|
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 ... |
899-969 |
5.52e-44 |
|
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.
Pssm-ID: 188961 Cd Length: 71 Bit Score: 153.49 E-value: 5.52e-44
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442626410 899 FALWNGPTIVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 969
Cdd:cd09562 1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
|
|
| SAM_liprin-alpha1,2,3,4_repeat3 |
cd09568 |
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ... |
1071-1142 |
4.25e-42 |
|
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.
Pssm-ID: 188967 Cd Length: 72 Bit Score: 147.85 E-value: 4.25e-42
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626410 1071 DVLVWSNERVIRWVGSIGLKEYANNLLESGVHGGLMALDEGFDANAMGLALQIPTQNAQARQILDTEFNNLL 1142
Cdd:cd09568 1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
|
|
| SAM_liprin-alpha1,2,3,4_repeat2 |
cd09565 |
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ... |
986-1051 |
2.86e-40 |
|
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.
Pssm-ID: 188964 Cd Length: 66 Bit Score: 142.61 E-value: 2.86e-40
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442626410 986 MNHEWIGNYWLPGLGLPQYRTTFMECLVDARMLDHLTKKDLRGQLKMVDSFHRTSLQYGISMLKRL 1051
Cdd:cd09565 1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
|
|
| SAM_liprin-kazrin_repeat1 |
cd09494 |
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
906-964 |
1.34e-26 |
|
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of the SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and adherens junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188893 Cd Length: 58 Bit Score: 103.46 E-value: 1.34e-26
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 442626410 906 TIVAWLELWVGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 964
Cdd:cd09494 1 RVCAWLEDFGLMP-MYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
|
|
| SAM_liprin-kazrin_repeat2 |
cd09495 |
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ... |
990-1049 |
1.93e-25 |
|
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and in adheren junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188894 Cd Length: 60 Bit Score: 99.92 E-value: 1.93e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 990 WIGNYWLPGLGLPQYRTTFMECLVDARMLDHLTKKDLRGQLKMVDSFHRTSLQYGISMLK 1049
Cdd:cd09495 1 WWVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLVHLKVTSQLHHLSLKCGIHVLH 60
|
|
| SAM_liprin-kazrin_repeat3 |
cd09496 |
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of ... |
1079-1140 |
3.21e-24 |
|
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and in adherens junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188895 Cd Length: 62 Bit Score: 96.84 E-value: 3.21e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626410 1079 RVIRWVGSIGLKEYANNLLESGVHGGLMALDEGFDANAMGLALQIPTQNAQARQILDTEFNN 1140
Cdd:cd09496 1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETEFNN 62
|
|
| SAM_kazrin_repeat3 |
cd09570 |
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin ... |
1071-1142 |
4.91e-24 |
|
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188969 Cd Length: 72 Bit Score: 96.36 E-value: 4.91e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626410 1071 DVLVWSNERVIRWVGSIGLKEYANNLLESGVHGGLMALDEGFDANAMGLALQIPTQNAQARQILDTEFNNLL 1142
Cdd:cd09570 1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
|
|
| SAM_liprin-beta1,2_repeat3 |
cd09569 |
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ... |
1071-1142 |
5.88e-16 |
|
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.
Pssm-ID: 188968 Cd Length: 72 Bit Score: 73.64 E-value: 5.88e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626410 1071 DVLVWSNERVIRWVGSIGLKEYANNLLESGVHGGLMALDEGFDANAMGLALQIPTQNAQARQILDTEFNNLL 1142
Cdd:cd09569 1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
249-490 |
1.22e-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: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 249 ANELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEER 328
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 329 ITTLEKRYLNAQREstslhdlNEKLEQELRHKEAQLKAQERH-GSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLR 407
Cdd:TIGR02168 784 IEELEAQIEQLKEE-------LKALREALDELRAELTLLNEEaANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 408 LSSTVDKL---LSESNERLQVHLKERMHALDEKNALTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQL--LQQ 482
Cdd:TIGR02168 857 LAAEIEELeelIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLegLEV 936
|
....*...
gi 442626410 483 EIAYNIQQ 490
Cdd:TIGR02168 937 RIDNLQER 944
|
|
| SAM_kazrin_repeat1 |
cd09564 |
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ... |
902-964 |
1.25e-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: 1.25e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442626410 902 WNGPTIVAWLELWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 964
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 ... |
985-1049 |
1.03e-14 |
|
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188966 Cd Length: 65 Bit Score: 69.75 E-value: 1.03e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626410 985 DMNHEWIGNYWLPGLGLPQYRTTFMECLVDARMLDHLTKKDLRGQLKMVDSFHRTSLQYGISMLK 1049
Cdd:cd09567 1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
|
|
| SAM_liprin-beta1,2_repeat2 |
cd09566 |
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ... |
985-1049 |
1.25e-14 |
|
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta potentially is able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.
