgllgensdlNEKLRARLEQAEEA 999
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 340 YRQSEEKSRQLAEWLDDAKQKLQQtLQ-----KAETLPEIEAQLAQ-RVAALNKAEER-HGNFEERLRQLEAQLEEKNQ- 411
Cdd:COG3096 1000 RREAREQLRQAQAQYSQYNQVLAS-LKssrdaKQQTLQELEQELEElGVQADAEAEERaRIRRDELHEELSQNRSRRSQl 1078
|
250 260
....*....|....*....|..
gi 161016786 412 ELQRARQREKMnDDHNKRLSET 433
Cdd:COG3096 1079 EKQLTRCEAEM-DSLQKRLRKA 1099
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
38-496 |
6.92e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.31 E-value: 6.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 38 ERERLLETLREAQDGLATAQLRLRELGHEKDSLQRQLS-------IALPQEFAALTKELN-----------LCREQLLER 99
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggdrlEQLEREIERLERELEererrrarleaLLAALGLPL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 100 EEEIAELKAERNNTRLLLEHLECLVSRHERSLRMTVV-----KRQAQSpggVSSEVEVLKALKSLFEHHkalDEKVRERL 174
Cdd:COG4913 376 PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAalrdlRRELRE---LEAEIASLERRKSNIPAR---LLALRDAL 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 175 RMAL-----------ERVAVLEEELE--------LSNQ------------------EALNLRDQLSRRR---SGLEEPGK 214
Cdd:COG4913 450 AEALgldeaelpfvgELIEVRPEEERwrgaiervLGGFaltllvppehyaaalrwvNRLHLRGRLVYERvrtGLPDPERP 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 215 DGDGQTLANGLgpVGESNRRTAELEEALERQRAEVC-----QL-RERLAV-LCRQMSQleeelGTAHRELGKaeeaNSKL 287
Cdd:COG4913 530 RLDPDSLAGKL--DFKPHPFRAWLEAELGRRFDYVCvdspeELrRHPRAItRAGQVKG-----NGTRHEKDD----RRRI 598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 288 QRDL---KEALAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELASKESL--YRQSEEKSRQLAEWLDDAKQKLQ 362
Cdd:COG4913 599 RSRYvlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLaeYSWDEIDVASAEREIAELEAELE 678
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 363 QTLQKAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQRekmnddhnkrlsetVDKLLSESN 442
Cdd:COG4913 679 RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR--------------LEAAEDLAR 744
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 161016786 443 ERLQLHLKERMGALEEKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQ 496
Cdd:COG4913 745 LELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
154-498 |
7.81e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.54 E-value: 7.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 154 KALKSLFEHHKALDEKVRERLRMALERVAVLEE-----ELELSNQEALNLRDQLSRR---RSGLEEPGKDGDGQTLANGL 225
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkkkadEAKKKAEEDKKKADELKKAaaaKKKADEAKKKAEEKKKADEA 1436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 226 GPVGESNRRTAELEE-ALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQRE----- 299
Cdd:PTZ00121 1437 KKKAEEAKKADEAKKkAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKadeak 1516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 300 DMEERITTLEKRYLSAQREATSLHDANDKLENELASKESLYRQSEEKSRqlAEWLDDAKQKLQQTLQKAETLPEIEAQLA 379
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKK--AEEAKKAEEDKNMALRKAEEAKKAEEARI 1594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 380 QRVAALN------KAEERHGNFEERLRQLEAQLEE------------------KNQELQRARQREKMNDDHNKRLSETvD 435
Cdd:PTZ00121 1595 EEVMKLYeeekkmKAEEAKKAEEAKIKAEELKKAEeekkkveqlkkkeaeekkKAEELKKAEEENKIKAAEEAKKAEE-D 1673
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161016786 436 KLLSESNERLQLHLKERMGALEEKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQLR 498
Cdd:PTZ00121 1674 KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAK 1736
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
26-488 |
9.51e-09 |
|
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: 59.80 E-value: 9.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 26 GELERLMVTMLTERERLLETLREAQDGLATAQLRLRELGHEKDSLQRQLsialpQEFAALTKELnlcreQLLEREEEIAE 105
Cdd:pfam01576 218 TDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKI-----RELEAQISEL-----QEDLESERAAR 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 106 LKAERNNtRLLLEHLECLVSRHERSLRMTVVKRQAQSPGgvSSEVEVLK-ALKSLFEHHKALDEKVRERLRMALERvavL 184
Cdd:pfam01576 288 NKAEKQR-RDLGEELEALKTELEDTLDTTAAQQELRSKR--EQEVTELKkALEEETRSHEAQLQEMRQKHTQALEE---L 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 185 EEELElsnqEALNLRDQLSRRRSGLEEPGKD--GDGQTLANGlgpVGESNRRTAELEEALERQRAEVCQLRERLAVLCRQ 262
Cdd:pfam01576 362 TEQLE----QAKRNKANLEKAKQALESENAElqAELRTLQQA---KQDSEHKRKKLEGQLQELQARLSESERQRAELAEK 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 263 MSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERIT--TLEKRYLSAQ-----REATSLHdanDKLENELAS 335
Cdd:pfam01576 435 LSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQeeTRQKLNLSTRlrqleDERNSLQ---EQLEEEEEA 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 336 KESLYRQSEEKSRQLAEWlddaKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQR 415
Cdd:pfam01576 512 KRNVERQLSTLQAQLSDM----KKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLV 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 416 ARQREKMNDDHNKRLSETVDKLLSESNERLQLHLKERMGALEEKN-------SLSEEIANMKKLQDELLLNKEQLLAEME 488
Cdd:pfam01576 588 DLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAReketralSLARALEEALEAKEELERTNKQLRAEME 667
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
164-500 |
1.11e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 164 KALDEKVRErLRMALERVAVLEEELELSNQEALNLRDQLSRRRSGLEEPGKDGDGQTLANGLgpvgesnrrtAELEEALE 243
Cdd:COG4717 74 KELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEL----------EALEAELA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 244 RQRAEVCQLRERLAV---LCRQMSQLEEELGTAHRELGKAEEANS-KLQRDLKEALAQREDMEERITTLEKRYLSAQREA 319
Cdd:COG4717 143 ELPERLEELEERLEElreLEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 320 TSLHDANDKLENELASKESLYRQSEEKSRQLAE------------------------------------WLDDAKQKLQQ 363
Cdd:COG4717 223 EELEEELEQLENELEAAALEERLKEARLLLLIAaallallglggsllsliltiagvlflvlgllallflLLAREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 364 TLQKAETLPEIE----AQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQREKMnDDHNKRLSETVDKLLS 439
Cdd:COG4717 303 EAEELQALPALEeleeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL-EELEQEIAALLAEAGV 381
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161016786 440 ESNERLQLHLK---ERMGALEEKNSLSEEIANMKKLQDELL--LNKEQLLAEMERMQMEIDQLRGR 500
Cdd:COG4717 382 EDEEELRAALEqaeEYQELKEELEELEEQLEELLGELEELLeaLDEEELEEELEELEEELEELEEE 447
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
161-493 |
1.60e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.38 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 161 EHHKALDEKVRERLRMAlERVAVLEEELELSNQEalnlRDQLSRRRSGLEEPGKDGDGQTLANGlgpvgESNRRTAELEE 240
Cdd:PTZ00121 1216 EARKAEDAKKAEAVKKA-EEAKKDAEEAKKAEEE----RNNEEIRKFEEARMAHFARRQAAIKA-----EEARKADELKK 1285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 241 ALERQRAEVCQLRERLavlcrqmsQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREAT 320
Cdd:PTZ00121 1286 AEEKKKADEAKKAEEK--------KKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD 1357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 321 SLHDANDKLENELASKESLYRQSEEKSRQLAEW--LDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEERHGNFEER 398
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKkkADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAK 1437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 399 LRQLEA----QLEEKNQELQRARQREKMNDDhnKRLSETVDKLLSESneRLQLHLKERMGALEEKNSLSEEIANMKKLQD 474
Cdd:PTZ00121 1438 KKAEEAkkadEAKKKAEEAKKAEEAKKKAEE--AKKADEAKKKAEEA--KKADEAKKKAEEAKKKADEAKKAAEAKKKAD 1513
|
330
....*....|....*....
gi 161016786 475 ELLLNKEQLLAEMERMQME 493
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEE 1532
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
233-474 |
2.55e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 233 RRTAELEEALERQRAEVCQLRERlAVLCRQMSQLEEELGTAHRELGKAEEANSKlqrdlKEALAQREDMEERITTLEKRY 312
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEE-ARIEEVMKLYEEEKKMKAEEAKKAEEAKIK-----AEELKKAEEEKKKVEQLKKKE 1642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 313 LSAQREATSLHDANdklENELASKESLYRQSEE---KSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAE 389
Cdd:PTZ00121 1643 AEEKKKAEELKKAE---EENKIKAAEEAKKAEEdkkKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAE 1719
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 390 ERHGNFEERLRQLEAQLEEKNQELQRARQREKMNDDHNKrlsetVDKLLSESNERLQLHLKERMGALEEKNSLSEEIANM 469
Cdd:PTZ00121 1720 ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKK-----IAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRM 1794
|
....*...
gi 161016786 470 ---KKLQD 474
Cdd:PTZ00121 1795 evdKKIKD 1802
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
248-412 |
2.56e-08 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 55.30 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 248 EVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDME---ERITTLEKRYLSAQREATSLHD 324
Cdd:pfam13851 34 EIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKnlkARLKVLEKELKDLKWEHEVLEQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 325 ANDKLENElasKESLYRQSEEKsrqlaewLDDAKQK-------LQQTLQK-AETLPEIEAQLAQRVAALNKAEERHGNFE 396
Cdd:pfam13851 114 RFEKVERE---RDELYDKFEAA-------IQDVQQKtglknllLEKKLQAlGETLEKKEAQLNEVLAAANLDPDALQAVT 183
|
170
....*....|....*.
gi 161016786 397 ERLRQLeaqLEEKNQE 412
Cdd:pfam13851 184 EKLEDV---LESKNQL 196
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
48-499 |
3.34e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 58.06 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 48 EAQDGLATAQLRLRELGHEKDSLQRQLSIALPQEFAALTKELNLCREQLLEREEEIAELKAERNNTRLLLEHLECLVSRH 127
Cdd:TIGR00618 430 KKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGS 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 128 ERSLRMTVVkrQAQSPGGVSSEVEvlkALKSLFEHHKALDEKVRERLRMALERVAVLEEELELSNQEALNLRDQLSRRRS 207
Cdd:TIGR00618 510 CIHPNPARQ--DIDNPGPLTRRMQ---RGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKE 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 208 GLEEPgkdgdgQTLANGLGPVGESNrrtAELEEAL-ERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSK 286
Cdd:TIGR00618 585 DIPNL------QNITVRLQDLTEKL---SEAEDMLaCEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTL 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 287 LQRDLKEA-LAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEW---LDDAKQKLQ 362
Cdd:TIGR00618 656 TQERVREHaLSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIenaSSSLGSDLA 735
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 363 QTLQK-AETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQ-RARQREKMNDDHNKRLSETVDKL--- 437
Cdd:TIGR00618 736 AREDAlNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQfFNRLREEDTHLLKTLEAEIGQEIpsd 815
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161016786 438 ---LSESNERLQLHLKERMGALEEKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQLRG 499
Cdd:TIGR00618 816 ediLNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNG 880
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
261-512 |
3.55e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.08 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 261 RQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELaskesly 340
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 341 rqsEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQre 420
Cdd:COG4942 100 ---EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA-- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 421 kmnddhnkRLSETVDKlLSESNERLQLHLKERMGALEEknsLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQLRGR 500
Cdd:COG4942 175 --------ELEALLAE-LEEERAALEALKAERQKLLAR---LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
250
....*....|..
gi 161016786 501 PPSSYSRSLPGS 512
Cdd:COG4942 243 TPAAGFAALKGK 254
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
26-422 |
3.63e-08 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 57.00 E-value: 3.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 26 GELERLMVTMLTERERLLETLREAQDGLATAQLRLRELGHEKDSLQRQLSiALPQEFAALTKELNLCREQLLEREEEIAE 105
Cdd:pfam19220 30 SQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLS-AAEGELEELVARLAKLEAALREAEAAKEE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 106 LKAERNNTRLLLEHLEclvsrherslrmtvvKRQAQspggvssEVEVLKALKslfEHHKALdekvRERLRMALERVAVLE 185
Cdd:pfam19220 109 LRIELRDKTAQAEALE---------------RQLAA-------ETEQNRALE---EENKAL----REEAQAAEKALQRAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 186 EELeLSNQEALNLRDQLSRRRSGLEEpgkdgdgQTLANglgpVGESNRRTAELEEALERQRAEVCQLRERLAVL----CR 261
Cdd:pfam19220 160 GEL-ATARERLALLEQENRRLQALSE-------EQAAE----LAELTRRLAELETQLDATRARLRALEGQLAAEqaerER 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 262 QMSQLEEELGTAHRELG----KAEEANSKL---QRDLKEALAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELA 334
Cdd:pfam19220 228 AEAQLEEAVEAHRAERAslrmKLEALTARAaatEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 335 SKESLYRQSEEKSRQLAEWLDdakqklqqTLQKAetlpeieaqLAQRVAALNKAEERHGNFEERLRQLE-------AQLE 407
Cdd:pfam19220 308 RRTQQFQEMQRARAELEERAE--------MLTKA---------LAAKDAALERAEERIASLSDRIAELTkrfeverAALE 370
|
410
....*....|....*
gi 161016786 408 EKNQELQRARQREKM 422
Cdd:pfam19220 371 QANRRLKEELQRERA 385
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
166-405 |
4.46e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.33 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 166 LDEKVRERLRMALERVAVLEEELELSNQEALNLRDQLS--RRRSGLEEPgkDGDGQTLANglgpvgesnrRTAELEEALE 243
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDL--SEEAKLLLQ----------QLSELESQLA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 244 RQRAEVCQLRERLAVLCRQMSQLEEELgtahrelgkAEEANSKLQRDLKEALAQredMEERITTLEKRYLSAQREATSLH 323
Cdd:COG3206 230 EARAELAEAEARLAALRAQLGSGPDAL---------PELLQSPVIQQLRAQLAE---LEAELAELSARYTPNHPDVIALR 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 324 DANDKLENELASKESLYRQSEEKSRQ-LAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQL 402
Cdd:COG3206 298 AQIAALRAQLQQEAQRILASLEAELEaLQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
...
gi 161016786 403 EAQ 405
Cdd:COG3206 378 RLA 380
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
230-444 |
4.75e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 4.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 230 ESNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLE 309
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 310 KRYlSAQREATSLHDANDKLE--------NELASKESLYRQSEEKSRQLAEWLDDAKQKLQQ-----TLQKAEtLPEIEA 376
Cdd:COG4942 104 EEL-AELLRALYRLGRQPPLAlllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAAlraelEAERAE-LEALLA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161016786 377 QLAQRVAALNKAEERHgnfEERLRQLEAQLEEKNQELQRARQREkmnddhnKRLSETVDKLLSESNER 444
Cdd:COG4942 182 ELEEERAALEALKAER---QKLLARLEKELAELAAELAELQQEA-------EELEALIARLEAEAAAA 239
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
263-492 |
4.90e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 4.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 263 MSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYlsaqreatslhdanDKLENELASKESLYRQ 342
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEEL--------------EELEEELEELEAELEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 343 SEEKSRQLaewldDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQRekM 422
Cdd:COG4717 114 LREELEKL-----EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQ--L 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 423 NDDHNKRLSETVDKLlSESNERLQLHLKERMGALEEKNSLSEEIANMKKLQdeLLLNKEQLLAEMERMQM 492
Cdd:COG4717 187 SLATEEELQDLAEEL-EELQQRLAELEEELEEAQEELEELEEELEQLENEL--EAAALEERLKEARLLLL 253
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
261-500 |
4.90e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 4.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 261 RQMSQLEEeLGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELASKESLY 340
Cdd:PRK03918 152 RQILGLDD-YENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 341 RQSEEKsrqlaewlddakqklqqtlqkAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQ---LEEKNQELQRAR 417
Cdd:PRK03918 231 KELEEL---------------------KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEieeLEEKVKELKELK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 418 QRE-------KMNDDHNKRLSEtVDKLLSESNERLQlHLKERMGALEEKNSLSEEIAN-MKKLQDEL--LLNKEQLLAEM 487
Cdd:PRK03918 290 EKAeeyiklsEFYEEYLDELRE-IEKRLSRLEEEIN-GIEERIKELEEKEERLEELKKkLKELEKRLeeLEERHELYEEA 367
|
250
....*....|...
