|
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 |
2.21e-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: 2.21e-42
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32189362 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 |
2.22e-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: 139.92 E-value: 2.22e-39
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32189362 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 |
1.87e-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: 1.87e-37
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32189362 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 |
7.72e-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: 7.72e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 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 |
8.62e-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: 8.62e-26
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 32189362 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 |
1.20e-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: 84.03 E-value: 1.20e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32189362 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 |
2.13e-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: 2.13e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32189362 1045 RVMGWVSGLGLKEFATNLTESGVHGALLALDETFDYSDLALLLQIPTQNAQARQLLEKEFSN 1106
Cdd:cd09496 1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETEFNN 62
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
39-635 |
7.56e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 92.69 E-value: 7.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 39 RERLLETLREAQDGLATAQLRLRELGHEKDSLQRQLSIAlpQEFAALTKELNLcrEQLLEREEEIAELKAERNNTRLLLE 118
Cdd:COG1196 174 KEEAERKLEATEENLERLEDILGELERQLEPLERQAEKA--ERYRELKEELKE--LEAELLLLKLRELEAELEELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 119 HLEclvsRHERSLRMTVVKRQAQspggvssevevLKALKSLFEHHKALDEKVRERLRMALERVAVLEEELELSNQETLNL 198
Cdd:COG1196 250 ELE----AELEELEAELAELEAE-----------LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 199 REQLSRRRSGLEEpgkdgdgqtlanglgpggdSNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELG 278
Cdd:COG1196 315 EERLEELEEELAE-------------------LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 279 KAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAK 358
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 359 QKLQQTLQKAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQREKmnddhNKRLSETVDKLL 438
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG-----LRGLAGAVAVLI 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 439 SESnERLQLHLKERMGALEEkNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQLRGRPPSSYSRSLP--GSALEL 516
Cdd:COG1196 531 GVE-AAYEAALEAALAAALQ-NIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAvdLVASDL 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 517 RYSQAPTLPSGAHLDPYVAGSGRAGKRGRWS----GVKEEPSKDWERSAPAGSIPPPFPGELDGSDEEEAEGMFGAELLS 592
Cdd:COG1196 609 READARYYVLGDTLLGRTLVAARLEAALRRAvtlaGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERL 688
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 32189362 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 |
3.65e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 84.34 E-value: 3.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 153 LKALKSLFEHHKALDEKVRERLRMALERVAVLEEELELSNQETLNLREQLSRRRSGLEEpgKDGDGQTLANGLGpggDSN 232
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE--LEAEIEELEERLE---EAE 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 233 RRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRY 312
Cdd:TIGR02168 775 EELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 313 LSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQqtlqkaetlpEIEAQLAQRVAALNKAEERH 392
Cdd:TIGR02168 855 ESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR----------ELESKRSELRRELEELREKL 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 393 GNFEERLRQLEAQLEEKnqeLQRARQREKMNDDHNKRLSETVDKLLSESNERLQLHLKER-------MGALEEKNSLSEE 465
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNL---QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIkelgpvnLAAIEEYEELKER 1001
|
330 340
....*....|....*....|....*....
gi 32189362 466 IANMKKLQDELLLNKEQLLAEMERMQMEI 494
Cdd:TIGR02168 1002 YDFLTAQKEDLTEAKETLEEAIEEIDREA 1030
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
232-509 |
1.05e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 82.80 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 232 NRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKR 311
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 312 YLSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQtLQKAETLPEIEAQLAQRvaALNKAEER 391
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE-LRAELTLLNEEAANLRE--RLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 392 HGNFEERLRQLEAQLEEKNQELQR-ARQREKMNDDHNKRLSET--VDKLLSESNERLQLHLKERMGALEEKNSLSEEIAN 468
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESlAAEIEELEELIEELESELeaLLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 32189362 469 MKKLQDELLLNKEQLLAEMERMQMEIDQLRGRPPSSYSRSL 509
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTL 953
|
|
| SAM_kazrin_repeat1 |
cd09564 |
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ... |
838-900 |
1.14e-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: 1.14e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32189362 838 WDGPTVVSWLELWVGMPAwYVAACRANVKSGAIMANLSDTEIQREIGISNPLHRLKLRLAIQE 900
Cdd:cd09564 4 WKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
|
|
| SAM_kazrin_repeat2 |
cd09567 |
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ... |
951-1015 |
1.18e-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: 72.44 E-value: 1.18e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32189362 951 DMNHEWVGNDWLPSLGLPQYRSYFMESLVDARMLDHLNKKELRGQLKMVDSFHRVSLHYGIMCLK 1015
Cdd:cd09567 1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
233-498 |
1.36e-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: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 233 RRTAELEEALERQRAEVCQLRERLAVLcrQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRY 312
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRELELALLVL--RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 313 LSAQREATSLHDANDKLENEL----ASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKA 388
Cdd:TIGR02168 284 EELQKELYALANEISRLEQQKqilrERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 389 EERHGNFEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVdKLLSESNERLQLHLKERMGALEE--KNSLSEEI 466
Cdd:TIGR02168 364 EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL-ERLEDRRERLQQEIEELLKKLEEaeLKELQAEL 442
|
250 260 270
....*....|....*....|....*....|..
gi 32189362 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 |
7.67e-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: 7.67e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32189362 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 |
8.52e-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: 8.52e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32189362 1037 DVMVWSNERVMGWVSGLGLKEFATNLTESGVHGALLALDETFDYSDLALLLQIPTQNAQARQLLEKEFSNLI 1108
Cdd:cd09569 1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
230-497 |
8.94e-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: 76.26 E-value: 8.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 230 DSNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDL---KEALAQREDM--EER 304
Cdd:TIGR02169 713 DASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLhklEEALNDLEARlsHSR 792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 305 ITTLEKRyLSAQREATS-----LHDANDKLENELASKESLYRQSEEKSRQLAEWlDDAKQKLQQTLQKAET-LPEIEAQL 378
Cdd:TIGR02169 793 IPEIQAE-LSKLEEEVSriearLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL-KEQIKSIEKEIENLNGkKEELEEEL 870
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 379 AQRVAALNKAEERHGNFEERLRQLEAQL---EEKNQELQRARQREKMND-----------DHNKRLSETVDKLLSESNER 444
Cdd:TIGR02169 871 EELEAALRDLESRLGDLKKERDELEAQLrelERKIEELEAQIEKKRKRLselkaklealeEELSEIEDPKGEDEEIPEEE 950
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32189362 445 LQL--------HLKERMGALEEKNSLS-EEIANMKKLQDELLLNKEQLLAEMERMQMEIDQL 497
Cdd:TIGR02169 951 LSLedvqaelqRVEEEIRALEPVNMLAiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
172-497 |
1.54e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.48 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 172 ERLRMALERVAVLEEELElSNQETLNLREQLSRRRSGLEEPGKDGDGQTLANglgpggdsnrRTAELEEALERQRAEVCQ 251
Cdd:TIGR02168 182 ERTRENLDRLEDILNELE-RQLKSLERQAEKAERYKELKAELRELELALLVL----------RLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 252 LRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERIttlekRYLSAQREatSLHDANDKLEN 331
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK-----QILRERLA--NLERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 332 ELASKESlyrQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQ 411
Cdd:TIGR02168 324 QLEELES---KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 412 ELQRARQREKMNDDHNKRLSETVDKLLSESNE----RLQLHLKERMGALEEKNS-LSEEIANMKKLQDELLLNKEQL--- 483
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLQQEIEELLKKLEEaelkELQAELEELEEELEELQEeLERLEEALEELREELEEAEQALdaa 480
|
330 340
....*....|....*....|....
gi 32189362 484 ----------LAEMERMQMEIDQL 497
Cdd:TIGR02168 481 erelaqlqarLDSLERLQENLEGF 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
39-422 |
2.48e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.09 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 39 RERLLET---LREAQDGLATAQLRLRELGHEKDSLQRQLSIAlpQEFAALTKELNlcREQLLEREEEIAELKAERNNTRL 115
Cdd:TIGR02168 171 KERRKETerkLERTRENLDRLEDILNELERQLKSLERQAEKA--ERYKELKAELR--ELELALLVLRLEELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 116 LLEHLECLVSRHERSLRMTvvkrqaqspggvSSEVEVLKALKSlfEHHKALDEkVRERLRMALERVAVLEEELELSNQET 195
Cdd:TIGR02168 247 ELKEAEEELEELTAELQEL------------EEKLEELRLEVS--ELEEEIEE-LQKELYALANEISRLEQQKQILRERL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 196 LNLREQLSRRrsgleepgkdgdgqtlanglgpggdsNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHR 275
Cdd:TIGR02168 312 ANLERQLEEL--------------------------EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 276 ELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLhdandklenelasKESLYRQSEEKSRQLAEWLD 355
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL-------------EDRRERLQQEIEELLKKLEE 432
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32189362 356 DAKQKLQqtlqkaETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQREKM 422
Cdd:TIGR02168 433 AELKELQ------AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
235-500 |
1.68e-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: 72.41 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 235 TAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANsKLQRDLKEA-----LAQREDMEERITTLE 309
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQ-ALLKEKREYegyelLKEKEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 310 KRYLSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEwlddakqklQQTLQKAETLPEIEAQLAQRVAALNKAE 389
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE---------EEQLRVKEKIGELEAEIASLERSIAEKE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 390 ERHGNFEERLRQLEAQLEEKNQEL--------QRARQREKMNDDHNKRLSETVDKL--LSESNERLQLHLKERMGALEEK 459
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIeelereieEERKRRDKLTEEYAELKEELEDLRaeLEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 32189362 460 NSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQLRGR 500
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
237-419 |
3.39e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.10 E-value: 3.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 237 ELEEALERQRA--EVCQLRERLAVLCRQMSQLEEELGT-----AHRELGKAEEANSKLQRDLKEALAQREDMEERITTLE 309
Cdd:COG4913 243 ALEDAREQIELlePIRELAERYAAARERLAELEYLRAAlrlwfAQRRLELLEAELEELRAELARLEAELERLEARLDALR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 310 KRYLSAQRE-ATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQK-AETLPEIEAQLAQRVAALNK 387
Cdd:COG4913 323 EELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEfAALRAEAAALLEALEEELEA 402
|
170 180 190
....*....|....*....|....*....|..
gi 32189362 388 AEERHGNFEERLRQLEAQLEEKNQELQRARQR 419
Cdd:COG4913 403 LEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
951-1015 |
9.33e-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: 61.13 E-value: 9.33e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32189362 951 DMNHEWVGNDWLPSLGLPQYRSYFMESLVDARMLDHLNKKELRgQLKMVDSFHRVSLHYGIMCLK 1015
Cdd:pfam00536 1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
27-500 |
9.74e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 9.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 27 ELERLMVTMLTERERLLETLREAQDGLATAQLRLRELGHEKDSLQRQLSIALPQEFAALTKELNLCREQLLEREEEIAEL 106
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 107 KAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpggvssevEVLKALKSLFEHHKALDEKVRERLRmALERVAVLEE 186
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEE--------ALAELEEEEEEEEEALEEAAEEEAE-LEEEEEALLE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 187 ELELSNQETLNLREQLSRRRSGLEEPGKDGDGQTLANGLGPGGDSNRRTAELEEALERQRAEVCQLRERLAVLCRQMsqL 266
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAL--E 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 267 EEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELASKESLYRQSEEK 346
Cdd:COG1196 542 AALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDT 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 347 SRQLAEWLDDAKQKLQQTLQKAETLpeIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQREKMNDDH 426
Cdd:COG1196 622 LLGRTLVAARLEAALRRAVTLAGRL--REVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEAL 699
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32189362 427 NKRLSETVDKLLSESNERLQLHLKERM--GALEEKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQLRGR 500
Cdd:COG1196 700 LAEEEEERELAEAEEERLEEELEEEALeeQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| 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 |
1.12e-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: 1.12e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32189362 835 FAAWDGPTVVSWL-ELWVGMpawYVAACRANVKSGAIMANLSDTEIQREIGISNPLHRLKLRLAIQ 899
Cdd:cd09563 1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
237-498 |
1.90e-11 |
|
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: 68.51 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 237 ELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQredmeerITTLEKRYLSAQ 316
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNE-------IEKLKKENQSYK 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 317 REATSLHDANDKLENELASKESLYRQSEEKSRQLA---EWLDDAKQKL-QQTLQKAETLPEIEAQLAQRVAALNKAEERH 392
Cdd:TIGR04523 384 QEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQqekELLEKEIERLkETIIKNNSEIKDLTNQDSVKELIIKNLDNTR 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 393 GNFEERLRQLEAQ-------LEEKNQELQRARQREKMNDDHNKRLSETVDKLLSESNErlqlhLKERMGALE-EKNSLSE 464
Cdd:TIGR04523 464 ESLETQLKVLSRSinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS-----LKEKIEKLEsEKKEKES 538
|
250 260 270
....*....|....*....|....*....|....*.
gi 32189362 465 EIANMKK--LQDELLLNKEQLLAEMERMQMEIDQLR 498
Cdd:TIGR04523 539 KISDLEDelNKDDFELKKENLEKEIDEKNKEIEELK 574
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
234-497 |
4.51e-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: 4.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 234 RTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYL 313
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 314 SAQREATSLHDANDKLENELASKeslyrqsEEKSRQLAEWLDDAKQKL--QQTLQKAETLPEIEAQLAQRVAALNKAEER 391
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEEL-------EEDLHKLEEALNDLEARLshSRIPEIQAELSKLEEEVSRIEARLREIEQK 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 392 hgnfEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKLLSESNERLQLHLKERMGALEEKNSLSEEIANMKK 471
Cdd:TIGR02169 821 ----LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA 896
|
250 260
....*....|....*....|....*.
gi 32189362 472 LQDELLLNKEQLLAEMERMQMEIDQL 497
Cdd:TIGR02169 897 QLRELERKIEELEAQIEKKRKRLSEL 922
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
65-498 |
7.73e-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: 66.68 E-value: 7.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 65 HEKDSLQ----RQLSIALPQEFAALTKELNLCREQLLEREEEIAELKAE-RNNTRLLLEH----LECLVSRHERSL---- 131
Cdd:pfam15921 205 YEHDSMStmhfRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSEsQNKIELLLQQhqdrIEQLISEHEVEItglt 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 132 -RMTVVKRQAQSpggVSSEVEV------------LKALKSLFEHHKALDEKVRERLRMALERVAVLEEELELSN------ 192
Cdd:pfam15921 285 eKASSARSQANS---IQSQLEIiqeqarnqnsmyMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANseltea 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 193 --------QETLNLREQLSRRRSGLEEPGKD----------------GDGQTLANGLGPGGDSNRRTAELEEAL------ 242
Cdd:pfam15921 362 rterdqfsQESGNLDDQLQKLLADLHKREKElslekeqnkrlwdrdtGNSITIDHLRRELDDRNMEVQRLEALLkamkse 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 243 -----ERQRAEVCQLRERLAVLCRQMSQLE----------EELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITT 307
Cdd:pfam15921 442 cqgqmERQMAAIQGKNESLEKVSSLTAQLEstkemlrkvvEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITK 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 308 LEKRYLSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNK 387
Cdd:pfam15921 522 LRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEIND 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 388 AEERHGNF-------EERLRQLEAQLEEknQELQRArqreKMNDDHNKRLSETVDKllseSNERLQLhLKERMGALEEKN 460
Cdd:pfam15921 602 RRLELQEFkilkdkkDAKIRELEARVSD--LELEKV----KLVNAGSERLRAVKDI----KQERDQL-LNEVKTSRNELN 670
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 32189362 461 SLSEEIA----NMKKLQDELLLNKEQLLAEMERMQMEIDQLR 498
Cdd:pfam15921 671 SLSEDYEvlkrNFRNKSEEMETTTNKLKMQLKSAQSELEQTR 712
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
153-497 |
8.82e-11 |
|
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: 8.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 153 LKALKSLFEHHKALDEKVRErlrmaLER-VAVLEEELELSNQETLNLREQLSRRRSGLEepgkdgdgQTLanglgpggDS 231
Cdd:TIGR04523 203 LSNLKKKIQKNKSLESQISE-----LKKqNNQLKDNIEKKQQEINEKTTEISNTQTQLN--------QLK--------DE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 232 NRRTaelEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRElgKAEEANSKLQRDLKEALAQREDMEERITTLEKR 311
Cdd:TIGR04523 262 QNKI---KKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ--KEQDWNKELKSELKNQEKKLEEIQNQISQNNKI 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 312 ylsaqreATSLHDANDKLENELASKESlyrQSEEKSRQLAEwlddaKQKLQQTLQK--AETLPEIEaQLAQRVAALN--- 386
Cdd:TIGR04523 337 -------ISQLNEQISQLKKELTNSES---ENSEKQRELEE-----KQNEIEKLKKenQSYKQEIK-NLESQINDLEski 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 387 -KAEERHGNFEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSE--TVDKLLSESNERLQLHLKERMGALE------ 457
Cdd:TIGR04523 401 qNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNqdSVKELIIKNLDNTRESLETQLKVLSrsinki 480
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32189362 458 -----------------------EKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQL 497
Cdd:TIGR04523 481 kqnleqkqkelkskekelkklneEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
38-419 |
9.50e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.94 E-value: 9.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 38 ERERLLETLREAQDGLATAQLRLRELGHEKDSLQRQLSIA-LPQEFAALTKELNLCREQLLEREEEIAELKAERNNTRLL 116
Cdd:COG4717 89 EYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLpLYQELEALEAELAELPERLEELEERLEELRELEEELEEL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 117 LEHLEclvsRHERSLRMTVVKRQAQSPGGVSSEVEVLKALKSLFEHHKALDEKVRERLRMALERVAVLEEELElsnqeTL 196
Cdd:COG4717 169 EAELA----ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE-----AA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 197 NLREQLSRRRSGLEEPGkdgdgqTLANGLGPGGDSNRRTAELEEAL--------------ERQRAEVCQLRERLAVLCRQ 262
Cdd:COG4717 240 ALEERLKEARLLLLIAA------ALLALLGLGGSLLSLILTIAGVLflvlgllallflllAREKASLGKEAEELQALPAL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 263 MSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATS---LHDANDKLENELASKESL 339
Cdd:COG4717 314 EELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIaalLAEAGVEDEEELRAALEQ 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 340 YRQSEEKSRQLAEWLD--DAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEERH-------GNFEERLRQLEAQ--LEE 408
Cdd:COG4717 394 AEEYQELKEELEELEEqlEELLGELEELLEALDEEELEEELEELEEELEELEEELeelreelAELEAELEQLEEDgeLAE 473
|
410
....*....|.
gi 32189362 409 KNQELQRARQR 419
Cdd:COG4717 474 LLQELEELKAE 484
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
26-387 |
1.68e-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: 65.86 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 26 GELERLMVTMLTERERLLETLREAQDGLATAQLRLRELGHEKDSLQRQLSiALPQEFAALTKELNLCREQllereeeIAE 105
Cdd:TIGR02169 684 EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE-KLKERLEELEEDLSSLEQE-------IEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 106 LKAE--RNNTRL-----LLEHLECLVSRHERSLRMTVVKrqaqspggvssevEVLKALKSLFEHHKALDEKVRErLRMAL 178
Cdd:TIGR02169 756 VKSElkELEARIeeleeDLHKLEEALNDLEARLSHSRIP-------------EIQAELSKLEEEVSRIEARLRE-IEQKL 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 179 ERVAVLEEELELSNQETLNLREQLSRRRSGLEepgkdgdgQTLANGlgpggdsNRRTAELEEALERQRAEVCQLRERLAV 258
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE--------KEIENL-------NGKKEELEEELEELEAALRDLESRLGD 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 259 LCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHDAND------KLENE 332
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDvqaelqRVEEE 966
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 32189362 333 LASKESLYRQSEEKSRQLAEWLDDAKQKLqqtlqkaETLPEIEAQLAQRVAALNK 387
Cdd:TIGR02169 967 IRALEPVNMLAIQEYEEVLKRLDELKEKR-------AKLEEERKAILERIEEYEK 1014
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
42-422 |
2.57e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.79 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 42 LLETLREAQDGLATAQLRLRELGHEK-DSLQRQLSIA--LPQEFAALTKELNLCREQLLEREEEIAELKAERNNTRLLLE 118
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKElKELEEELKEAeeKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 119 HLECLVSRHE------------RSLRMTVVKRQAQSPGGVSSEVEVLKALKSLFEHHKALDEKVRERLRMALERVAVLEE 186
Cdd:COG4717 127 LLPLYQELEAleaelaelperlEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 187 ELELSNQETLNLREQLSRRRSGLEEPGKDGDGQTLAN-------------------GLGPGGDSNRRT------------ 235
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEErlkearlllliaaallallGLGGSLLSLILTiagvlflvlgll 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 236 AELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSA 315
Cdd:COG4717 287 ALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 316 QREATS---LHDANDKLENELASKESLYRQSEEKSRQLAEWLD--DAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEE 390
Cdd:COG4717 367 ELEQEIaalLAEAGVEDEEELRAALEQAEEYQELKEELEELEEqlEELLGELEELLEALDEEELEEELEELEEELEELEE 446
|
410 420 430
....*....|....*....|....*....|....
gi 32189362 391 RHGNFEERLRQLEAQLE--EKNQELQRARQREKM 422
Cdd:COG4717 447 ELEELREELAELEAELEqlEEDGELAELLQELEE 480
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
46-493 |
3.25e-10 |
|
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: 64.86 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 46 LREAQDGLATAQLRLRELGHEKDSLQRQLSiALPQEFAALTKELNLcreQLLEREEEIAELKAERNNTRLLL-------- 117
Cdd:pfam12128 246 LQQEFNTLESAELRLSHLHFGYKSDETLIA-SRQEERQETSAELNQ---LLRTLDDQWKEKRDELNGELSAAdaavakdr 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 118 EHLECLVSRHERSLRMTVVKR---QAQSPGgVSSEVEVL-KALKSLFEHHKALDEKVRERLRMALERvavLEEELELSNQ 193
Cdd:pfam12128 322 SELEALEDQHGAFLDADIETAaadQEQLPS-WQSELENLeERLKALTGKHQDVTAKYNRRRSKIKEQ---NNRDIAGIKD 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 194 ETLNLREQLSRRRSGLEepgkdGDGQTLANGLGPGGDSNRRTAELEEALERQRAEVCQLRERLAV----LCRQMSQLEEE 269
Cdd:pfam12128 398 KLAKIREARDRQLAVAE-----DDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATatpeLLLQLENFDER 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 270 LGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHD----ANDKLENELASKESLYRQSEE 345
Cdd:pfam12128 473 IERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELqlfpQAGTLLHFLRKEAPDWEQSIG 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 346 K--SRQ------LAEWLDDAKQKLQQTL-------------QKAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEA 404
Cdd:pfam12128 553 KviSPEllhrtdLDPEVWDGSVGGELNLygvkldlkridvpEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANG 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 405 QLEEKNQELQRARQREKMNDDHNKRLsetvdkllseSNERLQLHLKERMGALEEKNSLSEEIANMKKLQDELLLNKEQLL 484
Cdd:pfam12128 633 ELEKASREETFARTALKNARLDLRRL----------FDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWL 702
|
....*....