Pssm-ID: 188965 Cd Length: 63 Bit Score: 69.26 E-value: 1.25e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626410 985 DMNHEWIGNyWLPGLGLPQYRTTFMECLVDARMLDHLTKKDLRgQLKMVDSFHRTSLQYGISMLK 1049
Cdd:cd09566 1 KLDTHWVLR-WLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDLL-HLKVTSALHHASIRRGIQVLR 63
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
58-471 |
1.80e-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: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 58 ETENKLRDVEKERDSLQRQINAnlpqefatLTKELTQARETLLERDEEIGELKAERNNTRLLLEHLECLVSRHERslrmt 137
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAE--------LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA----- 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 138 vvKRQAAAQSGVSSEVEVLKAlkslfehhkaldEKVRERLRLSIEKNnmmEEELSSAKEELAQYKAGVvpagvgsgsgag 217
Cdd:TIGR02168 741 --EVEQLEERIAQLSKELTEL------------EAEIEELEERLEEA---EEELAEAEAEIEELEAQI------------ 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 218 saattaggggaENGLKEKMAGVGGSGGVNGEANELNDYAaktHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRV 297
Cdd:TIGR02168 792 -----------EQLKEELKALREALDELRAELTLLNEEA---ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 298 QKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQREstslhdlNEKLEQELRHKEAQL-KAQERHGSAEDR 376
Cdd:TIGR02168 858 AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE-------LRELESKRSELRRELeELREKLAQLELR 930
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 377 IRGLETNLDEKTNevvRLNQRLKMNEEHNLRLSSTVDKLLSESNERLQvHLKERMHALDEKN-ALTQELEKARKVAEELH 455
Cdd:TIGR02168 931 LEGLEVRIDNLQE---RLSEEYSLTLEEAEALENKIEDDEEEARRRLK-RLENKIKELGPVNlAAIEEYEELKERYDFLT 1006
|
410
....*....|....*.
gi 442626410 456 HEKSEIMKelSKTRLE 471
Cdd:TIGR02168 1007 AQKEDLTE--AKETLE 1020
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
985-1049 |
3.14e-13 |
|
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.
Pssm-ID: 425739 Cd Length: 64 Bit Score: 65.37 E-value: 3.14e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626410 985 DMNHEWIGNYWLPGLGLPQYRTTFMECLVDARMLDHLTKKDLRgQLKMVDSFHRTSLQYGISMLK 1049
Cdd:pfam00536 1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
248-481 |
3.40e-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: 74.32 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 248 EANELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEE 327
Cdd:TIGR02168 258 LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 328 RITTLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQLKAQERHgsaedrIRGLETNLDEKTNEVVRLNQRLKMNEEHNLR 407
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ------LETLRSKVAQLELQIASLNNEIERLEARLER 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626410 408 LSSTVDKLLSESNERLQVHLKERMHALDEK-NALTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQLLQ 481
Cdd:TIGR02168 412 LEDRRERLQQEIEELLKKLEEAELKELQAElEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
50-640 |
5.29e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.82 E-value: 5.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 50 REAQERLNETENKL-------RDVEKERDSLQRQinANLPQEFATLTKELT--QARETLLERDEeigeLKAERNNTRLLL 120
Cdd:COG1196 175 EEAERKLEATEENLerledilGELERQLEPLERQ--AEKAERYRELKEELKelEAELLLLKLRE----LEAELEELEAEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 121 EHLECLVSRHERSLRMTVVKRQAAAQSGVSSEVEVLKALKSLFEHHKALdEKVRERLRLSIEKNNMMEEELSSAKEELAQ 200
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL-ARLEQDIARLEERRRELEERLEELEEELAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 201 YKAgvvpagvgsgsgAGSAATTAGGGGAENGLKEKMAGVGGSGGVNGEANELNDYAAKTHELQTIIEKQTSELSQWQRRV 280
Cdd:COG1196 328 LEE------------ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 281 SDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQRESTSLHDLNEKLEQELRHK 360
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 361 EAQLKAQERH----GSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNL--RLSSTVDKLLSESNERLQVHLKERMHAL 434
Cdd:COG1196 476 EAALAELLEElaeaAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAvaVLIGVEAAYEAALEAALAAALQNIVVED 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 435 DEKNALTQELEKARKV--AEELHHEKseiMKELSKTRLEIENFKRQLLQQEIAYNIQQTEALTRSLSPSSVVDPSGAFSR 512
Cdd:COG1196 556 DEVAAAAIEYLKAAKAgrATFLPLDK---IRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARL 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 513 SNSHASFETHSLRRQSK----------QRLSEENALVRSMAEQEWEKLQQAAHAQQQAYELASAADCDDSDVLYAAATDM 582
Cdd:COG1196 633 EAALRRAVTLAGRLREVtlegeggsagGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEA 712
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442626410 583 MSPSGHTDAQTLAMMLQEQLDAINNEIRLIQEEK----------------QSTEARAEELESRVGSLEHVNLLA 640