gi 161016786 488 ERMQMEIDQLRGR 500
Cdd:PRK03918 368 KAKKEELERLKKR 380
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
38-498 |
5.90e-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: 5.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 38 ERERLLETLREAQDGLATAQLRLRELGHEKDSLQRQLSiALPQEFAALTKELNLCREQLLEREEEIAELKAERNNTRLLL 117
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS-ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 118 EHLECLVSRHERSLRMT------VVKRQAQSPGGVSSEVEVLKALKSLFEHHKALDEKVRERLRMALERVAVLEEELELS 191
Cdd:TIGR02168 319 EELEAQLEELESKLDELaeelaeLEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 192 NQEALNLRDQLSRRRSGLEEPGKDGDGQTLANGLGPVGESNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELG 271
Cdd:TIGR02168 399 NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 272 TAHRELGKA----------EEANSKLQRDLKEALAQREDM-------------------------EERITTLEKRYLSAQ 316
Cdd:TIGR02168 479 AAERELAQLqarldslerlQENLEGFSEGVKALLKNQSGLsgilgvlselisvdegyeaaieaalGGRLQAVVVENLNAA 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 317 REATSLHDANDK-----------LENELASKESLYRQSEEKSRQLAEWLDDAKQKLQ-------------QTLQKA---- 368
Cdd:TIGR02168 559 KKAIAFLKQNELgrvtflpldsiKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvDDLDNAlela 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 369 ---------------------------------------------ETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLE 403
Cdd:TIGR02168 639 kklrpgyrivtldgdlvrpggvitggsaktnssilerrreieeleEKIEELEEKIAELEKALAELRKELEELEEELEQLR 718
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 404 AQLEEKNQELQRARQREkmnddhnKRLSETVDKLLsesnERLQLHLKERMGALEEKNSLSEEIANMKKLQDELLLNKEQL 483
Cdd:TIGR02168 719 KELEELSRQISALRKDL-------ARLEAEVEQLE----ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL 787
|
570
....*....|....*
gi 161016786 484 LAEMERMQMEIDQLR 498
Cdd:TIGR02168 788 EAQIEQLKEELKALR 802
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
146-497 |
6.06e-08 |
|
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: 57.04 E-value: 6.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 146 VSSEVEVLKALKSLFEHHKALDEkvrerlrmalERVAVleEELELSNQE-ALNLRDQLSRRRSGLEEpgkDGDGQTLANG 224
Cdd:pfam05483 95 VSIEAELKQKENKLQENRKIIEA----------QRKAI--QELQFENEKvSLKLEEEIQENKDLIKE---NNATRHLCNL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 225 LGpvgESNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEEL----GTAHRELG-KAEEANSKLQRDLKEALAQRE 299
Cdd:pfam05483 160 LK---ETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELrvqaENARLEMHfKLKEDHEKIQHLEEEYKKEIN 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 300 DMEERITTLEKRYLSAQREATSL-------HDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLP 372
Cdd:pfam05483 237 DKEKQVSLLLIQITEKENKMKDLtflleesRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 373 EiEAQLAQR------------VAALNKAEERHGNFEERLRQLEAQLEEKnqeLQRARQREKMNDDHNKRLSETVDKLLSE 440
Cdd:pfam05483 317 E-DLQIATKticqlteekeaqMEELNKAKAAHSFVVTEFEATTCSLEEL---LRTEQQRLEKNEDQLKIITMELQKKSSE 392
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161016786 441 SNERLQL------HLKERMGALEEKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQL 497
Cdd:pfam05483 393 LEEMTKFknnkevELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDL 455
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
144-489 |
6.32e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 6.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 144 GGVSSEVEVLKALKSLFEHHKALDEKVRERLRMALERVAVLEEELELSNQEALNLRDQLSRrrsgLEEPGKDGDGQTLAN 223
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE----LKELKEKAEEYIKLS 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 224 GLgpVGESNRRTAELEEALERQRAEVCQLRERLAVLC---RQMSQLEEELGTAHRELGKAEEANSKLQrDLKEALAQRED 300
Cdd:PRK03918 300 EF--YEEYLDELREIEKRLSRLEEEINGIEERIKELEekeERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELER 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 301 MEERIT-----TLEKRYLSAQREATSLHDANDKLENELASKEslyrqSEEKSRQLA-EWLDDAKQKLqqTLQKAETLPEI 374
Cdd:PRK03918 377 LKKRLTgltpeKLEKELEELEKAKEEIEEEISKITARIGELK-----KEIKELKKAiEELKKAKGKC--PVCGRELTEEH 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 375 EAQLAQRVAA-LNKAEERHGNFEERLRQLEAQLEEKNQELQRARQREKMNDDHnKRLSETVDKLLSESNERLQLHLKERM 453
Cdd:PRK03918 450 RKELLEEYTAeLKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELA-EQLKELEEKLKKYNLEELEKKAEEYE 528
|
330 340 350
....*....|....*....|....*....|....*..
gi 161016786 454 GALEEKNSLSEEIANMKK-LQDELLLNKEqlLAEMER 489
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKeLEKLEELKKK--LAELEK 563
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
80-500 |
6.94e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 6.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 80 QEFAALTKELNLcreqlleREEEIAELKAERNNTRLLLEHLECLVSRHErSLRMTVVKRQAQSPGGVSSEVEVLKALKSL 159
Cdd:PRK03918 200 KELEEVLREINE-------ISSELPELREELEKLEKEVKELEELKEEIE-ELEKELESLEGSKRKLEEKIRELEERIEEL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 160 FEHHKALDEKVRE--RLRMALERVAVLEEELELSNQEALNLRDQLSR---RRSGLEEPGKDgdgqtLANGLGPVGESNRR 234
Cdd:PRK03918 272 KKEIEELEEKVKElkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRleeEINGIEERIKE-----LEEKEERLEELKKK 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 235 TAELEEALERQRAEVcQLRERLAVLCRQMSQLEEELG-----TAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLE 309
Cdd:PRK03918 347 LKELEKRLEELEERH-ELYEEAKAKKEELERLKKRLTgltpeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 310 K---RYLSAQ-------REATSLHDAN---------DKLENELASKESLYRQSEEKSRQLAEWLDDAKqKLQQTLQKAET 370
Cdd:PRK03918 426 KaieELKKAKgkcpvcgRELTEEHRKElleeytaelKRIEKELKEIEEKERKLRKELRELEKVLKKES-ELIKLKELAEQ 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 371 LPEIEAQLAQ-RVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRA-------RQREKMNDDHNKRLSETVDKLLSESN 442
Cdd:PRK03918 505 LKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLeelkkklAELEKKLDELEEELAELLKELEELGF 584
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161016786 443 ERLQlHLKERMGALEE-----------KNSLSEEIANMKKLQDELllnkEQLLAEMERMQMEIDQLRGR 500
Cdd:PRK03918 585 ESVE-ELEERLKELEPfyneylelkdaEKELEREEKELKKLEEEL----DKAFEELAETEKRLEELRKE 648
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
245-470 |
7.97e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 7.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 245 QRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHD 324
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 325 ANDKLENELASK-ESLYRQSE----------EKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAeerhg 393
Cdd:COG4942 98 ELEAQKEELAELlRALYRLGRqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE----- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 394 nfEERLRQLEAQLEEKNQELQRAR-QREKMNDDHNKRLSETVDKL--LSESNERLQLHLK--ERMGALEEKNSLSEEIAN 468
Cdd:COG4942 173 --RAELEALLAELEEERAALEALKaERQKLLARLEKELAELAAELaeLQQEAEELEALIArlEAEAAAAAERTPAAGFAA 250
|
..
gi 161016786 469 MK 470
Cdd:COG4942 251 LK 252
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
262-497 |
1.31e-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: 56.18 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 262 QMSQLEEELGTAHRELGKAEEAN-------SKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELA 334
Cdd:TIGR04523 118 QKNKLEVELNKLEKQKKENKKNIdkflteiKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 335 SKE---SLYRQSEEKSRQLAEWLDDAKQKlQQTLQKaeTLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQ 411
Cdd:TIGR04523 198 KLElllSNLKKKIQKNKSLESQISELKKQ-NNQLKD--NIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQK 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 412 ELQRArqrEKMNDDHNKRLSETVDKLLSESNERLQLHLKERMGALEEK------------------NSLSEEIANMKKLQ 473
Cdd:TIGR04523 275 ELEQN---NKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQekkleeiqnqisqnnkiiSQLNEQISQLKKEL 351
|
250 260
....*....|....*....|....
gi 161016786 474 DELLLNKEQLLAEMERMQMEIDQL 497
Cdd:TIGR04523 352 TNSESENSEKQRELEEKQNEIEKL 375
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
259-498 |
1.54e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.80 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 259 LCRQMSQLEEELGTAHRELGKAEE--ANSKLQRDLKE-ALAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELAS 335
Cdd:TIGR04523 164 LKKQKEELENELNLLEKEKLNIQKniDKIKNKLLKLElLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 336 KESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAET-----------LPEIEAQLA----QRVAALNKA-EERHGNFEERL 399
Cdd:TIGR04523 244 KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQnnkkikelekqLNQLKSEISdlnnQKEQDWNKElKSELKNQEKKL 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 400 RQLEAQLEEKNQELQRARQ------REKMNDDHNKrlsETVDKLLSESNERLQLHLKERMGALEE-------KNSLSEEI 466
Cdd:TIGR04523 324 EEIQNQISQNNKIISQLNEqisqlkKELTNSESEN---SEKQRELEEKQNEIEKLKKENQSYKQEiknlesqINDLESKI 400
|
250 260 270
....*....|....*....|....*....|..
gi 161016786 467 ANMKKLQDELLLNKEQLLAEMERMQMEIDQLR 498
Cdd:TIGR04523 401 QNQEKLNQQKDEQIKKLQQEKELLEKEIERLK 432
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
238-497 |
1.64e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 55.95 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 238 LEEALERQRAEVCQLRERLAvlcRQMSQLEEELGTAHR---ELGKA----EEANSKLQRDLKEALAQREDMEER------ 304
Cdd:pfam01576 336 LEEETRSHEAQLQEMRQKHT---QALEELTEQLEQAKRnkaNLEKAkqalESENAELQAELRTLQQAKQDSEHKrkkleg 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 305 -ITTLEKRYLSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQ--QTLQKAETLPEIeaQLAQR 381
Cdd:pfam01576 413 qLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQdtQELLQEETRQKL--NLSTR 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 382 VAAL----NKAEERHGNFEERLRQLEAQLEEKNQELQRARQreKMNDDhnkrlSETVDkLLSESNERLQLHLKERMGALE 457
Cdd:pfam01576 491 LRQLederNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKK--KLEED-----AGTLE-ALEEGKKRLQRELEALTQQLE 562
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 161016786 458 EKNSLSEEIANMKK-LQDEL------LLNKEQLLAEMERMQMEIDQL 497
Cdd:pfam01576 563 EKAAAYDKLEKTKNrLQQELddllvdLDHQRQLVSNLEKKQKKFDQM 609
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
230-496 |
2.15e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 230 ESNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEansklqrdlkeaLAQREDMEERITTLE 309
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE------------LKKAEEEKKKVEQLK 1639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 310 KRYLSAQREATSLHDANdklENELASKESLYRQSEEKSRQLAEwlddAKQKLQQTLQKAETLPEiEAQLAQRVAALNKAE 389
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAE---EENKIKAAEEAKKAEEDKKKAEE----AKKAEEDEKKAAEALKK-EAEEAKKAEELKKKE 1711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 390 ERHGNFEERLRQLEAQLEEKNQELQRARQREkmnddhnKRLSETVDKLLSESNERLQLHLKERMGALEEKNSLSEEIanm 469
Cdd:PTZ00121 1712 AEEKKKAEELKKAEEENKIKAEEAKKEAEED-------KKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI--- 1781
|
250 260
....*....|....*....|....*..
gi 161016786 470 kklqdelllnKEQLLAEMERMQMEIDQ 496
Cdd:PTZ00121 1782 ----------EEELDEEDEKRRMEVDK 1798
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
237-440 |
2.31e-07 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 55.08 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 237 ELEEALERQRAEVCQLRERLAVLCRQMSQLE---------EELGTAHRELGKAEeansKLQRDLKEALAQREDMEERITT 307
Cdd:COG0497 169 ALKKELEELRADEAERARELDLLRFQLEELEaaalqpgeeEELEEERRRLSNAE----KLREALQEALEALSGGEGGALD 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 308 LekryLS-AQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDD--------------------AKQKLQQTLq 366
Cdd:COG0497 245 L----LGqALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSlefdperleeveerlallrrLARKYGVTV- 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161016786 367 kaETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQRekmnddHNKRLSETVDKLLSE 440
Cdd:COG0497 320 --EELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKK------AAKKLEKAVTAELAD 385
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
234-497 |
2.40e-07 |
|
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: 55.13 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 234 RTAELEEALERQRAEVCQLRErlavLCRQMSQLEEELGTAHRELGKAEEA----------NSKLQRDLK--EALAQR--- 298
Cdd:pfam05557 198 RIPELEKELERLREHNKHLNE----NIENKLLLKEEVEDLKRKLEREEKYreeaatleleKEKLEQELQswVKLAQDtgl 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 299 -----EDMEERITTLEkrylsaQREATsLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLqqtlqkaETLPE 373
Cdd:pfam05557 274 nlrspEDLSRRIEQLQ------QREIV-LKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKL-------KRHKA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 374 IEAQLAQRVAALNKaeERHGnFEERLRQLEAQLEEKN---QELQRARQREKMNDDHNKRLSE------------TVDKLL 438
Cdd:pfam05557 340 LVRRLQRRVLLLTK--ERDG-YRAILESYDKELTMSNyspQLLERIEEAEDMTQKMQAHNEEmeaqlsvaeeelGGYKQQ 416
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 161016786 439 SESNERlQLHLKERMGALEEKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQL 497
Cdd:pfam05557 417 AQTLER-ELQALRQQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERR 474
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
286-452 |
2.42e-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: 53.00 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 286 KLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAewlddaKQKLQQTL 365
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR------NNKEYEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 366 QKaetlpEIEAQlaqrvaalnkaEERHGNFEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKLLSESNERL 445
Cdd:COG1579 95 QK-----EIESL-----------KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
....*..
gi 161016786 446 QLHLKER 452
Cdd:COG1579 159 EELEAER 165
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
40-418 |
2.57e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 40 ERLLETLREAQDGLATAQLRLRELGHEKDSLQRQLSIALPQEFAALTKELNlcreqllEREEEIAELKAERNNTRLLLEH 119
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE-------ELQQRLAELEEELEEAQEELEE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 120 LECLVSRHERSLRMTVVKRQAQSPGGVSSEVEVLKALKSLFEHHKALDEKVRERLRMALERVAVLEEELELSNQEALNLR 199
Cdd:COG4717 225 LEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 200 DQLSR--RRSGLEEpgkdgdgQTLANGLGPVGESNRRTAELEEALERQRAEVCQLRERLAVLCRQMsQLEEELGTAHREL 277
Cdd:COG4717 305 EELQAlpALEELEE-------EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL-QLEELEQEIAALL 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 278 GKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHDANDK--LENELASKESLYRQSEEKSRQLAEWLD 355
Cdd:COG4717 377 AEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEeeLEEELEELEEELEELEEELEELREELA 456
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161016786 356 DAKQKLQQtLQKAETLPEIEAQLAQRVAALNKAEERHGnfeeRLRQLEAQLEEKNQELQRARQ 418
Cdd:COG4717 457 ELEAELEQ-LEEDGELAELLQELEELKAELRELAEEWA----ALKLALELLEEAREEYREERL 514
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
156-432 |
3.47e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 53.75 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 156 LKSLFEHHKALDEKVRERLRMALERVAVLEEELELSNQEALNLRDQLSRRRSGLEEpgKDGDGQTLANGLGpvgESNRRT 235
Cdd:COG4372 15 LFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQ--ARSELEQLEEELE---ELNEQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 236 AELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYlsA 315
Cdd:COG4372 90 QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL--A 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 316 QREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEERHGNF 395
Cdd:COG4372 168 ALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEED 247
|
250 260 270
....*....|....*....|....*....|....*..
gi 161016786 396 EERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSE 432
Cdd:COG4372 248 KEELLEEVILKEIEELELAILVEKDTEEEELEIAALE 284
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
242-408 |
4.24e-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: 52.23 E-value: 4.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 242 LERQRAEvcqLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTL--EKRYLSAQREA 319
Cdd:COG1579 22 LEHRLKE---LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYEALQKEI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 320 TSLHDANDKLENELAskeSLYRQSEEKSRQLAEwLDDAKQKLQQTLQkaetlpEIEAQLAQRVAALNKAEERHgnfEERL 399
Cdd:COG1579 99 ESLKRRISDLEDEIL---ELMERIEELEEELAE-LEAELAELEAELE------EKKAELDEELAELEAELEEL---EAER 165
|
....*....
gi 161016786 400 RQLEAQLEE 408
Cdd:COG1579 166 EELAAKIPP 174
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
121-529 |
4.62e-07 |
|
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: 53.75 E-value: 4.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 121 ECLVSRHErslrmtVVKRQAQSPGGVSSEVEVLKALKSLFEH-HKALDEKVrERLRMALERVAVLEEELELSNQEALNLR 199
Cdd:pfam07888 38 ECLQERAE------LLQAQEAANRQREKEKERYKRDREQWERqRRELESRV-AELKEELRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 200 DQLSRRRSGLEEPGKD---------GDGQTLANglgpvgESNRRTAELEEALERQRAEVCQLRERLAvlcrQMSQLEEEL 270
Cdd:pfam07888 111 EELSEEKDALLAQRAAhearireleEDIKTLTQ------RVLERETELERMKERAKKAGAQRKEEEA----ERKQLQAKL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 271 GTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATslhdANDKLENELASKESLYRQSEEKSRQL 350
Cdd:pfam07888 181 QQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEA----ENEALLEELRSLQERLNASERKVEGL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 351 AEWL-------DDAKQKLQQT-LQKAE-TLPEIEAQLAQRVAALNKAEERHG---NFE---ERLRQLEAQLEEKNQELQR 415
Cdd:pfam07888 257 GEELssmaaqrDRTQAELHQArLQAAQlTLQLADASLALREGRARWAQERETlqqSAEadkDRIEKLSAELQRLEERLQE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 416 AR-QREKMNddhnkrlsetVDKLLSESNERLQLHlkermgalEEKNSLSEEIANMKKLQDElllnKEQLLAEMERMQMEI 494
Cdd:pfam07888 337 ERmEREKLE----------VELGREKDCNRVQLS--------ESRRELQELKASLRVAQKE----KEQLQAEKQELLEYI 394
|
410 420 430
....*....|....*....|....*....|....*
gi 161016786 495 DQLRGRppssysrslPGSALELRYSQAPTLPSGAP 529
Cdd:pfam07888 395 RQLEQR---------LETVADAKWSEAALTSTERP 420
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
27-498 |
5.48e-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: 5.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 27 ELERLMVTmLTERERLLETLREAQDGLATAQLRLRELghekdslqRQLSIALPQEFAAltKELNLCREQLLEREEEIAEL 106
Cdd:COG4913 239 RAHEALED-AREQIELLEPIRELAERYAAARERLAEL--------EYLRAALRLWFAQ--RRLELLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 107 KAERNNTRLLLEHLEclvsRHERSLRmtvvKRQAQSPGGvssEVEVLKALKSlfEHHKALDEKVRERLRMAlERVAVLEE 186
Cdd:COG4913 308 EAELERLEARLDALR----EELDELE----AQIRGNGGD---RLEQLEREIE--RLERELEERERRRARLE-ALLAALGL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 187 ELELSNQEALNLRDQLSRRRSGLEEpGKDGDGQTLANGLGPVGESNRRTAELE---EALERQR----AEVCQLRERlavL 259
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLEALEE-ELEALEEALAEAEAALRDLRRELRELEaeiASLERRKsnipARLLALRDA---L 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 260 CRQMSQLEEEL-----------------GTAHRELGKAeeANSKL--QRDLKEALA--QREDMEERITTLE-----KRYL 313
Cdd:COG4913 450 AEALGLDEAELpfvgelievrpeeerwrGAIERVLGGF--ALTLLvpPEHYAAALRwvNRLHLRGRLVYERvrtglPDPE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 314 SAQREATSL--------HDANDKLENELASKESLY--------------------------------------------- 340
Cdd:COG4913 528 RPRLDPDSLagkldfkpHPFRAWLEAELGRRFDYVcvdspeelrrhpraitragqvkgngtrhekddrrrirsryvlgfd 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 341 --RQSEEKSRQLAEwLDDAKQKLQQTLQKAEtlpEIEAQLAQRVAALNKAEERhgNFEE-RLRQLEAQLEEKNQELQRAR 417
Cdd:COG4913 608 nrAKLAALEAELAE-LEEELAEAEERLEALE---AELDALQERREALQRLAEY--SWDEiDVASAEREIAELEAELERLD 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 418 QrekmNDDHNKRLSETVDKLlsesNERLQLHLKERMGALEEKNSLSEEIANMKKLQDELllnkEQLLAEMERMQMEIDQL 497
Cdd:COG4913 682 A----SSDDLAALEEQLEEL----EAELEELEEELDELKGEIGRLEKELEQAEEELDEL----QDRLEAAEDLARLELRA 749
|
.