gi 32189362 485 AEMERMQME 493
Cdd:pfam12128 703 EEQKEQKRE 711
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
22-498 |
3.25e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.68 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 22 DEAGGELERLMvtmlTERERLLETLREAQDGLATAQLRLRE---LGHEKDSLQRQLSiALPQEFAALTKELNLCREQLLE 98
Cdd:PRK02224 216 AELDEEIERYE----EQREQARETRDEADEVLEEHEERREEletLEAEIEDLRETIA-ETEREREELAEEVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 99 REEEIAELKAERNNTRL----LLEHLECLVSRHERSLRMTVVKRQAQSpggvssevEVLKALKSLFEHHKALDEKVRErl 174
Cdd:PRK02224 291 LEEERDDLLAEAGLDDAdaeaVEARREELEDRDEELRDRLEECRVAAQ--------AHNEEAESLREDADDLEERAEE-- 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 175 rmALERVAVLEEELElsnqetlNLREQLSRRRSGLEEpgKDGDGQTLANGLGpggDSNRRTAELEEALERQRAEVCQLRE 254
Cdd:PRK02224 361 --LREEAAELESELE-------EAREAVEDRREEIEE--LEEEIEELRERFG---DAPVDLGNAEDFLEELREERDELRE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 255 RLAVLCRQMSQLEEELGTAHR---------------------ELGKAEEANSKLQRDLKEALAQREDMEERITTLEKrYL 313
Cdd:PRK02224 427 REAELEATLRTARERVEEAEAlleagkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAED-LV 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 314 SAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEERHG 393
Cdd:PRK02224 506 EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELK 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 394 NFEERLRQLEAQL---EEKNQELQRARQREK----MNDDHNKRLS---ETVDKLLSESNE-RLQlhlkermGALEEKNSL 462
Cdd:PRK02224 586 ERIESLERIRTLLaaiADAEDEIERLREKREalaeLNDERRERLAekrERKRELEAEFDEaRIE-------EAREDKERA 658
|
490 500 510
....*....|....*....|....*....|....*.
gi 32189362 463 SEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQLR 498
Cdd:PRK02224 659 EEYLEQVEEKLDELREERDDLQAEIGAVENELEELE 694
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
230-418 |
4.16e-10 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 63.31 E-value: 4.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 230 DSNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEalaQREDMEERITTLE 309
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE---RREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 310 KR-----YLSAQREATSLHDANDKLE--NELASKE----SLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAET-LPEIEAQ 377
Cdd:COG3883 97 RSggsvsYLDVLLGSESFSDFLDRLSalSKIADADadllEELKADKAELEAKKAELEAKLAELEALKAELEAaKAELEAQ 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 32189362 378 LAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQ 418
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
22-499 |
5.93e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 5.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 22 DEAGGELERLMVTML---TERERLLETLREAQDGLATAQLRLRELGHEKDSLQRQL------SIALPQEFAALTKELNLC 92
Cdd:COG1196 249 EELEAELEELEAELAeleAELEELRLELEELELELEEAQAEEYELLAELARLEQDIarleerRRELEERLEELEEELAEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 93 REQLLEREEEIAELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPGGVSSEVEVLKALKSLFEHHKALDEKVRE 172
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 173 RLRMALERVAVLEEELELSNQETLNLREQLSRRRSGLEEPGKDGDGQTLANGLgpggdSNRRTAELEEALERQRAEVCQL 252
Cdd:COG1196 409 EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL-----LELLAELLEEAALLEAALAELL 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 253 RERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQ------REATSLHDAN 326
Cdd:COG1196 484 EELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAlqnivvEDDEVAAAAI 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 327 DKLENELASKESLYRQSEEKSRQLAEWL----------DDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEERHGNFE 396
Cdd:COG1196 564 EYLKAAKAGRATFLPLDKIRARAALAAAlargaigaavDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLA 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 397 ERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKLLSESNERLQLHLKERMGALEEKNSLSEEIANMKKLQDEL 476
Cdd:COG1196 644 GRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEE 723
|
490 500
....*....|....*....|...
gi 32189362 477 LLNKEQLLAEMERMQMEIDQLRG 499
Cdd:COG1196 724 EALEEQLEAEREELLEELLEEEE 746
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
144-494 |
8.19e-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: 63.22 E-value: 8.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 144 GGVSSEVEVLKALKSLFEHHKALDEKVRERL--RMALERVAVLEEELelsnqetlnLREqLSRRRSgLEEPGKDGDGQtL 221
Cdd:pfam17380 262 GQTMTENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEK---------ARE-VERRRK-LEEAEKARQAE-M 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 222 ANGLGPGGDSNRRTAELEEALER-----QRAEVCQLR-ERLAVLCRQMSQLEeelgtahRELGKAEEANSKLQRDLKEAL 295
Cdd:pfam17380 330 DRQAAIYAEQERMAMERERELERirqeeRKRELERIRqEEIAMEISRMRELE-------RLQMERQQKNERVRQELEAAR 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 296 AQREDMEERittlEKRYLSAQREATSLhdandKLENELASKESLYRQSEEKSRQLaewlDDAKQKLQQTLQKAETLPEIE 375
Cdd:pfam17380 403 KVKILEEER----QRKIQQQKVEMEQI-----RAEQEEARQREVRRLEEERAREM----ERVRLEEQERQQQVERLRQQE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 376 AQLAQRVAALNKAEERHGNFEERLRQ-LEAQLEEKNQE-LQRARQR---EKMNDDHNKRLSETVDKLLSESNERLQLHLK 450
Cdd:pfam17380 470 EERKRKKLELEKEKRDRKRAEEQRRKiLEKELEERKQAmIEEERKRkllEKEMEERQKAIYEEERRREAEEERRKQQEME 549
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 32189362 451 ERMGALEEKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEI 494
Cdd:pfam17380 550 ERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEA 593
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
289-517 |
9.37e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.40 E-value: 9.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 289 RDLKEALAQREDMEERITTLE------KRYLSAQREATSLHDANDKLEnelaskeslYRQSEEKSRQLAEWLDDAKQKLQ 362
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEpirelaERYAAARERLAELEYLRAALR---------LWFAQRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 363 QTLQKAETLPEIEAQLAQRVAALNKAEERHGNfeERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDklLSESN 442
Cdd:COG4913 306 RLEAELERLEARLDALREELDELEAQIRGNGG--DRLEQLEREIERLERELEERERRRARLEALLAALGLPLP--ASAEE 381
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32189362 443 -ERLQLHLKERmgaleeKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQLRGRPpssysRSLPGSALELR 517
Cdd:COG4913 382 fAALRAEAAAL------LEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK-----SNIPARLLALR 446
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
38-439 |
1.14e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.78 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 38 ERERLLETLREAQDGLATAQLRLRELGHEKDSLQRQLSIALpqEFAALTKELnlcreqlleREEEIAELKAERNNTRLLL 117
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE--RYQALLKEK---------REYEGYELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 118 EHLECLVSRHERSLRmtvvKRQAQSPGGVSSEVEVLKALKSLFEHHKALDEKvrerlrmalERVAVLEEELELSNQetln 197
Cdd:TIGR02169 240 EAIERQLASLEEELE----KLTEEISELEKRLEEIEQLLEELNKKIKDLGEE---------EQLRVKEKIGELEAE---- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 198 lREQLSRRRSGLEEPGKDGDGQtLANGLGPGGDSNRRTAELEEALERQRAEVCQLRERLAvlcrqmsQLEEELGTAHREL 277
Cdd:TIGR02169 303 -IASLERSIAEKERELEDAEER-LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYA-------ELKEELEDLRAEL 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 278 GKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDA 357
Cdd:TIGR02169 374 EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 358 KQKLQQTlqkAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKL 437
Cdd:TIGR02169 454 EWKLEQL---AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQL 530
|
..
gi 32189362 438 LS 439
Cdd:TIGR02169 531 GS 532
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
27-494 |
1.22e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.77 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 27 ELERLMVTMLTERERLLETLREAQDGLATAQLRLRELgheKDSLQRQLSI-ALPQEFAALTKELNLCREQLLEREEEIAE 105
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL---EEKVKELKELkEKAEEYIKLSEFYEEYLDELREIEKRLSR 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 106 LKAERNNTRLLLEHLECLVSR-HERSLRMTVVKRQAQSPGGVSSEVEVLKALKSLFEHHKALD-----EKVRERLRMALE 179
Cdd:PRK03918 319 LEEEINGIEERIKELEEKEERlEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLtgltpEKLEKELEELEK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 180 RVAVLEEELELSNQETLNLREQLSRRRSGLEEPGK--------------DGDGQTLANGLGPGGDSNRRTAELEEALERQ 245
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelteEHRKELLEEYTAELKRIEKELKEIEEKERKL 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 246 RAEVCQLRE---------RLAVLCRQMSQLEEELGT--------AHRELGKAEEANSKL---QRDLKEALAQREDMEERI 305
Cdd:PRK03918 479 RKELRELEKvlkkeseliKLKELAEQLKELEEKLKKynleelekKAEEYEKLKEKLIKLkgeIKSLKKELEKLEELKKKL 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 306 TTLEKRYLSAQREATSLHD--------ANDKLENELASKESLYRQSEEksrqlaewLDDAKQKLQQTLQK----AETLPE 373
Cdd:PRK03918 559 AELEKKLDELEEELAELLKeleelgfeSVEELEERLKELEPFYNEYLE--------LKDAEKELEREEKElkklEEELDK 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 374 IEAQLAQRVAAL----NKAEERHGNF-EERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKLLSEsnerlqlh 448
Cdd:PRK03918 631 AFEELAETEKRLeelrKELEELEKKYsEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE-------- 702
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 32189362 449 LKERMGALEEKNSLSEEIANMKKLQDELL----LNKEQLLAEMERMQMEI 494
Cdd:PRK03918 703 LEEREKAKKELEKLEKALERVEELREKVKkykaLLKERALSKVGEIASEI 752
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
234-476 |
1.28e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.77 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 234 RTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSK---LQRDLKEALAQREDMEERITTLEK 310
Cdd:PRK03918 187 RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEieeLEKELESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 311 RYLSAQREATSLHDANDKLEnELASKESLYRQseeksrqLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEE 390
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELK-ELKEKAEEYIK-------LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 391 RHGNFEERLRQLE---AQLEEKNQELQRARQREKMNDDHNKRLS----ETVDKLLSESNERLQLHLKERMGALEEKNSLS 463
Cdd:PRK03918 339 RLEELKKKLKELEkrlEELEERHELYEEAKAKKEELERLKKRLTgltpEKLEKELEELEKAKEEIEEEISKITARIGELK 418
|
250
....*....|...
gi 32189362 464 EEIANMKKLQDEL 476
Cdd:PRK03918 419 KEIKELKKAIEEL 431
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
171-419 |
1.42e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.63 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 171 RERLRMALERVAVLEEELELSNQEtlnlREQLSRRRSGLEEpgkdgdGQTLANGLGPGGDSNRRTAELEEALERQRAEVC 250
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEER----LEALEAELDALQE------RREALQRLAEYSWDEIDVASAEREIAELEAELE 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 251 QLRE---RLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREatslhDAND 327
Cdd:COG4913 679 RLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA-----LLEE 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 328 KLENELAskeslyrqsEEKSRQLAEWLDDAKQKLQQTLQKAETlpEIEAQLAQ-------RVAALNKAEERHGNFEERLR 400
Cdd:COG4913 754 RFAAALG---------DAVERELRENLEERIDALRARLNRAEE--ELERAMRAfnrewpaETADLDADLESLPEYLALLD 822
|
250 260
....*....|....*....|
gi 32189362 401 QLEAQ-LEEKNQELQRARQR 419
Cdd:COG4913 823 RLEEDgLPEYEERFKELLNE 842
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
32-517 |
1.49e-09 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 62.68 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 32 MVTMLTERERLLE-TLREAQDGLATAQL------RLRELGHEKDSLQRQLSIALPQEFAALTKElnlcreqllereEEIA 104
Cdd:TIGR00618 213 MPDTYHERKQVLEkELKHLREALQQTQQshayltQKREAQEEQLKKQQLLKQLRARIEELRAQE------------AVLE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 105 ELKAERNNTRllleHLECLVsrhERSLRMTVVKRQAQSpggVSSEVEVLKA-LKSLFEHHKAL--DEKVRERLRMALERV 181
Cdd:TIGR00618 281 ETQERINRAR----KAAPLA---AHIKAVTQIEQQAQR---IHTELQSKMRsRAKLLMKRAAHvkQQSSIEEQRRLLQTL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 182 AVLEEELELSNQETLNLREQLSRRRsgleepgkdgdgqtlanglgpggdsnrrtaELEEALERQRAEVCQLRERLAVLCR 261
Cdd:TIGR00618 351 HSQEIHIRDAHEVATSIREISCQQH------------------------------TLTQHIHTLQQQKTTLTQKLQSLCK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 262 QMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLS---AQREATSLHDANDKLENELASKES 338
Cdd:TIGR00618 401 ELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCeklEKIHLQESAQSLKEREQQLQTKEQ 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 339 LYRQSEEKSRQLAEWLDDaKQKLQQTLQKAETLPEIEAQLA--------------QRVAALNKAEE--RHGNFEER--LR 400
Cdd:TIGR00618 481 IHLQETRKKAVVLARLLE-LQEEPCPLCGSCIHPNPARQDIdnpgpltrrmqrgeQTYAQLETSEEdvYHQLTSERkqRA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 401 QLEAQLEEKNQELQR-ARQREKMNDDHNKRLSETVDkLLSESNERLQLHLKERMGALEEKNSLSEEIANMKKLQDELLLN 479
Cdd:TIGR00618 560 SLKEQMQEIQQSFSIlTQCDNRSKEDIPNLQNITVR-LQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCS 638
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 32189362 480 KEQ--LLAEMERMQMEIDQLRGRPPSSYSRSLPGSALELR 517
Cdd:TIGR00618 639 QELalKLTALHALQLTLTQERVREHALSIRVLPKELLASR 678
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
81-500 |
1.53e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.36 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 81 EFAALTKELNLCREQLLEREEEIAELKAERNNTRLLLEHLECLVSRHERSL-RMTVVKrqaqspggvsSEVEVLKALKSL 159
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERReELETLE----------AEIEDLRETIAE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 160 FEHHK-ALDEKVRERLRMALERVAVLEE-----ELELSNQETLNLR-EQLSRRRSGLEEPGKD-----GDGQTLANGLGP 227
Cdd:PRK02224 270 TEREReELAEEVRDLRERLEELEEERDDllaeaGLDDADAEAVEARrEELEDRDEELRDRLEEcrvaaQAHNEEAESLRE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 228 GGDSNR--------RTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQRE 299
Cdd:PRK02224 350 DADDLEeraeelreEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 300 DMEERITTLEKRYlsaqREATSLHDANDKLENELASKESLY----RQSEEKSRQLAEWLDDAK---QKLQQTLQKAETLP 372
Cdd:PRK02224 430 ELEATLRTARERV----EEAEALLEAGKCPECGQPVEGSPHvetiEEDRERVEELEAELEDLEeevEEVEERLERAEDLV 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 373 EIEAQlaqrvaaLNKAEERHGNFEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKLLSESNERLqlhlkER 452
Cdd:PRK02224 506 EAEDR-------IERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAR-----EE 573
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 32189362 453 MGALEEKNS-LSEEIANMKKLQDelllnkeqLLAEMERMQMEIDQLRGR 500
Cdd:PRK02224 574 VAELNSKLAeLKERIESLERIRT--------LLAAIADAEDEIERLREK 614
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
163-520 |
1.76e-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: 62.30 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 163 HKALDE-----KVRERLRMALERVAvlEEELELSNQETLNLREQLSRRRSGLEEPGKDGDGQTLANglgpggdsnRRTAE 237
Cdd:pfam02463 155 RLEIEEeaagsRLKRKKKEALKKLI--EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEK---------LELEE 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 238 LEEALERQRAEvcqLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQR 317
Cdd:pfam02463 224 EYLLYLDYLKL---NEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKS 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 318 EATSL-HDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEERHGNFE 396
Cdd:pfam02463 301 ELLKLeRRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 397 ERLRQLEAQLEEKNQEL----------QRARQREKMNDDHNKRLSETVDKLLSESNERL---QLHLKERMGALEEKNSLS 463
Cdd:pfam02463 381 LESERLSSAAKLKEEELelkseeekeaQLLLELARQLEDLLKEEKKEELEILEEEEESIelkQGKLTEEKEELEKQELKL 460
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 32189362 464 EEIANMKKLQDELLLNKEQLLAEMERMQMEIDQLRGRPPSSYSRSLPGSALELRYSQ 520
Cdd:pfam02463 461 LKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIK 517
|
|
| 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 32189362 231 SNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEK 310
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 311 RYLSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQL--AQRVAALNKA 388
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALseAEAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 389 EERHGNFEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKLLSESNERLQLHLKERMGALEEKNSLSEEIAN 468
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260 270
....*....|....*....|....*....|
gi 32189362 469 MKKLQDELLLNKEQLLAEMERMQMEIDQLR 498
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLL 298
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
22-414 |
2.91e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.62 E-value: 2.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 22 DEAGGELERLMvtmlTER---ERLLETLREAQDglataqLRLRELGHEKDSLQRQLSiALPQEFAALTKELnlcreqlLE 98
Cdd:TIGR02169 194 DEKRQQLERLR----RERekaERYQALLKEKRE------YEGYELLKEKEALERQKE-AIERQLASLEEEL-------EK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 99 REEEIAELKAERNNTRLLLEHLECLVSRhERSLRMTVVKRQAQSpggVSSEVEVLKAlkslfehhkALDEKVRErLRMAL 178
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKD-LGEEEQLRVKEKIGE---LEAEIASLER---------SIAEKERE-LEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 179 ERVAVLEEELELSNQETLNLREQLS---RRRSGLEEpgkdgdgqtlanglgpggdsnrRTAELEEALERQRAEVCQLRER 255
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEeerKRRDKLTE----------------------EYAELKEELEDLRAELEEVDKE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 256 LAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLsaqreatslhdandKLENELAS 335
Cdd:TIGR02169 380 FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKIN--------------ELEEEKED 445
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32189362 336 KESLYRQSEEKSRQLAEWLDDAKQKLqqtLQKAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQ 414
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLSKYEQEL---YDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
36-408 |
4.18e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 36 LTERERLLETLREAQDGLATAQLRLRELGHEKDSLQRQLSIALPQEFAALTKELNLCREQLLEREEEIAELKAERNNTRL 115
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 116 LLEHLECLVSRHERSLRMtvVKRQAQSPGGVSSEVEVLKALKSLFEHHKALDEKVRERLRMALERVAVLEEELELSNQET 195
Cdd:COG1196 482 LLEELAEAAARLLLLLEA--EADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVA 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 196 LNLREQLSRRRSG------LEEPGKDGDGQTLANGLGPGGDSNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEE 269
Cdd:COG1196 560 AAAIEYLKAAKAGratflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRA 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 270 LGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELASKESLYRQSEEKSRQ 349
Cdd:COG1196 640 VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEE 719
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 32189362 350 LAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEE 408
Cdd:COG1196 720 ELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
251-425 |
4.47e-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: 4.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 251 QLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRylsaQREATSLHDANDkLE 330
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ----LGNVRNNKEYEA-LQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 331 NELASKESLYRQSEEKSRQLAEWLDDAKQKLQqtlqkaetlpEIEAQLAQRVAALNKAEERhgnFEERLRQLEAQLEEKN 410
Cdd:COG1579 96 KEIESLKRRISDLEDEILELMERIEELEEELA----------ELEAELAELEAELEEKKAE---LDEELAELEAELEELE 162
|
170
....*....|....*
gi 32189362 411 QElqRARQREKMNDD 425
Cdd:COG1579 163 AE--REELAAKIPPE 175
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
272-566 |
4.88e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.84 E-value: 4.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 272 TAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELASKEslyRQSEEKSRQLA 351
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE---AEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 352 EWLDDAkQKLQQTLQKAETLPEIE--AQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQREKMNDDHNKR 429
Cdd:COG3883 90 ERARAL-YRSGGSVSYLDVLLGSEsfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 430 LSETVDKLLSESNERLQLHLKERMGALEEKNSLSEEIAnmKKLQDELLLNKEQLLAEMERMQMEIDQLRGRPPSSYSRSL 509
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA--AAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 32189362 510 PGSALELRYSQAPTLPSGAHLDPYVAGSGRAGKRGRWSGVKEEPSKDWERSAPAGSI 566
Cdd:COG3883 247 AGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGS 303
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
164-500 |
5.40e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 5.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 164 KALDEKVRErLRMALERVAVLEEELELSNQETLNLREQLSRRRSGLEEPGKDGDGQTLANGLgpggdsnrrtAELEEALE 243
Cdd:COG4717 74 KELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEL----------EALEAELA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 244 RQRAEVCQLRERLAV---LCRQMSQLEEELGTAHRELGKAEEANS-KLQRDLKEALAQREDMEERITTLEKRYLSAQREA 319
Cdd:COG4717 143 ELPERLEELEERLEElreLEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 320 TSLHDANDKLENELASKESLYRQSEEKSRQLAE------------------------------------WLDDAKQKLQQ 363
Cdd:COG4717 223 EELEEELEQLENELEAAALEERLKEARLLLLIAaallallglggsllsliltiagvlflvlgllallflLLAREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 364 TLQKAETLPEIE----AQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQREKMnDDHNKRLSETVDKLLS 439
Cdd:COG4717 303 EAEELQALPALEeleeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL-EELEQEIAALLAEAGV 381
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32189362 440 ESNERLQLHLK---ERMGALEEKNSLSEEIANMKKLQDELL--LNKEQLLAEMERMQMEIDQLRGR 500
Cdd:COG4717 382 EDEEELRAALEqaeEYQELKEELEELEEQLEELLGELEELLeaLDEEELEEELEELEEELEELEEE 447
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
26-488 |
6.33e-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: 60.57 E-value: 6.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 26 GELERLMVTMLTERERLLETLREAQDGLATAQLRLRELGHEKDSLQRQLsialpQEFAALTKELnlcreQLLEREEEIAE 105
Cdd:pfam01576 218 TDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKI-----RELEAQISEL-----QEDLESERAAR 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 106 LKAERNNtRLLLEHLECLVSRHERSLRMTVVKRQAQSPGgvSSEVEVLK-ALKSLFEHHKALDEKVRERLRMALERvavL 184
Cdd:pfam01576 288 NKAEKQR-RDLGEELEALKTELEDTLDTTAAQQELRSKR--EQEVTELKkALEEETRSHEAQLQEMRQKHTQALEE---L 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 185 EEELELSNQETLNlreqLSRRRSGLEEPGKD--GDGQTLANGlgpGGDSNRRTAELEEALERQRAEVCQLRERLAVLCRQ 262
Cdd:pfam01576 362 TEQLEQAKRNKAN----LEKAKQALESENAElqAELRTLQQA---KQDSEHKRKKLEGQLQELQARLSESERQRAELAEK 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 263 MSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERIT--TLEKRYLSAQ-----REATSLHdanDKLENELAS 335
Cdd:pfam01576 435 LSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQeeTRQKLNLSTRlrqleDERNSLQ---EQLEEEEEA 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 336 KESLYRQSEEKSRQLAEWlddaKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQR 415
Cdd:pfam01576 512 KRNVERQLSTLQAQLSDM----KKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLV 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 416 ARQREKMNDDHNKRLSETVDKLLSESNERLQLHLKERMGALEEKN-------SLSEEIANMKKLQDELLLNKEQLLAEME 488
Cdd:pfam01576 588 DLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAReketralSLARALEEALEAKEELERTNKQLRAEME 667
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
838-901 |
6.34e-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: 6.34e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32189362 838 WDGPTVVSWLELWvGMPAwYVAACRANVKSGAIMANLSDTEIQREIGISNPLHRLKLRLAIQEM 901
Cdd:smart00454 4 WSPESVADWLESI-GLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
48-499 |
7.51e-09 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 60.37 E-value: 7.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 48 EAQDGLATAQLRLRELGHEKDSLQRQLSIALPQEFAALTKELNLCREQLLEREEEIAELKAERNNTRLLLEHLECLVSRH 127
Cdd:TIGR00618 430 KKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGS 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 128 ERSLRMTVVkrQAQSPGGVSSEVEvlkALKSLFEHHKALDEKVRERLRMALERVAVLEEELELSNQETLNLREQLSRRRS 207
Cdd:TIGR00618 510 CIHPNPARQ--DIDNPGPLTRRMQ---RGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKE 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 208 GLEEPGKDGDgqtLANGLGPGGDSNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAhrelgKAEEANSKL 287
Cdd:TIGR00618 585 DIPNLQNITV---RLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTA-----LHALQLTLT 656
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 288 QRDLKEA-LAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEW---LDDAKQKLQQ 363
Cdd:TIGR00618 657 QERVREHaLSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIenaSSSLGSDLAA 736
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 364 TLQK-AETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQ-RARQREKMNDDHNKRLSETVDKL---- 437
Cdd:TIGR00618 737 REDAlNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQfFNRLREEDTHLLKTLEAEIGQEIpsde 816
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32189362 438 --LSESNERLQLHLKERMGALEEKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQLRG 499
Cdd:TIGR00618 817 diLNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNG 880
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
228-419 |
9.23e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 9.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 228 GGDSNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELgTAHRELGKAEEAnsklQRDLKEALAQREDMEERITT 307
Cdd:COG4913 605 GFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERR-EALQRLAEYSWD----EIDVASAEREIAELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 308 LEKrylsAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIE-----AQLAQRV 382
Cdd:COG4913 680 LDA----SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLArlelrALLEERF 755
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 32189362 383 AALNKAEER---HGNFEERLRQLEAQLEEKNQELQRARQR 419
Cdd:COG4913 756 AAALGDAVErelRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
154-498 |
2.11e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 154 KALKSLFEHHKALDEKVRERLRMALERVAVLEE-----ELELSNQETLNLREQLSRR---RSGLEEPGKDGDGQTLANGL 225
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkkkadEAKKKAEEDKKKADELKKAaaaKKKADEAKKKAEEKKKADEA 1436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 226 GPGGDSNRRTAELEE-ALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQRE----- 299
Cdd:PTZ00121 1437 KKKAEEAKKADEAKKkAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKadeak 1516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 300 DMEERITTLEKRYLSAQREATSLHDANDKLENELASKESLYRQSEEKSRqlAEWLDDAKQKLQQTLQKAETLPEIEAQLA 379
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKK--AEEAKKAEEDKNMALRKAEEAKKAEEARI 1594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 380 QRVAALN------KAEERHGNFEERLRQLEAQLEE------------------KNQELQRARQREKMNDDHNKRLSETvD 435
Cdd:PTZ00121 1595 EEVMKLYeeekkmKAEEAKKAEEAKIKAEELKKAEeekkkveqlkkkeaeekkKAEELKKAEEENKIKAAEEAKKAEE-D 1673
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32189362 436 KLLSESNERLQLHLKERMGALEEKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQLR 498
Cdd:PTZ00121 1674 KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAK 1736
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
294-496 |
2.23e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 294 ALAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELASKESL--YRQSEEKSRQLAEWLDDAKQKLQQTLQKAETL 371
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLaeYSWDEIDVASAEREIAELEAELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 372 PEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQRekmnddhnkrlsetVDKLLSESNERLQLHLKE 451
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR--------------LEAAEDLARLELRALLEE 753
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 32189362 452 RMGALEEKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQ 496
Cdd:COG4913 754 RFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
177-507 |
2.33e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.82 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 177 ALERVAVLEEELELSNQETLNLREQLSRRRSGLEEPgkdgdgQTLAnglgpggdSNRRTAEleEALERQRaEVCQL---- 252
Cdd:PRK04863 374 ADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQ------QTRA--------IQYQQAV--QALERAK-QLCGLpdlt 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 253 ----RERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALA-----QREDMEERITTLEKRYLSAQREATSLH 323
Cdd:PRK04863 437 adnaEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKiagevSRSEAWDVARELLRRLREQRHLAEQLQ 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 324 dandKLENELASKEslyrQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEErhgNFEERLRQLE 403
Cdd:PRK04863 517 ----QLRMRLSELE----QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVS---EARERRMALR 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 404 AQLEEKNQELQRARQRekmnddhnkrlsETVDKLLSESNERLQLHLKErmgALEEKNSLSEEIANMKKLQDELLLNKEQL 483
Cdd:PRK04863 586 QQLEQLQARIQRLAAR------------APAWLAAQDALARLREQSGE---EFEDSQDVTEYMQQLLERERELTVERDEL 650
|
330 340
....*....|....*....|....
gi 32189362 484 LAEMERMQMEIDQLRGRPPSSYSR 507
Cdd:PRK04863 651 AARKQALDEEIERLSQPGGSEDPR 674
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
233-474 |
2.50e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 233 RRTAELEEALERQRAEVCQLRERlAVLCRQMSQLEEELGTAHRELGKAEEANSKlqrdlKEALAQREDMEERITTLEKRY 312
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEE-ARIEEVMKLYEEEKKMKAEEAKKAEEAKIK-----AEELKKAEEEKKKVEQLKKKE 1642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 313 LSAQREATSLHDANdklENELASKESLYRQSEE---KSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAE 389
Cdd:PTZ00121 1643 AEEKKKAEELKKAE---EENKIKAAEEAKKAEEdkkKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAE 1719
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 390 ERHGNFEERLRQLEAQLEEKNQELQRARQREKMNDDHNKrlsetVDKLLSESNERLQLHLKERMGALEEKNSLSEEIANM 469
Cdd:PTZ00121 1720 ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKK-----IAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRM 1794
|
....*...
gi 32189362 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 |
3.01e-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: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 248 EVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDME---ERITTLEKRYLSAQREATSLHD 324
Cdd:pfam13851 34 EIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKnlkARLKVLEKELKDLKWEHEVLEQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 325 ANDKLENElasKESLYRQSEEKsrqlaewLDDAKQK-------LQQTLQK-AETLPEIEAQLAQRVAALNKAEERHGNFE 396
Cdd:pfam13851 114 RFEKVERE---RDELYDKFEAA-------IQDVQQKtglknllLEKKLQAlGETLEKKEAQLNEVLAAANLDPDALQAVT 183
|
170
....*....|....*.
gi 32189362 397 ERLRQLeaqLEEKNQE 412
Cdd:pfam13851 184 EKLEDV---LESKNQL 196
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
261-512 |
3.28e-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: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 261 RQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELaskesly 340
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 341 rqsEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQre 420
Cdd:COG4942 100 ---EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA-- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 421 kmnddhnkRLSETVDKlLSESNERLQLHLKERMGALEEknsLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQLRGR 500
Cdd:COG4942 175 --------ELEALLAE-LEEERAALEALKAERQKLLAR---LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
250
....*....|..
gi 32189362 501 PPSSYSRSLPGS 512
Cdd:COG4942 243 TPAAGFAALKGK 254
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
161-493 |
4.15e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 4.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 161 EHHKALDEKVRERLRMAlERVAVLEEELELSNQEtlnlreqlsRRRSGLEEPGKDGDGQTLANGLGPGGDSNRRTAELEE 240
Cdd:PTZ00121 1216 EARKAEDAKKAEAVKKA-EEAKKDAEEAKKAEEE---------RNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK 1285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 241 ALERQRAEVCQLRERLavlcrqmsQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREAT 320
Cdd:PTZ00121 1286 AEEKKKADEAKKAEEK--------KKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD 1357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 321 SLHDANDKLENELASKESLYRQSEEKSRQLAEW--LDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEERHGNFEER 398
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKkkADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAK 1437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 399 LRQLEA----QLEEKNQELQRARQREKMNDDhnKRLSETVDKLLSESneRLQLHLKERMGALEEKNSLSEEIANMKKLQD 474
Cdd:PTZ00121 1438 KKAEEAkkadEAKKKAEEAKKAEEAKKKAEE--AKKADEAKKKAEEA--KKADEAKKKAEEAKKKADEAKKAAEAKKKAD 1513
|
330
....*....|....*....
gi 32189362 475 ELLLNKEQLLAEMERMQME 493
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEE 1532
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
263-492 |
4.94e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 4.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 263 MSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYlsaqreatslhdanDKLENELASKESLYRQ 342
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEEL--------------EELEEELEELEAELEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 343 SEEKSRQLaewldDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQRekM 422
Cdd:COG4717 114 LREELEKL-----EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQ--L 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 423 NDDHNKRLSETVDKLlSESNERLQLHLKERMGALEEKNSLSEEIANMKKLQdeLLLNKEQLLAEMERMQM 492
Cdd:COG4717 187 SLATEEELQDLAEEL-EELQQRLAELEEELEEAQEELEELEEELEQLENEL--EAAALEERLKEARLLLL 253
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
26-422 |
5.29e-08 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 56.61 E-value: 5.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 26 GELERLMVTMLTERERLLETLREAQDGLATAQLRLRELGHEKDSLQRQLSiALPQEFAALTKELNLCREQLLEREEEIAE 105
Cdd:pfam19220 30 SQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLS-AAEGELEELVARLAKLEAALREAEAAKEE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 106 LKAERNNTRLLLEHLEclvsrherslrmtvvKRQAQspggvssEVEVLKALKslfEHHKALdekvRERLRMALERVAVLE 185
Cdd:pfam19220 109 LRIELRDKTAQAEALE---------------RQLAA-------ETEQNRALE---EENKAL----REEAQAAEKALQRAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 186 EELeLSNQETLNLREQLSRRRSGLEEpgkdgdgQTLANGLgpggDSNRRTAELEEALERQRAEVCQLRERLAVL----CR 261
Cdd:pfam19220 160 GEL-ATARERLALLEQENRRLQALSE-------EQAAELA----ELTRRLAELETQLDATRARLRALEGQLAAEqaerER 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 262 QMSQLEEELGTAHRELG----KAEEANSKL---QRDLKEALAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELA 334
Cdd:pfam19220 228 AEAQLEEAVEAHRAERAslrmKLEALTARAaatEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 335 SKESLYRQSEEKSRQLAEWLDdakqklqqTLQKAetlpeieaqLAQRVAALNKAEERHGNFEERLRQLE-------AQLE 407
Cdd:pfam19220 308 RRTQQFQEMQRARAELEERAE--------MLTKA---------LAAKDAALERAEERIASLSDRIAELTkrfeverAALE 370
|
410
....*....|....*
gi 32189362 408 EKNQELQRARQREKM 422
Cdd:pfam19220 371 QANRRLKEELQRERA 385
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
230-444 |
5.42e-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: 56.31 E-value: 5.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 230 DSNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLE 309
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 310 KRYlSAQREATSLHDANDKLE--------NELASKESLYRQSEEKSRQLAEWLDDAKQKLQQ-----TLQKAEtLPEIEA 376
Cdd:COG4942 104 EEL-AELLRALYRLGRQPPLAlllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAAlraelEAERAE-LEALLA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32189362 377 QLAQRVAALNKAEERHgnfEERLRQLEAQLEEKNQELQRARQREkmnddhnKRLSETVDKLLSESNER 444
Cdd:COG4942 182 ELEEERAALEALKAER---QKLLARLEKELAELAAELAELQQEA-------EELEALIARLEAEAAAA 239
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
261-500 |
6.11e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 6.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 261 RQMSQLEEeLGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELASKESLY 340
Cdd:PRK03918 152 RQILGLDD-YENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 341 RQSEEKsrqlaewlddakqklqqtlqkAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQ---LEEKNQELQRAR 417
Cdd:PRK03918 231 KELEEL---------------------KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEieeLEEKVKELKELK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 418 QRE-------KMNDDHNKRLSEtVDKLLSESNERLQlHLKERMGALEEKNSLSEEIAN-MKKLQDEL--LLNKEQLLAEM 487
Cdd:PRK03918 290 EKAeeyiklsEFYEEYLDELRE-IEKRLSRLEEEIN-GIEERIKELEEKEERLEELKKkLKELEKRLeeLEERHELYEEA 367
|
250
....*....|...
gi 32189362 488 ERMQMEIDQLRGR 500
Cdd:PRK03918 368 KAKKEELERLKKR 380
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
103-498 |
6.94e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 56.98 E-value: 6.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 103 IAELKAERNNTRLLLEHLECLVSRHERSLRMtvVKRQAQSPGGVSSEV-----EVLKALK--SLFEHHKALDEKVRERLR 175
Cdd:TIGR00606 428 ADEIRDEKKGLGRTIELKKEILEKKQEELKF--VIKELQQLEGSSDRIleldqELRKAERelSKAEKNSLTETLKKEVKS 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 176 MALERVAV------LEEELELSNQETLNLR--EQLSRRRSGLEEPGKDGDGQTLANGLGPGGDSNRrTAELEEALERQRA 247
Cdd:TIGR00606 506 LQNEKADLdrklrkLDQEMEQLNHHTTTRTqmEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPN-KKQLEDWLHSKSK 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 248 EVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQrEDMEERITTLEKRYLSAQREATSLHDAN- 326
Cdd:TIGR00606 585 EINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS-QDEESDLERLKEEIEKSSKQRAMLAGATa 663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 327 --DKLENELASKES----LYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETL-PEIEAQLAQRVAALNKAEERHGNFEERL 399
Cdd:TIGR00606 664 vySQFITQLTDENQsccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTeSELKKKEKRRDEMLGLAPGRQSIIDLKE 743
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 400 RQLEaQLEEKNQELQRARQREKMNDDHNKRLSETVDKLLSESN---------ERLQLHLKERMGALEEKNSLSEEIANMK 470
Cdd:TIGR00606 744 KEIP-ELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKvcltdvtimERFQMELKDVERKIAQQAAKLQGSDLDR 822
|
410 420
....*....|....*....|....*...
gi 32189362 471 KLQdELLLNKEQLLAEMERMQMEIDQLR 498
Cdd:TIGR00606 823 TVQ-QVNQEKQEKQHELDTVVSKIELNR 849
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
245-470 |
7.11e-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: 7.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 245 QRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHD 324
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 325 ANDKLENELASK-ESLYRQSE----------EKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAeerhg 393
Cdd:COG4942 98 ELEAQKEELAELlRALYRLGRqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE----- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 394 nfEERLRQLEAQLEEKNQELQRAR-QREKMNDDHNKRLSETVDKL--LSESNERLQLHLK--ERMGALEEKNSLSEEIAN 468
Cdd:COG4942 173 --RAELEALLAELEEERAALEALKaERQKLLARLEKELAELAAELaeLQQEAEELEALIArlEAEAAAAAERTPAAGFAA 250
|
..
gi 32189362 469 MK 470
Cdd:COG4942 251 LK 252
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
146-497 |
7.13e-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: 7.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 146 VSSEVEVLKALKSLFEHHKALDEkvrerlrmalERVAVleEELELSNQE-TLNLREQLSRRRSGLEEpgkDGDGQTLANG 224
Cdd:pfam05483 95 VSIEAELKQKENKLQENRKIIEA----------QRKAI--QELQFENEKvSLKLEEEIQENKDLIKE---NNATRHLCNL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 225 LGpggDSNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEEL----GTAHRELG-KAEEANSKLQRDLKEALAQRE 299
Cdd:pfam05483 160 LK---ETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELrvqaENARLEMHfKLKEDHEKIQHLEEEYKKEIN 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 300 DMEERITTLEKRYLSAQREATSL-------HDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLP 372
Cdd:pfam05483 237 DKEKQVSLLLIQITEKENKMKDLtflleesRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 373 EiEAQLAQR------------VAALNKAEERHGNFEERLRQLEAQLEEKnqeLQRARQREKMNDDHNKRLSETVDKLLSE 440
Cdd:pfam05483 317 E-DLQIATKticqlteekeaqMEELNKAKAAHSFVVTEFEATTCSLEEL---LRTEQQRLEKNEDQLKIITMELQKKSSE 392
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32189362 441 SNERLQL------HLKERMGALEEKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQL 497
Cdd:pfam05483 393 LEEMTKFknnkevELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDL 455
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
166-405 |
8.83e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.56 E-value: 8.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 166 LDEKVRERLRMALERVAVLEEELELSNQETLNLREQLS--RRRSGLEEPgkDGDGQTLANglgpggdsnrRTAELEEALE 243
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDL--SEEAKLLLQ----------QLSELESQLA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 244 RQRAEVCQLRERLAVLCRQMSQLEEELgtahrelgkAEEANSKLQRDLKEALAQredMEERITTLEKRYLSAQREATSLH 323
Cdd:COG3206 230 EARAELAEAEARLAALRAQLGSGPDAL---------PELLQSPVIQQLRAQLAE---LEAELAELSARYTPNHPDVIALR 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 324 DANDKLENELASKESLYRQSEEKSRQ-LAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQL 402
Cdd:COG3206 298 AQIAALRAQLQQEAQRILASLEAELEaLQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
...
gi 32189362 403 EAQ 405
Cdd:COG3206 378 RLA 380
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
144-500 |
1.03e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 144 GGVSSEVEVLKALKSLFE-----------HHKALDEKVRE---RLRMALERVAVLEE------ELELSNQETLNLREQLS 203
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEelekeleslegSKRKLEEKIREleeRIEELKKEIEELEEkvkelkELKEKAEEYIKLSEFYE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 204 RRRSGLEEPGKD-GDGQTLANG----LGPGGDSNRRTAELEEALERQRAEVCQLR------ERLAVLCRQMSQLEEELG- 271
Cdd:PRK03918 304 EYLDELREIEKRlSRLEEEINGieerIKELEEKEERLEELKKKLKELEKRLEELEerhelyEEAKAKKEELERLKKRLTg 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 272 ----TAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEK---RYLSAQ-------REATSLHDAN---------DK 328
Cdd:PRK03918 384 ltpeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKaieELKKAKgkcpvcgRELTEEHRKElleeytaelKR 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 329 LENELASKESLYRQSEEKSRQLAEWLDDAKqKLQQTLQKAETLPEIEAQLAQ-RVAALNKAEERHGNFEERLRQLEAQLE 407
Cdd:PRK03918 464 IEKELKEIEEKERKLRKELRELEKVLKKES-ELIKLKELAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIK 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 408 EKNQELQRA-------RQREKMNDDHNKRLSETVDKLLSESNERLQlHLKERMGALEE-----------KNSLSEEIANM 469
Cdd:PRK03918 543 SLKKELEKLeelkkklAELEKKLDELEEELAELLKELEELGFESVE-ELEERLKELEPfyneylelkdaEKELEREEKEL 621
|
410 420 430
....*....|....*....|....*....|.
gi 32189362 470 KKLQDELllnkEQLLAEMERMQMEIDQLRGR 500
Cdd:PRK03918 622 KKLEEEL----DKAFEELAETEKRLEELRKE 648
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
151-440 |
1.38e-07 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 55.85 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 151 EVLKALKSLFEHHKALDEKVRERLRMALERvavlEEELELsnqetlnLREQLSRrrsgLEEpgkdgdgqtlANgLGPGGD 230
Cdd:COG0497 155 ELLEEYREAYRAWRALKKELEELRADEAER----ARELDL-------LRFQLEE----LEA----------AA-LQPGEE 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 231 snrrtAELEEALER-QRAEvcQLRERLAVLCRQMSQLE----EELGTAHRELGKAEEANSKLQ---RDLKEALAQREDMe 302
Cdd:COG0497 209 -----EELEEERRRlSNAE--KLREALQEALEALSGGEggalDLLGQALRALERLAEYDPSLAelaERLESALIELEEA- 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 303 erittlekrylsaqreATSLHDANDKLE---NELASKESlyRQSEeksrqlaewLDDAKQKLQQTLqkaETLPEIEAQLA 379
Cdd:COG0497 281 ----------------ASELRRYLDSLEfdpERLEEVEE--RLAL---------LRRLARKYGVTV---EELLAYAEELR 330
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32189362 380 QRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQRekmnddHNKRLSETVDKLLSE 440
Cdd:COG0497 331 AELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKK------AAKKLEKAVTAELAD 385
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
238-497 |
1.70e-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: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 238 LEEALERQRAEVCQLRERLAvlcRQMSQLEEELGTAHR---ELGKA----EEANSKLQRDLKEALAQREDMEER------ 304
Cdd:pfam01576 336 LEEETRSHEAQLQEMRQKHT---QALEELTEQLEQAKRnkaNLEKAkqalESENAELQAELRTLQQAKQDSEHKrkkleg 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 305 -ITTLEKRYLSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQ--QTLQKAETLPEIeaQLAQR 381
Cdd:pfam01576 413 qLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQdtQELLQEETRQKL--NLSTR 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 382 VAAL----NKAEERHGNFEERLRQLEAQLEEKNQELQRARQreKMNDDhnkrlSETVDkLLSESNERLQLHLKERMGALE 457
Cdd:pfam01576 491 LRQLederNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKK--KLEED-----AGTLE-ALEEGKKRLQRELEALTQQLE 562
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 32189362 458 EKNSLSEEIANMKK-LQDEL------LLNKEQLLAEMERMQMEIDQL 497
Cdd:pfam01576 563 EKAAAYDKLEKTKNrLQQELddllvdLDHQRQLVSNLEKKQKKFDQM 609
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
262-497 |
1.96e-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: 55.41 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 262 QMSQLEEELGTAHRELGKAEEAN-------SKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELA 334
Cdd:TIGR04523 118 QKNKLEVELNKLEKQKKENKKNIdkflteiKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 335 SKE---SLYRQSEEKSRQLAEWLDDAKQKlQQTLQKaeTLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQ 411
Cdd:TIGR04523 198 KLElllSNLKKKIQKNKSLESQISELKKQ-NNQLKD--NIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQK 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 412 ELQRArqrEKMNDDHNKRLSETVDKLLSESNERLQLHLKERMGALEEK------------------NSLSEEIANMKKLQ 473
Cdd:TIGR04523 275 ELEQN---NKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQekkleeiqnqisqnnkiiSQLNEQISQLKKEL 351
|
250 260
....*....|....*....|....