gi 161016786 498 R 498
Cdd:COG4913 750 L 750
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
180-298 |
5.55e-07 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 53.05 E-value: 5.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 180 RVAVLEEELELSNQEALNLRDQLSRRRSGLEEPGKDGDG-QTLANGL-GPVGESNRRTAELEEALERQRAEVCQLRERLA 257
Cdd:PRK09039 61 QIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRlQALLAELaGAGAAAEGRAGELAQELDSEKQVSARALAQVE 140
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 161016786 258 VLCRQMSQLEEELGTAHRELGKAE----EANSKLQ---RDLKEALAQR 298
Cdd:PRK09039 141 LLNQQIAALRRQLAALEAALDASEkrdrESQAKIAdlgRRLNVALAQR 188
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
230-500 |
5.73e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.19 E-value: 5.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 230 ESNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHrelgkaeeansklqrdlkeaLAQREDMEERITTLE 309
Cdd:PRK04863 841 QLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLN--------------------LLADETLADRVEEIR 900
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 310 KRYLSAQrEATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLpeieAQLAQRVAALN--K 387
Cdd:PRK04863 901 EQLDEAE-EAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFAL----TEVVQRRAHFSyeD 975
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 388 AEERHGNFEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKLLSESNERLQLH--LKERMGALEEKNSLSEE 465
Cdd:PRK04863 976 AAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLqeLKQELQDLGVPADSGAE 1055
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 161016786 466 I---ANMKKLQDELLLN---KEQLLAEMERMQMEIDQLRGR 500
Cdd:PRK04863 1056 ErarARRDELHARLSANrsrRNQLEKQLTFCEAEMDNLTKK 1096
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
155-413 |
6.35e-07 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 53.67 E-value: 6.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 155 ALKSLFEhhkALDEKVR--ERLRMALERV-AVLEEELELSNQEALNLRDQLSRRRSGLEEPGKDG-DGQTLANGLGPVG- 229
Cdd:pfam10174 437 ALTTLEE---ALSEKERiiERLKEQREREdRERLEELESLKKENKDLKEKVSALQPELTEKESSLiDLKEHASSLASSGl 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 230 ESNRRTAELEEALERQRAEVCQLRERL-------------AVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALA 296
Cdd:pfam10174 514 KKDSKLKSLEIAVEQKKEECSKLENQLkkahnaeeavrtnPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVEN 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 297 QREDMEERITTLEKRYLSAQREATSLH------------DANDKLENELASKESLYRQSEEKS-RQLAEWLDDAKQKLQQ 363
Cdd:pfam10174 594 EKNDKDKKIAELESLTLRQMKEQNKKVanikhgqqemkkKGAQLLEEARRREDNLADNSQQLQlEELMGALEKTRQELDA 673
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 161016786 364 TLQKaetLPEIEAQLAQRVAALNKAeeRHgnfeERLRQLEAQLEEKNQEL 413
Cdd:pfam10174 674 TKAR---LSSTQQSLAEKDGHLTNL--RA----ERRKQLEEILEMKQEAL 714
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
262-500 |
6.59e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.89 E-value: 6.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 262 QMSQLEEelgtaHRE-LGKAEEANSKLQRDLKEALaqrEDMEERIttlekrylsAQREATSLHDANDKLENELASKESLY 340
Cdd:PRK02224 160 QLGKLEE-----YRErASDARLGVERVLSDQRGSL---DQLKAQI---------EEKEEKDLHERLNGLESELAELDEEI 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 341 RQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQRE 420
Cdd:PRK02224 223 ERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 421 KMNDDHNKRLS---ETVDKLLSESNERLQLHLKERMGALEEKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQL 497
Cdd:PRK02224 303 GLDDADAEAVEarrEELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDR 382
|
...
gi 161016786 498 RGR 500
Cdd:PRK02224 383 REE 385
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
235-498 |
6.63e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 53.90 E-value: 6.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 235 TAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQrEDMEERITTLEKRYLS 314
Cdd:TIGR00606 572 KKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS-QDEESDLERLKEEIEK 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 315 AQREATSLHDAN---DKLENELASKES----LYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETL-PEIEAQLAQRVAALN 386
Cdd:TIGR00606 651 SSKQRAMLAGATavySQFITQLTDENQsccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTeSELKKKEKRRDEMLG 730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 387 KAEERHGNFEERLRQLEaQLEEKNQELQRARQREKMNDDHNKRLSETVDKLLSESN---------ERLQLHLKERMGALE 457
Cdd:TIGR00606 731 LAPGRQSIIDLKEKEIP-ELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKvcltdvtimERFQMELKDVERKIA 809
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 161016786 458 EKNSLSEEIANMKKLQdELLLNKEQLLAEMERMQMEIDQLR 498
Cdd:TIGR00606 810 QQAAKLQGSDLDRTVQ-QVNQEKQEKQHELDTVVSKIELNR 849
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
147-338 |
8.79e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 8.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 147 SSEVEVLKALKSLFEHHKALDEKVRE---RLRMALERVAVLEEELELSNQEALNLRDQLSRRRSGLEEPGKDGDGQTLAN 223
Cdd:COG4942 48 KEEKALLKQLAALERRIAALARRIRAleqELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLS 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 224 GLGPvGESNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEE 303
Cdd:COG4942 128 PEDF-LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEK 206
|
170 180 190
....*....|....*....|....*....|....*
gi 161016786 304 RITTLEKRYLSAQREATSLHDANDKLENELASKES 338
Cdd:COG4942 207 ELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
225-471 |
8.87e-07 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 53.04 E-value: 8.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 225 LGPVGESNRRTAELEEALERQRAEVCQLRERLAVLCRQMS---QLEEELGTAHRELGKAEEANSKLQRDlKEALAQREDM 301
Cdd:COG5185 267 LEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDikkATESLEEQLAAAEAEQELEESKRETE-TGIQNLTAEI 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 302 EERITTLEKRYLSAQREATSLHDAND------KLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETlpeie 375
Cdd:COG5185 346 EQGQESLTENLEAIKEEIENIVGEVElsksseELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADR----- 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 376 aQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQreKMNDDHNKRLSETVDKLLSESNERLQlHLKERMGA 455
Cdd:COG5185 421 -QIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQ--SRLEEAYDEINRSVRSKKEDLNEELT-QIESRVST 496
|
250
....*....|....*.
gi 161016786 456 LeeKNSLSEEIANMKK 471
Cdd:COG5185 497 L--KATLEKLRAKLER 510
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
171-497 |
9.85e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 53.42 E-value: 9.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 171 RERLRMALERVAVLEEELeLSNQEALNLR-----------DQLSRRRSGLEEpgkdgDGQTLANGLGPVGESNRrtaeLE 239
Cdd:COG3096 277 ANERRELSERALELRREL-FGARRQLAEEqyrlvemarelEELSARESDLEQ-----DYQAASDHLNLVQTALR----QQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 240 EALERQRAEVCQLRERLAvlcRQMSQLEEelgtAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREA 319
Cdd:COG3096 347 EKIERYQEDLEELTERLE---EQEEVVEE----AAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAV 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 320 TSLHDANDKLEN---ELASKESLYRQSEEKSRQLAEWLDDAKQKLQ-------------QTLQK---------------- 367
Cdd:COG3096 420 QALEKARALCGLpdlTPENAEDYLAAFRAKEQQATEEVLELEQKLSvadaarrqfekayELVCKiageversqawqtare 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 368 -----------AETLPEIEAQLA---QRVAALNKAEE-------RHG-------NFEERLRQLEAQLEEKNQELQRARQR 419
Cdd:COG3096 500 llrryrsqqalAQRLQQLRAQLAeleQRLRQQQNAERlleefcqRIGqqldaaeELEELLAELEAQLEELEEQAAEAVEQ 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 420 EKMNDDHNKRLSETVDKLLS------ESNERLQlHLKERMG-ALEEKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQM 492
Cdd:COG3096 580 RSELRQQLEQLRARIKELAArapawlAAQDALE-RLREQSGeALADSQEVTAAMQQLLEREREATVERDELAARKQALES 658
|
....*
gi 161016786 493 EIDQL 497
Cdd:COG3096 659 QIERL 663
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
234-498 |
1.17e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 53.26 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 234 RTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYL 313
Cdd:pfam01576 69 RKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 314 SAQREATSLHDANDKLENELASKE--------------------SLYRQSEEKSRQLaewLDDAKQKL--------QQTL 365
Cdd:pfam01576 149 KLSKERKLLEERISEFTSNLAEEEekakslsklknkheamisdlEERLKKEEKGRQE---LEKAKRKLegestdlqEQIA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 366 QKAETLPEIEAQLAQR----VAALNKAEE---RHGNFEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKLL 438
Cdd:pfam01576 226 ELQAQIAELRAQLAKKeeelQAALARLEEetaQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALK 305
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161016786 439 SESNERLqlhlkERMGALEEKNSLSE-EIANMKKLQDELLLNKEQLLAEM--------ERMQMEIDQLR 498
Cdd:pfam01576 306 TELEDTL-----DTTAAQQELRSKREqEVTELKKALEEETRSHEAQLQEMrqkhtqalEELTEQLEQAK 369
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
960-1015 |
1.22e-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: 46.91 E-value: 1.22e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 161016786 960 DWLPSLGLPQYRSYFMESLVDARMLDHLNKKELRGQLKMVDSFHRVSLHYGIMCLK 1015
Cdd:smart00454 11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
32-369 |
1.26e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.81 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 32 MVTMLTERERLLE-TLREAQDGLATAQLRLRELGH---EKDSLQR--------QLSIA--------LPQEFAALTKELNL 91
Cdd:pfam15921 501 LTASLQEKERAIEaTNAEITKLRSRVDLKLQELQHlknEGDHLRNvqtecealKLQMAekdkvieiLRQQIENMTQLVGQ 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 92 CREQLLEREEEIAELKAERNNTRLLLEHLECLVSRHE---RSLRMTVVKRQAQSPGGVSSEVEVLKALKSLFEHHKALDE 168
Cdd:pfam15921 581 HGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDakiRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLN 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 169 KV---RERLRMALERVAVLE-------EELELSNQEalnLRDQLSRRRSGLEEpgkdgDGQTLANGLGPVGESNRRTAEL 238
Cdd:pfam15921 661 EVktsRNELNSLSEDYEVLKrnfrnksEEMETTTNK---LKMQLKSAQSELEQ-----TRNTLKSMEGSDGHAMKVAMGM 732
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 239 EEALERQRAEVCQLRERLAVLcrqmsqlEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQRE 318
Cdd:pfam15921 733 QKQITAKRGQIDALQSKIQFL-------EEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEK 805
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 161016786 319 ATSLHDANDKLENELASKESLYRQSEEKSRQLaewlddakqKLQQTLQKAE 369
Cdd:pfam15921 806 VANMEVALDKASLQFAECQDIIQRQEQESVRL---------KLQHTLDVKE 847
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
268-494 |
1.84e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 52.15 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 268 EELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQRE----ATSLHDANDKLENELASKESLYRQS 343
Cdd:PRK04778 105 HEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSllanRFSFGPALDELEKQLENLEEEFSQF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 344 EEKS-----RQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRV-AALNKAEE------------RHGNFEERLRQLEAQ 405
Cdd:PRK04778 185 VELTesgdyVEAREILDQLEEELAALEQIMEEIPELLKELQTELpDQLQELKAgyrelveegyhlDHLDIEKEIQDLKEQ 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 406 L---------------EEKNQELQR--------------ARQR-EKmnddHNKRLSETVDKlLSESNERLQL---HLKER 452
Cdd:PRK04778 265 IdenlalleeldldeaEEKNEEIQEridqlydilerevkARKYvEK----NSDTLPDFLEH-AKEQNKELKEeidRVKQS 339
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161016786 453 M----GALEEKNSLSEEIANMKK------------------LQDELLLNKEQlLAEMERMQMEI 494
Cdd:PRK04778 340 YtlneSELESVRQLEKQLESLEKqydeiteriaeqeiayseLQEELEEILKQ-LEEIEKEQEKL 402
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
313-507 |
4.70e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 4.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 313 LSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTlqkAETLPEIEAQLAQRVAALNKAEERH 392
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAL---ARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 393 GNFEERLRQLEAQLEEKNQELQRARQREKMN--------DDHNKRLsetvdKLLSESNERLQLHLKERMGALEEKNSLSE 464
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLAlllspedfLDAVRRL-----QYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 161016786 465 EIANMKKLQDELLLNKEQLLAEMERMQMEIDQLRGRPPSSYSR 507
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAE 210
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
239-417 |
5.43e-06 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 49.96 E-value: 5.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 239 EEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKrylsaqre 318
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQ-------- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 319 atslhdandklenELASKESLyrqSEEKSRQLAewlddakqKLQQTLQkaetlpEIEAQLAQRVAALNKAEERHGNFEER 398
Cdd:PRK09039 124 -------------ELDSEKQV---SARALAQVE--------LLNQQIA------ALRRQLAALEAALDASEKRDRESQAK 173
|
170 180
....*....|....*....|...
gi 161016786 399 L----RQLEAQLEEKNQELQRAR 417
Cdd:PRK09039 174 IadlgRRLNVALAQRVQELNRYR 196
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
179-499 |
6.66e-06 |
|
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: 50.74 E-value: 6.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 179 ERVAVLEE--ELELSNQEALNLRDQLSRRRSGLEEPGKDGDGQTLanglgpvgESNRRTAELEEALERQRAEVCQLRERL 256
Cdd:TIGR00618 164 EKKELLMNlfPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTL--------CTPCMPDTYHERKQVLEKELKHLREAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 257 AvlcrQMSQLEEELgtahRELGKAEEANSKLQRDLKEALAQREDMEERITTL----EKRYLSAQREATSLHDA------- 325
Cdd:TIGR00618 236 Q----QTQQSHAYL----TQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLeetqERINRARKAAPLAAHIKavtqieq 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 326 -----NDKLENELASKESLYRQSEEKSRQLAEWldDAKQKLQQTLQKAETLPEIEAQlaqrVAALNKAE-ERHGNFEERL 399
Cdd:TIGR00618 308 qaqriHTELQSKMRSRAKLLMKRAAHVKQQSSI--EEQRRLLQTLHSQEIHIRDAHE----VATSIREIsCQQHTLTQHI 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 400 RQLEAQLEEKNQELQRARQREkmndDHNKRLSETVD-KLLSESNERLQLHLKERMGALEEKNSLSEEIANMKKLQDELLl 478
Cdd:TIGR00618 382 HTLQQQKTTLTQKLQSLCKEL----DILQREQATIDtRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKL- 456
|
330 340
....*....|....*....|.
gi 161016786 479 nKEQLLAEMERMQMEIDQLRG 499
Cdd:TIGR00618 457 -EKIHLQESAQSLKEREQQLQ 476
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
230-497 |
7.35e-06 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 50.07 E-value: 7.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 230 ESNRRTAELEEALERQ----------RAEVCQLRERLAVLCRQMSQLEEELGTA-----HRELGKAE--EANSKLQRDLK 292
Cdd:pfam05622 125 ESSDKVKKLEATVETYkkkledlgdlRRQVKLLEERNAEYMQRTLQLEEELKKAnalrgQLETYKRQvqELHGKLSEESK 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 293 EAlaqrEDMEERITTLEKRYLSAQREATSLHDANDKLENelASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQkAETLP 372
Cdd:pfam05622 205 KA----DKLEFEYKKLEEKLEALQKEKERLIIERDTLRE--TNEELRCAQLQQAELSQADALLSPSSDPGDNLA-AEIMP 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 373 -EIEAQLaQRVAALNKA--EERHGNFEERLRQLEAQLEEKNQELQRARQREKMNddhNKRLSEtvdkllsesnerLQLHL 449
Cdd:pfam05622 278 aEIREKL-IRLQHENKMlrLGQEGSYRERLTELQQLLEDANRRKNELETQNRLA---NQRILE------------LQQQV 341
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 161016786 450 KERMGALEEKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQL 497
Cdd:pfam05622 342 EELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEEL 389
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
229-430 |
9.63e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 9.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 229 GESNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQ--------LEEELGTAHRELGKAEEANSKLQRDLKeALAQ--- 297
Cdd:PRK04863 847 VELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRlnlladetLADRVEEIREQLDEAEEAKRFVQQHGN-ALAQlep 925
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 298 -----REDmEERITTLEKRYLSAQ-------------------REATSLHDA----------NDKLENELASKESLYRQS 343
Cdd:PRK04863 926 ivsvlQSD-PEQFEQLKQDYQQAQqtqrdakqqafaltevvqrRAHFSYEDAaemlaknsdlNEKLRQRLEQAEQERTRA 1004
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 344 EEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAAL-----NKAEERHGNFEERL-RQLEAQLEEKNQ-ELQRA 416
Cdd:PRK04863 1005 REQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLgvpadSGAEERARARRDELhARLSANRSRRNQlEKQLT 1084
|
250
....*....|....
gi 161016786 417 RQREKMnDDHNKRL 430
Cdd:PRK04863 1085 FCEAEM-DNLTKKL 1097
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
268-506 |
1.10e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 49.47 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 268 EELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRY------LSAQREatSLHDANDKLENELASKESLYR 341
Cdd:pfam06160 86 KALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYrelrktLLANRF--SYGPAIDELEKQLAEIEEEFS 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 342 QSEEKSR-----QLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRV-AALNKAEE------------RHGNFEERLRQLE 403
Cdd:pfam06160 164 QFEELTEsgdylEAREVLEKLEEETDALEELMEDIPPLYEELKTELpDQLEELKEgyremeeegyalEHLNVDKEIQQLE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 404 AQLEE-----KNQELQRArqrEKMNDDHNKRLSETVDKLLSESNERLQLH-----LKERMGALEEKNS-LSEEIANMKK- 471
Cdd:pfam06160 244 EQLEEnlallENLELDEA---EEALEEIEERIDQLYDLLEKEVDAKKYVEknlpeIEDYLEHAEEQNKeLKEELERVQQs 320
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 161016786 472 --LQDELLLNKEQL---LAEMERMQMEIDQLRGRPPSSYS 506
Cdd:pfam06160 321 ytLNENELERVRGLekqLEELEKRYDEIVERLEEKEVAYS 360
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
242-488 |
1.30e-05 |
|
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: 49.66 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 242 LERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEeANSKLQRDLKEALAQREDMEERITTLEKRY--LSAQREA 319
Cdd:TIGR00606 739 IDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIM-PEEESAKVCLTDVTIMERFQMELKDVERKIaqQAAKLQG 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 320 TSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAalnkaeerhgnfeeRL 399
Cdd:TIGR00606 818 SDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQ--------------RR 883
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 400 RQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKLLSESNERLQLHLKERMGALEEKNSLSEEIAN----MKKLQDE 475
Cdd:TIGR00606 884 QQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNihgyMKDIENK 963
|
250
....*....|...