gi 32189362 474 DELLLNKEQLLAEMERMQMEIDQL 497
Cdd:TIGR04523 352 TNSESENSEKQRELEEKQNEIEKL 375
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
40-418 |
2.02e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 40 ERLLETLREAQDGLATAQLRLRELGHEKDSLQRQLSIALPQEFAALTKELNlcreqllEREEEIAELKAERNNTRLLLEH 119
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE-------ELQQRLAELEEELEEAQEELEE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 120 LECLVSRHERSLRMTVVKRQAQSPGGVsseVEVLKALKSLFEHHKALDEKVRERLRMALERVAVLEEELELSNQETLNLR 199
Cdd:COG4717 225 LEEELEQLENELEAAALEERLKEARLL---LLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLG 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 200 EQlsRRRSGLEEPGKDGDGQTLANGLGPGGDSNRRTAELEEALERQRAEVCQLRERLAVLCRQMsQLEEELGTAHRELGK 279
Cdd:COG4717 302 KE--AEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL-QLEELEQEIAALLAE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 280 AEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHDANDK--LENELASKESLYRQSEEKSRQLAEWLDDA 357
Cdd:COG4717 379 AGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEeeLEEELEELEEELEELEEELEELREELAEL 458
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32189362 358 KQKLQQtLQKAETLPEIEAQLAQRVAALNKAEERHGnfeeRLRQLEAQLEEKNQELQRARQ 418
Cdd:COG4717 459 EAELEQ-LEEDGELAELLQELEELKAELRELAEEWA----ALKLALELLEEAREEYREERL 514
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
259-498 |
2.24e-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: 55.41 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 259 LCRQMSQLEEELGTAHRELGKAEE--ANSKLQRDLKE-ALAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELAS 335
Cdd:TIGR04523 164 LKKQKEELENELNLLEKEKLNIQKniDKIKNKLLKLElLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 336 KESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAET-----------LPEIEAQLA----QRVAALNKA-EERHGNFEERL 399
Cdd:TIGR04523 244 KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQnnkkikelekqLNQLKSEISdlnnQKEQDWNKElKSELKNQEKKL 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 400 RQLEAQLEEKNQELQRARQ------REKMNDDHNKrlsETVDKLLSESNERLQLHLKERMGALEE-------KNSLSEEI 466
Cdd:TIGR04523 324 EEIQNQISQNNKIISQLNEqisqlkKELTNSESEN---SEKQRELEEKQNEIEKLKKENQSYKQEiknlesqINDLESKI 400
|
250 260 270
....*....|....*....|....*....|..
gi 32189362 467 ANMKKLQDELLLNKEQLLAEMERMQMEIDQLR 498
Cdd:TIGR04523 401 QNQEKLNQQKDEQIKKLQQEKELLEKEIERLK 432
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
38-498 |
2.27e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 38 ERERLLETLREAQDGLATAQLRLRELGHEKDSLQRQLSiALPQEFAALTKELNLCREQLLEREEEIAELKAERNNTRLLL 117
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS-ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 118 EHLECLVSRHERSLRMT------VVKRQAQSPGGVSSEVEVLKALKSLFEHHKALDEKVRERLRMALERVAVLEEELELS 191
Cdd:TIGR02168 319 EELEAQLEELESKLDELaeelaeLEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 192 NQETLNLR---EQLSRRRSGLEEPGKDGDGQTLANGLGpggDSNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEE 268
Cdd:TIGR02168 399 NNEIERLEarlERLEDRRERLQQEIEELLKKLEEAELK---ELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 269 ELGTAHRELGKA----------EEANSKLQRDLKEALAQREDM-------------------------EERITTLEKRYL 313
Cdd:TIGR02168 476 ALDAAERELAQLqarldslerlQENLEGFSEGVKALLKNQSGLsgilgvlselisvdegyeaaieaalGGRLQAVVVENL 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 314 SAQREATSLHDANDK-----------LENELASKESLYRQSEEKSRQLAEWLDDAKQKLQ-------------QTLQKA- 368
Cdd:TIGR02168 556 NAAKKAIAFLKQNELgrvtflpldsiKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvDDLDNAl 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 369 ------------------------------------------------ETLPEIEAQLAQRVAALNKAEERHGNFEERLR 400
Cdd:TIGR02168 636 elakklrpgyrivtldgdlvrpggvitggsaktnssilerrreieeleEKIEELEEKIAELEKALAELRKELEELEEELE 715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 401 QLEAQLEEKNQELQRARQREkmnddhnKRLSETVDKLLsesnERLQLHLKERMGALEEKNSLSEEIANMKKLQDELLLNK 480
Cdd:TIGR02168 716 QLRKELEELSRQISALRKDL-------ARLEAEVEQLE----ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
|
570
....*....|....*...
gi 32189362 481 EQLLAEMERMQMEIDQLR 498
Cdd:TIGR02168 785 EELEAQIEQLKEELKALR 802
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
286-452 |
2.35e-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: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 286 KLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAewlddaKQKLQQTL 365
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR------NNKEYEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 366 QKaetlpEIEAQlaqrvaalnkaEERHGNFEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKLLSESNERL 445
Cdd:COG1579 95 QK-----EIESL-----------KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
....*..
gi 32189362 446 QLHLKER 452
Cdd:COG1579 159 EELEAER 165
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
234-497 |
2.50e-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: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 234 RTAELEEALERQRAEVCQLRErlavLCRQMSQLEEELGTAHRELGKAEEA----------NSKLQRDLK--EALAQR--- 298
Cdd:pfam05557 198 RIPELEKELERLREHNKHLNE----NIENKLLLKEEVEDLKRKLEREEKYreeaatleleKEKLEQELQswVKLAQDtgl 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 299 -----EDMEERITTLEkrylsaQREATsLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLqqtlqkaETLPE 373
Cdd:pfam05557 274 nlrspEDLSRRIEQLQ------QREIV-LKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKL-------KRHKA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 374 IEAQLAQRVAALNKaeERHGnFEERLRQLEAQLEEKN---QELQRARQREKMNDDHNKRLSE------------TVDKLL 438
Cdd:pfam05557 340 LVRRLQRRVLLLTK--ERDG-YRAILESYDKELTMSNyspQLLERIEEAEDMTQKMQAHNEEmeaqlsvaeeelGGYKQQ 416
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 32189362 439 SESNERlQLHLKERMGALEEKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQL 497
Cdd:pfam05557 417 AQTLER-ELQALRQQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERR 474
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
155-413 |
3.13e-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: 54.83 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 155 ALKSLFEhhkALDEKVR--ERLRMALERV-AVLEEELELSNQETLNLREQLSRRRSGLEEPGKDG-DGQTLANGLGPGG- 229
Cdd:pfam10174 437 ALTTLEE---ALSEKERiiERLKEQREREdRERLEELESLKKENKDLKEKVSALQPELTEKESSLiDLKEHASSLASSGl 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 230 DSNRRTAELEEALERQRAEVCQLRERL-------------AVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALA 296
Cdd:pfam10174 514 KKDSKLKSLEIAVEQKKEECSKLENQLkkahnaeeavrtnPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVEN 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 297 QREDMEERITTLEKRYLSAQREATSLH------------DANDKLENELASKESLYRQSEEKS-RQLAEWLDDAKQKLQQ 363
Cdd:pfam10174 594 EKNDKDKKIAELESLTLRQMKEQNKKVanikhgqqemkkKGAQLLEEARRREDNLADNSQQLQlEELMGALEKTRQELDA 673
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 32189362 364 TLQKaetLPEIEAQLAQRVAALNKAeeRHgnfeERLRQLEAQLEEKNQEL 413
Cdd:pfam10174 674 TKAR---LSSTQQSLAEKDGHLTNL--RA----ERRKQLEEILEMKQEAL 714
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
242-408 |
4.09e-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: 52.62 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 242 LERQRAEvcqLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTL--EKRYLSAQREA 319
Cdd:COG1579 22 LEHRLKE---LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYEALQKEI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 320 TSLHDANDKLENELAskeSLYRQSEEKSRQLAEwLDDAKQKLQQTLQkaetlpEIEAQLAQRVAALNKAEERHgnfEERL 399
Cdd:COG1579 99 ESLKRRISDLEDEIL---ELMERIEELEEELAE-LEAELAELEAELE------EKKAELDEELAELEAELEEL---EAER 165
|
....*....
gi 32189362 400 RQLEAQLEE 408
Cdd:COG1579 166 EELAAKIPP 174
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
232-500 |
4.53e-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: 54.57 E-value: 4.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 232 NRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHrelgkaeeansklqrdlkeaLAQREDMEERITTLEKR 311
Cdd:COG3096 842 RQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQAN--------------------LLADETLADRLEELREE 901
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 312 YLSAQrEATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLpeieAQLAQRVAALN----- 386
Cdd:COG3096 902 LDAAQ-EAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFAL----SEVVQRRPHFSyedav 976
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 387 ------------------KAEERHGNFEERLRQLEAQLEEKNQELQRARQREkmnddhnkrlsETVDKLLSEsnerlqlh 448
Cdd:COG3096 977 gllgensdlneklrarleQAEEARREAREQLRQAQAQYSQYNQVLASLKSSR-----------DAKQQTLQE-------- 1037
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 32189362 449 LKERMGALEEKNSLSEEIA---NMKKLQDELLLN---KEQLLAEMERMQMEIDQLRGR 500
Cdd:COG3096 1038 LEQELEELGVQADAEAEERariRRDELHEELSQNrsrRSQLEKQLTRCEAEMDSLQKR 1095
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
157-498 |
5.09e-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: 54.06 E-value: 5.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 157 KSLFEHHKaldekVRERLRMALERVAVLEEELELSNQETLNLREQLSRRRSGLEEPGKDGDGQTLANGlgpggdSNRRTA 236
Cdd:pfam10174 175 KSGEEDWE-----RTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPDPAKTKALQTVIEM------KDTKIS 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 237 ELEEALERQRAEVCQLRERLAVLCRQ----MSQLE----------EELGTAHRELGKAEEANSKLQRDLKEALAQREDME 302
Cdd:pfam10174 244 SLERNIRDLEDEVQMLKTNGLLHTEDreeeIKQMEvykshskfmkNKIDQLKQELSKKESELLALQTKLETLTNQNSDCK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 303 ERITTLEKRYLSAQREATSLHDANDKLENELASKES--------LYRQSEEKSRQLAEWLD-----DAKQKLQQTLQK-- 367
Cdd:pfam10174 324 QHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESflnkktkqLQDLTEEKSTLAGEIRDlkdmlDVKERKINVLQKki 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 368 ---AETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQ------REKMND-----DHNKRLSET 433
Cdd:pfam10174 404 enlQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEqreredRERLEEleslkKENKDLKEK 483
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32189362 434 VDKLLSESNERLQ--LHLKERMGALE----EKNSL--SEEIANMKKLQD----ELLLNKEQLLAEMERMQMEI-DQLR 498
Cdd:pfam10174 484 VSALQPELTEKESslIDLKEHASSLAssglKKDSKlkSLEIAVEQKKEEcsklENQLKKAHNAEEAVRTNPEInDRIR 561
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
156-432 |
5.15e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 53.37 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 156 LKSLFEHHKALDEKVRERLRMALERVAVLEEELELSNQETLNLREQLSRRRSGLEEpgKDGDGQTLANGLGpggDSNRRT 235
Cdd:COG4372 15 LFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQ--ARSELEQLEEELE---ELNEQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 236 AELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYlsA 315
Cdd:COG4372 90 QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL--A 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 316 QREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEERHGNF 395
Cdd:COG4372 168 ALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEED 247
|
250 260 270
....*....|....*....|....*....|....*..
gi 32189362 396 EERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSE 432
Cdd:COG4372 248 KEELLEEVILKEIEELELAILVEKDTEEEELEIAALE 284
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
32-568 |
5.23e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 54.35 E-value: 5.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 32 MVTMLTERERLLE-TLREAQDGLATAQLRLRELGH---EKDSLQR--------QLSIA--------LPQEFAALTKELNL 91
Cdd:pfam15921 501 LTASLQEKERAIEaTNAEITKLRSRVDLKLQELQHlknEGDHLRNvqtecealKLQMAekdkvieiLRQQIENMTQLVGQ 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 92 CREQLLEREEEIAELKAERNNTRLLLEHLECLVSRHE---RSLRMTVVKRQAQSPGGVSSEVEVLKALKSLFEHHKALDE 168
Cdd:pfam15921 581 HGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDakiRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLN 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 169 KV---RERLRMALERVAVLEEELELSNQE----TLNLREQLSRRRSGLEEpgkdgDGQTLANGLGPGGDSNRRTAELEEA 241
Cdd:pfam15921 661 EVktsRNELNSLSEDYEVLKRNFRNKSEEmettTNKLKMQLKSAQSELEQ-----TRNTLKSMEGSDGHAMKVAMGMQKQ 735
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 242 LERQRAEVCQLRERLAVLcrqmsqlEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATS 321
Cdd:pfam15921 736 ITAKRGQIDALQSKIQFL-------EEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVAN 808
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 322 LHDANDKLENELASKESLYRQSEEKSRQLaewlddakqKLQQTLQKAE-------TLPEIEAQLAQRVAA------LNKA 388
Cdd:pfam15921 809 MEVALDKASLQFAECQDIIQRQEQESVRL---------KLQHTLDVKElqgpgytSNSSMKPRLLQPASFtrthsnVPSS 879
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 389 EERHGNFEERLRQLEAQLEEKNQELQRARQ--REKMNDDHNKRLSETVDKLLSESNERLQLHLKERMGALEEKNSLSEEI 466
Cdd:pfam15921 880 QSTASFLSHHSRKTNALKEDPTRDLKQLLQelRSVINEEPTVQLSKAEDKGRAPSLGALDDRVRDCIIESSLRSDICHSS 959
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 467 AN---MKKLQDELLLNKEQLLaeMERMQMEIDQLRGRPPSSYSRSLPGSALELRYSQAPTLPSGAHLDPYVAGSgrAGKR 543
Cdd:pfam15921 960 SNslqTEGSKSSETCSREPVL--LHAGELEDPSSCFTFPSTASPSVKNSASRSFHSSPKKSPVHSLLTSSAEGS--IGSS 1035
|
570 580
....*....|....*....|....*
gi 32189362 544 GRWSGVKEEPSKDwerSAPAGSIPP 568
Cdd:pfam15921 1036 SQYRSAKTIHSPD---SVKDSQSLP 1057
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
147-338 |
5.43e-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: 53.23 E-value: 5.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 147 SSEVEVLKALKSLFEHHKALDEKVRE---RLRMALERVAVLEEELELSNQETLNLREQLSRRRSGLEEPGKDGDGQTLAN 223
Cdd:COG4942 48 KEEKALLKQLAALERRIAALARRIRAleqELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLS 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 224 GLGPGgDSNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEE 303
Cdd:COG4942 128 PEDFL-DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEK 206
|
170 180 190
....*....|....*....|....*....|....*
gi 32189362 304 RITTLEKRYLSAQREATSLHDANDKLENELASKES 338
Cdd:COG4942 207 ELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
262-500 |
6.05e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.89 E-value: 6.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 262 QMSQLEEelgtaHRE-LGKAEEANSKLQRDLKEALaqrEDMEERIttlekrylsAQREATSLHDANDKLENELASKESLY 340
Cdd:PRK02224 160 QLGKLEE-----YRErASDARLGVERVLSDQRGSL---DQLKAQI---------EEKEEKDLHERLNGLESELAELDEEI 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 341 RQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQRE 420
Cdd:PRK02224 223 ERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 421 KMNDDHNKRLS---ETVDKLLSESNERLQLHLKERMGALEEKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQL 497
Cdd:PRK02224 303 GLDDADAEAVEarrEELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDR 382
|
...
gi 32189362 498 RGR 500
Cdd:PRK02224 383 REE 385
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
180-298 |
9.09e-07 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 52.28 E-value: 9.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 180 RVAVLEEELELSNQETLNLREQLSRRRSGLEEPGKDGDG-QTLANGL-GPGGDSNRRTAELEEALERQRAEVCQLRERLA 257
Cdd:PRK09039 61 QIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRlQALLAELaGAGAAAEGRAGELAQELDSEKQVSARALAQVE 140
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 32189362 258 VLCRQMSQLEEELGTAHRELGKAE----EANSKLQ---RDLKEALAQR 298
Cdd:PRK09039 141 LLNQQIAALRRQLAALEAALDASEkrdrESQAKIAdlgRRLNVALAQR 188
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
121-500 |
1.10e-06 |
|
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: 52.59 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 121 ECLVSRHErslrmtVVKRQAQSPGGVSSEVEVLKALKSLFEH-HKALDEKVrERLRMALERVAVLEEELELSNQETLNLR 199
Cdd:pfam07888 38 ECLQERAE------LLQAQEAANRQREKEKERYKRDREQWERqRRELESRV-AELKEELRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 200 EQLSRRRSGLeepgkdgdgqtlangLGPGGDSNRRTAELEE--------ALERQrAEVCQLRERLAVLCRQMSQLEEELG 271
Cdd:pfam07888 111 EELSEEKDAL---------------LAQRAAHEARIRELEEdiktltqrVLERE-TELERMKERAKKAGAQRKEEEAERK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 272 TAHRELGKAEEANSKLQRDLKEA---LAQRED----MEERITTLEKRYLSAQREATslhdANDKLENELASKESLYRQSE 344
Cdd:pfam07888 175 QLQAKLQQTEEELRSLSKEFQELrnsLAQRDTqvlqLQDTITTLTQKLTTAHRKEA----ENEALLEELRSLQERLNASE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 345 EKSRQLAEWL-------DDAKQKLQQT-LQKAE-TLPEIEAQLAQRVAALNKAEERHG---NFE---ERLRQLEAQLEEK 409
Cdd:pfam07888 251 RKVEGLGEELssmaaqrDRTQAELHQArLQAAQlTLQLADASLALREGRARWAQERETlqqSAEadkDRIEKLSAELQRL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 410 NQELQRAR-QREKMNddhnkrlsetVDKLLSESNERLQLHlkermgalEEKNSLSEEIANMKKLQDElllnKEQLLAEME 488
Cdd:pfam07888 331 EERLQEERmEREKLE----------VELGREKDCNRVQLS--------ESRRELQELKASLRVAQKE----KEQLQAEKQ 388
|
410
....*....|..
gi 32189362 489 RMQMEIDQLRGR 500
Cdd:pfam07888 389 ELLEYIRQLEQR 400
|
|
| 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 32189362 234 RTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYL 313
Cdd:pfam01576 69 RKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 314 SAQREATSLHDANDKLENELASKE--------------------SLYRQSEEKSRQLaewLDDAKQKL--------QQTL 365
Cdd:pfam01576 149 KLSKERKLLEERISEFTSNLAEEEekakslsklknkheamisdlEERLKKEEKGRQE---LEKAKRKLegestdlqEQIA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 366 QKAETLPEIEAQLAQR----VAALNKAEE---RHGNFEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKLL 438
Cdd:pfam01576 226 ELQAQIAELRAQLAKKeeelQAALARLEEetaQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALK 305
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32189362 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 |
1.43e-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: 1.43e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 32189362 960 DWLPSLGLPQYRSYFMESLVDARMLDHLNKKELRGQLKMVDSFHRVSLHYGIMCLK 1015
Cdd:smart00454 11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
268-494 |
1.95e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 52.15 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 268 EELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQRE----ATSLHDANDKLENELASKESLYRQS 343
Cdd:PRK04778 105 HEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSllanRFSFGPALDELEKQLENLEEEFSQF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 344 EEKS-----RQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRV-AALNKAEE------------RHGNFEERLRQLEAQ 405
Cdd:PRK04778 185 VELTesgdyVEAREILDQLEEELAALEQIMEEIPELLKELQTELpDQLQELKAgyrelveegyhlDHLDIEKEIQDLKEQ 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 406 L---------------EEKNQELQR--------------ARQR-EKmnddHNKRLSETVDKlLSESNERLQL---HLKER 452
Cdd:PRK04778 265 IdenlalleeldldeaEEKNEEIQEridqlydilerevkARKYvEK----NSDTLPDFLEH-AKEQNKELKEeidRVKQS 339
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32189362 453 M----GALEEKNSLSEEIANMKK------------------LQDELLLNKEQlLAEMERMQMEI 494
Cdd:PRK04778 340 YtlneSELESVRQLEKQLESLEKqydeiteriaeqeiayseLQEELEEILKQ-LEEIEKEQEKL 402
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
27-498 |
2.43e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 27 ELERLMVTmLTERERLLETLREAQDGLATAQLRLRELghekdslqRQLSIALPQEFAAltKELNLCREQLLEREEEIAEL 106
Cdd:COG4913 239 RAHEALED-AREQIELLEPIRELAERYAAARERLAEL--------EYLRAALRLWFAQ--RRLELLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 107 KAERNNTRLLLEHLEclvsRHERSLRmtvvKRQAQSPGGvssEVEVLKALKSlfEHHKALDEKVRERLRMAlERVAVLEE 186
Cdd:COG4913 308 EAELERLEARLDALR----EELDELE----AQIRGNGGD---RLEQLEREIE--RLERELEERERRRARLE-ALLAALGL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 187 ELELSNQETLNLREQLSRRRSGLEEpGKDGDGQTLANGLGPGGDSNRRTAELE---EALERQR----AEVCQLRERlavL 259
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLEALEE-ELEALEEALAEAEAALRDLRRELRELEaeiASLERRKsnipARLLALRDA---L 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 260 CRQMSQLEEEL-----------------GTAHRELGKAeeANSKL--QRDLKEALA--QREDMEERITTLE-----KRYL 313
Cdd:COG4913 450 AEALGLDEAELpfvgelievrpeeerwrGAIERVLGGF--ALTLLvpPEHYAAALRwvNRLHLRGRLVYERvrtglPDPE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 314 SAQREATSL--------HDANDKLENELASKESLY--------------------------------------------- 340
Cdd:COG4913 528 RPRLDPDSLagkldfkpHPFRAWLEAELGRRFDYVcvdspeelrrhpraitragqvkgngtrhekddrrrirsryvlgfd 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 341 --RQSEEKSRQLAEwLDDAKQKLQQTLQKAEtlpEIEAQLAQRVAALNKAEERhgNFEE-RLRQLEAQLEEKNQELQRAR 417
Cdd:COG4913 608 nrAKLAALEAELAE-LEEELAEAEERLEALE---AELDALQERREALQRLAEY--SWDEiDVASAEREIAELEAELERLD 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 418 QrekmNDDHNKRLSETVDKLlsesNERLQLHLKERMGALEEKNSLSEEIANMKKLQDELllnkEQLLAEMERMQMEIDQL 497
Cdd:COG4913 682 A----SSDDLAALEEQLEEL----EAELEELEEELDELKGEIGRLEKELEQAEEELDEL----QDRLEAAEDLARLELRA 749
|
.