gi 161016786 476 LLLNKEQLLAEME 488
Cdd:TIGR00606 964 IQDGKDDYLKQKE 976
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
234-422 |
1.46e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.40 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 234 RTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYL 313
Cdd:pfam01576 890 RIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSSI 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 314 SA-QREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLpeieaqlaqrvaalnkaeerh 392
Cdd:pfam01576 970 AAlEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKG--------------------- 1028
|
170 180 190
....*....|....*....|....*....|.
gi 161016786 393 gnfEERLRQLEAQLEEKNQELQRAR-QREKM 422
Cdd:pfam01576 1029 ---NSRMKQLKRQLEEAEEEASRANaARRKL 1056
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
114-310 |
1.50e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 114 RLLLEHLECLVSRHERslrmtVVKRQAQspggvsseVEVLKALKSLFEHHKALDEKVR--ERLRMAL------ERVAVLE 185
Cdd:COG4913 228 DALVEHFDDLERAHEA-----LEDAREQ--------IELLEPIRELAERYAAARERLAelEYLRAALrlwfaqRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 186 EELELSNQEALNLRDQLSRRRSGLEEPGKDGDG---QTLANGLgpvgesnRRTAELE---EALERQRAEVCQLRERLAVL 259
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDEleaQIRGNGG-------DRLEQLEreiERLERELEERERRRARLEAL 367
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 161016786 260 CRQM--------SQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEK 310
Cdd:COG4913 368 LAALglplpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
138-500 |
1.70e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.40 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 138 RQAQSPGGVSSEVEVLKALKSLFEHHKALDEKVRERLRMALERVAVLEEELELSNQEALNLRDQLSRRRSGLEEpgkdgd 217
Cdd:pfam01576 160 RISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAE------ 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 218 gqtLANGLGpvgesnRRTAELEEALERQRAEVCQ---LRERLAVLCRQMSQLEEELGTAHRELGKAEeansKLQRDLKEA 294
Cdd:pfam01576 234 ---LRAQLA------KKEEELQAALARLEEETAQknnALKKIRELEAQISELQEDLESERAARNKAE----KQRRDLGEE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 295 L-AQREDMEERI-TTLEKRYLSAQREaTSLHDANDKLENELASKESLYRQSEEKSRQ----LAEWLDDAKqKLQQTLQKA 368
Cdd:pfam01576 301 LeALKTELEDTLdTTAAQQELRSKRE-QEVTELKKALEEETRSHEAQLQEMRQKHTQaleeLTEQLEQAK-RNKANLEKA 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 369 ETLPEIE-AQLAQRVAALNKAEerhGNFEERLRQLEAQLEEKNQELQRA-RQREKMNDDHNKRLSE-------------- 432
Cdd:pfam01576 379 KQALESEnAELQAELRTLQQAK---QDSEHKRKKLEGQLQELQARLSESeRQRAELAEKLSKLQSElesvssllneaegk 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 433 ---------TVDKLLSESNERLQ------LHLKERMGALE-EKNSLSE---------------------EIANMKKLQDE 475
Cdd:pfam01576 456 niklskdvsSLESQLQDTQELLQeetrqkLNLSTRLRQLEdERNSLQEqleeeeeakrnverqlstlqaQLSDMKKKLEE 535
|
410 420
....*....|....*....|....*
gi 161016786 476 LLLNKEQLLAEMERMQMEIDQLRGR 500
Cdd:pfam01576 536 DAGTLEALEEGKKRLQRELEALTQQ 560
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
104-476 |
2.35e-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: 48.81 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 104 AELKAERNNTRLLLEHLEclvsRHERSLRMTVVKRQAQS---PGGVSSEVEVLKALKSLFEHHKALDEKVRERLRMALER 180
Cdd:TIGR00618 549 HQLTSERKQRASLKEQMQ----EIQQSFSILTQCDNRSKediPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPE 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 181 VAVLEEELELSNQEALNLRDQLSRRRSGLEEPGKDGDGQTLANGLGPVGESNRRTAELEEALERQRaEVCQLRERLAVLC 260
Cdd:TIGR00618 625 QDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKE-QLTYWKEMLAQCQ 703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 261 RQMSQLEEELGTAHRELGKAEEANSKLQRDLK---EALAQ--REDMEERITTLEKRYLSAQR---EATSLHDANDKLENE 332
Cdd:TIGR00618 704 TLLRELETHIEEYDREFNEIENASSSLGSDLAareDALNQslKELMHQARTVLKARTEAHFNnneEVTAALQTGAELSHL 783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 333 LASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQ----KAETLPEIEAQLAQRVAALNKA----EERHGNFEERLRQLEA 404
Cdd:TIGR00618 784 AAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDilnlQCETLVQEEEQFLSRLEEKSATlgeiTHQLLKYEECSKQLAQ 863
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161016786 405 QLEEKNQELQRARQREKMNDDHNKRLSETVDKLLSESNERLQLHL-KERMGALEEKNSLSEEIANMKKLQDEL 476
Cdd:TIGR00618 864 LTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHEITLYANVRLaNQSEGRFHGRYADSHVNARKYQGLALL 936
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
1040-1107 |
2.47e-05 |
|
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: 43.44 E-value: 2.47e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161016786 1040 VWSNERVMGWVSGLGLKEFATNLTESGVHGALLALDETFDysdlaLLLQIPTQNAQARQLLEKEFSNL 1107
Cdd:smart00454 3 QWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEE-----DLKELGITKLGHRKKILKAIQKL 65
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
327-500 |
2.50e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 327 DKLENElasKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQL 406
Cdd:COG4717 49 ERLEKE---ADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 407 EEKNQELQRARQREKMNDdhnkrlsetvdklLSESNERLQLHLKERMGALEEKNSLSEEIANMK-KLQDELLLNKEQLLA 485
Cdd:COG4717 126 QLLPLYQELEALEAELAE-------------LPERLEELEERLEELRELEEELEELEAELAELQeELEELLEQLSLATEE 192
|
170
....*....|....*
gi 161016786 486 EMERMQMEIDQLRGR 500
Cdd:COG4717 193 ELQDLAEELEELQQR 207
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
237-476 |
2.57e-05 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 48.15 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 237 ELEEALErqraEVCQLRERLAVLCRQMSQLEEELGTAHRELGKaeeansklqrdLKEALAQREDMEERITTLEKRYLSAQ 316
Cdd:pfam05622 1 DLSEAQE----EKDELAQRCHELDQQVSLLQEEKNSLQQENKK-----------LQERLDQLESGDDSGTPGGKKYLLLQ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 317 REATSLHDANDKLENelaSKESLYRQSEEKSRQLAEwlddakqkLQQTLQKAETLPEIEAQLAQRVAALNKAEERHGNFE 396
Cdd:pfam05622 66 KQLEQLQEENFRLET---ARDDYRIKCEELEKEVLE--------LQHRNEELTSLAEEAQALKDEMDILRESSDKVKKLE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 397 ----------ERLRQLEAQ---LEEKNQE-LQRARQRE----KMN------DDHNKRLSETVDKLLSESN--ERLQL--- 447
Cdd:pfam05622 135 atvetykkklEDLGDLRRQvklLEERNAEyMQRTLQLEeelkKANalrgqlETYKRQVQELHGKLSEESKkaDKLEFeyk 214
|
250 260 270
....*....|....*....|....*....|
gi 161016786 448 HLKERMGALE-EKNSLSEEIANMKKLQDEL 476
Cdd:pfam05622 215 KLEEKLEALQkEKERLIIERDTLRETNEEL 244
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
181-500 |
2.68e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 48.66 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 181 VAVLEEELELSNQEALNLRDQLSRRRSGLEEPgkdgdgQTLANglgpvgESNRRTAELEEALERQRAEVCQLRERL---- 256
Cdd:pfam10174 326 IEVLKESLTAKEQRAAILQTEVDALRLRLEEK------ESFLN------KKTKQLQDLTEEKSTLAGEIRDLKDMLdvke 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 257 ---AVLCRQMSQLEEELGTAHRELGKAEEANSKLQRD----------LKEALAQREDMEERITTLEKRYLSAQREATS-- 321
Cdd:pfam10174 394 rkiNVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDssntdtalttLEEALSEKERIIERLKEQREREDRERLEELEsl 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 322 ---LHDANDK---LENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQ----TLQKAETLPEIEAQL--AQRVAALNKAE 389
Cdd:pfam10174 474 kkeNKDLKEKvsaLQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSleiaVEQKKEECSKLENQLkkAHNAEEAVRTN 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 390 ErhgNFEERLRQLEAQLEEKNQELQRARQ---------REKMNDDHNKrlsetvDKLLSESNERLQLHLKE--------R 452
Cdd:pfam10174 554 P---EINDRIRLLEQEVARYKEESGKAQAeverllgilREVENEKNDK------DKKIAELESLTLRQMKEqnkkvaniK 624
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 161016786 453 MGALEEKNSLSEEIANMKKLQDELLLNK-----EQLLAEMERMQMEIDQLRGR 500
Cdd:pfam10174 625 HGQQEMKKKGAQLLEEARRREDNLADNSqqlqlEELMGALEKTRQELDATKAR 677
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
282-498 |
2.76e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.60 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 282 EANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKL 361
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 362 QQTLQKAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLE------EKNQEL--------QRARQREKMNDDHN 427
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQtevlspEEEKELvekikeleKELEKAKKALEKNE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161016786 428 KrLSETVDKLLSESNERLQLHlkERMGAL-EEKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQLR 498
Cdd:COG1340 161 K-LKELRAELKELRKEAEEIH--KKIKELaEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELH 229
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
280-496 |
2.91e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 280 AEEANSKLQRDLKEALAQREDMEERITTLEKRY--LSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDA 357
Cdd:COG3206 173 ARKALEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 358 KQKLQQTLQkAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQrekmnddhnkRLSETVDKL 437
Cdd:COG3206 253 PDALPELLQ-SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQ----------RILASLEAE 321
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161016786 438 LSESNERLQLhLKERMGALEEK-NSLSEEIANMKKLQDELLLNK---EQLLAEMERMQMEIDQ 496
Cdd:COG3206 322 LEALQAREAS-LQAQLAQLEARlAELPELEAELRRLEREVEVARelyESLLQRLEEARLAEAL 383
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
234-440 |
2.94e-05 |
|
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: 46.95 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 234 RTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEEL-------GTAHRELGKAEEANSKLQRDLKeALAQREDM-EERI 305
Cdd:pfam00261 16 RLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELerteerlAEALEKLEEAEKAADESERGRK-VLENRALKdEEKM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 306 TTLEKRYLSAQREAtslHDANDKLEnELASKESLYRQSEEKSRQLAEWLDDAKQKLQqtlqkaETLPEIEAQLAQRVAAL 385
Cdd:pfam00261 95 EILEAQLKEAKEIA---EEADRKYE-EVARKLVVVEGDLERAEERAELAESKIVELE------EELKVVGNNLKSLEASE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161016786 386 NKAEERHGNFEERLRQLEAQLEEKNQELQRARQR----EKMNDD----------HNKRLSETVDKLLSE 440
Cdd:pfam00261 165 EKASEREDKYEEQIRFLTEKLKEAETRAEFAERSvqklEKEVDRledeleaekeKYKAISEELDQTLAE 233
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
333-498 |
3.37e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 333 LASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAET----LPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEE 408
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKAllkqLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 409 KNQELQRARQR-EKMNDDHNKRLSETVDKLL------SESNERLQLH---LKERMGALEEKNSLSEEIANMKKLQDELLL 478
Cdd:COG4942 95 LRAELEAQKEElAELLRALYRLGRQPPLALLlspedfLDAVRRLQYLkylAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180
....*....|....*....|
gi 161016786 479 NKEQLLAEMERMQMEIDQLR 498
Cdd:COG4942 175 ELEALLAELEEERAALEALK 194
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
293-498 |
3.98e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.98 E-value: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 293 EALAQREDMEERITTLEKRylsaqreatSLHDANDK-----LENELASKESLYRQsEEKSRQLAEWLDDAKQKLQQTLQK 367
Cdd:PRK11281 33 GDLPTEADVQAQLDALNKQ---------KLLEAEDKlvqqdLEQTLALLDKIDRQ-KEETEQLKQQLAQAPAKLRQAQAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 368 AETLPEIEAQ-LAQRVAALNkaeerhgnfeerLRQLEAQLEEKNQELQRARQREkmnDDHNKRL------SETVDKLLSE 440
Cdd:PRK11281 103 LEALKDDNDEeTRETLSTLS------------LRQLESRLAQTLDQLQNAQNDL---AEYNSQLvslqtqPERAQAALYA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 161016786 441 SNERLQlhlkermgalEEKNSLSEEIANMKKLQDELllnKEQLLAEMERMQMEIDQLR 498
Cdd:PRK11281 168 NSQRLQ----------QIRNLLKGGKVGGKALRPSQ---RVLLQAEQALLNAQNDLQR 212
|
|
| SAM_superfamily |
cd09487 |
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
960-1004 |
4.18e-05 |
|
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: 42.23 E-value: 4.18e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 161016786 960 DWLPSLGLPQYRSYFMESLVDARMLDHLNKKELRgQLKMVDSFHR 1004
Cdd:cd09487 4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHR 47
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
237-483 |
4.36e-05 |
|
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: 48.12 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 237 ELEEALERQRaEVCQLRERLAVLCRQMSQLEEELGTAHRELGkaeeaNSKLQrdLKEALAQREDMEERITTLEKRYLSAQ 316
Cdd:TIGR00606 830 EKQEKQHELD-TVVSKIELNRKLIQDQQEQIQHLKSKTNELK-----SEKLQ--IGTNLQRRQQFEEQLVELSTEVQSLI 901
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 317 REatsLHDANDK-------LENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTL------------QKAETLPEIEAQ 377
Cdd:TIGR00606 902 RE---IKDAKEQdspletfLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHgymkdienkiqdGKDDYLKQKETE 978
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 378 LAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQE---LQRARQREKMNDDHnKRLSETVDKLLSESNERLQLHLKERMG 454
Cdd:TIGR00606 979 LNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQerwLQDNLTLRKRENEL-KEVEEELKQHLKEMGQMQVLQMKQEHQ 1057
|
250 260 270
....*....|....*....|....*....|....
gi 161016786 455 ALEE-----KNSLSEEIANMKKLQDELLLNKEQL 483
Cdd:TIGR00606 1058 KLEEnidliKRNHVLALGRQKGYEKEIKHFKKEL 1091
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
305-414 |
4.51e-05 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 47.03 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 305 ITTLEKRYLSAQREATSLHDANDKLENELASKESLYRQSEEKsrqlaewLDDAKQKLQQtlQKAETLPEIEAQLAQRVAA 384
Cdd:TIGR04320 256 LAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAA-------LATAQKELAN--AQAQALQTAQNNLATAQAA 326
|
90 100 110
....*....|....*....|....*....|
gi 161016786 385 LNKAEERHGNFEERLRQLEAQLEEKNQELQ 414
Cdd:TIGR04320 327 LANAEARLAKAKEALANLNADLAKKQAALD 356
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
237-419 |
5.16e-05 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153280 [Multi-domain] Cd Length: 218 Bit Score: 45.81 E-value: 5.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 237 ELEEALERQRAEVCQLRERLAVLCRQMSQL---EEELGTAHRELGKAEEANSKLQRDLKEALAQredmeerittlekryl 313
Cdd:cd07596 1 EEDQEFEEAKDYILKLEEQLKKLSKQAQRLvkrRRELGSALGEFGKALIKLAKCEEEVGGELGE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 314 sAQREATSLHDANDKLENELASKESLyrqseeksrQLAEWLDD-------AKQKLQQTLQKAETLPEIEAQLAQRVAALN 386
Cdd:cd07596 65 -ALSKLGKAAEELSSLSEAQANQELV---------KLLEPLKEylrycqaVKETLDDRADALLTLQSLKKDLASKKAQLE 134
|
170 180 190
....*....|....*....|....*....|...
gi 161016786 387 KAEERHGNFEERLRQLEAQLEEKNQELQRARQR 419
Cdd:cd07596 135 KLKAAPGIKPAKVEELEEELEEAESALEEARKR 167
|
|
| SAM_STIM-1,2-like |
cd09504 |
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ... |
838-896 |
6.36e-05 |
|
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: 42.32 E-value: 6.36e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161016786 838 WDGPTVVSWLELWVGMPAwYVAACRANVKSGAIMANLSDTE---IQREIGISNPLHRLKLRL 896
Cdd:cd09504 5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
|
|
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
237-460 |
8.14e-05 |
|
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.