gi 32189362 498 R 498
Cdd:COG4913 750 L 750
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
313-507 |
4.42e-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: 50.53 E-value: 4.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 313 LSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTlqkAETLPEIEAQLAQRVAALNKAEERH 392
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAL---ARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 393 GNFEERLRQLEAQLEEKNQELQRARQREKMN--------DDHNKRLsetvdKLLSESNERLQLHLKERMGALEEKNSLSE 464
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLAlllspedfLDAVRRL-----QYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 32189362 465 EIANMKKLQDELLLNKEQLLAEMERMQMEIDQLRGRPPSSYSR 507
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAE 210
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
229-471 |
4.54e-06 |
|
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: 50.73 E-value: 4.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 229 GDSNRRTAELEEALERQRAEVCQLRERLAVLCRQMS---QLEEELGTAHRELGKAEEANSKLQRDlKEALAQREDMEERI 305
Cdd:COG5185 271 GENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDikkATESLEEQLAAAEAEQELEESKRETE-TGIQNLTAEIEQGQ 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 306 TTLEKRYLSAQREATSLHDAND------KLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETlpeieaQLA 379
Cdd:COG5185 350 ESLTENLEAIKEEIENIVGEVElsksseELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADR------QIE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 380 QRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQreKMNDDHNKRLSETVDKLLSESNERLQlHLKERMGALeeK 459
Cdd:COG5185 424 ELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQ--SRLEEAYDEINRSVRSKKEDLNEELT-QIESRVSTL--K 498
|
250
....*....|..
gi 32189362 460 NSLSEEIANMKK 471
Cdd:COG5185 499 ATLEKLRAKLER 510
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
239-417 |
4.80e-06 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 49.96 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 239 EEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKrylsaqre 318
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQ-------- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 319 atslhdandklenELASKESLyrqSEEKSRQLAewlddakqKLQQTLQkaetlpEIEAQLAQRVAALNKAEERHGNFEER 398
Cdd:PRK09039 124 -------------ELDSEKQV---SARALAQVE--------LLNQQIA------ALRRQLAALEAALDASEKRDRESQAK 173
|
170 180
....*....|....*....|...
gi 32189362 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 ... |
230-499 |
5.39e-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: 5.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 230 DSNRRTAELEEALERQRAEVCQLRERLAvlcrQMSQLEEELgtahRELGKAEEANSKLQRDLKEALAQREDMEERITTL- 308
Cdd:TIGR00618 209 CTPCMPDTYHERKQVLEKELKHLREALQ----QTQQSHAYL----TQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLe 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 309 ---EKRYLSAQREATSLHDA------------NDKLENELASKESLYRQSEEKSRQLAEWldDAKQKLQQTLQKAETLPE 373
Cdd:TIGR00618 281 etqERINRARKAAPLAAHIKavtqieqqaqriHTELQSKMRSRAKLLMKRAAHVKQQSSI--EEQRRLLQTLHSQEIHIR 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 374 IEAQlaqrVAALNKAE-ERHGNFEERLRQLEAQLEEKNQELQRARQREkmndDHNKRLSETVD-KLLSESNERLQLHLKE 451
Cdd:TIGR00618 359 DAHE----VATSIREIsCQQHTLTQHIHTLQQQKTTLTQKLQSLCKEL----DILQREQATIDtRTSAFRDLQGQLAHAK 430
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 32189362 452 RMGALEEKNSLSEEIANMKKLQDELLlnKEQLLAEMERMQMEIDQLRG 499
Cdd:TIGR00618 431 KQQELQQRYAELCAAAITCTAQCEKL--EKIHLQESAQSLKEREQQLQ 476
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
246-497 |
1.13e-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: 49.30 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 246 RAEVCQLRERLAVLCRQMSQLEEELGTA-----HRELGKAE--EANSKLQRDLKEAlaqrEDMEERITTLEKRYLSAQRE 318
Cdd:pfam05622 151 RRQVKLLEERNAEYMQRTLQLEEELKKAnalrgQLETYKRQvqELHGKLSEESKKA----DKLEFEYKKLEEKLEALQKE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 319 ATSLHDANDKLENelASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQkAETLP-EIEAQLaQRVAALNKA--EERHGNF 395
Cdd:pfam05622 227 KERLIIERDTLRE--TNEELRCAQLQQAELSQADALLSPSSDPGDNLA-AEIMPaEIREKL-IRLQHENKMlrLGQEGSY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 396 EERLRQLEAQLEEKNQELQRARQREKMNddhNKRLSEtvdkllsesnerLQLHLKERMGALEEKNSLSEEIANMKKLQDE 475
Cdd:pfam05622 303 RERLTELQQLLEDANRRKNELETQNRLA---NQRILE------------LQQQVEELQKALQEQGSKAEDSSLLKQKLEE 367
|
250 260
....*....|....*....|..
gi 32189362 476 LLLNKEQLLAEMERMQMEIDQL 497
Cdd:pfam05622 368 HLEKLHEAQSELQKKKEQIEEL 389
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
268-506 |
1.23e-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: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 268 EELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRY------LSAQREatSLHDANDKLENELASKESLYR 341
Cdd:pfam06160 86 KALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYrelrktLLANRF--SYGPAIDELEKQLAEIEEEFS 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 342 QSEEKSR-----QLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRV-AALNKAEE------------RHGNFEERLRQLE 403
Cdd:pfam06160 164 QFEELTEsgdylEAREVLEKLEEETDALEELMEDIPPLYEELKTELpDQLEELKEgyremeeegyalEHLNVDKEIQQLE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 404 AQLEE-----KNQELQRArqrEKMNDDHNKRLSETVDKLLSESNERLQLH-----LKERMGALEEKNS-LSEEIANMKK- 471
Cdd:pfam06160 244 EQLEEnlallENLELDEA---EEALEEIEERIDQLYDLLEKEVDAKKYVEknlpeIEDYLEHAEEQNKeLKEELERVQQs 320
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 32189362 472 --LQDELLLNKEQL---LAEMERMQMEIDQLRGRPPSSYS 506
Cdd:pfam06160 321 ytLNENELERVRGLekqLEELEKRYDEIVERLEEKEVAYS 360
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
36-497 |
1.32e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 49.73 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 36 LTERERLLE-TLREAQDGLATAQLRLRELGHEKDSLQRQ---LSIALPQEFAAL---TKELNLCREQLLE-------REE 101
Cdd:pfam15921 333 LREAKRMYEdKIEELEKQLVLANSELTEARTERDQFSQEsgnLDDQLQKLLADLhkrEKELSLEKEQNKRlwdrdtgNSI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 102 EIAELKAERNNTRLLLEHLECLVsRHERSLRMTVVKRQAQSPGGVSSEVEVLKALKSLFEHHKALDEKVRERL---RMAL 178
Cdd:pfam15921 413 TIDHLRRELDDRNMEVQRLEALL-KAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELtakKMTL 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 179 ER--------VAVLEEE---LELSNQETLNLREQLSRRRSGLEEPGKDGDgqtlanglgpggdsNRRTAELE-EALERQR 246
Cdd:pfam15921 492 ESsertvsdlTASLQEKeraIEATNAEITKLRSRVDLKLQELQHLKNEGD--------------HLRNVQTEcEALKLQM 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 247 AEVCQLRERLAVLCRQMSQLeeeLGTAHRELGKAEEANSKLQRDLKEalaqredmeERITTLEKRYLSAQREAtSLHDAN 326
Cdd:pfam15921 558 AEKDKVIEILRQQIENMTQL---VGQHGRTAGAMQVEKAQLEKEIND---------RRLELQEFKILKDKKDA-KIRELE 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 327 DKLENELASKESLYRQSEEKSRQLAewldDAKQKLQQTLQKAETLPEIEAQLAQRVAAL-----NKAEErhgnFEERLRQ 401
Cdd:pfam15921 625 ARVSDLELEKVKLVNAGSERLRAVK----DIKQERDQLLNEVKTSRNELNSLSEDYEVLkrnfrNKSEE----METTTNK 696
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 402 LEAQLEEKNQELQRARQREKM---NDDHNKRLSETVDKLLSESN---ERLQLHL-----------KERMGALEEKNSLSE 464
Cdd:pfam15921 697 LKMQLKSAQSELEQTRNTLKSmegSDGHAMKVAMGMQKQITAKRgqiDALQSKIqfleeamtnanKEKHFLKEEKNKLSQ 776
|
490 500 510
....*....|....*....|....*....|...
gi 32189362 465 EIANMKKLQDELLLNKEQLLAEMERMQMEIDQL 497
Cdd:pfam15921 777 ELSTVATEKNKMAGELEVLRSQERRLKEKVANM 809
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
138-500 |
1.40e-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: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 138 RQAQSPGGVSSEVEVLKALKSLFEHHKALDEKVRERLRMALERVAVLEEELELSNQETLNLREQLSRRRSGLEEpgkdgd 217
Cdd:pfam01576 160 RISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAE------ 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 218 gqtLANGLGpggdsnRRTAELEEALERQRAEVCQ---LRERLAVLCRQMSQLEEELGTAHRELGKAEeansKLQRDLKEA 294
Cdd:pfam01576 234 ---LRAQLA------KKEEELQAALARLEEETAQknnALKKIRELEAQISELQEDLESERAARNKAE----KQRRDLGEE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 295 L-AQREDMEERI-TTLEKRYLSAQREaTSLHDANDKLENELASKESLYRQSEEKSRQ----LAEWLDDAKqKLQQTLQKA 368
Cdd:pfam01576 301 LeALKTELEDTLdTTAAQQELRSKRE-QEVTELKKALEEETRSHEAQLQEMRQKHTQaleeLTEQLEQAK-RNKANLEKA 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 369 ETLPEIE-AQLAQRVAALNKAEerhGNFEERLRQLEAQLEEKNQELQRA-RQREKMNDDHNKRLSE-------------- 432
Cdd:pfam01576 379 KQALESEnAELQAELRTLQQAK---QDSEHKRKKLEGQLQELQARLSESeRQRAELAEKLSKLQSElesvssllneaegk 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 433 ---------TVDKLLSESNERLQ------LHLKERMGALE-EKNSLSE---------------------EIANMKKLQDE 475
Cdd:pfam01576 456 niklskdvsSLESQLQDTQELLQeetrqkLNLSTRLRQLEdERNSLQEqleeeeeakrnverqlstlqaQLSDMKKKLEE 535
|
410 420
....*....|....*....|....*
gi 32189362 476 LLLNKEQLLAEMERMQMEIDQLRGR 500
Cdd:pfam01576 536 DAGTLEALEEGKKRLQRELEALTQQ 560
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
242-488 |
1.44e-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: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 242 LERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEeANSKLQRDLKEALAQREDMEERITTLEKRY--LSAQREA 319
Cdd:TIGR00606 739 IDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIM-PEEESAKVCLTDVTIMERFQMELKDVERKIaqQAAKLQG 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 320 TSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAalnkaeerhgnfeeRL 399
Cdd:TIGR00606 818 SDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQ--------------RR 883
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 400 RQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKLLSESNERLQLHLKERMGALEEKNSLSEEIAN----MKKLQDE 475
Cdd:TIGR00606 884 QQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNihgyMKDIENK 963
|
250
....*....|...
gi 32189362 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 |
1.45e-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: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 234 RTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYL 313
Cdd:pfam01576 890 RIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSSI 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 314 SA-QREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLpeieaqlaqrvaalnkaeerh 392
Cdd:pfam01576 970 AAlEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKG--------------------- 1028
|
170 180 190
....*....|....*....|....*....|.
gi 32189362 393 gnfEERLRQLEAQLEEKNQELQRAR-QREKM 422
Cdd:pfam01576 1029 ---NSRMKQLKRQLEEAEEEASRANaARRKL 1056
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
104-476 |
1.49e-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: 49.58 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 104 AELKAERNNTRLLLEHLEclvsRHERSLRMTVVKRQAQS---PGGVSSEVEVLKALKSLFEHHKALDEKVRERLRMALER 180
Cdd:TIGR00618 549 HQLTSERKQRASLKEQMQ----EIQQSFSILTQCDNRSKediPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPE 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 181 VAVLEEELELSNQETLNLREQLSRRRSGLEEPGKDGDGQTLANGLGPGGDSNRRTAELEEALERQRaEVCQLRERLAVLC 260
Cdd:TIGR00618 625 QDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKE-QLTYWKEMLAQCQ 703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 261 RQMSQLEEELGTAHRELGKAEEANSKLQRDLK---EALAQ--REDMEERITTLEKRYLSAQR---EATSLHDANDKLENE 332
Cdd:TIGR00618 704 TLLRELETHIEEYDREFNEIENASSSLGSDLAareDALNQslKELMHQARTVLKARTEAHFNnneEVTAALQTGAELSHL 783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 333 LASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQ----KAETLPEIEAQLAQRVAALNKA----EERHGNFEERLRQLEA 404
Cdd:TIGR00618 784 AAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDilnlQCETLVQEEEQFLSRLEEKSATlgeiTHQLLKYEECSKQLAQ 863
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32189362 405 QLEEKNQELQRARQREKMNDDHNKRLSETVDKLLSESNERLQLHL-KERMGALEEKNSLSEEIANMKKLQDEL 476
Cdd:TIGR00618 864 LTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHEITLYANVRLaNQSEGRFHGRYADSHVNARKYQGLALL 936
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
114-310 |
2.02e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 114 RLLLEHLECLVSRHERslrmtVVKRQAQspggvsseVEVLKALKSLFEHHKALDEKVR--ERLRMAL------ERVAVLE 185
Cdd:COG4913 228 DALVEHFDDLERAHEA-----LEDAREQ--------IELLEPIRELAERYAAARERLAelEYLRAALrlwfaqRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 186 EELELSNQETLNLREQLSRRRSGLEEPGKDGDG---QTLANGLgpggdsnRRTAELE---EALERQRAEVCQLRERLAVL 259
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDEleaQIRGNGG-------DRLEQLEreiERLERELEERERRRARLEAL 367
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 32189362 260 CRQM--------SQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEK 310
Cdd:COG4913 368 LAALglplpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
280-496 |
2.25e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 280 AEEANSKLQRDLKEALAQREDMEERITTLEKRY--LSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDA 357
Cdd:COG3206 173 ARKALEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 358 KQKLQQTLQkAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQrekmnddhnkRLSETVDKL 437
Cdd:COG3206 253 PDALPELLQ-SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQ----------RILASLEAE 321
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32189362 438 LSESNERLQLhLKERMGALEEK-NSLSEEIANMKKLQDELLLNK---EQLLAEMERMQMEIDQ 496
Cdd:COG3206 322 LEALQAREAS-LQAQLAQLEARlAELPELEAELRRLEREVEVARelyESLLQRLEEARLAEAL 383
|
|
| 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 32189362 327 DKLENElasKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQL 406
Cdd:COG4717 49 ERLEKE---ADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 407 EEKNQELQRARQREKMNDdhnkrlsetvdklLSESNERLQLHLKERMGALEEKNSLSEEIANMK-KLQDELLLNKEQLLA 485
Cdd:COG4717 126 QLLPLYQELEALEAELAE-------------LPERLEELEERLEELRELEEELEELEAELAELQeELEELLEQLSLATEE 192
|
170
....*....|....*
gi 32189362 486 EMERMQMEIDQLRGR 500
Cdd:COG4717 193 ELQDLAEELEELQQR 207
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
228-483 |
2.56e-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: 48.89 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 228 GGDSNRRTAELEEALERQRAE---VCQLRERLAVLCRQMSQLEEELGTAHRELGkaeeaNSKLQrdLKEALAQREDMEER 304
Cdd:TIGR00606 817 GSDLDRTVQQVNQEKQEKQHEldtVVSKIELNRKLIQDQQEQIQHLKSKTNELK-----SEKLQ--IGTNLQRRQQFEEQ 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 305 ITTLEKRYLSAQREatsLHDANDK-------LENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTL------------ 365
Cdd:TIGR00606 890 LVELSTEVQSLIRE---IKDAKEQdspletfLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHgymkdienkiqd 966
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 366 QKAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQE---LQRARQREKMNDDHnKRLSETVDKLLSESN 442
Cdd:TIGR00606 967 GKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQerwLQDNLTLRKRENEL-KEVEEELKQHLKEMG 1045
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 32189362 443 ERLQLHLKERMGALEE-----KNSLSEEIANMKKLQDELLLNKEQL 483
Cdd:TIGR00606 1046 QMQVLQMKQEHQKLEEnidliKRNHVLALGRQKGYEKEIKHFKKEL 1091
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
237-476 |
2.70e-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: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 237 ELEEALErqraEVCQLRERLAVLCRQMSQLEEELGTAHRELGKaeeansklqrdLKEALAQREDMEERITTLEKRYLSAQ 316
Cdd:pfam05622 1 DLSEAQE----EKDELAQRCHELDQQVSLLQEEKNSLQQENKK-----------LQERLDQLESGDDSGTPGGKKYLLLQ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 317 REATSLHDANDKLENelaSKESLYRQSEEKSRQLAEwlddakqkLQQTLQKAETLPEIEAQLAQRVAALNKAEERHGNFE 396
Cdd:pfam05622 66 KQLEQLQEENFRLET---ARDDYRIKCEELEKEVLE--------LQHRNEELTSLAEEAQALKDEMDILRESSDKVKKLE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 397 ----------ERLRQLEAQ---LEEKNQE-LQRARQRE----KMN------DDHNKRLSETVDKLLSESN--ERLQL--- 447
Cdd:pfam05622 135 atvetykkklEDLGDLRRQvklLEERNAEyMQRTLQLEeelkKANalrgqlETYKRQVQELHGKLSEESKkaDKLEFeyk 214
|
250 260 270
....*....|....*....|....*....|
gi 32189362 448 HLKERMGALE-EKNSLSEEIANMKKLQDEL 476
Cdd:pfam05622 215 KLEEKLEALQkEKERLIIERDTLRETNEEL 244
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
1040-1107 |
2.84e-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: 43.05 E-value: 2.84e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32189362 1040 VWSNERVMGWVSGLGLKEFATNLTESGVHGALLALDETFDysdlaLLLQIPTQNAQARQLLEKEFSNL 1107
Cdd:smart00454 3 QWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEE-----DLKELGITKLGHRKKILKAIQKL 65
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
234-440 |
2.91e-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: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 234 RTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEEL-------GTAHRELGKAEEANSKLQRDLKeALAQREDM-EERI 305
Cdd:pfam00261 16 RLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELerteerlAEALEKLEEAEKAADESERGRK-VLENRALKdEEKM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 306 TTLEKRYLSAQREAtslHDANDKLEnELASKESLYRQSEEKSRQLAEWLDDAKQKLQqtlqkaETLPEIEAQLAQRVAAL 385
Cdd:pfam00261 95 EILEAQLKEAKEIA---EEADRKYE-EVARKLVVVEGDLERAEERAELAESKIVELE------EELKVVGNNLKSLEASE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32189362 386 NKAEERHGNFEERLRQLEAQLEEKNQELQRARQR----EKMNDD----------HNKRLSETVDKLLSE 440
Cdd:pfam00261 165 EKASEREDKYEEQIRFLTEKLKEAETRAEFAERSvqklEKEVDRledeleaekeKYKAISEELDQTLAE 233
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
39-433 |
2.92e-05 |
|
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: 48.41 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 39 RERLLETLREAQDGLAtaqlrlrelghekdslqrqlsialpqefaaltkelnlcreqllereEEIAELKAERNNTRLLLE 118
Cdd:COG3096 783 REKRLEELRAERDELA----------------------------------------------EQYAKASFDVQKLQRLHQ 816
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 119 HLECLVSRHerslrMTVvkrqaqspggvssevevlkalkslfehhkALDEKVRERLRMALERVAVLEEELELSNQETLNL 198
Cdd:COG3096 817 AFSQFVGGH-----LAV-----------------------------AFAPDPEAELAALRQRRSELERELAQHRAQEQQL 862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 199 REQLSRRRSGLEEPGKDgdgQTLANGLGPGGDSNRRtaeleEALERQRAEVCQLRERLAVLCRQMSQLEEELGTahreLG 278
Cdd:COG3096 863 RQQLDQLKEQLQLLNKL---LPQANLLADETLADRL-----EELREELDAAQEAQAFIQQHGKALAQLEPLVAV----LQ 930
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 279 KAEEANSKLQRDLKEALAQREDMEERITTLEkrYLSAQREATSLHDA----------NDKLENELASKESLYRQSEEKSR 348
Cdd:COG3096 931 SDPEQFEQLQADYLQAKEQQRRLKQQIFALS--EVVQRRPHFSYEDAvgllgensdlNEKLRARLEQAEEARREAREQLR 1008
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 349 QLAEWLDDAKQKLQQtLQ-----KAETLPEIEAQLAQ-RVAALNKAEER-HGNFEERLRQLEAQLEEKNQ-ELQRARQRE 420
Cdd:COG3096 1009 QAQAQYSQYNQVLAS-LKssrdaKQQTLQELEQELEElGVQADAEAEERaRIRRDELHEELSQNRSRRSQlEKQLTRCEA 1087
|
410
....*....|...