Pssm-ID: 464371 [Multi-domain] Cd Length: 304 Bit Score: 46.13 E-value: 8.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 237 ELEEALERQRAEVCQLRERLAVlcrQMSQLEEELGTAHRELGKAE-EANSklqrdlkealaqredmeerittLEkrylsa 315
Cdd:pfam14915 116 DLELAFQRERDEWLRLQDKMNF---DVSNLRDENEILSQQLSKAEsKANS----------------------LE------ 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 316 qreaTSLHDANDKL-ENELASkESLYRQSEEKSRQlaewlddaKQKLQQTLQKAEtlpeieaqlaqrvAALNKAEERHGN 394
Cdd:pfam14915 165 ----NELHRTRDALrEKTLLL-ESVQRDLSQAQCQ--------KKELEHMYQNEQ-------------DKVNKYIGKQES 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 395 FEERLRQLEA-------QLEEKNQElqrARQREKMNDDHNKRLSETVDKLLSESNERLQL-------------HLKERMG 454
Cdd:pfam14915 219 LEERLAQLQSenmllrqQLEDAQNK---ADAKEKTVIDIQDQFQDIVKKLQAESEKQVLLleernkelinecnHLKERLY 295
|
....*..
gi 161016786 455 ALE-EKN 460
Cdd:pfam14915 296 QYEkEKA 302
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
230-497 |
8.22e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.09 E-value: 8.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 230 ESNRRTAELEEALERQ---RAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLqrdlkeaLAQREDMEERIT 306
Cdd:pfam01576 6 EMQAKEEELQKVKERQqkaESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARL-------AARKQELEEILH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 307 TLEKRYLSAQREATSLHDANDKLENELASKESlyrqseeksrQLAEWlDDAKQKLQqtLQKAET---LPEIEAQLAQRVA 383
Cdd:pfam01576 79 ELESRLEEEEERSQQLQNEKKKMQQHIQDLEE----------QLDEE-EAARQKLQ--LEKVTTeakIKKLEEDILLLED 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 384 ALNKAEERHGNFEERLRQLEAQLEEknqELQRARQREKMNDDHNKRLSETVDKLLSESNERLQLH-LKERMGAleEKNSL 462
Cdd:pfam01576 146 QNSKLSKERKLLEERISEFTSNLAE---EEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEkAKRKLEG--ESTDL 220
|
250 260 270
....*....|....*....|....*....|....*
gi 161016786 463 SEEIANMKKLQDELllnKEQLLAEMERMQMEIDQL 497
Cdd:pfam01576 221 QEQIAELQAQIAEL---RAQLAKKEEELQAALARL 252
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
310-451 |
8.94e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.74 E-value: 8.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 310 KRY-LSAQ--REA-TSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLaqrvaaL 385
Cdd:PRK00409 495 KRLgLPENiiEEAkKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL------L 568
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161016786 386 NKAEERhgnFEERLRQLEAQLEEKNQELqRARQREKMNDDHNKRLSEtVDKLLSESNERLQLHLKE 451
Cdd:PRK00409 569 EEAEKE---AQQAIKEAKKEADEIIKEL-RQLQKGGYASVKAHELIE-ARKRLNKANEKKEKKKKK 629
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
237-407 |
9.02e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 45.20 E-value: 9.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 237 ELEEAL---ERQRAEVCQLRERLAvlcRQMSQLEEELGTAHRelgKAEEANSKLQRDL-KEALAQREDMEERITTLEKRY 312
Cdd:COG1842 34 DMEEDLveaRQALAQVIANQKRLE---RQLEELEAEAEKWEE---KARLALEKGREDLaREALERKAELEAQAEALEAQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 313 LSAQREATSLHDANDKLENELASKESlyRQSEEKSRQLAEwldDAKQKLQQTLQKA------ETLPEIEAQLAQRVAALN 386
Cdd:COG1842 108 AQLEEQVEKLKEALRQLESKLEELKA--KKDTLKARAKAA---KAQEKVNEALSGIdsddatSALERMEEKIEEMEARAE 182
|
170 180
....*....|....*....|...
gi 161016786 387 KAEE--RHGNFEERLRQLEAQLE 407
Cdd:COG1842 183 AAAElaAGDSLDDELAELEADSE 205
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
344-500 |
1.03e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 344 EEKSRQLAEwLDDAKQKLQQTLQKAETLP----EIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARqr 419
Cdd:COG1579 3 PEDLRALLD-LQELDSELDRLEHRLKELPaelaELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 420 EKMNDDHNKRLSETVDKLLSESNERLQLHLKERMGALEEKNSLSEEIAN----MKKLQDELLLNKEQLLAEMERMQMEID 495
Cdd:COG1579 80 EQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAEleaeLAELEAELEEKKAELDEELAELEAELE 159
|
....*
gi 161016786 496 QLRGR 500
Cdd:COG1579 160 ELEAE 164
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
263-458 |
1.04e-04 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 44.74 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 263 MSQLEEELgtAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKrylSAQREATSLHDANDKLENELASKESLYRQ 342
Cdd:cd00176 16 LSEKEELL--SSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNE---LGEQLIEEGHPDAEEIQERLEELNQRWEE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 343 SEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQ-----RVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRAR 417
Cdd:cd00176 91 LRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAAlasedLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 161016786 418 QREKMNDDHNKRLSETVDKLLSESNERLQLHLKERMGALEE 458
Cdd:cd00176 171 ELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
838-901 |
1.07e-04 |
|
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.
Pssm-ID: 425739 Cd Length: 64 Bit Score: 41.49 E-value: 1.07e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161016786 838 WDGPTVVSWLElWVGMPAwYVAACRANVKSGAIMANLSDTEIqREIGISNPLHRLKLRLAIQEM 901
Cdd:pfam00536 3 WSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
163-500 |
1.35e-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: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 163 HKALDEKVRERLRMALERVAVLEEELELSNQEALNLRDQlsrrrsgleepgKDGDGQTLANglgpvgesnrRTAELEEAL 242
Cdd:TIGR00606 396 HTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDE------------KKGLGRTIEL----------KKEILEKKQ 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 243 ERQRAEVCQLRERLAVLCRQMsQLEEELGTAHRELGKAEEaNSKLQRDLKEALA---QREDMEERITTLEKRYLSAQREA 319
Cdd:TIGR00606 454 EELKFVIKELQQLEGSSDRIL-ELDQELRKAERELSKAEK-NSLTETLKKEVKSlqnEKADLDRKLRKLDQEMEQLNHHT 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 320 TSLHD----ANDKLENELASKESLYRQSEE---------KSRQLAEWL----------DDAKQKLQQTLQKAETLP-EIE 375
Cdd:TIGR00606 532 TTRTQmemlTKDKMDKDEQIRKIKSRHSDEltsllgyfpNKKQLEDWLhskskeinqtRDRLAKLNKELASLEQNKnHIN 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 376 AQLAQRVAALNKAEERHgnFEERLRQ-LEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKLLSESNE---------RL 445
Cdd:TIGR00606 612 NELESKEEQLSSYEDKL--FDVCGSQdEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSccpvcqrvfQT 689
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161016786 446 QLHLKERMGALEEK--------NSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQLRGR 500
Cdd:TIGR00606 690 EAELQEFISDLQSKlrlapdklKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNK 752
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
1040-1108 |
1.37e-04 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 41.10 E-value: 1.37e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161016786 1040 VWSNERVMGWVSGLGLKEFATNLTESGVHGALLALDetFDYSDLAlllQIPTQNAQARQLLEKEFSNLI 1108
Cdd:pfam07647 3 SWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLR--LTLEDLK---RLGITSVGHRRKILKKIQELK 66
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
236-498 |
1.50e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.98 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 236 AELEEALERQRAEVCQLRERLAVLCRQ-----------MSQLEEELGTAHRELGKAEEANSK---------LQRdLKEAL 295
Cdd:PRK04778 129 QELLESEEKNREEVEQLKDLYRELRKSllanrfsfgpaLDELEKQLENLEEEFSQFVELTESgdyveareiLDQ-LEEEL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 296 AQREDMEERI----TTLEKRY------LSA---QREATSLHDANDKLENELASKESLYRQSEEKSRQLAewLDDAKQKLQ 362
Cdd:PRK04778 208 AALEQIMEEIpellKELQTELpdqlqeLKAgyrELVEEGYHLDHLDIEKEIQDLKEQIDENLALLEELD--LDEAEEKNE 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 363 QTLQKAETLPEIeaqLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQREKMNDDhnkrLSETVDKLLSESN 442
Cdd:PRK04778 286 EIQERIDQLYDI---LEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNES----ELESVRQLEKQLE 358
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 161016786 443 --ERLQLHLKERMGalEEKNSLSEEIANMKKLQDELllnkEQLLAEMERMQMEIDQLR 498
Cdd:PRK04778 359 slEKQYDEITERIA--EQEIAYSELQEELEEILKQL----EEIEKEQEKLSEMLQGLR 410
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
239-494 |
1.62e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 45.29 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 239 EEALERQRAEVCQLRERLAVLCRQMSQLEEELgtahRELGKAEEANSKLQRDLKEALAQREDMEErittleKRYLSAQRE 318
Cdd:pfam13868 84 EREQKRQEEYEEKLQEREQMDEIVERIQEEDQ----AEAEEKLEKQRQLREEIDEFNEEQAEWKE------LEKEEEREE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 319 ATSLHDANDKLENELASKEslyRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQ-------RVAALNKAEER 391
Cdd:pfam13868 154 DERILEYLKEKAEREEERE---AEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQeeqerkeRQKEREEAEKK 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 392 HGNFEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKLLSESNERLQLHLKERMGALEeknSLSEEIANMKK 471
Cdd:pfam13868 231 ARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELE---KQIEEREEQRA 307
|
250 260
....*....|....*....|...
gi 161016786 472 LQDELLLNKEQLLAEMERMQMEI 494
Cdd:pfam13868 308 AEREEELEEGERLREEEAERRER 330
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
38-411 |
1.68e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.10 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 38 ERERLLE-------TLREAQDGLATAQLRLRELGHEKDSLQRQLSiALPQEFAALTKELNLCREQLLER------EEEIA 104
Cdd:COG3096 279 ERRELSEralelrrELFGARRQLAEEQYRLVEMARELEELSARES-DLEQDYQAASDHLNLVQTALRQQekieryQEDLE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 105 ELkAERnntrlLLEHLECLVSRHERSLRMTVVKRQAQSpggvssEVEVLKAlkSLFEHHKALD----------------E 168
Cdd:COG3096 358 EL-TER-----LEEQEEVVEEAAEQLAEAEARLEAAEE------EVDSLKS--QLADYQQALDvqqtraiqyqqavqalE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 169 KVRERLRM-------ALERVAVLEEELELSNQEALNLRDQLSrrrsgLEEPGKDGDGQTLANGLGPVGESNRRTA--ELE 239
Cdd:COG3096 424 KARALCGLpdltpenAEDYLAAFRAKEQQATEEVLELEQKLS-----VADAARRQFEKAYELVCKIAGEVERSQAwqTAR 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 240 EALERQRAEVCQLrERLAVLCRQMSQLEEELgtahRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREA 319
Cdd:COG3096 499 ELLRRYRSQQALA-QRLQQLRAQLAELEQRL----RQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQA 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 320 TSLHDANDKLENELaskESLYRQSEEKSRQLAEWL--DDAKQKLQ-QTLQKAETLPEIEAQLAQRVAALNKAEERHGNFE 396
Cdd:COG3096 574 AEAVEQRSELRQQL---EQLRARIKELAARAPAWLaaQDALERLReQSGEALADSQEVTAAMQQLLEREREATVERDELA 650
|
410
....*....|....*
gi 161016786 397 ERLRQLEAQLEEKNQ 411
Cdd:COG3096 651 ARKQALESQIERLSQ 665
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
273-498 |
1.82e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.98 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 273 AHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELASK-ESLYRQSEEKSRQLA 351
Cdd:pfam12128 228 RDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLlRTLDDQWKEKRDELN 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 352 EWLDDAKQKLQQtlqKAETLPEIEAQLAQ----RVAALNKAEERHGNFEERLRQLEAQ---LEEKNQELQRARQREKMN- 423
Cdd:pfam12128 308 GELSAADAAVAK---DRSELEALEDQHGAfldaDIETAAADQEQLPSWQSELENLEERlkaLTGKHQDVTAKYNRRRSKi 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 424 --------DDHNKRLS---ETVDKLLSESN---ERLQLHLKERMGAL-----EEKNSLSEEIANMKKLQD------ELLL 478
Cdd:pfam12128 385 keqnnrdiAGIKDKLAkirEARDRQLAVAEddlQALESELREQLEAGklefnEEEYRLKSRLGELKLRLNqatatpELLL 464
|
250 260
....*....|....*....|
gi 161016786 479 NKEQLLAEMERMQMEIDQLR 498
Cdd:pfam12128 465 QLENFDERIERAREEQEAAN 484
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
137-447 |
2.00e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 137 KRQAQSPGGVSSEVEVLKALKslfehhKALDEKVRERLR-MALERvavLEEELE-----LSN-QEALN-LRDQLSRRRSG 208
Cdd:PRK11281 87 QQLAQAPAKLRQAQAELEALK------DDNDEETRETLStLSLRQ---LESRLAqtldqLQNaQNDLAeYNSQLVSLQTQ 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 209 LEEpgkdgdGQTLANglgpvgESNRRTAELEEALERQRAEVCQLRERLavlcRQMSQLEEELGTAHRELGKAE-EANSKL 287
Cdd:PRK11281 158 PER------AQAALY------ANSQRLQQIRNLLKGGKVGGKALRPSQ----RVLLQAEQALLNAQNDLQRKSlEGNTQL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 288 ------QRDLKEALAQRedMEERITTL-----EKRYLSAQ---REATSLHDANDKLENELASKES---------LYRQSE 344
Cdd:PRK11281 222 qdllqkQRDYLTARIQR--LEHQLQLLqeainSKRLTLSEktvQEAQSQDEAARIQANPLVAQELeinlqlsqrLLKATE 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 345 E------KSRQLAEWLDDAKQK----------LQQTL-------QKAETLPEIE--AQLAQRVAAL-------NKAEERH 392
Cdd:PRK11281 300 KlntltqQNLRVKNWLDRLTQSernikeqisvLKGSLllsrilyQQQQALPSADliEGLADRIADLrleqfeiNQQRDAL 379
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161016786 393 GNFEERLRQLEAQL------EEKNQELQRARQREKMNDDHNKRLSEtvdkLLSESNErLQL 447
Cdd:PRK11281 380 FQPDAYIDKLEAGHksevtdEVRDALLQLLDERRELLDQLNKQLNN----QLNLAIN-LQL 435
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
309-415 |
2.01e-04 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 43.72 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 309 EKRYLSAQREATSL-----HDAND-KLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRV 382
Cdd:pfam12072 26 EAKIGSAEELAKRIieeakKEAETkKKEALLEAKEEIHKLRAEAERELKERRNELQRQERRLLQKEETLDRKDESLEKKE 105
|
90 100 110
....*....|....*....|....*....|....*..
gi 161016786 383 AALNKAEERHGNFEERLRQLEAQLEEK----NQELQR 415
Cdd:pfam12072 106 ESLEKKEKELEAQQQQLEEKEEELEELieeqRQELER 142
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
251-484 |
2.18e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.21 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 251 QLRErLAVLCRQMS---------QLEEELGTAHRELGKAEEANSKLqrDLKEALAQREDMEERITTL----EKRYlSAQR 317
Cdd:PRK04778 231 QLQE-LKAGYRELVeegyhldhlDIEKEIQDLKEQIDENLALLEEL--DLDEAEEKNEEIQERIDQLydilEREV-KARK 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 318 EATSLHD-----------ANDKLENELAS-KESlYRQSE---EKSRQLAEWLDDAKQKLQQTLQK--AETLP--EIEAQL 378
Cdd:PRK04778 307 YVEKNSDtlpdflehakeQNKELKEEIDRvKQS-YTLNEselESVRQLEKQLESLEKQYDEITERiaEQEIAysELQEEL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 379 AQRVAALNKAEERHGNFEERLRQL---EAQLEEKNQELQR-----ARQREKMN-----DDHNKRLSETVDKL--LSESNE 443
Cdd:PRK04778 386 EEILKQLEEIEKEQEKLSEMLQGLrkdELEAREKLERYRNklheiKRYLEKSNlpglpEDYLEMFFEVSDEIeaLAEELE 465
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 161016786 444 RLQLHLKERMGALEEknsLSEEIANMKKLQDELLLNK---EQLL 484
Cdd:PRK04778 466 EKPINMEAVNRLLEE---ATEDVETLEEETEELVENAtltEQLI 506
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
286-496 |
2.26e-04 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 43.97 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 286 KLQRDLKEALAQREDMEERITTLEkrYLSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTL 365
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTD--YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 366 QKAETL-PEIEAQLAQRVAALNKAEERHGNFEErLRQLEAQLEEKNQELQRarqrEKMNDDHN------KRLSETVDKLL 438
Cdd:cd00176 82 EELNQRwEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALAS----EDLGKDLEsveellKKHKELEEELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 161016786 439 SESNERLQLhlkERMGALEEKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQ 496
Cdd:cd00176 157 AHEPRLKSL---NELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
229-491 |
2.31e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 44.80 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 229 GESNRRTAELEEALERQRAEVCQ-LRERLAvlcrqmsqLEEELGTAHRELGKAEEANSKLQRDLKEALAQREdmeERITT 307
Cdd:pfam15905 90 GEQDKRLQALEEELEKVEAKLNAaVREKTS--------LSASVASLEKQLLELTRVNELLKAKFSEDGTQKK---MSSLS 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 308 LEKRYLSAQREAT--SLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQklqqtlQKAETLPEIEAQLAQrVAAL 385
Cdd:pfam15905 159 MELMKLRNKLEAKmkEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEK------EKIEEKSETEKLLEY-ITEL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 386 NKAEERHGNFEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVD---KLLSESNERLQLHLKERmgaleeKNSL 462
Cdd:pfam15905 232 SCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNekcKLLESEKEELLREYEEK------EQTL 305
|
250 260
....*....|....*....|....*....
gi 161016786 463 SEEIANMKklqdELLLNKEQllaEMERMQ 491
Cdd:pfam15905 306 NAELEELK----EKLTLEEQ---EHQKLQ 327
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
309-488 |
2.41e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 309 EKRYLSAQREATS-LHDAndKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQtLQKAETlpeieaQLAQRvaalnk 387
Cdd:PRK12704 30 EAKIKEAEEEAKRiLEEA--KKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNE-LQKLEK------RLLQK------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 388 aeerhgnfEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKLLSESNERLqlhlkermgaleeknslsEEIA 467
Cdd:PRK12704 95 --------EENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL------------------ERIS 148
|
170 180
....*....|....*....|.
gi 161016786 468 NMKklQDELllnKEQLLAEME 488
Cdd:PRK12704 149 GLT--AEEA---KEILLEKVE 164
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
184-493 |
2.42e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 184 LEEELELSNQealnlrDQLSRRRSGLEEPgKDGDGQTLANGLGPVGESNRRTAELEE----ALERQRAEvcqlrerlavl 259
Cdd:PTZ00121 1029 IEELTEYGNN------DDVLKEKDIIDED-IDGNHEGKAEAKAHVGQDEGLKPSYKDfdfdAKEDNRAD----------- 1090
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 260 crqmSQLEEELGTAHR----ELGKAEEANSKlqrdlKEALAQREDMEEritTLEKRYLSAQREATSLHDANDKLENELAS 335
Cdd:PTZ00121 1091 ----EATEEAFGKAEEakktETGKAEEARKA-----EEAKKKAEDARK---AEEARKAEDARKAEEARKAEDAKRVEIAR 1158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 336 KESLYRQSEEKSR-QLAEWLDDAKQKLQ----QTLQKAETLPEIEAqlAQRVAALNKAEERHGNFEERLRQLEAQLEEKN 410
Cdd:PTZ00121 1159 KAEDARKAEEARKaEDAKKAEAARKAEEvrkaEELRKAEDARKAEA--ARKAEEERKAEEARKAEDAKKAEAVKKAEEAK 1236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 411 QELQRARQREKMNDDHNKRLSEtvdkllsesnERLQLHLKERMGALE-EKNSLSEEI--ANMKKLQDELLLNKEQLLAEM 487
Cdd:PTZ00121 1237 KDAEEAKKAEEERNNEEIRKFE----------EARMAHFARRQAAIKaEEARKADELkkAEEKKKADEAKKAEEKKKADE 1306
|
....*.
gi 161016786 488 ERMQME 493
Cdd:PTZ00121 1307 AKKKAE 1312
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
230-440 |
2.54e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 45.23 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 230 ESNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTA----------HRELGKAEEANSKLQRDLKEALAQRE 299
Cdd:COG2433 410 EEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEArseerreirkDREISRLDREIERLERELEEERERIE 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 300 DMEERITTLEK-RYLSAQREATSL-------HDANDKLENELASKES--LY-RQSEEKSRQLAEWLDDAK---------- 358
Cdd:COG2433 490 ELKRKLERLKElWKLEHSGELVPVkvvekftKEAIRRLEEEYGLKEGdvVYlRDASGAGRSTAELLAEAGpravivpgel 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 359 -QKLQQTLQKAE----TLPEIEAQLAQRVAALNKAEerhgnfeerlrqLEAQLEEKnQELQRARQREKMnddhnkrlSET 433
Cdd:COG2433 570 sEAADEVLFEEGipvlPAEDVTIQEVDDLAVVDEEE------------LEAAIEDW-EERAEERRREKK--------AEM 628
|
....*..
gi 161016786 434 VDKLLSE 440
Cdd:COG2433 629 LERLISE 635
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
174-466 |
2.57e-04 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 44.33 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 174 LRMALERVAVLEEELElsnqealNLRDQLSRRRSGLEEPGKDGDGqtlanglgpvgesnrrtaeLEEALERQRAEVCQLR 253
Cdd:pfam06008 7 LTGALPAPYKINYNLE-------NLTKQLQEYLSPENAHKIQIEI-------------------LEKELSSLAQETEELQ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 254 ERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREdmeerittlekrYLSAQREATslhdANDKLENEL 333
Cdd:pfam06008 61 KKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVA------------TLGENDFAL----PSSDLSRML 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 334 ASKESLYRqsEEKSRQLAEWLDDAKQKL---QQTLQKAETLpeIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKn 410
Cdd:pfam06008 125 AEAQRMLG--EIRSRDFGTQLQNAEAELkaaQDLLSRIQTW--FQSPQEENKALANALRDSLAEYEAKLSDLRELLREA- 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 161016786 411 qeLQRARQREKMNDDHNKRLSETVDKLL--SESNERLQLHLKERMGALEEKNSLSEEI 466
Cdd:pfam06008 200 --AAKTRDANRLNLANQANLREFQRKKEevSEQKNQLEETLKTARDSLDAANLLLQEI 255
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
167-464 |
2.85e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.86 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 167 DEKVRERLRMALERVAVLEEELELSNQ----EALNLRDQLS-RRRSGLEEPGKDGDGQTLANGLGPVGEsnRRTAELEEA 241
Cdd:pfam02029 5 EEAARERRRRAREERRRQKEEEEPSGQvtesVEPNEHNSYEeDSELKPSGQGGLDEEEAFLDRTAKREE--RRQKRLQEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 242 LERQRAEVCQLRE-RLAVLCRQMSQLEEELGTAHRE------LGKAEEANS-----KLQRDLKE----ALAQREDMEERI 305
Cdd:pfam02029 83 LERQKEFDPTIADeKESVAERKENNEEEENSSWEKEekrdsrLGRYKEEETeirekEYQENKWStevrQAEEEGEEEEDK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 306 TTLEKRYLSAQREATSLHDANDKLENELASKESLYRQ-----SEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQ 380
Cdd:pfam02029 163 SEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDqkrghPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 381 RVAALNKAEE---RHGNFEE------RLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKLLSESNERLQlhLKE 451
Cdd:pfam02029 243 FLEAEQKLEElrrRRQEKESeefeklRQKQQEAELELEELKKKREERRKLLEEEEQRRKQEEAERKLREEEEKRR--MKE 320
|
330
....*....|....*...
gi 161016786 452 -----RMGALEEKNSLSE 464
Cdd:pfam02029 321 eierrRAEAAEKRQKLPE 338
|
|
| Yuri_gagarin |
pfam15934 |
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis. |
282-498 |
3.65e-04 |
|
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis.
Pssm-ID: 318204 [Multi-domain] Cd Length: 234 Bit Score: 43.41 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 282 EANSKLQRDLKEALAQREDMEERITTLEkrylsaqreaTSLHDANDKLeNELASKESLYRQSEEKSRqLAEWLDDAKQKL 361
Cdd:pfam15934 41 ENKNEQEQQLKEFTVQNQRLACQIDNLH----------ETLKDRDHQI-KQLQSMITGYSDISENNR-LKEEIHDLKQKN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 362 QQTLQKAETLP-EIEAQLAQRVAALNKAEERHGNFEERLrqleaqleeknQELQRARQREKmndDHNKRLSEtVDKLLSE 440
Cdd:pfam15934 109 CVQARVVRKMGlELKGQEEQRVELCDKYESLLGSFEEQC-----------QELKRANRRVQ---SLQTRLSQ-VEKLQEE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 161016786 441 SNERLQLhLKERMGALEEKNSLSeeIANMKKLQDELllnkeqllaemERMQMEIDQLR 498
Cdd:pfam15934 174 LRTERKI-LREEVIALKEKDAKS--NGRERALQDQL-----------KCCQTEIEKSR 217
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
374-500 |
3.97e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 374 IEAQLAQRVAALNKAEERhgnFEERLRQLEAQLEEKNQELQRARQREKMNDdhNKRLSETVDKLLSESNERLQLHLKERM 453
Cdd:COG3206 162 LEQNLELRREEARKALEF---LEEQLPELRKELEEAEAALEEFRQKNGLVD--LSEEAKLLLQQLSELESQLAEARAELA 236
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 161016786 454 GALEEKNSLSEEIANMKKLQDELLLNKE--QLLAEMERMQMEIDQLRGR 500
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQSPViqQLRAQLAELEAELAELSAR 285
|
|
| F-BAR_GAS7 |
cd07649 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Growth Arrest Specific protein ... |
286-435 |
4.26e-04 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Growth Arrest Specific protein 7; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Growth Arrest Specific protein 7 (GAS7) is mainly expressed in the brain and is required for neurite outgrowth. It may also play a role in the protection and migration of embryonic stem cells. Treatment-related acute myeloid leukemia (AML) has been reported resulting from mixed-lineage leukemia (MLL)-GAS7 translocations as a complication of primary cancer treatment. GAS7 contains an N-terminal SH3 domain, followed by a WW domain, and a central F-BAR domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153333 [Multi-domain] Cd Length: 233 Bit Score: 43.46 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 286 KLQRDLKEALAQREDMEER----ITTLEKRYLSAQREATsLHDANDKLENELASKESLYRQSEEKSR-QLAEWLDDAKQK 360
Cdd:cd07649 19 QMQKEMAEFIRERIKIEEEyaknLSKLSQSSLAAQEEGT-LGEAWAQVKKSLADEAEVHLKFSSKLQsEVEKPLLNFREN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 361 LQQTLQKAET-LPEIEAQLAQRVAALNKAE----ERHGNFEERLRQLEAQLEEKNQE-LQRARQRekmNDDHNKRLSETV 434
Cdd:cd07649 98 FKKDMKKLDHhIADLRKQLASRYAAVEKARkallERQKDLEGKTQQLEIKLSNKTEEdIKKARRK---STQAGDDLMRCV 174
|
.
gi 161016786 435 D 435
Cdd:cd07649 175 D 175
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
254-476 |
4.26e-04 |
|
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: 43.09 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 254 ERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLkEALAQR-EDMEERITTLEKRYLSAQREATSLHDANDKLENE 332
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEV-AALNRRiQLLEEELERTEERLAEALEKLEEAEKAADESERG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 333 LASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAEtlpEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQE 412
Cdd:pfam00261 80 RKVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYE---EVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNN 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161016786 413 LQ-------RARQREKMNDDH----NKRLSETVDKllSESNERLQLHLKERMGALEEKnsLSEEIANMKKLQDEL 476
Cdd:pfam00261 157 LKsleaseeKASEREDKYEEQirflTEKLKEAETR--AEFAERSVQKLEKEVDRLEDE--LEAEKEKYKAISEEL 227
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
36-415 |
4.91e-04 |
|
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: 44.35 E-value: 4.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 36 LTERERLLETLREAQDGLATAQLRLRELGHE-----------KDSLQRQLSIA-LPQEFAALTKElnlcreqllereeeI 103
Cdd:pfam05557 148 ASEAEQLRQNLEKQQSSLAEAEQRIKELEFEiqsqeqdseivKNSKSELARIPeLEKELERLREH--------------N 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 104 AELKAERNNTRLLLEHLECLVSRHER--SLRMTVVKRQAQ-----------------------SPGGVSSEVE------- 151
Cdd:pfam05557 214 KHLNENIENKLLLKEEVEDLKRKLEReeKYREEAATLELEkekleqelqswvklaqdtglnlrSPEDLSRRIEqlqqrei 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 152 VLKALKSLFEHHKALDEKVRERLR--MALERVAVLEEELELSNQEALNLRDQ-----LSRRRSGLEEPGKDGDGQTLANG 224
Cdd:pfam05557 294 VLKEENSSLTSSARQLEKARRELEqeLAQYLKKIEDLNKKLKRHKALVRRLQrrvllLTKERDGYRAILESYDKELTMSN 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 225 LGPvgESNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHREL------------GKAEEANSKLQRDLK 292
Cdd:pfam05557 374 YSP--QLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELqalrqqesladpSYSKEEVDSLRRKLE 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 293 EALAQREDMEERITTLEKRYlsAQREATSLHDANDKLENELASKESLyrQSEEKSRQLAEWLDDAKQKLQQTLQKAETLP 372
Cdd:pfam05557 452 TLELERQRLREQKNELEMEL--ERRCLQGDYDPKKTKVLHLSMNPAA--EAYQQRKNQLEKLQAEIERLKRLLKKLEDDL 527
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 161016786 373 EIEAQLAQRVAALNkaeerhgnfEERLRQLEAQLEEKNQELQR 415
Cdd:pfam05557 528 EQVLRLPETTSTMN---------FKEVLDLRKELESAELKNQR 561
|
|
| PRK13729 |
PRK13729 |
conjugal transfer pilus assembly protein TraB; Provisional |
535-747 |
5.02e-04 |
|
conjugal transfer pilus assembly protein TraB; Provisional
Pssm-ID: 184281 [Multi-domain] Cd Length: 475 Bit Score: 44.04 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 535 AGSGRAGKRGRWSGAKDESSKDwdRSAPAGSIPPPFPGELDGSDEEEaegmfgaelLSPSGQADVQTLAIMLQEQLEAIN 614
Cdd:PRK13729 21 VGAAAAIGGALYLSDVDMSGNG--EAVAEQEPVPDMTGVVDTTFDDK---------VRQHATTEMQVTAAQMQKQYEEIR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 615 KEIKLIQEEKETTEQRAEELESRVS--SSGLDSLGryrsscslpPSLTTSTlaspsppssGHSTPRLAPPSPAREGTDKT 692
Cdd:PRK13729 90 RELDVLNKQRGDDQRRIEKLGQDNAalAEQVKALG---------ANPVTAT---------GEPVPQMPASPPGPEGEPQP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 693 NHVSkeeAGVPRGEGPAVP---------GDTPPP------TPRSARLERMAQALALQAGSPEDGAPPRGS 747
Cdd:PRK13729 152 GNTP---VSFPPQGSVAVPpptafypgnGVTPPPqvtyqsVPVPNRIQRKTFTYNEGKKGPSLPYIPSGS 218
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
280-368 |
5.68e-04 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 41.42 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 280 AEEANSKLQRDLKEALAQREDMEERITTLEKRYlsaQREATSL-HDANDKLENELASKESLYRQ-SEEKSRQLAEWLDDA 357
Cdd:smart00935 16 GKAAQKQLEKEFKKRQAELEKLEKELQKLKEKL---QKDAATLsEAAREKKEKELQKKVQEFQRkQQKLQQDLQKRQQEE 92
|
90
....*....|.
gi 161016786 358 KQKLQQTLQKA 368
Cdd:smart00935 93 LQKILDKINKA 103
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
38-440 |
5.94e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 5.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 38 ERERLLET-------LREAQDGLATAQLRLRELGHEKDSLQRQLSIaLPQEFAALTKELNLcreqllEREEEIAELKAER 110
Cdd:PRK04863 280 ERRVHLEEalelrreLYTSRRQLAAEQYRLVEMARELAELNEAESD-LEQDYQAASDHLNL------VQTALRQQEKIER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 111 NNTRL------LLEHLECLVSRHERSLRMTVVKRQAqspggvssEVEVLKALKSLFEHHKALD----------------E 168
Cdd:PRK04863 353 YQADLeeleerLEEQNEVVEEADEQQEENEARAEAA--------EEEVDELKSQLADYQQALDvqqtraiqyqqavqalE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 169 KVRERLR---MALERVAVLEEELELSNQEALNLRDQLSRRRSgLEEPGKDGDGQTLANGLGPVGESNRRTA-----ELEE 240
Cdd:PRK04863 425 RAKQLCGlpdLTADNAEDWLEEFQAKEQEATEELLSLEQKLS-VAQAAHSQFEQAYQLVRKIAGEVSRSEAwdvarELLR 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 241 ALERQRAE---VCQLRERLAVL---CRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLS 314
Cdd:PRK04863 504 RLREQRHLaeqLQQLRMRLSELeqrLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMA 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 315 AQREATSLhdanDKLENELASKESLYRQSEEKSRQLAEWLDDakqklqqTLQKAETLPEIEAQLAQRVAALNKAEERhgn 394
Cdd:PRK04863 584 LRQQLEQL----QARIQRLAARAPAWLAAQDALARLREQSGE-------EFEDSQDVTEYMQQLLERERELTVERDE--- 649
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 161016786 395 FEERLRQLEAQLEeknqelqRARQREKMNDDHNKRLSETVDK-LLSE 440
Cdd:PRK04863 650 LAARKQALDEEIE-------RLSQPGGSEDPRLNALAERFGGvLLSE 689
|
|
| PLN03237 |
PLN03237 |
DNA topoisomerase 2; Provisional |
481-776 |
6.52e-04 |
|
DNA topoisomerase 2; Provisional
Pssm-ID: 215641 [Multi-domain] Cd Length: 1465 Bit Score: 44.08 E-value: 6.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 481 EQLLAEMERMQMEIDQLRGRPPSS-YSRSLpgSALELRYSQaptlpsgapLDPYGAGSGRAGKRGRWSGAKDESSKDWDR 559
Cdd:PLN03237 1129 QELCADRDKLNIEVEDLKKTTPKSlWLKDL--DALEKELDK---------LDKEDAKAEEAREKLQRAAARGESGAAKKV 1197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 560 SAPAGSIPPPFPGELDGSDEEEAEGMFG---------AELLSPSGQADVQTLAIMLQEQLEAinkeikliqeekettEQR 630
Cdd:PLN03237 1198 SRQAPKKPAPKKTTKKASESETTEETYGssametenvAEVVKPKGRAGAKKKAPAAAKEKEE---------------EDE 1262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 631 AEELESRVSSSGLDslgryrSSCSLPPSLTTSTLASPSPPSSGHSTPRLAPPSPAREgTDKTNHVSKEEAGVPR-----G 705
Cdd:PLN03237 1263 ILDLKDRLAAYNLD------SAPAQSAKMEETVKAVPARRAAARKKPLASVSVISDS-DDDDDDFAVEVSLAERlkkkgG 1335
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161016786 706 EGPAVPGDTPPPTPRSARLERMAQALALQAGSPEDGAPPRGSESTPDS----LHKAPKRKSIKSSIGRLFGKKEK 776
Cdd:PLN03237 1336 RKPAAANKKAAKPPAAAKKRGPATVQSGQKLLTEMLKPAEAIGISPEKkvrkMRASPFNKKSGSVLGRAATNKET 1410
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
357-488 |
6.79e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.54 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 357 AKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDK 436
Cdd:PRK12705 27 KRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQ 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161016786 437 L------LSESNERLQLHLKERMGALEEKNSLSEEIAN---MKKLQDELLLNKEQLLAEME 488
Cdd:PRK12705 107 LeerekaLSARELELEELEKQLDNELYRVAGLTPEQARkllLKLLDAELEEEKAQRVKKIE 167
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
268-492 |
6.98e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.76 E-value: 6.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 268 EELGTAHRELGKAEEANSKLQRDLKEA--------LAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELASKESl 339
Cdd:PRK05771 43 ERLRKLRSLLTKLSEALDKLRSYLPKLnplreekkKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQ- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 340 yrqseEKSRqLAEW----LDDAKQKLQQTLQ-KAETLPEIEAQLAQRVAALNKAEERHGNFEER---LRQLEAQLEEKNQ 411
Cdd:PRK05771 122 -----EIER-LEPWgnfdLDLSLLLGFKYVSvFVGTVPEDKLEELKLESDVENVEYISTDKGYVyvvVVVLKELSDEVEE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 412 ELQRARQREKMNDDhnkrlSETVDKLLSESNERLQLhLKermgalEEKNSLSEEIANM-KKLQDELLLNKEQLLAEMERM 490
Cdd:PRK05771 196 ELKKLGFERLELEE-----EGTPSELIREIKEELEE-IE------KERESLLEELKELaKKYLEELLALYEYLEIELERA 263
|
..