gi 32189362 421 KMnDDHNKRLSET 433
Cdd:COG3096 1088 EM-DSLQKRLRKA 1099
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
282-498 |
3.16e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.21 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 282 EANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKL 361
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 362 QQTLQKAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLE------EKNQEL--------QRARQREKMNDDHN 427
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQtevlspEEEKELvekikeleKELEKAKKALEKNE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32189362 428 KrLSETVDKLLSESNERLQLHlkERMGAL-EEKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQLR 498
Cdd:COG1340 161 K-LKELRAELKELRKEAEEIH--KKIKELaEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELH 229
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
333-498 |
3.25e-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: 47.84 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 333 LASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAET----LPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEE 408
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKAllkqLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 409 KNQELQRARQR-EKMNDDHNKRLSETVDKLL------SESNERLQLH---LKERMGALEEKNSLSEEIANMKKLQDELLL 478
Cdd:COG4942 95 LRAELEAQKEElAELLRALYRLGRQPPLALLlspedfLDAVRRLQYLkylAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180
....*....|....*....|
gi 32189362 479 NKEQLLAEMERMQMEIDQLR 498
Cdd:COG4942 175 ELEALLAELEEERAALEALK 194
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
251-503 |
3.61e-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: 47.89 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 251 QLRER---LAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRdLKEALAQREDMEERITTLEKRylSAQREATSLHDAND 327
Cdd:pfam10174 409 QLRDKdkqLAGLKERVKSLQTDSSNTDTALTTLEEALSEKER-IIERLKEQREREDRERLEELE--SLKKENKDLKEKVS 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 328 KLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQ----TLQKAETLPEIEAQL--AQRVAALNKAEErhgNFEERLRQ 401
Cdd:pfam10174 486 ALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSleiaVEQKKEECSKLENQLkkAHNAEEAVRTNP---EINDRIRL 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 402 LEAQLEEKNQELQRARQ---------REKMNDDHNKrlsetvDKLLSESNERLQLHLKE--------RMGALEEKNSLSE 464
Cdd:pfam10174 563 LEQEVARYKEESGKAQAeverllgilREVENEKNDK------DKKIAELESLTLRQMKEqnkkvaniKHGQQEMKKKGAQ 636
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 32189362 465 EIANMKKLQDELLLNK-----EQLLAEMERMQMEIDQLRGRPPS 503
Cdd:pfam10174 637 LLEEARRREDNLADNSqqlqlEELMGALEKTRQELDATKARLSS 680
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
293-498 |
3.78e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.98 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 293 EALAQREDMEERITTLEKRylsaqreatSLHDANDK-----LENELASKESLYRQsEEKSRQLAEWLDDAKQKLQQTLQK 367
Cdd:PRK11281 33 GDLPTEADVQAQLDALNKQ---------KLLEAEDKlvqqdLEQTLALLDKIDRQ-KEETEQLKQQLAQAPAKLRQAQAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 368 AETLPEIEAQ-LAQRVAALNkaeerhgnfeerLRQLEAQLEEKNQELQRARQREkmnDDHNKRL------SETVDKLLSE 440
Cdd:PRK11281 103 LEALKDDNDEeTRETLSTLS------------LRQLESRLAQTLDQLQNAQNDL---AEYNSQLvslqtqPERAQAALYA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 32189362 441 SNERLQlhlkermgalEEKNSLSEEIANMKKLQDELllnKEQLLAEMERMQMEIDQLR 498
Cdd:PRK11281 168 NSQRLQ----------QIRNLLKGGKVGGKALRPSQ---RVLLQAEQALLNAQNDLQR 212
|
|
| 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 32189362 305 ITTLEKRYLSAQREATSLHDANDKLENELASKESLYRQSEEKsrqlaewLDDAKQKLQQtlQKAETLPEIEAQLAQRVAA 384
Cdd:TIGR04320 256 LAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAA-------LATAQKELAN--AQAQALQTAQNNLATAQAA 326
|
90 100 110
....*....|....*....|....*....|
gi 32189362 385 LNKAEERHGNFEERLRQLEAQLEEKNQELQ 414
Cdd:TIGR04320 327 LANAEARLAKAKEALANLNADLAKKQAALD 356
|
|
| SAM_superfamily |
cd09487 |
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
960-1004 |
4.52e-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: 4.52e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 32189362 960 DWLPSLGLPQYRSYFMESLVDARMLDHLNKKELRgQLKMVDSFHR 1004
Cdd:cd09487 4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHR 47
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
237-419 |
5.02e-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: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 237 ELEEALERQRAEVCQLRERLAVLCRQMSQL---EEELGTAHRELGKAEEANSKLQRDLKEALAQredmeerittlekryl 313
Cdd:cd07596 1 EEDQEFEEAKDYILKLEEQLKKLSKQAQRLvkrRRELGSALGEFGKALIKLAKCEEEVGGELGE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 314 sAQREATSLHDANDKLENELASKESLyrqseeksrQLAEWLDD-------AKQKLQQTLQKAETLPEIEAQLAQRVAALN 386
Cdd:cd07596 65 -ALSKLGKAAEELSSLSEAQANQELV---------KLLEPLKEylrycqaVKETLDDRADALLTLQSLKKDLASKKAQLE 134
|
170 180 190
....*....|....*....|....*....|...
gi 32189362 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 32189362 838 WDGPTVVSWLELWVGMPAwYVAACRANVKSGAIMANLSDTE---IQREIGISNPLHRLKLRL 896
Cdd:cd09504 5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
237-407 |
7.64e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 45.20 E-value: 7.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 237 ELEEAL---ERQRAEVCQLRERLAvlcRQMSQLEEELGTAHRelgKAEEANSKLQRDL-KEALAQREDMEERITTLEKRY 312
Cdd:COG1842 34 DMEEDLveaRQALAQVIANQKRLE---RQLEELEAEAEKWEE---KARLALEKGREDLaREALERKAELEAQAEALEAQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 313 LSAQREATSLHDANDKLENELASKESlyRQSEEKSRQLAEwldDAKQKLQQTLQKA------ETLPEIEAQLAQRVAALN 386
Cdd:COG1842 108 AQLEEQVEKLKEALRQLESKLEELKA--KKDTLKARAKAA---KAQEKVNEALSGIdsddatSALERMEEKIEEMEARAE 182
|
170 180
....*....|....*....|...
gi 32189362 387 KAEE--RHGNFEERLRQLEAQLE 407
Cdd:COG1842 183 AAAElaAGDSLDDELAELEADSE 205
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
310-451 |
9.33e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.74 E-value: 9.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 310 KRY-LSAQ--REA-TSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLaqrvaaL 385
Cdd:PRK00409 495 KRLgLPENiiEEAkKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL------L 568
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32189362 386 NKAEERhgnFEERLRQLEAQLEEKNQELqRARQREKMNDDHNKRLSEtVDKLLSESNERLQLHLKE 451
Cdd:PRK00409 569 EEAEKE---AQQAIKEAKKEADEIIKEL-RQLQKGGYASVKAHELIE-ARKRLNKANEKKEKKKKK 629
|
|
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
237-460 |
9.63e-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: 45.75 E-value: 9.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 237 ELEEALERQRAEVCQLRERLAVlcrQMSQLEEELGTAHRELGKAE-EANSklqrdlkealaqredmeerittLEkrylsa 315
Cdd:pfam14915 116 DLELAFQRERDEWLRLQDKMNF---DVSNLRDENEILSQQLSKAEsKANS----------------------LE------ 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 316 qreaTSLHDANDKL-ENELASkESLYRQSEEKSRQlaewlddaKQKLQQTLQKAEtlpeieaqlaqrvAALNKAEERHGN 394
Cdd:pfam14915 165 ----NELHRTRDALrEKTLLL-ESVQRDLSQAQCQ--------KKELEHMYQNEQ-------------DKVNKYIGKQES 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 395 FEERLRQLEA-------QLEEKNQElqrARQREKMNDDHNKRLSETVDKLLSESNERLQL-------------HLKERMG 454
Cdd:pfam14915 219 LEERLAQLQSenmllrqQLEDAQNK---ADAKEKTVIDIQDQFQDIVKKLQAESEKQVLLleernkelinecnHLKERLY 295
|
....*..
gi 32189362 455 ALE-EKN 460
Cdd:pfam14915 296 QYEkEKA 302
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
344-500 |
1.02e-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: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 344 EEKSRQLAEwLDDAKQKLQQTLQKAETLP----EIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARqr 419
Cdd:COG1579 3 PEDLRALLD-LQELDSELDRLEHRLKELPaelaELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 420 EKMNDDHNKRLSETVDKLLSESNERLQLHLKERMGALEEKNSLSEEIAN----MKKLQDELLLNKEQLLAEMERMQMEID 495
Cdd:COG1579 80 EQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAEleaeLAELEAELEEKKAELDEELAELEAELE 159
|
....*
gi 32189362 496 QLRGR 500
Cdd:COG1579 160 ELEAE 164
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
263-458 |
1.06e-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: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 263 MSQLEEELgtAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKrylSAQREATSLHDANDKLENELASKESLYRQ 342
Cdd:cd00176 16 LSEKEELL--SSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNE---LGEQLIEEGHPDAEEIQERLEELNQRWEE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 343 SEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQ-----RVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRAR 417
Cdd:cd00176 91 LRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAAlasedLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 32189362 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 |
1.19e-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: 41.10 E-value: 1.19e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32189362 838 WDGPTVVSWLElWVGMPAwYVAACRANVKSGAIMANLSDTEIqREIGISNPLHRLKLRLAIQEM 901
Cdd:pfam00536 3 WSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
165-497 |
1.58e-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: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 165 ALDEKVrERLRMALERvavLEEELELSNQETLNLREQLSRRRSGLEEPGKDGDGqtLANGLgpggdsnrrtAELEEALER 244
Cdd:COG3096 344 RQQEKI-ERYQEDLEE---LTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDS--LKSQL----------ADYQQALDV 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 245 Q--RA--------------EVCQL--------RERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLK--EALA-- 296
Cdd:COG3096 408 QqtRAiqyqqavqalekarALCGLpdltpenaEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYElvCKIAge 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 297 -QREDMEERITTLEKRYLSAQREATSLHdandKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIE 375
Cdd:COG3096 488 vERSQAWQTARELLRRYRSQQALAQRLQ----QLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELE 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 376 AQLAQRVAALNKAEERHGNFEERLRQLEAQLEEknqelqrARQREKMNDDHNKRLsetvdkllsesnERLQLHLKErmgA 455
Cdd:COG3096 564 AQLEELEEQAAEAVEQRSELRQQLEQLRARIKE-------LAARAPAWLAAQDAL------------ERLREQSGE---A 621
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 32189362 456 LEEKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQL 497
Cdd:COG3096 622 LADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERL 663
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
239-494 |
1.59e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 45.29 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 239 EEALERQRAEVCQLRERLAVLCRQMSQLEEELgtahRELGKAEEANSKLQRDLKEALAQREDMEErittleKRYLSAQRE 318
Cdd:pfam13868 84 EREQKRQEEYEEKLQEREQMDEIVERIQEEDQ----AEAEEKLEKQRQLREEIDEFNEEQAEWKE------LEKEEEREE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 319 ATSLHDANDKLENELASKEslyRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQ-------RVAALNKAEER 391
Cdd:pfam13868 154 DERILEYLKEKAEREEERE---AEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQeeqerkeRQKEREEAEKK 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 392 HGNFEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKLLSESNERLQLHLKERMGALEeknSLSEEIANMKK 471
Cdd:pfam13868 231 ARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELE---KQIEEREEQRA 307
|
250 260
....*....|....*....|...
gi 32189362 472 LQDELLLNKEQLLAEMERMQMEI 494
Cdd:pfam13868 308 AEREEELEEGERLREEEAERRER 330
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
1040-1108 |
1.59e-04 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 41.10 E-value: 1.59e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32189362 1040 VWSNERVMGWVSGLGLKEFATNLTESGVHGALLALDetFDYSDLAlllQIPTQNAQARQLLEKEFSNLI 1108
Cdd:pfam07647 3 SWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLR--LTLEDLK---RLGITSVGHRRKILKKIQELK 66
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
273-498 |
1.61e-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: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 273 AHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELASK-ESLYRQSEEKSRQLA 351
Cdd:pfam12128 228 RDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLlRTLDDQWKEKRDELN 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 352 EWLDDAKQKLQQtlqKAETLPEIEAQLAQ----RVAALNKAEERHGNFEERLRQLEAQ---LEEKNQELQRARQREKMN- 423
Cdd:pfam12128 308 GELSAADAAVAK---DRSELEALEDQHGAfldaDIETAAADQEQLPSWQSELENLEERlkaLTGKHQDVTAKYNRRRSKi 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 424 --------DDHNKRLS---ETVDKLLSESN---ERLQLHLKERMGAL-----EEKNSLSEEIANMKKLQD------ELLL 478
Cdd:pfam12128 385 keqnnrdiAGIKDKLAkirEARDRQLAVAEddlQALESELREQLEAGklefnEEEYRLKSRLGELKLRLNqatatpELLL 464
|
250 260
....*....|....*....|
gi 32189362 479 NKEQLLAEMERMQMEIDQLR 498
Cdd:pfam12128 465 QLENFDERIERAREEQEAAN 484
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
236-498 |
1.61e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.98 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 236 AELEEALERQRAEVCQLRERLAVLCRQ-----------MSQLEEELGTAHRELGKAEEANSK---------LQRdLKEAL 295
Cdd:PRK04778 129 QELLESEEKNREEVEQLKDLYRELRKSllanrfsfgpaLDELEKQLENLEEEFSQFVELTESgdyveareiLDQ-LEEEL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 296 AQREDMEERI----TTLEKRY------LSA---QREATSLHDANDKLENELASKESLYRQSEEKSRQLAewLDDAKQKLQ 362
Cdd:PRK04778 208 AALEQIMEEIpellKELQTELpdqlqeLKAgyrELVEEGYHLDHLDIEKEIQDLKEQIDENLALLEELD--LDEAEEKNE 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 363 QTLQKAETLPEIeaqLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQREKMNDDhnkrLSETVDKLLSESN 442
Cdd:PRK04778 286 EIQERIDQLYDI---LEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNES----ELESVRQLEKQLE 358
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 32189362 443 --ERLQLHLKERMGalEEKNSLSEEIANMKKLQDELllnkEQLLAEMERMQMEIDQLR 498
Cdd:PRK04778 359 slEKQYDEITERIA--EQEIAYSELQEELEEILKQL----EEIEKEQEKLSEMLQGLR 410
|
|
| PRK13729 |
PRK13729 |
conjugal transfer pilus assembly protein TraB; Provisional |
534-735 |
1.70e-04 |
|
conjugal transfer pilus assembly protein TraB; Provisional
Pssm-ID: 184281 [Multi-domain] Cd Length: 475 Bit Score: 45.58 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 534 VAGSGRAGKRGRW-SGVKEEPSKDwerSAPAGSIPPPFPGELDGSDEEEaegmfgaelLSPSGQADVQTLAIMLQEQLEA 612
Cdd:PRK13729 20 VVGAAAAIGGALYlSDVDMSGNGE---AVAEQEPVPDMTGVVDTTFDDK---------VRQHATTEMQVTAAQMQKQYEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 613 INKEIKLIQEEKETTEQRAEELESRVS--SSGLDSLGryrsscslpPSLTTSTlaspsppssGHSTPRLAPPSPAREGTD 690
Cdd:PRK13729 88 IRRELDVLNKQRGDDQRRIEKLGQDNAalAEQVKALG---------ANPVTAT---------GEPVPQMPASPPGPEGEP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 32189362 691 KANHV----PKEEAGAPRGEGPAIPGD--TPPP------TPRSARLERMTQALALQA 735
Cdd:PRK13729 150 QPGNTpvsfPPQGSVAVPPPTAFYPGNgvTPPPqvtyqsVPVPNRIQRKTFTYNEGK 206
|
|
| 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 32189362 309 EKRYLSAQREATSL-----HDAND-KLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRV 382
Cdd:pfam12072 26 EAKIGSAEELAKRIieeakKEAETkKKEALLEAKEEIHKLRAEAERELKERRNELQRQERRLLQKEETLDRKDESLEKKE 105
|
90 100 110
....*....|....*....|....*....|....*..
gi 32189362 383 AALNKAEERHGNFEERLRQLEAQLEEK----NQELQR 415
Cdd:pfam12072 106 ESLEKKEKELEAQQQQLEEKEEELEELieeqRQELER 142
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
286-496 |
2.37e-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: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 286 KLQRDLKEALAQREDMEERITTLEkrYLSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTL 365
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTD--YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 366 QKAETL-PEIEAQLAQRVAALNKAEERHGNFEErLRQLEAQLEEKNQELQRarqrEKMNDDHN------KRLSETVDKLL 438
Cdd:cd00176 82 EELNQRwEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALAS----EDLGKDLEsveellKKHKELEEELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 32189362 439 SESNERLQLhlkERMGALEEKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQ 496
Cdd:cd00176 157 AHEPRLKSL---NELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
309-488 |
2.45e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 309 EKRYLSAQREATS-LHDAndKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQtLQKAETlpeieaQLAQRvaalnk 387
Cdd:PRK12704 30 EAKIKEAEEEAKRiLEEA--KKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNE-LQKLEK------RLLQK------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 388 aeerhgnfEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKLLSESNERLqlhlkermgaleeknslsEEIA 467
Cdd:PRK12704 95 --------EENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL------------------ERIS 148
|
170 180
....*....|....*....|.
gi 32189362 468 NMKklQDELllnKEQLLAEME 488
Cdd:PRK12704 149 GLT--AEEA---KEILLEKVE 164
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
251-484 |
2.52e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.21 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 251 QLRErLAVLCRQMS---------QLEEELGTAHRELGKAEEANSKLqrDLKEALAQREDMEERITTL----EKRYlSAQR 317
Cdd:PRK04778 231 QLQE-LKAGYRELVeegyhldhlDIEKEIQDLKEQIDENLALLEEL--DLDEAEEKNEEIQERIDQLydilEREV-KARK 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 318 EATSLHD-----------ANDKLENELAS-KESlYRQSE---EKSRQLAEWLDDAKQKLQQTLQK--AETLP--EIEAQL 378
Cdd:PRK04778 307 YVEKNSDtlpdflehakeQNKELKEEIDRvKQS-YTLNEselESVRQLEKQLESLEKQYDEITERiaEQEIAysELQEEL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 379 AQRVAALNKAEERHGNFEERLRQL---EAQLEEKNQELQR-----ARQREKMN-----DDHNKRLSETVDKL--LSESNE 443
Cdd:PRK04778 386 EEILKQLEEIEKEQEKLSEMLQGLrkdELEAREKLERYRNklheiKRYLEKSNlpglpEDYLEMFFEVSDEIeaLAEELE 465
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 32189362 444 RLQLHLKERMGALEEknsLSEEIANMKKLQDELLLNK---EQLL 484
Cdd:PRK04778 466 EKPINMEAVNRLLEE---ATEDVETLEEETEELVENAtltEQLI 506
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
230-440 |
2.68e-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: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 230 DSNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTA----------HRELGKAEEANSKLQRDLKEALAQRE 299
Cdd:COG2433 410 EEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEArseerreirkDREISRLDREIERLERELEEERERIE 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 300 DMEERITTLEK-RYLSAQREATSL-------HDANDKLENELASKES--LY-RQSEEKSRQLAEWLDDAK---------- 358
Cdd:COG2433 490 ELKRKLERLKElWKLEHSGELVPVkvvekftKEAIRRLEEEYGLKEGdvVYlRDASGAGRSTAELLAEAGpravivpgel 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 359 -QKLQQTLQKAE----TLPEIEAQLAQRVAALNKAEerhgnfeerlrqLEAQLEEKnQELQRARQREKMnddhnkrlSET 433
Cdd:COG2433 570 sEAADEVLFEEGipvlPAEDVTIQEVDDLAVVDEEE------------LEAAIEDW-EERAEERRREKK--------AEM 628
|
....*..
gi 32189362 434 VDKLLSE 440
Cdd:COG2433 629 LERLISE 635
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
172-500 |
2.68e-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: 45.42 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 172 ERLRMALERVAVLEEELELSNQETLNLREQLSRRRSGLEEPGKDGDGQTlanglgpggDSNRRTAELEEALERQRAEVCQ 251
Cdd:TIGR00606 419 SKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLE---------GSSDRILELDQELRKAERELSK 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 252 LRERLAVLCRQMSQ--LEEELGTAHRELGKAEEANSKLQRDlKEALAQREDM-EERITTLEKRYLSAQREATSLHDANDK 328
Cdd:TIGR00606 490 AEKNSLTETLKKEVksLQNEKADLDRKLRKLDQEMEQLNHH-TTTRTQMEMLtKDKMDKDEQIRKIKSRHSDELTSLLGY 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 329 LENELASKESLYRQSEEKSRqlaewLDDAKQKLQQTLQKAETLP-EIEAQLAQRVAALNKAEERHgnFEERLRQ-LEAQL 406
Cdd:TIGR00606 569 FPNKKQLEDWLHSKSKEINQ-----TRDRLAKLNKELASLEQNKnHINNELESKEEQLSSYEDKL--FDVCGSQdEESDL 641
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 407 EEKNQELQRARQREKMNDDHNKRLSETVDKLLSESNE---------RLQLHLKERMGALEEK--------NSLSEEIANM 469
Cdd:TIGR00606 642 ERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSccpvcqrvfQTEAELQEFISDLQSKlrlapdklKSTESELKKK 721
|
330 340 350
....*....|....*....|....*....|.
gi 32189362 470 KKLQDELLLNKEQLLAEMERMQMEIDQLRGR 500
Cdd:TIGR00606 722 EKRRDEMLGLAPGRQSIIDLKEKEIPELRNK 752
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
167-464 |
3.08e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.86 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 167 DEKVRERLRMALERVAVLEEELELSNQETLNLREQ-----LSRRRSGLEEPGKDGDGQTLANGLGPGgdSNRRTAELEEA 241
Cdd:pfam02029 5 EEAARERRRRAREERRRQKEEEEPSGQVTESVEPNehnsyEEDSELKPSGQGGLDEEEAFLDRTAKR--EERRQKRLQEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 242 LERQRAEVCQLRE-RLAVLCRQMSQLEEELGTAHRE------LGKAEEANS-----KLQRDLKE----ALAQREDMEERI 305
Cdd:pfam02029 83 LERQKEFDPTIADeKESVAERKENNEEEENSSWEKEekrdsrLGRYKEEETeirekEYQENKWStevrQAEEEGEEEEDK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 306 TTLEKRYLSAQREATSLHDANDKLENELASKESLYRQ-----SEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQ 380
Cdd:pfam02029 163 SEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDqkrghPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 381 RVAALNKAEE---RHGNFEE------RLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKLLSESNERLQlhLKE 451
Cdd:pfam02029 243 FLEAEQKLEElrrRRQEKESeefeklRQKQQEAELELEELKKKREERRKLLEEEEQRRKQEEAERKLREEEEKRR--MKE 320
|
330
....*....|....*...