gi 161016786 491 QM 492
Cdd:PRK05771 264 EA 265
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
299-421 |
7.11e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.05 E-value: 7.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 299 EDMEERITTLEKRYLSAQREATSLHDANDKLENELaskeslyrqsEEKSRQLAEWLDDAKQKLQQTLQKA-----ETLPE 373
Cdd:PRK00409 519 NELIASLEELERELEQKAEEAEALLKEAEKLKEEL----------EEKKEKLQEEEDKLLEEAEKEAQQAikeakKEADE 588
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 161016786 374 IEAQLAQRVAALNKAEERHgNFEERLRQLEAQLEEKNQELQRARQREK 421
Cdd:PRK00409 589 IIKELRQLQKGGYASVKAH-ELIEARKRLNKANEKKEKKKKKQKEKQE 635
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
230-498 |
7.66e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 7.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 230 ESNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELgtahrelgkaEEANSKLQ---RDLKEALAQREDMEERIT 306
Cdd:COG1340 5 ELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKR----------DELNAQVKelrEEAQELREKRDELNEKVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 307 TLEKRYLSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLaewlddakQKLQQTLQKAETLPEIEAQLAQRVAALn 386
Cdd:COG1340 75 ELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEI--------ERLEWRQQTEVLSPEEEKELVEKIKEL- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 387 kaeerhgnfEERLRQLEAQLEEKNQ---ELQRARQREKMNDDHNKRLSETVDKLLSESNERLQLhLKERMGALEEKNSLS 463
Cdd:COG1340 146 ---------EKELEKAKKALEKNEKlkeLRAELKELRKEAEEIHKKIKELAEEAQELHEEMIEL-YKEADELRKEADELH 215
|
250 260 270
....*....|....*....|....*....|....*
gi 161016786 464 EEIANMKKLQDELLLNKEQLLAEMERMQMEIDQLR 498
Cdd:COG1340 216 KEIVEAQEKADELHEEIIELQKELRELRKELKKLR 250
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
265-499 |
9.32e-04 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 41.97 E-value: 9.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 265 QLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQreatslhdanDKLENELAsKESLYRqse 344
Cdd:pfam04012 26 MLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAAL----------TKGNEELA-REALAE--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 345 eksrqlaewlddaKQKLQQTLQkaetlpEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQREKMNd 424
Cdd:pfam04012 92 -------------KKSLEKQAE------ALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAAKAQEAVQ- 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161016786 425 dhnkrlsETVDKLLSESNERLQLHLKERMGALEEKNSLSEEIANMKKLQDELllnkEQLLAEMERMQMEIDQLRG 499
Cdd:pfam04012 152 -------TSLGSLSTSSATDSFERIEEKIEEREARADAAAELASAVDLDAKL----EQAGIQMEVSEDVLARLKA 215
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
22-500 |
9.37e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.42 E-value: 9.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 22 DEAGGELERLMVTMLTERERLLETLREAQDGLATAQLRLRELGHEKDSLQRQLSIALPQEfAALTKELNLCREQLLEREE 101
Cdd:TIGR00618 336 QQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKL-QSLCKELDILQREQATIDT 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 102 EIAELKAERNntRLLLEHLECLVSRHERSLRMTVVKRQAQSPGGVSSEV----EVLKALKSLFEHHKALDEKVRERLRMA 177
Cdd:TIGR00618 415 RTSAFRDLQG--QLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLqesaQSLKEREQQLQTKEQIHLQETRKKAVV 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 178 LERVAVL-EEELELSNQE--------ALNLRDQLSRRRSGLEEPGKDGdGQTLANGLGPVGESNRRTAELEEALERQRAE 248
Cdd:TIGR00618 493 LARLLELqEEPCPLCGSCihpnparqDIDNPGPLTRRMQRGEQTYAQL-ETSEEDVYHQLTSERKQRASLKEQMQEIQQS 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 249 ---VCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHda 325
Cdd:TIGR00618 572 fsiLTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALH-- 649
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 326 ndKLENELASKESlyRQSEEKSRQLAEWLDDAKQKLQQTLQ-KAETLPEIEAQLAQRVAALNKAEERHGN----FEE--- 397
Cdd:TIGR00618 650 --ALQLTLTQERV--REHALSIRVLPKELLASRQLALQKMQsEKEQLTYWKEMLAQCQTLLRELETHIEEydreFNEien 725
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 398 ----RLRQLEAQLEEKNQELQRARQ------REKMNDDHNKRLSETVDKLLSESNERLQLHLKERMGALEEK----NSLS 463
Cdd:TIGR00618 726 asssLGSDLAAREDALNQSLKELMHqartvlKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDthllKTLE 805
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 161016786 464 EEIAN-------MKKLQDELLLNKEQ----LLAEMERMQMEIDQLRGR 500
Cdd:TIGR00618 806 AEIGQeipsdedILNLQCETLVQEEEqflsRLEEKSATLGEITHQLLK 853
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
38-456 |
9.56e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 43.59 E-value: 9.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 38 ERERLLET---LREAQDGLATA----QLRLRELGH----EKDSLQRQLSIALPQEFAALTKELNLCREQLLEREEEIAEL 106
Cdd:pfam07111 243 ERQELLDTmqhLQEDRADLQATvellQVRVQSLTHmlalQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREKVFALMVQL 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 107 KAE----RNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPGGVSSEVEVLKALKSLFEHHKALDEKVRERlrmalERVA 182
Cdd:pfam07111 323 KAQdlehRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQ-----QQTA 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 183 VLEEELELSNQEALNLRDQLSRRRSGLEEPGkdGDGQTLANGLGPVGESNRRTAEL---EEALERQRAEVCQLRERL--- 256
Cdd:pfam07111 398 SAEEQLKFVVNAMSSTQIWLETTMTRVEQAV--ARIPSLSNRLSYAVRKVHTIKGLmarKVALAQLRQESCPPPPPAppv 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 257 -AVLCRQMSQLEEELGTAHRELG-KAEEANSKLQRDLKEALAQREDMEERITTLEKRYlsaQREATSLHDANDKLENELA 334
Cdd:pfam07111 476 dADLSLELEQLREERNRLDAELQlSAHLIQQEVGRAREQGEAERQQLSEVAQQLEQEL---QRAQESLASVGQQLEVARQ 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 335 SKEslyrQSEEKSRQLAEWLDDAKQKLQQTLQK--AETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLE---AQLEEK 409
Cdd:pfam07111 553 GQQ----ESTEEAASLRQELTQQQEIYGQALQEkvAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQhraTQEKER 628
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 161016786 410 NQELQRArqREKMNDDHNKRLSETVDKLlsESNERLQLHLKERMGAL 456
Cdd:pfam07111 629 NQELRRL--QDEARKEEGQRLARRVQEL--ERDKNLMLATLQQEGLL 671
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
83-363 |
9.69e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 9.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 83 AALTKELNLCREQLLEREEEIAELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpggVSSEVE-------VLKA 155
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAE---LEAELErldassdDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 156 LKSLFEHHKALDEKVRERLRMALERVAVLEEELElsnqEALNLRDQLSRRRSGLEEPGKDGDGQTLAnglgpvgesNRRT 235
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELE----QAEEELDELQDRLEAAEDLARLELRALLE---------ERFA 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 236 AELEEALERQRAEvcQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSklqRDLKEALAQREDMEERITTLekrylsa 315
Cdd:COG4913 757 AALGDAVERELRE--NLEERIDALRARLNRAEEELERAMRAFNREWPAET---ADLDADLESLPEYLALLDRL------- 824
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 161016786 316 qrEATSLHDANDKLenelasKESLYRQSEEK----SRQLAEWLDDAKQKLQQ 363
Cdd:COG4913 825 --EEDGLPEYEERF------KELLNENSIEFvadlLSKLRRAIREIKERIDP 868
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
234-499 |
1.25e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 234 RTAELEEALERQRAEVcQLRERLAVLCRQMSQLEEELGtaHRElgKAEEANSKLQRDLKEALAQREDMEERITTLEKRYL 313
Cdd:pfam01576 614 KAISARYAEERDRAEA-EAREKETRALSLARALEEALE--AKE--ELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKR 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 314 SAQREATSLHDANDKLENEL---------------ASKESLYR-------QSEEKSRQL--------AEWLDDAKQKLQQ 363
Cdd:pfam01576 689 ALEQQVEEMKTQLEELEDELqatedaklrlevnmqALKAQFERdlqardeQGEEKRRQLvkqvreleAELEDERKQRAQA 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 364 TLQKAE---TLPEIEAQlaqrVAALNKAEERHGnfeERLRQLEAQLEEKNQELQRARQ-REKM--NDDHNKRLSETVDKL 437
Cdd:pfam01576 769 VAAKKKlelDLKELEAQ----IDAANKGREEAV---KQLKKLQAQMKDLQRELEEARAsRDEIlaQSKESEKKLKNLEAE 841
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161016786 438 LSESNERLQLHLKERMGALEEKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQLRG 499
Cdd:pfam01576 842 LLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQS 903
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
38-459 |
1.29e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.17 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 38 ERERLLETLREAQdglATAQLRLRELGHEKDSLQRQLSIAlPQEFAALTKELNLCREQLLEREEEIAELKAERNNTRLLL 117
Cdd:pfam05483 332 EKEAQMEELNKAK---AAHSFVVTEFEATTCSLEELLRTE-QQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVEL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 118 EHLECLVSRHERSL-RMTVVKRQAQSPGGVSSEVEVLKALKSLFEHHKALDEKV-RERLRMALERVAVLEEELE---LSN 192
Cdd:pfam05483 408 EELKKILAEDEKLLdEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAiKTSEEHYLKEVEDLKTELEkekLKN 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 193 QEALNLRDQLSRRRSGLEEPGKDGDGQtLANGLGPVGESNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGT 272
Cdd:pfam05483 488 IELTAHCDKLLLENKELTQEASDMTLE-LKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKC 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 273 ahrELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHDAN---------------------DKLEN 331
Cdd:pfam05483 567 ---KLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENkalkkkgsaenkqlnayeikvNKLEL 643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 332 ELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETL--------PEIEAQLAQRVAALNKAEERHGNfeerlrQLE 403
Cdd:pfam05483 644 ELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIadeavklqKEIDKRCQHKIAEMVALMEKHKH------QYD 717
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161016786 404 AQLEEKNQELQRARQREKMNDDHNK----RLSETVDKLLS---------ESNERLQLHLKERMGALEEK 459
Cdd:pfam05483 718 KIIEERDSELGLYKNKEQEQSSAKAaleiELSNIKAELLSlkkqleiekEEKEKLKMEAKENTAILKDK 786
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
168-425 |
1.30e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 168 EKVRERLRMALERVAVLEEELELSNQEALNLRDQLSRRRSGLEEpgkdgDGQTLANGLGPVGESNRRTAELEEALERQRA 247
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA-----AQAELAQAQEELESLQEEAEELQEELEELQK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 248 EVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLK--EALAQREDMEERITTLEKRYLSAQREATSL--H 323
Cdd:COG4372 123 ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAalEQELQALSEAEAEQALDELLKEANRNAEKEeeL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 324 DANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLE 403
Cdd:COG4372 203 AEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAA 282
|
250 260
....*....|....*....|..
gi 161016786 404 AQLEEKNQELQRARQREKMNDD 425
Cdd:COG4372 283 LELEALEEAALELKLLALLLNL 304
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
501-797 |
1.56e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.85 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 501 PPSSYSRSLPGSALELRYSQAPTLPSGA--PLDPYGAGSGRAGKRGRWSGAkDESSKDWDRSAPAGSIPPPFPGEldgSD 578
Cdd:PHA03307 123 PASPPPSPAPDLSEMLRPVGSPGPPPAAspPAAGASPAAVASDAASSRQAA-LPLSSPEETARAPSSPPAEPPPS---TP 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 579 EEEAEGmfGAELLSPSGQADVQTLAIMLqeqleainkeikliqeEKETTEQRAEELESRVSSSGLDSLGRYRSSCSLPPS 658
Cdd:PHA03307 199 PAAASP--RPPRRSSPISASASSPAPAP----------------GRSAADDAGASSSDSSSSESSGCGWGPENECPLPRP 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 659 LTTSTLASPSPPSSGHSTPRLAPPSPAREGTdktnhvsKEEAGVPRgegPAVPGDTPPPTPRSARLERMAQALALQAGSP 738
Cdd:PHA03307 261 APITLPTRIWEASGWNGPSSRPGPASSSSSP-------RERSPSPS---PSSPGSGPAPSSPRASSSSSSSRESSSSSTS 330
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161016786 739 EDGAPPRG--------------SESTPDSLHKAPKRKSIKSSIGRLFGKKEKGRMGPP-GRESVSLAGTPSDET 797
Cdd:PHA03307 331 SSSESSRGaavspgpspsrspsPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRrARAAVAGRARRRDAT 404
|
|
| SAM_SARM1-like_repeat1 |
cd09501 |
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
961-1004 |
1.64e-03 |
|
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of SARM1-like adaptor proteins is a protein-protein interaction domain. SARM1-like proteins contain two tandem SAM domains. SARM1-like proteins are involved in TLR (Toll-like receptor) signaling. They are responsible for targeted localization of the whole protein to post-synaptic regions of axons. In humans SARM1 expression is detected in kidney and liver.
Pssm-ID: 188900 [Multi-domain] Cd Length: 69 Bit Score: 38.05 E-value: 1.64e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 161016786 961 WLPSLGLPQYRSYFMESLVDARMLDHLNKKELRGQLKMVDSFHR 1004
Cdd:cd09501 12 WLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLR 55
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
293-498 |
1.72e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 41.52 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 293 EALAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKaETLP 372
Cdd:pfam12795 3 DELEKAKLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQELAALQAKAEAAPKEILAS-LSLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 373 EIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQR-EKMNDDHNkrLSETVDKLLSESnerLQLHLKE 451
Cdd:pfam12795 82 ELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRlQQIRNRLN--GPAPPGEPLSEA---QRWALQA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 161016786 452 RMGALEEKNSLSE-EIANMKKLQDELLLNKEQLLAEMERMQMEIDQLR 498
Cdd:pfam12795 157 ELAALKAQIDMLEqELLSNNNRQDLLKARRDLLTLRIQRLEQQLQALQ 204
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
262-443 |
1.78e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.61 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 262 QMSQLEEELGTAHRELGKA-----EEANSKLQRDLKEALAQREDMEERITTLE---KRYLSAQREATSLHDANDKLENEL 333
Cdd:PRK05771 61 KLRSYLPKLNPLREEKKKVsvkslEELIKDVEEELEKIEKEIKELEEEISELEneiKELEQEIERLEPWGNFDLDLSLLL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 334 A-----------SKESLYRQSEEKSRQLAEWLDDAKQKLQQTL-QKAETLPEIEAQLAqRVAALNKAEERHGNFEERLRQ 401
Cdd:PRK05771 141 GfkyvsvfvgtvPEDKLEELKLESDVENVEYISTDKGYVYVVVvVLKELSDEVEEELK-KLGFERLELEEEGTPSELIRE 219
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 161016786 402 LEAQLEEKNQELQRARQR-EKMNDDHNKRLSETVDKLLSESNE 443
Cdd:PRK05771 220 IKEELEEIEKERESLLEElKELAKKYLEELLALYEYLEIELER 262
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
383-500 |
2.30e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.96 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 383 AALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKL-------LSESNERLqlhLKErmgA 455
Cdd:COG1842 16 ALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWeekarlaLEKGREDL---ARE---A 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 161016786 456 LEEKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQLRGR 500
Cdd:COG1842 90 LERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAK 134
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
36-347 |
2.33e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 36 LTER-ERLLETLREAQDGLATAQLRLRELGHEKDSLQRQLS-------------IALPQEFAALTKELNLCRE---QLLE 98
Cdd:PRK04863 360 LEERlEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLAdyqqaldvqqtraIQYQQAVQALERAKQLCGLpdlTADN 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 99 REEEIAELKA---ERNNTRLLLEH----LECLVSRHERSLRMtvVKRQAqspGGVSSEV--EVLKALKSLFEHHKALDEK 169
Cdd:PRK04863 440 AEDWLEEFQAkeqEATEELLSLEQklsvAQAAHSQFEQAYQL--VRKIA---GEVSRSEawDVARELLRRLREQRHLAEQ 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 170 VrERLRMALervAVLEEELELsNQEALNLRDQLSrRRSGLEEPGKDgdgqtlanglgpvgESNRRTAELEEALERQRAEV 249
Cdd:PRK04863 515 L-QQLRMRL---SELEQRLRQ-QQRAERLLAEFC-KRLGKNLDDED--------------ELEQLQEELEARLESLSESV 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 250 CQLRERLAvlcrQMSQLEEELGTAHRELGK-------AEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREatsl 322
Cdd:PRK04863 575 SEARERRM----ALRQQLEQLQARIQRLAArapawlaAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVE---- 646
|
330 340
....*....|....*....|....*
gi 161016786 323 hdaNDKLEnelASKESLYRQSEEKS 347
Cdd:PRK04863 647 ---RDELA---ARKQALDEEIERLS 665
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
231-389 |
2.37e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.72 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 231 SNRRTAELEEALERQRAEvcQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSklqrdlKEALAQREDMEERITTLEK 310
Cdd:PRK09510 73 SAKRAEEQRKKKEQQQAE--ELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAK------QAALKQKQAEEAAAKAAAA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 311 RYLSAQREATSLHDANDKLENELASKEslyrQSEEKSRQLAEwlddAKQKLQQTLQK---AETLPEIEAQLAQRVAALNK 387
Cdd:PRK09510 145 AKAKAEAEAKRAAAAAKKAAAEAKKKA----EAEAAKKAAAE----AKKKAEAEAAAkaaAEAKKKAEAEAKKKAAAEAK 216
|
..
gi 161016786 388 AE 389
Cdd:PRK09510 217 KK 218
|
|
| SAM_superfamily |
cd09487 |
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
843-900 |
2.55e-03 |
|
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.
Pssm-ID: 188886 [Multi-domain] Cd Length: 56 Bit Score: 37.22 E-value: 2.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 161016786 843 VVSWLElWVGMPaWYVAACRANVKSGAIMANLSDTEIQrEIGISNPLHRLKLRLAIQE 900
Cdd:cd09487 2 VAEWLE-SLGLE-QYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAIQR 56
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
340-498 |
2.94e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.02 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 340 YRQSEEKSRQLAEWLDD---AKQKLQQTLQKAETL-----PEIEAQLAQRVAALNKAEERhgnfEERLRQLEAQLE--EK 409
Cdd:cd16269 158 YRQVPRKGVKAEEVLQEflqSKEAEAEAILQADQAltekeKEIEAERAKAEAAEQERKLL----EEQQRELEQKLEdqER 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 410 NQELQRARQREKMNDDHNKRLSEtvdkllsesNERLQLHlkermgaleeknslseeianmkKLQDELLLNKEQLLAEMER 489
Cdd:cd16269 234 SYEEHLRQLKEKMEEERENLLKE---------QERALES----------------------KLKEQEALLEEGFKEQAEL 282
|
....*....
gi 161016786 490 MQMEIDQLR 498
Cdd:cd16269 283 LQEEIRSLK 291
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
291-500 |
3.12e-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: 41.88 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 291 LKEALAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELASKESLyrqsEEKSRQLAEWLDDAKQKLQQTLQKAET 370
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLL----TLCTPCMPDTYHERKQVLEKELKHLRE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 371 ----LPEIEAQLAQRVAALNKAEERHGNF------EERLRQLEAQLEEKNQELQRARQREKMNdDHNKRLSEtVDKLLSE 440
Cdd:TIGR00618 234 alqqTQQSHAYLTQKREAQEEQLKKQQLLkqlrarIEELRAQEAVLEETQERINRARKAAPLA-AHIKAVTQ-IEQQAQR 311
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 441 SNERLQLHLKERMGALEEKNSLSEEIANMKKLQDELllnkEQLLAEMERMQMEIDQLRGR 500
Cdd:TIGR00618 312 IHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLL----QTLHSQEIHIRDAHEVATSI 367
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
309-452 |
3.15e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 41.62 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 309 EKRYLSAQREATSLHDANdklenELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLP----EIEAQLAQRVAA 384
Cdd:PRK12705 36 ERILQEAQKEAEEKLEAA-----LLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDaraeKLDNLENQLEER 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161016786 385 LNKAEERHGNFEERLRQLEAQLEEKNQeLQRARQREKMNDDHNKRLSETVDKLLSESNERLQLHLKER 452
Cdd:PRK12705 111 EKALSARELELEELEKQLDNELYRVAG-LTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERK 177
|
|
| CDC37_N |
smart01071 |
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ... |
398-498 |
3.73e-03 |
|
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domain corresponds to the N terminal domain which binds predominantly to protein kinases.and is found N terminal to the Hsp (Heat shocked protein) 90-binding domain. Expression of a construct consisting of only the N-terminal domain of Saccharomyces pombe Cdc37 results in cellular viability. This indicates that interactions with the cochaperone Hsp90 may not be essential for Cdc37 function.
Pssm-ID: 198139 [Multi-domain] Cd Length: 154 Bit Score: 39.32 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 398 RLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKLLSESNERLQLHLKERMGALEEKNSLSEEIANM--KKLQDE 475
Cdd:smart01071 33 KQRDIHQARVERMEEIKNLKYELIMNDHLNKRIDKLLKGLREEELSPETPTYNEMLAELQDQLKKELEEANGdsEGLLEE 112
|
90 100
....*....|....*....|...
gi 161016786 476 LLLNKEQLLAEMERMQMEIDQLR 498
Cdd:smart01071 113 LKKHRDKLKKEQKELRKKLDELE 135
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
236-440 |
3.91e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.06 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 236 AELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEAN-SKLQRDLKEALAQREDMEERITTLEKRYLS 314
Cdd:pfam13868 137 EEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREiARLRAQQEKAQDEKAERDELRAKLYQEEQE 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 315 AQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKaeeRHGN 394
Cdd:pfam13868 217 RKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRL---EHRR 293
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 161016786 395 FEERLRQL--EAQLEEKNQELQRARQREKMNDDHNKRLSETVDKLLSE 440
Cdd:pfam13868 294 ELEKQIEEreEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
236-408 |
3.93e-03 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 38.82 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 236 AELEEALERqrAEvcQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEkrylsa 315
Cdd:pfam12718 7 LEAENAQER--AE--ELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNE------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 316 qreatSLHDANDKLENELaskeslyrqsEEKSRQLAEwlddAKQKLQQTLQKAEtlpeieaQLAQRVAALnkaEERHGNF 395
Cdd:pfam12718 77 -----NLTRKIQLLEEEL----------EESDKRLKE----TTEKLRETDVKAE-------HLERKVQAL---EQERDEW 127
|
170
....*....|...
gi 161016786 396 EERLRQLEAQLEE 408
Cdd:pfam12718 128 EKKYEELEEKYKE 140
|
|
| SAM_Ste50-like_fungal |
cd09533 |
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ... |
960-1007 |
3.97e-03 |
|
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or Ubc2 for Ustilago bypass of cyclase) subfamily is a putative protein-protein interaction domain. This group includes only fungal proteins. Basidiomycetes have an N-terminal SAM domain, central UBQ domain, and C-terminal SH3 domain, while Ascomycetes lack the SH3 domain. Ubc2 of Ustilago maydis is a major virulence and maize pathogenicity factor. It is required for filamentous growth (the budding haploid form of Ustilago maydis is a saprophyte, while filamentous dikaryotic form is a pathogen). Also the Ubc2 protein is involved in the pheromone-responsive morphogenesis via the MAP kinase cascade. The SAM domain is necessary for ubc2 function; deletion of SAM eliminates this function. A Lys-to-Glu mutation in the SAM domain of ubc2 gene induces temperature sensitivity.
Pssm-ID: 188932 Cd Length: 58 Bit Score: 36.91 E-value: 3.97e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 161016786 960 DWLPSLGLPQYRSYFMESLVDARMLDHLNKKELRgQLKMVDSFHRVSL 1007
Cdd:cd09533 4 DWLSSLGLPQYEDQFIENGITGDVLVALDHEDLK-EMGITSVGHRLTI 50
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
353-498 |
4.02e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.58 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 353 WLDDAKQKLQ--QTLQKA-ETLPEIEAQLAQRVAALN------KAEERHGNFEERLRQLEAQLEEKNQELQRARQREKMN 423
Cdd:PRK10929 56 WLEERKGSLEraKQYQQViDNFPKLSAELRQQLNNERdeprsvPPNMSTDALEQEILQVSSQLLEKSRQAQQEQDRAREI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 424 DDHNKRL----SETvDKLLSESNERLQLHLKERMGALEEKN-SLSEEIANMKKLQDELLLnkEQLLA----EMERMQMEI 494
Cdd:PRK10929 136 SDSLSQLpqqqTEA-RRQLNEIERRLQTLGTPNTPLAQAQLtALQAESAALKALVDELEL--AQLSAnnrqELARLRSEL 212
|
....
gi 161016786 495 DQLR 498
Cdd:PRK10929 213 AKKR 216
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
57-498 |
4.39e-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: 41.35 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 57 QLRLRELGHEKDSLQRQLSI------------------------ALPQEFAA----LTKELNLCREQLLEREEEI----A 104
Cdd:pfam10174 2 QAQLRDLQRENELLRRELDIkesklgssmnsiktfwspelkkerALRKEEAArisvLKEQYRVTQEENQHLQLTIqalqD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 105 ELKAERNNTRLLL---------------------EHLECLVSRHERS------LRMTV------VKRQAQSPGGVSSEVE 151
Cdd:pfam10174 82 ELRAQRDLNQLLQqdfttspvdgedkfstpelteENFRRLQSEHERQakelflLRKTLeemelrIETQKQTLGARDESIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 152 VLKALKSLFEHHKALDEKVRERLRMALE---RVAVLEEELELSNQEALNLRDQLSRRRSGLEEPGKDGDGQTLanglgpV 228
Cdd:pfam10174 162 KLLEMLQSKGLPKKSGEEDWERTRRIAEaemQLGHLEVLLDQKEKENIHLREELHRRNQLQPDPAKTKALQTV------I 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 229 GESNRRTAELEEALERQRAEVCQLRERLAVLCRQ----MSQLE----------EELGTAHRELGKAEEANSKLQRDLKEA 294
Cdd:pfam10174 236 EMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDreeeIKQMEvykshskfmkNKIDQLKQELSKKESELLALQTKLETL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 295 LAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELASKES--------LYRQSEEKSRQLAEWLD-----DAKQKL 361
Cdd:pfam10174 316 TNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESflnkktkqLQDLTEEKSTLAGEIRDlkdmlDVKERK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 362 QQTLQK-----AETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQ------REKMND-----D 425
Cdd:pfam10174 396 INVLQKkienlQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEqreredRERLEEleslkK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 426 HNKRLSETVDKLLSESNERLQ--LHLKERMGALE----EKNSL--SEEIANMKKLQD----ELLLNKEQLLAEMERMQME 493
Cdd:pfam10174 476 ENKDLKEKVSALQPELTEKESslIDLKEHASSLAssglKKDSKlkSLEIAVEQKKEEcsklENQLKKAHNAEEAVRTNPE 555
|
....*.
gi 161016786 494 I-DQLR 498
Cdd:pfam10174 556 InDRIR 561
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
233-498 |
4.70e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.22 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 233 RRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRD----LKEALAQREDMEERITTL 308
Cdd:COG5022 871 LQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTEliarLKKLLNNIDLEEGPSIEY 950
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 309 EKrylsaQREATSLHDANDKLENELASKESLYRQSEEKSRQL---AEWLDDAKQKLQQTLQKAETLPEIEAQLAQR---V 382
Cdd:COG5022 951 VK-----LPELNKLHEVESKLKETSEEYEDLLKKSTILVREGnkaNSELKNFKKELAELSKQYGALQESTKQLKELpveV 1025
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 383 AALNKAEERHGNFEERLRQ------LEAQLEEKNQELQ------RARQREKMNDDHNKRLSETVDKLLSESNErLQLHLK 450
Cdd:COG5022 1026 AELQSASKIISSESTELSIlkplqkLKGLLLLENNQLQarykalKLRRENSLLDDKQLYQLESTENLLKTINV-KDLEVT 1104
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 161016786 451 ERMGALEEK---NSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQLR 498
Cdd:COG5022 1105 NRNLVKPANvlqFIVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLE 1155
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
197-490 |
5.13e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 40.78 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 197 NLRDQLSR--RRSGLEEPGKDGDGQTLANGLGPVGESNRRTAELEEALERQRAEVCQLRerlavlcrqmsqleeelgtah 274
Cdd:pfam05667 251 RIAEQLRSaaLAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTEKLQFT--------------------- 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 275 RELGKAEEANSKLQRDLKEALAQREdmeERITTLEKRYLSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWL 354
Cdd:pfam05667 310 NEAPAATSSPPTKVETEEELQQQRE---EELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQY 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 355 DDAKQKLqqtlqkaETLPEIEAQLAQrvaaLNKAEErhgNFEERLRQLEAQLEEKNQELQRARQREKmnDDHNKRLSETV 434
Cdd:pfam05667 387 KVKKKTL-------DLLPDAEENIAK----LQALVD---ASAQRLVELAGQWEKHRVPLIEEYRALK--EAKSNKEDESQ 450
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 161016786 435 DKLlsesnERLQLhLKERMgaleeknslsEEIANMKKLQDELllnKEQLLAEMERM 490
Cdd:pfam05667 451 RKL-----EEIKE-LREKI----------KEVAEEAKQKEEL---YKQLVAEYERL 487
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
234-496 |
5.35e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 40.29 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 234 RTAELEEAlERQRAEVCQLRERLAvlcrqmSQLEEELGTAHRELGKAEEANSKLQRDLKEALaqREDMEERITTLEKRYL 313
Cdd:pfam13868 24 RDAQIAEK-KRIKAEEKEEERRLD------EMMEEERERALEEEEEKEEERKEERKRYRQEL--EEQIEEREQKRQEEYE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 314 SAQREATSLHDANDKLENElasKESLYRQSEEKSRQLAEWLDDAKQklQQTLQKAETLPEIEAQLAQRVAALNKAEERhg 393
Cdd:pfam13868 95 EKLQEREQMDEIVERIQEE---DQAEAEEKLEKQRQLREEIDEFNE--EQAEWKELEKEEEREEDERILEYLKEKAER-- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 394 nFEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKLLSESNERlqlhlKERMGALEEKnslseeianMKKLQ 473
Cdd:pfam13868 168 -EEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQER-----KERQKEREEA---------EKKAR 232
|
250 260
....*....|....*....|....*.
gi 161016786 474 DELLL---NKEQLLAEMERMQMEIDQ 496
Cdd:pfam13868 233 QRQELqqaREEQIELKERRLAEEAER 258
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
173-418 |
5.46e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 40.29 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 173 RLRMALERVAVLEEELELSNQEALNLRDQLSRRRSGLEEPGKdgdgQTLANGLGPVGESNRRTAELEEALERQRAEVCQL 252
Cdd:pfam00038 12 RLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYE----KEIEDLRRQLDTLTVERARLQLELDNLRLAAEDF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 253 RERLavlcrqmsqlEEELGtaHRELgkAEEANSKLQRDLKEALAQREDMEERITTL-------------EKRYLSAQREA 319
Cdd:pfam00038 88 RQKY----------EDELN--LRTS--AENDLVGLRKDLDEATLARVDLEAKIESLkeelaflkknheeEVRELQAQVSD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 320 TSLH---DANDKLE------------NELASK-----ESLYRQSEEKSRQLA----EWLDDAKQKLQQTLQKAETLP-EI 374
Cdd:pfam00038 154 TQVNvemDAARKLDltsalaeiraqyEEIAAKnreeaEEWYQSKLEELQQAAarngDALRSAKEEITELRRTIQSLEiEL 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 161016786 375 EAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQ 418
Cdd:pfam00038 234 QSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETRQ 277
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
236-498 |
6.17e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.05 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 236 AELEEAL------ERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGK-AEEANSK-----LQRDLKEALAQREDMEE 303
Cdd:PRK11281 63 QDLEQTLalldkiDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEeTRETLSTlslrqLESRLAQTLDQLQNAQN 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 304 RITTLEKRYLSAQ----REATSLHDA-------NDKLENELASKESLyrQSEEKSRQLAEW-LDDAKQKLQQT-LQKAET 370
Cdd:PRK11281 143 DLAEYNSQLVSLQtqpeRAQAALYANsqrlqqiRNLLKGGKVGGKAL--RPSQRVLLQAEQaLLNAQNDLQRKsLEGNTQ 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 371 LPEIE-----------AQLAQRVAALNKAeerhGNfEERLRQLEAQLEEknQELQRARQREKMND------DHNKRLSET 433
Cdd:PRK11281 221 LQDLLqkqrdyltariQRLEHQLQLLQEA----IN-SKRLTLSEKTVQE--AQSQDEAARIQANPlvaqelEINLQLSQR 293
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161016786 434 VDKLLSESNERLQLHLKERM---GALEEKNSLSEEIAnmkKLQDELLL----NKEQL----LAEMERMQMEIDQLR 498
Cdd:PRK11281 294 LLKATEKLNTLTQQNLRVKNwldRLTQSERNIKEQIS---VLKGSLLLsrilYQQQQalpsADLIEGLADRIADLR 366
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
321-437 |
6.42e-03 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 40.61 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 321 SLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRvaaLNKAEERHGNFEERLR 400
Cdd:COG5283 11 PFKSALESAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQA---LDQAGIDTRQLSAAQR 87
|
90 100 110
....*....|....*....|....*....|....*..
gi 161016786 401 QLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKL 437
Cdd:COG5283 88 RLRSSLEQTNRQLERQQQRLARLGARQDRLKAARARL 124
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
230-414 |
6.52e-03 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 39.27 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 230 ESNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELgTAHRELGKAEEAnsKLQRDLKEALAQREDMEERITTLE 309
Cdd:pfam05010 19 EKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEK-QKQKELEHAEIQ--KVLEEKDQALADLNSVEKSFSDLF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 310 KRYLSaQREATSLHDANDKLENELAsKESLYRQSEEKSRQLAeWLDDAKQKLQQTlqkAETLPEIEAQLAQRVAALnKAE 389
Cdd:pfam05010 96 KRYEK-QKEVISGYKKNEESLKKCA-QDYLARIKKEEQRYQA-LKAHAEEKLDQA---NEEIAQVRSKAKAETAAL-QAS 168
|
170 180
....*....|....*....|....*
gi 161016786 390 ERHGnfEERLRQLEAQLEEKNQELQ 414
Cdd:pfam05010 169 LRKE--QMKVQSLERQLEQKTKENE 191
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
357-498 |
6.66e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 39.96 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 357 AKQKLQQTLQKAETLPEIEAQLAQRVAALNKA-EERHGNFEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSEtvd 435
Cdd:pfam02841 174 AEEVLQEFLQSKEAVEEAILQTDQALTAKEKAiEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIE--- 250
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161016786 436 KLlsESNERLQLHLKERMGAleeknslseeianmKKLQDELLLNKEQLLAEMERMQMEIDQLR 498
Cdd:pfam02841 251 KM--EAEREQLLAEQERMLE--------------HKLQEQEELLKEGFKTEAESLQKEIQDLK 297
|
|
| SAM_Neurabin-like |
cd09512 |
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ... |
1036-1075 |
6.83e-03 |
|
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like (Neural actin-binding) subfamily is a putative protein-protein interaction domain. This group currently includes the SAM domains of neurobin-I, SAMD14 and neurobin-I/SAMD14-like proteins. Most are multidomain proteins and in addition to SAM domain they contain other protein-binding domains such as PDZ and actin-binding domains. Members of this subfamily participate in signal transduction. Neurabin-I is involved in the regulation of Ca signaling intensity in alpha-adrenergic receptors; it forms a functional pair of opposing regulators with neurabin-II. Neurabins are expressed almost exclusively in neuronal cells. They are known to interact with protein phosphatase 1 and inhibit its activity; they also can bind actin filaments; however, the exact role of the SAM domain is unclear, since SAM doesn't participate in these interactions.
Pssm-ID: 188911 [Multi-domain] Cd Length: 70 Bit Score: 36.48 E-value: 6.83e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 161016786 1036 RDVMVWSNERVMGWVSGLGLKEFATNLTESGVHG-ALLALD 1075
Cdd:cd09512 2 RPVSEWSVQQVCQWLMGLGLEQYIPEFTANNIDGqQLLQLD 42
|
|
| Vps5 |
pfam09325 |
Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is ... |
262-418 |
7.33e-03 |
|
Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is the C terminal dimerization domain.
Pssm-ID: 430527 [Multi-domain] Cd Length: 236 Bit Score: 39.57 E-value: 7.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 262 QMSQLEEELgtahRELGKAEEANSKLQRDLKEALAqreDMEERITTLekrylSAQREATSLHDANDKL-ENELASKESLY 340
Cdd:pfam09325 32 YIDSLESQL----KKLYKALELLVSQRKELASATG---EFAKSLASL-----ASLELSTGLSRALSQLaEVEERIKELLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 341 RQSEEKSRQLAEWLDD-------------AKQKLQQTLQkaetlpEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLE 407
Cdd:pfam09325 100 RQALQDVLTLGETIDEylrligsvkavfnQRVKAWQSWQ------NAEQELSKKKEQLEKLLRANKSQNDKLQQAKKEVE 173
|
170
....*....|.
gi 161016786 408 EKNQELQRARQ 418
Cdd:pfam09325 174 ELERRVQQAEK 184
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
185-384 |
7.85e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 7.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 185 EEELELSNQEA-LNLRDQLSRRRSGLEEpgkdgdgqtlanglgpvgESNRRTAELEEALER--QRAEvcQLRERLAVLCR 261
Cdd:PRK12704 48 KKEAEAIKKEAlLEAKEEIHKLRNEFEK------------------ELRERRNELQKLEKRllQKEE--NLDRKLELLEK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 262 QmsqlEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLekrylsAQREATS--LHDANDKLENELAskeSL 339
Cdd:PRK12704 108 R----EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGL------TAEEAKEilLEKVEEEARHEAA---VL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 161016786 340 YRQSEEKSRQLAEwlddakqklqqtlQKAEtlpEIEAQLAQRVAA 384
Cdd:PRK12704 175 IKEIEEEAKEEAD-------------KKAK---EILAQAIQRCAA 203
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
396-490 |
8.37e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.23 E-value: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016786 396 EERLRQLEAQ---LEEKNQELqRARQREKmnDDHNKRLSETVDKLLSESNERLqlhLKERmgaleEKNSLSEEIANMKKL 472
Cdd:COG2433 412 EEEIRRLEEQverLEAEVEEL-EAELEEK--DERIERLERELSEARSEERREI---RKDR-----EISRLDREIERLERE 480
|
90
....*....|....*...
gi 161016786 473 QDELLLNKEQLLAEMERM 490
Cdd:COG2433 481 LEEERERIEELKRKLERL 498
|
|
| |