gi 32189362 452 -----RMGALEEKNSLSE 464
Cdd:pfam02029 321 eierrRAEAAEKRQKLPE 338
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
374-500 |
3.32e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 374 IEAQLAQRVAALNKAEERhgnFEERLRQLEAQLEEKNQELQRARQREKMNDdhNKRLSETVDKLLSESNERLQLHLKERM 453
Cdd:COG3206 162 LEQNLELRREEARKALEF---LEEQLPELRKELEEAEAALEEFRQKNGLVD--LSEEAKLLLQQLSELESQLAEARAELA 236
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 32189362 454 GALEEKNSLSEEIANMKKLQDELLLNKE--QLLAEMERMQMEIDQLRGR 500
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQSPViqQLRAQLAELEAELAELSAR 285
|
|
| Yuri_gagarin |
pfam15934 |
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis. |
282-498 |
3.89e-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: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 282 EANSKLQRDLKEALAQREDMEERITTLEkrylsaqreaTSLHDANDKLeNELASKESLYRQSEEKSRqLAEWLDDAKQKL 361
Cdd:pfam15934 41 ENKNEQEQQLKEFTVQNQRLACQIDNLH----------ETLKDRDHQI-KQLQSMITGYSDISENNR-LKEEIHDLKQKN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 362 QQTLQKAETLP-EIEAQLAQRVAALNKAEERHGNFEERLrqleaqleeknQELQRARQREKmndDHNKRLSEtVDKLLSE 440
Cdd:pfam15934 109 CVQARVVRKMGlELKGQEEQRVELCDKYESLLGSFEEQC-----------QELKRANRRVQ---SLQTRLSQ-VEKLQEE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 32189362 441 SNERLQLhLKERMGALEEKNSLSeeIANMKKLQDELllnkeqllaemERMQMEIDQLR 498
Cdd:pfam15934 174 LRTERKI-LREEVIALKEKDAKS--NGRERALQDQL-----------KCCQTEIEKSR 217
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
240-411 |
4.11e-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: 44.94 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 240 EALERQRAEVCQLrERLAVLCRQMSQLEEELgtahRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREA 319
Cdd:COG3096 499 ELLRRYRSQQALA-QRLQQLRAQLAELEQRL----RQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQA 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 320 TSLHDANDKLENELaskESLYRQSEEKSRQLAEWL--DDAKQKLQ-QTLQKAETLPEIEAQLAQRVAALNKAEERHGNFE 396
Cdd:COG3096 574 AEAVEQRSELRQQL---EQLRARIKELAARAPAWLaaQDALERLReQSGEALADSQEVTAAMQQLLEREREATVERDELA 650
|
170
....*....|....*
gi 32189362 397 ERLRQLEAQLEEKNQ 411
Cdd:COG3096 651 ARKQALESQIERLSQ 665
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
254-476 |
4.23e-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: 43.48 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 254 ERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLkEALAQR-EDMEERITTLEKRYLSAQREATSLHDANDKLENE 332
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEV-AALNRRiQLLEEELERTEERLAEALEKLEEAEKAADESERG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 333 LASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAEtlpEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQE 412
Cdd:pfam00261 80 RKVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYE---EVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNN 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32189362 413 LQ-------RARQREKMNDDH----NKRLSETVDKllSESNERLQLHLKERMGALEEKnsLSEEIANMKKLQDEL 476
Cdd:pfam00261 157 LKsleaseeKASEREDKYEEQirflTEKLKEAETR--AEFAERSVQKLEKEVDRLEDE--LEAEKEKYKAISEEL 227
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
272-493 |
4.52e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 272 TAHRELGKAEEANSKLQRDLKEALAQREDM---EERITTLEKRYLSAQREATSLHDANDKLENELASKESLYRQSEEKSR 348
Cdd:PTZ00121 1092 ATEEAFGKAEEAKKTETGKAEEARKAEEAKkkaEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARK 1171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 349 -QLAEWLDDAKQKLQ----QTLQKAETLPEIEAqlAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQREKMN 423
Cdd:PTZ00121 1172 aEDAKKAEAARKAEEvrkaEELRKAEDARKAEA--ARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEER 1249
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32189362 424 DDHNKRLSEtvdkllsesnERLQLHLKERMGALE-EKNSLSEEI--ANMKKLQDELLLNKEQLLAEMERMQME 493
Cdd:PTZ00121 1250 NNEEIRKFE----------EARMAHFARRQAAIKaEEARKADELkkAEEKKKADEAKKAEEKKKADEAKKKAE 1312
|
|
| F-BAR_GAS7 |
cd07649 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Growth Arrest Specific protein ... |
286-435 |
4.54e-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: 43.08 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 286 KLQRDLKEALAQREDMEER----ITTLEKRYLSAQREATsLHDANDKLENELASKESLYRQSEEKSR-QLAEWLDDAKQK 360
Cdd:cd07649 19 QMQKEMAEFIRERIKIEEEyaknLSKLSQSSLAAQEEGT-LGEAWAQVKKSLADEAEVHLKFSSKLQsEVEKPLLNFREN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 361 LQQTLQKAET-LPEIEAQLAQRVAALNKAE----ERHGNFEERLRQLEAQLEEKNQE-LQRARQRekmNDDHNKRLSETV 434
Cdd:cd07649 98 FKKDMKKLDHhIADLRKQLASRYAAVEKARkallERQKDLEGKTQQLEIKLSNKTEEdIKKARRK---STQAGDDLMRCV 174
|
.
gi 32189362 435 D 435
Cdd:cd07649 175 D 175
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
137-447 |
5.00e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.52 E-value: 5.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 137 KRQAQSPGGVSSEVEVLKALKslfehhKALDEKVRERLR-MALERvavLEEELE-----LSN-QETL--------NLREQ 201
Cdd:PRK11281 87 QQLAQAPAKLRQAQAELEALK------DDNDEETRETLStLSLRQ---LESRLAqtldqLQNaQNDLaeynsqlvSLQTQ 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 202 LSRRRSGLEEpgkdgdgqtlanglgpggdSNRRTAELEEALERQRAEVCQLRERLavlcRQMSQLEEELGTAHRELGKAE 281
Cdd:PRK11281 158 PERAQAALYA-------------------NSQRLQQIRNLLKGGKVGGKALRPSQ----RVLLQAEQALLNAQNDLQRKS 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 282 -EANSKL------QRDLKEALAQRedMEERITTL-----EKRYLSAQ---REATSLHDANDKLENELASKES-------- 338
Cdd:PRK11281 215 lEGNTQLqdllqkQRDYLTARIQR--LEHQLQLLqeainSKRLTLSEktvQEAQSQDEAARIQANPLVAQELeinlqlsq 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 339 -LYRQSEE------KSRQLAEWLDDAKQK----------LQQTL-------QKAETLPEIE--AQLAQRVAAL------- 385
Cdd:PRK11281 293 rLLKATEKlntltqQNLRVKNWLDRLTQSernikeqisvLKGSLllsrilyQQQQALPSADliEGLADRIADLrleqfei 372
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32189362 386 NKAEERHGNFEERLRQLEAQL------EEKNQELQRARQREKMNDDHNKRLSEtvdkLLSESNErLQL 447
Cdd:PRK11281 373 NQQRDALFQPDAYIDKLEAGHksevtdEVRDALLQLLDERRELLDQLNKQLNN----QLNLAIN-LQL 435
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
280-368 |
5.16e-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: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 280 AEEANSKLQRDLKEALAQREDMEERITTLEKRYlsaQREATSL-HDANDKLENELASKESLYRQ-SEEKSRQLAEWLDDA 357
Cdd:smart00935 16 GKAAQKQLEKEFKKRQAELEKLEKELQKLKEKL---QKDAATLsEAAREKKEKELQKKVQEFQRkQQKLQQDLQKRQQEE 92
|
90
....*....|.
gi 32189362 358 KQKLQQTLQKA 368
Cdd:smart00935 93 LQKILDKINKA 103
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
174-466 |
6.09e-04 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 43.17 E-value: 6.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 174 LRMALERVAVLEEELElsnqetlNLREQLSRRRSGLEEPGKDGDGqtlanglgpggdsnrrtaeLEEALERQRAEVCQLR 253
Cdd:pfam06008 7 LTGALPAPYKINYNLE-------NLTKQLQEYLSPENAHKIQIEI-------------------LEKELSSLAQETEELQ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 254 ERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREdmeerittlekrYLSAQREATslhdANDKLENEL 333
Cdd:pfam06008 61 KKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVA------------TLGENDFAL----PSSDLSRML 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 334 ASKESLYRqsEEKSRQLAEWLDDAKQKL---QQTLQKAETLpeIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKn 410
Cdd:pfam06008 125 AEAQRMLG--EIRSRDFGTQLQNAEAELkaaQDLLSRIQTW--FQSPQEENKALANALRDSLAEYEAKLSDLRELLREA- 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 32189362 411 qeLQRARQREKMNDDHNKRLSETVDKLL--SESNERLQLHLKERMGALEEKNSLSEEI 466
Cdd:pfam06008 200 --AAKTRDANRLNLANQANLREFQRKKEevSEQKNQLEETLKTARDSLDAANLLLQEI 255
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
357-488 |
6.68e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.54 E-value: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 357 AKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDK 436
Cdd:PRK12705 27 KRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQ 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32189362 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 32189362 268 EELGTAHRELGKAEEANSKLQRDLKEA--------LAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELASKESl 339
Cdd:PRK05771 43 ERLRKLRSLLTKLSEALDKLRSYLPKLnplreekkKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQ- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 340 yrqseEKSRqLAEW----LDDAKQKLQQTLQ-KAETLPEIEAQLAQRVAALNKAEERHGNFEER---LRQLEAQLEEKNQ 411
Cdd:PRK05771 122 -----EIER-LEPWgnfdLDLSLLLGFKYVSvFVGTVPEDKLEELKLESDVENVEYISTDKGYVyvvVVVLKELSDEVEE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 412 ELQRARQREKMNDDhnkrlSETVDKLLSESNERLQLhLKermgalEEKNSLSEEIANM-KKLQDELLLNKEQLLAEMERM 490
Cdd:PRK05771 196 ELKKLGFERLELEE-----EGTPSELIREIKEELEE-IE------KERESLLEELKELaKKYLEELLALYEYLEIELERA 263
|
..
gi 32189362 491 QM 492
Cdd:PRK05771 264 EA 265
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
299-421 |
7.42e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.66 E-value: 7.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 299 EDMEERITTLEKRYLSAQREATSLHDANDKLENELaskeslyrqsEEKSRQLAEWLDDAKQKLQQTLQKA-----ETLPE 373
Cdd:PRK00409 519 NELIASLEELERELEQKAEEAEALLKEAEKLKEEL----------EEKKEKLQEEEDKLLEEAEKEAQQAikeakKEADE 588
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 32189362 374 IEAQLAQRVAALNKAEERHgNFEERLRQLEAQLEEKNQELQRARQREK 421
Cdd:PRK00409 589 IIKELRQLQKGGYASVKAH-ELIEARKRLNKANEKKEKKKKKQKEKQE 635
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
265-499 |
7.84e-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: 42.36 E-value: 7.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 265 QLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQreatslhdanDKLENELAsKESLYRqse 344
Cdd:pfam04012 26 MLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAAL----------TKGNEELA-REALAE--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 345 eksrqlaewlddaKQKLQQTLQkaetlpEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQREKMNd 424
Cdd:pfam04012 92 -------------KKSLEKQAE------ALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAAKAQEAVQ- 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32189362 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 |
1.00e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.42 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 22 DEAGGELERLMVTMLTERERLLETLREAQDGLATAQLRLRELGHEKDSLQRQLSIALPQEfAALTKELNLCREQLLEREE 101
Cdd:TIGR00618 336 QQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKL-QSLCKELDILQREQATIDT 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 102 EIAELKAERNntRLLLEHLECLVSRHERSLRMTVVKRQAQSPGGVSSEV----EVLKALKSLFEHHKALDEKVRERLRMA 177
Cdd:TIGR00618 415 RTSAFRDLQG--QLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLqesaQSLKEREQQLQTKEQIHLQETRKKAVV 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 178 LERVAVL-EEELELSNQET--------LNLREQLSRRRSGLEEPGKDGdGQTLANGLGPGGDSNRRTAELEEALERQRAE 248
Cdd:TIGR00618 493 LARLLELqEEPCPLCGSCIhpnparqdIDNPGPLTRRMQRGEQTYAQL-ETSEEDVYHQLTSERKQRASLKEQMQEIQQS 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 249 ---VCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHda 325
Cdd:TIGR00618 572 fsiLTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALH-- 649
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 326 ndKLENELASKESlyRQSEEKSRQLAEWLDDAKQKLQQTLQ-KAETLPEIEAQLAQRVAALNKAEERHGN----FEE--- 397
Cdd:TIGR00618 650 --ALQLTLTQERV--REHALSIRVLPKELLASRQLALQKMQsEKEQLTYWKEMLAQCQTLLRELETHIEEydreFNEien 725
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 398 ----RLRQLEAQLEEKNQELQRARQ------REKMNDDHNKRLSETVDKLLSESNERLQLHLKERMGALEEK----NSLS 463
Cdd:TIGR00618 726 asssLGSDLAAREDALNQSLKELMHqartvlKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDthllKTLE 805
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 32189362 464 EEIAN-------MKKLQDELLLNKEQ----LLAEMERMQMEIDQLRGR 500
Cdd:TIGR00618 806 AEIGQeipsdedILNLQCETLVQEEEqflsRLEEKSATLGEITHQLLK 853
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
229-491 |
1.06e-03 |
|
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: 42.49 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 229 GDSNRRTAELEEALERQRAEVCQ-LRERLAvlcrqmsqLEEELGTAHRELGKAEEANSKLQRDLKEALAQREdmeERITT 307
Cdd:pfam15905 90 GEQDKRLQALEEELEKVEAKLNAaVREKTS--------LSASVASLEKQLLELTRVNELLKAKFSEDGTQKK---MSSLS 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 308 LEKRYLSAQREAT--SLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQklqqtlQKAETLPEIEAQLAQrVAAL 385
Cdd:pfam15905 159 MELMKLRNKLEAKmkEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEK------EKIEEKSETEKLLEY-ITEL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 386 NKAEERHGNFEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVD---KLLSESNERLQLHLKERmgaleeKNSL 462
Cdd:pfam15905 232 SCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNekcKLLESEKEELLREYEEK------EQTL 305
|
250 260
....*....|....*....|....*....
gi 32189362 463 SEEIANMKklqdELLLNKEQllaEMERMQ 491
Cdd:pfam15905 306 NAELEELK----EKLTLEEQ---EHQKLQ 327
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
234-499 |
1.28e-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: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 234 RTAELEEALERQRAEVcQLRERLAVLCRQMSQLEEELGtaHRElgKAEEANSKLQRDLKEALAQREDMEERITTLEKRYL 313
Cdd:pfam01576 614 KAISARYAEERDRAEA-EAREKETRALSLARALEEALE--AKE--ELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKR 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 314 SAQREATSLHDANDKLENEL---------------ASKESLYR-------QSEEKSRQL--------AEWLDDAKQKLQQ 363
Cdd:pfam01576 689 ALEQQVEEMKTQLEELEDELqatedaklrlevnmqALKAQFERdlqardeQGEEKRRQLvkqvreleAELEDERKQRAQA 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 364 TLQKAE---TLPEIEAQlaqrVAALNKAEERHGnfeERLRQLEAQLEEKNQELQRARQ-REKM--NDDHNKRLSETVDKL 437
Cdd:pfam01576 769 VAAKKKlelDLKELEAQ----IDAANKGREEAV---KQLKKLQAQMKDLQRELEEARAsRDEIlaQSKESEKKLKNLEAE 841
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32189362 438 LSESNERLQLHLKERMGALEEKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQLRG 499
Cdd:pfam01576 842 LLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQS 903
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
168-425 |
1.35e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 168 EKVRERLRMALERVAVLEEELELSNQETLNLREQLSRRRSGLEEPGKDGDG--QTLAnglgpggDSNRRTAELEEALERQ 245
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQaqEELE-------SLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 246 RAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLK--EALAQREDMEERITTLEKRYLSAQREATSL- 322
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAalEQELQALSEAEAEQALDELLKEANRNAEKEe 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 323 -HDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQ 401
Cdd:COG4372 201 eLAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI 280
|
250 260
....*....|....*....|....
gi 32189362 402 LEAQLEEKNQELQRARQREKMNDD 425
Cdd:COG4372 281 AALELEALEEAALELKLLALLLNL 304
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
293-498 |
1.46e-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: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 293 EALAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKaETLP 372
Cdd:pfam12795 3 DELEKAKLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQELAALQAKAEAAPKEILAS-LSLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 373 EIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQR-EKMNDDHNkrLSETVDKLLSESnerLQLHLKE 451
Cdd:pfam12795 82 ELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRlQQIRNRLN--GPAPPGEPLSEA---QRWALQA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 32189362 452 RMGALEEKNSLSE-EIANMKKLQDELLLNKEQLLAEMERMQMEIDQLR 498
Cdd:pfam12795 157 ELAALKAQIDMLEqELLSNNNRQDLLKARRDLLTLRIQRLEQQLQALQ 204
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
228-440 |
1.50e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 228 GGDSNRRTA-----ELEEALERQRAE---VCQLRERLAVL---CRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALA 296
Cdd:PRK04863 486 AGEVSRSEAwdvarELLRRLREQRHLaeqLQQLRMRLSELeqrLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEA 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 297 QREDMEERITTLEKRYLSAQREATSLhdanDKLENELASKESLYRQSEEKSRQLAEWLDDakqklqqTLQKAETLPEIEA 376
Cdd:PRK04863 566 RLESLSESVSEARERRMALRQQLEQL----QARIQRLAARAPAWLAAQDALARLREQSGE-------EFEDSQDVTEYMQ 634
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32189362 377 QLAQRVAALNKAEERhgnFEERLRQLEAQLEeknqelqRARQREKMNDDHNKRLSETVDK-LLSE 440
Cdd:PRK04863 635 QLLERERELTVERDE---LAARKQALDEEIE-------RLSQPGGSEDPRLNALAERFGGvLLSE 689
|
|
| SAM_SARM1-like_repeat1 |
cd09501 |
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
961-1004 |
1.68e-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: 1.68e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 32189362 961 WLPSLGLPQYRSYFMESLVDARMLDHLNKKELRGQLKMVDSFHR 1004
Cdd:cd09501 12 WLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLR 55
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
36-415 |
1.72e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.42 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 36 LTERERLLETLREAQDGLATAQLRLRELGHE-----------KDSLQRQLSIA-LPQEFAALTKElnlcreqllereeeI 103
Cdd:pfam05557 148 ASEAEQLRQNLEKQQSSLAEAEQRIKELEFEiqsqeqdseivKNSKSELARIPeLEKELERLREH--------------N 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 104 AELKAERNNTRLLLEHLECLVSRHER--SLRMTVVKRQAQ-----------------------SPGGVSSEVE------- 151
Cdd:pfam05557 214 KHLNENIENKLLLKEEVEDLKRKLEReeKYREEAATLELEkekleqelqswvklaqdtglnlrSPEDLSRRIEqlqqrei 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 152 VLKALKSLFEHHKALDEKVRERLR--MALERVAVLEEELELSNQETLNLREQ-----LSRRRSGLEEPGKDGDGQTLANG 224
Cdd:pfam05557 294 VLKEENSSLTSSARQLEKARRELEqeLAQYLKKIEDLNKKLKRHKALVRRLQrrvllLTKERDGYRAILESYDKELTMSN 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 225 LGPggDSNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHREL------------GKAEEANSKLQRDLK 292
Cdd:pfam05557 374 YSP--QLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELqalrqqesladpSYSKEEVDSLRRKLE 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 293 EALAQREDMEERITTLEKRYlsAQREATSLHDANDKLENELASKESLyrQSEEKSRQLAEWLDDAKQKLQQTLQKAETLP 372
Cdd:pfam05557 452 TLELERQRLREQKNELEMEL--ERRCLQGDYDPKKTKVLHLSMNPAA--EAYQQRKNQLEKLQAEIERLKRLLKKLEDDL 527
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 32189362 373 EIEAQLAQRVAALNkaeerhgnfEERLRQLEAQLEEKNQELQR 415
Cdd:pfam05557 528 EQVLRLPETTSTMN---------FKEVLDLRKELESAELKNQR 561
|
|
| 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 32189362 262 QMSQLEEELGTAHRELGKA-----EEANSKLQRDLKEALAQREDMEERITTLE---KRYLSAQREATSLHDANDKLENEL 333
Cdd:PRK05771 61 KLRSYLPKLNPLREEKKKVsvkslEELIKDVEEELEKIEKEIKELEEEISELEneiKELEQEIERLEPWGNFDLDLSLLL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 334 A-----------SKESLYRQSEEKSRQLAEWLDDAKQKLQQTL-QKAETLPEIEAQLAqRVAALNKAEERHGNFEERLRQ 401
Cdd:PRK05771 141 GfkyvsvfvgtvPEDKLEELKLESDVENVEYISTDKGYVYVVVvVLKELSDEVEEELK-KLGFERLELEEEGTPSELIRE 219
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 32189362 402 LEAQLEEKNQELQRARQR-EKMNDDHNKRLSETVDKLLSESNE 443
Cdd:PRK05771 220 IKEELEEIEKERESLLEElKELAKKYLEELLALYEYLEIELER 262
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
231-389 |
1.91e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.10 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 231 SNRRTAELEEALERQRAEvcQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSklqrdlKEALAQREDMEERITTLEK 310
Cdd:PRK09510 73 SAKRAEEQRKKKEQQQAE--ELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAK------QAALKQKQAEEAAAKAAAA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 311 RYLSAQREATSLHDANDKLENELASKEslyrQSEEKSRQLAEwlddAKQKLQQTLQK---AETLPEIEAQLAQRVAALNK 387
Cdd:PRK09510 145 AKAKAEAEAKRAAAAAKKAAAEAKKKA----EAEAAKKAAAE----AKKKAEAEAAAkaaAEAKKKAEAEAKKKAAAEAK 216
|
..
gi 32189362 388 AE 389
Cdd:PRK09510 217 KK 218
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
383-500 |
1.99e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.96 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 383 AALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKL-------LSESNERLqlhLKErmgA 455
Cdd:COG1842 16 ALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWeekarlaLEKGREDL---ARE---A 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 32189362 456 LEEKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQLRGR 500
Cdd:COG1842 90 LERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAK 134
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
83-363 |
2.50e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 83 AALTKELNLCREQLLEREEEIAELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpggVSSEVE-------VLKA 155
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAE---LEAELErldassdDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 156 LKSLFEHHKALDEKVRERLRMALERVAVLEEELELSNQEtlnlREQLSRRRSGLEEPGKDGDGQTLAnglgpggdsNRRT 235
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE----LDELQDRLEAAEDLARLELRALLE---------ERFA 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 236 AELEEALERQRAEvcQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSklqRDLKEALAQREDMEERITTLekrylsa 315
Cdd:COG4913 757 AALGDAVERELRE--NLEERIDALRARLNRAEEELERAMRAFNREWPAET---ADLDADLESLPEYLALLDRL------- 824
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 32189362 316 qrEATSLHDANDKLenelasKESLYRQSEEK----SRQLAEWLDDAKQKLQQ 363
Cdd:COG4913 825 --EEDGLPEYEERF------KELLNENSIEFvadlLSKLRRAIREIKERIDP 868
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
38-456 |
2.59e-03 |
|
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: 42.05 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 38 ERERLLET---LREAQDGLATA----QLRLRELGH----EKDSLQRQLSIALPQEFAALTKELNLCREQLLEREEEIAEL 106
Cdd:pfam07111 243 ERQELLDTmqhLQEDRADLQATvellQVRVQSLTHmlalQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREKVFALMVQL 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 107 KAE----RNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPGGVSSEVEVLKALKSLFEHHKALDEKVRERlrmalERVA 182
Cdd:pfam07111 323 KAQdlehRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQ-----QQTA 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 183 VLEEELELSNQETLNLREQLSRRRSGLEEPGkdGDGQTLANGLGPGGDSNRRTAEL---EEALERQRAEVCQLRERL--- 256
Cdd:pfam07111 398 SAEEQLKFVVNAMSSTQIWLETTMTRVEQAV--ARIPSLSNRLSYAVRKVHTIKGLmarKVALAQLRQESCPPPPPAppv 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 257 -AVLCRQMSQLEEELGTAHRELG-KAEEANSKLQRDLKEALAQREDMEERITTLEKRYlsaQREATSLHDANDKLENELA 334
Cdd:pfam07111 476 dADLSLELEQLREERNRLDAELQlSAHLIQQEVGRAREQGEAERQQLSEVAQQLEQEL---QRAQESLASVGQQLEVARQ 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 335 SKEslyrQSEEKSRQLAEWLDDAKQKLQQTLQK--AETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLE---AQLEEK 409
Cdd:pfam07111 553 GQQ----ESTEEAASLRQELTQQQEIYGQALQEkvAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQhraTQEKER 628
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 32189362 410 NQELQRArqREKMNDDHNKRLSETVDKLlsESNERLQLHLKERMGAL 456
Cdd:pfam07111 629 NQELRRL--QDEARKEEGQRLARRVQEL--ERDKNLMLATLQQEGLL 671
|
|
| SAM_superfamily |
cd09487 |
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
843-900 |
2.71e-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: 2.71e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 32189362 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 |
3.04e-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: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 340 YRQSEEKSRQLAEWLDD---AKQKLQQTLQKAETL-----PEIEAQLAQRVAALNKAEERhgnfEERLRQLEAQLE--EK 409
Cdd:cd16269 158 YRQVPRKGVKAEEVLQEflqSKEAEAEAILQADQAltekeKEIEAERAKAEAAEQERKLL----EEQQRELEQKLEdqER 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 410 NQELQRARQREKMNDDHNKRLSEtvdkllsesNERLQLHlkermgaleeknslseeianmkKLQDELLLNKEQLLAEMER 489
Cdd:cd16269 234 SYEEHLRQLKEKMEEERENLLKE---------QERALES----------------------KLKEQEALLEEGFKEQAEL 282
|
....*....
gi 32189362 490 MQMEIDQLR 498
Cdd:cd16269 283 LQEEIRSLK 291
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
309-452 |
3.09e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 41.62 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 309 EKRYLSAQREATSLHDANdklenELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLP----EIEAQLAQRVAA 384
Cdd:PRK12705 36 ERILQEAQKEAEEKLEAA-----LLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDaraeKLDNLENQLEER 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32189362 385 LNKAEERHGNFEERLRQLEAQLEEKNQeLQRARQREKMNDDHNKRLSETVDKLLSESNERLQLHLKER 452
Cdd:PRK12705 111 EKALSARELELEELEKQLDNELYRVAG-LTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERK 177
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
291-500 |
3.25e-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: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 291 LKEALAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELASKESLyrqsEEKSRQLAEWLDDAKQKLQQTLQKAET 370
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLL----TLCTPCMPDTYHERKQVLEKELKHLRE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 371 ----LPEIEAQLAQRVAALNKAEERHGNF------EERLRQLEAQLEEKNQELQRARQREKMNdDHNKRLSEtVDKLLSE 440
Cdd:TIGR00618 234 alqqTQQSHAYLTQKREAQEEQLKKQQLLkqlrarIEELRAQEAVLEETQERINRARKAAPLA-AHIKAVTQ-IEQQAQR 311
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 441 SNERLQLHLKERMGALEEKNSLSEEIANMKKLQDELllnkEQLLAEMERMQMEIDQLRGR 500
Cdd:TIGR00618 312 IHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLL----QTLHSQEIHIRDAHEVATSI 367
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
236-494 |
3.61e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 236 AELEEALERQRAEVCQLRERLAVLCRQMSQLEEELgtahrelgkaEEANSKLQ---RDLKEALAQREDMEERITTLEKRY 312
Cdd:COG1340 11 EELEEKIEELREEIEELKEKRDELNEELKELAEKR----------DELNAQVKelrEEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 313 LSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLaewlddakQKLQQTLQKAETLPEIE-------AQLAQRVAAL 385
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEI--------ERLEWRQQTEVLSPEEEkelvekiKELEKELEKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 386 NKAEERHGNFEE---RLRQLEAQLEEKNQELQRARQ-----REKMNDDHNKR--LSETVDKL---LSESNERLQLHLKER 452
Cdd:COG1340 153 KKALEKNEKLKElraELKELRKEAEEIHKKIKELAEeaqelHEEMIELYKEAdeLRKEADELhkeIVEAQEKADELHEEI 232
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 32189362 453 MGALEEKNSLSEEIANMKKLQDELLLNKEQllAEMERMQMEI 494
Cdd:COG1340 233 IELQKELRELRKELKKLRKKQRALKREKEK--EELEEKAEEI 272
|
|
| CDC37_N |
smart01071 |
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ... |
398-498 |
3.87e-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: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 398 RLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKLLSESNERLQLHLKERMGALEEKNSLSEEIANM--KKLQDE 475
Cdd:smart01071 33 KQRDIHQARVERMEEIKNLKYELIMNDHLNKRIDKLLKGLREEELSPETPTYNEMLAELQDQLKKELEEANGdsEGLLEE 112
|
90 100
....*....|....*....|...
gi 32189362 476 LLLNKEQLLAEMERMQMEIDQLR 498
Cdd:smart01071 113 LKKHRDKLKKEQKELRKKLDELE 135
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
353-498 |
3.88e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.58 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 353 WLDDAKQKLQ--QTLQKA-ETLPEIEAQLAQRVAALN------KAEERHGNFEERLRQLEAQLEEKNQELQRARQREKMN 423
Cdd:PRK10929 56 WLEERKGSLEraKQYQQViDNFPKLSAELRQQLNNERdeprsvPPNMSTDALEQEILQVSSQLLEKSRQAQQEQDRAREI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 424 DDHNKRL----SETvDKLLSESNERLQLHLKERMGALEEKN-SLSEEIANMKKLQDELLLnkEQLLA----EMERMQMEI 494
Cdd:PRK10929 136 SDSLSQLpqqqTEA-RRQLNEIERRLQTLGTPNTPLAQAQLtALQAESAALKALVDELEL--AQLSAnnrqELARLRSEL 212
|
....
gi 32189362 495 DQLR 498
Cdd:PRK10929 213 AKKR 216
|
|
| 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 32189362 236 AELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEAN-SKLQRDLKEALAQREDMEERITTLEKRYLS 314
Cdd:pfam13868 137 EEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREiARLRAQQEKAQDEKAERDELRAKLYQEEQE 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 315 AQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKaeeRHGN 394
Cdd:pfam13868 217 RKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRL---EHRR 293
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 32189362 395 FEERLRQL--EAQLEEKNQELQRARQREKMNDDHNKRLSETVDKLLSE 440
Cdd:pfam13868 294 ELEKQIEEreEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| SAM_Ste50-like_fungal |
cd09533 |
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ... |
960-1007 |
4.01e-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: 4.01e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 32189362 960 DWLPSLGLPQYRSYFMESLVDARMLDHLNKKELRgQLKMVDSFHRVSL 1007
Cdd:cd09533 4 DWLSSLGLPQYEDQFIENGITGDVLVALDHEDLK-EMGITSVGHRLTI 50
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
236-408 |
4.20e-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: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 236 AELEEALERqrAEvcQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEkrylsa 315
Cdd:pfam12718 7 LEAENAQER--AE--ELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNE------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 316 qreatSLHDANDKLENELaskeslyrqsEEKSRQLAEwlddAKQKLQQTLQKAEtlpeieaQLAQRVAALnkaEERHGNF 395
Cdd:pfam12718 77 -----NLTRKIQLLEEEL----------EESDKRLKE----TTEKLRETDVKAE-------HLERKVQAL---EQERDEW 127
|
170
....*....|...
gi 32189362 396 EERLRQLEAQLEE 408
Cdd:pfam12718 128 EKKYEELEEKYKE 140
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
234-496 |
4.70e-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: 40.67 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 234 RTAELEEAlERQRAEVCQLRERLAvlcrqmSQLEEELGTAHRELGKAEEANSKLQRDLKEALaqREDMEERITTLEKRYL 313
Cdd:pfam13868 24 RDAQIAEK-KRIKAEEKEEERRLD------EMMEEERERALEEEEEKEEERKEERKRYRQEL--EEQIEEREQKRQEEYE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 314 SAQREATSLHDANDKLENElasKESLYRQSEEKSRQLAEWLDDAKQklQQTLQKAETLPEIEAQLAQRVAALNKAEERhg 393
Cdd:pfam13868 95 EKLQEREQMDEIVERIQEE---DQAEAEEKLEKQRQLREEIDEFNE--EQAEWKELEKEEEREEDERILEYLKEKAER-- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 394 nFEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKLLSESNERlqlhlKERMGALEEKnslseeianMKKLQ 473
Cdd:pfam13868 168 -EEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQER-----KERQKEREEA---------EKKAR 232
|
250 260
....*....|....*....|....*.
gi 32189362 474 DELLL---NKEQLLAEMERMQMEIDQ 496
Cdd:pfam13868 233 QRQELqqaREEQIELKERRLAEEAER 258
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
233-498 |
4.99e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.22 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 233 RRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRD----LKEALAQREDMEERITTL 308
Cdd:COG5022 871 LQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTEliarLKKLLNNIDLEEGPSIEY 950
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 309 EKrylsaQREATSLHDANDKLENELASKESLYRQSEEKSRQL---AEWLDDAKQKLQQTLQKAETLPEIEAQLAQR---V 382
Cdd:COG5022 951 VK-----LPELNKLHEVESKLKETSEEYEDLLKKSTILVREGnkaNSELKNFKKELAELSKQYGALQESTKQLKELpveV 1025
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 383 AALNKAEERHGNFEERLRQ------LEAQLEEKNQELQ------RARQREKMNDDHNKRLSETVDKLLSESNErLQLHLK 450
Cdd:COG5022 1026 AELQSASKIISSESTELSIlkplqkLKGLLLLENNQLQarykalKLRRENSLLDDKQLYQLESTENLLKTINV-KDLEVT 1104
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 32189362 451 ERMGALEEK---NSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQLR 498
Cdd:COG5022 1105 NRNLVKPANvlqFIVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLE 1155
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
44-358 |
5.02e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.36 E-value: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 44 ETLREAQDGLATAQLRLRELGHEKDSLQRQLSIALPQEFAALTKELnlcreqllereeeiAELKAERNNTRLLLEHLECL 123
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFAR--------------TALKNARLDLRRLFDEKQSE 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 124 VSRHERSLrmTVVKRQAQSpggvsSEVEVLKALKSLFEHHKALDEKVRERLRMA----LERVAVLEEE----LELSNQET 195
Cdd:pfam12128 666 KDKKNKAL--AERKDSANE-----RLNSLEAQLKQLDKKHQAWLEEQKEQKREArtekQAYWQVVEGAldaqLALLKAAI 738
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 196 LNLREQLSRRRSGLEE------PGKDGDGQTLAnglgpggDSNRRTAELEEALER---QRAEVCQL-----------RER 255
Cdd:pfam12128 739 AARRSGAKAELKALETwykrdlASLGVDPDVIA-------KLKREIRTLERKIERiavRRQEVLRYfdwyqetwlqrRPR 811
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 256 LAVLCRQMSQLEEELgtaHRELGKAEE------ANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHDANDKL 329
Cdd:pfam12128 812 LATQLSNIERAISEL---QQQLARLIAdtklrrAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSI 888
|
330 340
....*....|....*....|....*....
gi 32189362 330 ENELASKESLYRQSEEKSRQLAEWLDDAK 358
Cdd:pfam12128 889 GERLAQLEDLKLKRDYLSESVKKYVEHFK 917
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
242-490 |
5.31e-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: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 242 LERQRAEVCQLRERlavlcrqmsqlEEELGTA--HRELGKAEEANSKLQRDLKEALAQ-REDMEERITTLEKRYLSAQRE 318
Cdd:pfam05667 209 LERNAAELAAAQEW-----------EEEWNSQglASRLTPEEYRKRKRTKLLKRIAEQlRSAALAGTEATSGASRSAQDL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 319 ATSLHDANDKLE-NELASKESLYRQSE----EKSRQLAEWLDDAKQKLQQTLQKA--ETLPEIEAQLAQRVAALNKAEER 391
Cdd:pfam05667 278 AELLSSFSGSSTtDTGLTKGSRFTHTEklqfTNEAPAATSSPPTKVETEEELQQQreEELEELQEQLEDLESSIQELEKE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 392 HGNFEERLRQLEAQLEEK---NQELQRARQREKM------NDDHNkrlSETVDKLLSESNERLQlHLKERMGA-----LE 457
Cdd:pfam05667 358 IKKLESSIKQVEEELEELkeqNEELEKQYKVKKKtldllpDAEEN---IAKLQALVDASAQRLV-ELAGQWEKhrvplIE 433
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 32189362 458 EKNSLSEEIAN-----------MKKLQDEL------LLNKE----QLLAEMERM 490
Cdd:pfam05667 434 EYRALKEAKSNkedesqrkleeIKELREKIkevaeeAKQKEelykQLVAEYERL 487
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
630-836 |
5.34e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 41.31 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 630 RAEELESRVSSSGLDSLGRYRSSCSLPPSLTTSTLASPSPPSSGHSTPRLAPPSPAREGtdkanhvPKEEAGAPRgegPA 709
Cdd:PHA03307 232 AGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSS-------PRERSPSPS---PS 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 710 IPGDTPPPTPRSARLERMTQALALQAGSLEDGGPPRGSEGTPDSLHkapkkksikssigrlfgkkekGRMGPPGRDSSSL 789
Cdd:PHA03307 302 SPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSP---------------------SRSPSPSRPPPPA 360
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 32189362 790 AGTPSDETLATDPLGLAKLTGPGDKDRRNKRKhELLEEACRQGLPFA 836
Cdd:PHA03307 361 DPSSPRKRPRPSRAPSSPAASAGRPTRRRARA-AVAGRARRRDATGR 406
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
321-437 |
5.89e-03 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 40.99 E-value: 5.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 321 SLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRvaaLNKAEERHGNFEERLR 400
Cdd:COG5283 11 PFKSALESAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQA---LDQAGIDTRQLSAAQR 87
|
90 100 110
....*....|....*....|....*....|....*..
gi 32189362 401 QLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKL 437
Cdd:COG5283 88 RLRSSLEQTNRQLERQQQRLARLGARQDRLKAARARL 124
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
229-489 |
5.99e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 229 GDSNRRTAELEEALERQRAE--VCQLRERLAVLCRQMSQ---LEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEE 303
Cdd:PRK01156 146 GDPAQRKKILDEILEINSLErnYDKLKDVIDMLRAEISNidyLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSI 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 304 RITTLEKRYL---SAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEwlddakqkLQQTLQKAETLPEIEAQlaQ 380
Cdd:PRK01156 226 EYNNAMDDYNnlkSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKE--------LEERHMKIINDPVYKNR--N 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 381 RVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKllseSNERLQLHLKErmgalEEKN 460
Cdd:PRK01156 296 YINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDL----NNQILELEGYE-----MDYN 366
|
250 260
....*....|....*....|....*....
gi 32189362 461 SLSEEIANMKKLQDELLLNKEQLLAEMER 489
Cdd:PRK01156 367 SYLKSIESLKKKIEEYSKNIERMSAFISE 395
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
236-498 |
6.01e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.05 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 236 AELEEAL------ERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGK-AEEANSK-----LQRDLKEALAQREDMEE 303
Cdd:PRK11281 63 QDLEQTLalldkiDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEeTRETLSTlslrqLESRLAQTLDQLQNAQN 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 304 RITTLEKRYLSAQ----REATSLHDA-------NDKLENELASKESLyrQSEEKSRQLAEW-LDDAKQKLQQT-LQKAET 370
Cdd:PRK11281 143 DLAEYNSQLVSLQtqpeRAQAALYANsqrlqqiRNLLKGGKVGGKAL--RPSQRVLLQAEQaLLNAQNDLQRKsLEGNTQ 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 371 LPEIE-----------AQLAQRVAALNKAeerhGNfEERLRQLEAQLEEknQELQRARQREKMND------DHNKRLSET 433
Cdd:PRK11281 221 LQDLLqkqrdyltariQRLEHQLQLLQEA----IN-SKRLTLSEKTVQE--AQSQDEAARIQANPlvaqelEINLQLSQR 293
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32189362 434 VDKLLSESNERLQLHLKERM---GALEEKNSLSEEIAnmkKLQDELLL----NKEQL----LAEMERMQMEIDQLR 498
Cdd:PRK11281 294 LLKATEKLNTLTQQNLRVKNwldRLTQSERNIKEQIS---VLKGSLLLsrilYQQQQalpsADLIEGLADRIADLR 366
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
357-498 |
6.78e-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: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 357 AKQKLQQTLQKAETLPEIEAQLAQRVAALNKA-EERHGNFEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSEtvd 435
Cdd:pfam02841 174 AEEVLQEFLQSKEAVEEAILQTDQALTAKEKAiEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIE--- 250
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32189362 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 |
7.25e-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: 7.25e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 32189362 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 |
7.74e-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: 7.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 262 QMSQLEEELgtahRELGKAEEANSKLQRDLKEALAqreDMEERITTLekrylSAQREATSLHDANDKL-ENELASKESLY 340
Cdd:pfam09325 32 YIDSLESQL----KKLYKALELLVSQRKELASATG---EFAKSLASL-----ASLELSTGLSRALSQLaEVEERIKELLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 341 RQSEEKSRQLAEWLDD-------------AKQKLQQTLQkaetlpEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLE 407
Cdd:pfam09325 100 RQALQDVLTLGETIDEylrligsvkavfnQRVKAWQSWQ------NAEQELSKKKEQLEKLLRANKSQNDKLQQAKKEVE 173
|
170
....*....|.
gi 32189362 408 EKNQELQRARQ 418
Cdd:pfam09325 174 ELERRVQQAEK 184
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
396-490 |
7.82e-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: 7.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 396 EERLRQLEAQ---LEEKNQELqRARQREKmnDDHNKRLSETVDKLLSESNERLqlhLKERmgaleEKNSLSEEIANMKKL 472
Cdd:COG2433 412 EEEIRRLEEQverLEAEVEEL-EAELEEK--DERIERLERELSEARSEERREI---RKDR-----EISRLDREIERLERE 480
|
90
....*....|....*...
gi 32189362 473 QDELLLNKEQLLAEMERM 490
Cdd:COG2433 481 LEEERERIEELKRKLERL 498
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
236-414 |
8.13e-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: 38.89 E-value: 8.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 236 AELEEALERQRAEVCQLRERLAVLCRQMSQLEEE------------------LGTAHRELGKAEEANSKLQRDLKEALAQ 297
Cdd:pfam05010 4 KDMDAALEKARNEIEEKELEINELKAKYEELRREnlemrkivaefektiaqmIEEKQKQKELEHAEIQKVLEEKDQALAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 298 REDMEERITTLEKRYLSaQREATSLHDANDKLENELAsKESLYRQSEEKSRQLAeWLDDAKQKLQQTlqkAETLPEIEAQ 377
Cdd:pfam05010 84 LNSVEKSFSDLFKRYEK-QKEVISGYKKNEESLKKCA-QDYLARIKKEEQRYQA-LKAHAEEKLDQA---NEEIAQVRSK 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 32189362 378 LAQRVAALnKAEERHGnfEERLRQLEAQLEEKNQELQ 414
Cdd:pfam05010 158 AKAETAAL-QASLRKE--QMKVQSLERQLEQKTKENE 191
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
36-347 |
8.64e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 8.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 36 LTER-ERLLETLREAQDGLATAQLRLRELGHEKDSLQRQLS-------------IALPQEFAALTKELNLCRE---QLLE 98
Cdd:PRK04863 360 LEERlEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLAdyqqaldvqqtraIQYQQAVQALERAKQLCGLpdlTADN 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 99 REEEIAELKA---ERNNTRLLLEH----LECLVSRHERSLRMtvVKRQAqspGGVSSEV--EVLKALKSLFEHHKALDEK 169
Cdd:PRK04863 440 AEDWLEEFQAkeqEATEELLSLEQklsvAQAAHSQFEQAYQL--VRKIA---GEVSRSEawDVARELLRRLREQRHLAEQ 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 170 VrERLRMALErvavlEEELELSNQETLNLREQLSRRRSGLEEPGKDgdgqtlanglgpggDSNRRTAELEEALERQRAEV 249
Cdd:PRK04863 515 L-QQLRMRLS-----ELEQRLRQQQRAERLLAEFCKRLGKNLDDED--------------ELEQLQEELEARLESLSESV 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 250 CQLRERLAvlcrQMSQLEEELGTAHRELGK-------AEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREatsl 322
Cdd:PRK04863 575 SEARERRM----ALRQQLEQLQARIQRLAArapawlaAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVE---- 646
|
330 340
....*....|....*....|....*
gi 32189362 323 hdaNDKLEnelASKESLYRQSEEKS 347
Cdd:PRK04863 647 ---RDELA---ARKQALDEEIERLS 665
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
318-500 |
9.35e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.11 E-value: 9.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 318 EATSLHDANDKLENELASKESLYRQ----SEEKSRQLAEWLDDAKQKLQQTLQKAETLpeiEAQLAQRVAALNKAEERHG 393
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRarieLEKKASALKRQLDRESDRNQELQKRIRLL---EKREAEAEEALREQAELNR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 394 NFEERLRQLEAQLEEKNQELQRARQrekMNDDHNKRLSE-------------TVDKLLSESNERLQLhLKERMGALEEKN 460
Cdd:pfam05557 80 LKKKYLEALNKKLNEKESQLADARE---VISCLKNELSElrrqiqraelelqSTNSELEELQERLDL-LKAKASEAEQLR 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 32189362 461 --------SLSEEIANMKKLQDELLL---------NKEQLLAEMERMQMEIDQLRGR 500
Cdd:pfam05557 156 qnlekqqsSLAEAEQRIKELEFEIQSqeqdseivkNSKSELARIPELEKELERLREH 212
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
495-752 |
9.90e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 40.15 E-value: 9.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 495 DQLRGRPPSSYSRSL-PGSALELRYSQAPTLPSGAHLDPYVAGSGRAGKRGRWS-GVKEEPSKDWERSAPAGSIPPPFPG 572
Cdd:PHA03307 206 PPRRSSPISASASSPaPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRpAPITLPTRIWEASGWNGPSSRPGPA 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 573 ELDGSDEEE----AEGMFGAELLSPSGQADvqtlaimlqeqleainKEIKLIQEEKETTEQRAEELESRVSSSGLDSLGR 648
Cdd:PHA03307 286 SSSSSPRERspspSPSSPGSGPAPSSPRAS----------------SSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSR 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 649 YRSSCSLPPSLTTSTLASPSPPSSGHSTPRLAPPSPAREGTDKANhvpkeeagaprgEGPAIPGDTPPPTPRSarlerMT 728
Cdd:PHA03307 350 SPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAV------------AGRARRRDATGRFPAG-----RP 412
|
250 260
....*....|....*....|....
gi 32189362 729 QALALQAGSLEDGGPPRGSEGTPD 752
Cdd:PHA03307 413 RPSPLDAGAASGAFYARYPLLTPS 436
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
251-414 |
9.96e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 38.40 E-value: 9.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 251 QLRERLAVLCRQMSQLEEELGTAhrelgkAEEANSKLQRDLKEALAQ-REDMEERITTLEKrYLSAQREAtsLHDANDKL 329
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGPV------AQELVDRLEKETEALRERlQKDLEEVRAKLEP-YLEELQAK--LGQNVEEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32189362 330 ENELAS-----KESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAET-----LPEIEAQLAQRVAALNK-----AEERHGN 394
Cdd:pfam01442 72 RQRLEPyteelRKRLNADAEELQEKLAPYGEELRERLEQNVDALRArlapyAEELRQKLAERLEELKEslapyAEEVQAQ 151
|
170 180
....*....|....*....|
gi 32189362 395 FEERLRQLEAQLEEKNQELQ 414
Cdd:pfam01442 152 LSQRLQELREKLEPQAEDLR 171
|
|
| |