Cdd:COG1196 713 EEERLEEELEEEALEEQLEAEREELLEELLEEEElleeealeelpeppdlEELERELERLEREIEALGPVNLLA 786
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
49-402 |
5.38e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.94 E-value: 5.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 49 LREAQERLNETENKLRDVEKERDSLQRQinANLPQEFATLTKEL------------TQARETLLERDEEIGELKAERNNT 116
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKSLERQ--AEKAERYKELKAELrelelallvlrlEELREELEELQEELKEAEEELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 117 RLLLEHLECLVSRHErsLRMTVVKRQAAAQSGvssEVEVLKALKSLFEHHKALDEKVRERLRLSIEKNNMMEEELSSAKE 196
Cdd:TIGR02168 259 TAELQELEEKLEELR--LEVSELEEEIEELQK---ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 197 ELAQYKAGVVPAGVGSGSGAgsaattaggggaeNGLKEKMAgvggsggvnGEANELNDYAAKTHELQTIIEKQTSELSQW 276
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEEL-------------ESLEAELE---------ELEAELEELESRLEELEEQLETLRSKVAQL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 277 QRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLREnvAQKEDQEERITTLEKrylnaqrestslhdLNEKLEQE 356
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEE--------------ELEELQEE 455
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 442626410 357 LRHKEAQLKaqerhgSAEDRIRGLETNLDEKTNEVVRLNQRLKMNE 402
Cdd:TIGR02168 456 LERLEEALE------ELREELEEAEQALDAAERELAQLQARLDSLE 495
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
40-485 |
2.48e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 2.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 40 DERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINANLpQEFATLTKELTQARETLLERDEEIGELKAERNNTRLL 119
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE-ERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 120 LEHLECLVSRHERSLRMTVVKRQAAAQSGVSSEVEVLKALKSLFEHHKALDEKVRERLRLSIEKNNMMEEELSSAKEELA 199
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 200 QYKAGVVPAGVGSGSGAGSAATTAGGGGAENGLKEKMAGVGGSGGVNGEANELNDYAAKTHELQTIIEKQTSELSQWQRR 279
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 280 VSDLNNK--ISELEENMSRVQKEHCKAQDQC--AKLQRDLRENVAQ--------KEDQEERITTL------EKRYLNAQR 341
Cdd:COG1196 513 ALLLAGLrgLAGAVAVLIGVEAAYEAALEAAlaAALQNIVVEDDEVaaaaieylKAAKAGRATFLpldkirARAALAAAL 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 342 ESTSLHDLNEKLEQELRHKEAQLKA-----------QERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSS 410
Cdd:COG1196 593 ARGAIGAAVDLVASDLREADARYYVlgdtllgrtlvAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLA 672
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626410 411 TVDKLLSESNERLQVHLKERMHALDEKNALTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQLLQQEIA 485
Cdd:COG1196 673 ALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEEL 747
|
|
| SAM_liprin-beta1,2_repeat1 |
cd09563 |
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
899-963 |
4.36e-11 |
|
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta protein contain three copies (repeats) of SAM domain. They may form heterodimers with liprins-alpha through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta is potentially able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.
Pssm-ID: 188962 Cd Length: 64 Bit Score: 59.55 E-value: 4.36e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442626410 899 FALWNGPTIVAWL-ELWVGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQ 963
Cdd:cd09563 1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
47-487 |
1.67e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.47 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 47 DSLREAQERLNETENKLRDVEKERDSLQRQInanlpQEFATLTKELTQARETLLERDEEIGELKAERNNTRLLLEHLEcl 126
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEV-----KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK-- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 127 vsRHERSLRmTVVKRQAAAQsGVSSEVEVLKALKSLFEHHKALDEKVRERLRLSIEKNNMMEEELSSAKEELAQYKAGVV 206
Cdd:PRK03918 273 --KEIEELE-EKVKELKELK-EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 207 PAGVGSGSGAGSAATTAGGGGAENGLkEKMAGVGGSGGVNGEANELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNK 286
Cdd:PRK03918 349 ELEKRLEELEERHELYEEAKAKKEEL-ERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKA 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 287 ISELEE--------------------------NMSRVQKEHCKAQDQCAKLQRDLREnVAQKEDQEERITTLEKRY--LN 338
Cdd:PRK03918 428 IEELKKakgkcpvcgrelteehrkelleeytaELKRIEKELKEIEEKERKLRKELRE-LEKVLKKESELIKLKELAeqLK 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 339 AQRESTSLHDLnEKLEQELRHKEaqlKAQERHGSAEDRIRGLETNLDEKT---NEVVRLNQRLKMNEEHNLRLSSTVDKL 415
Cdd:PRK03918 507 ELEEKLKKYNL-EELEKKAEEYE---KLKEKLIKLKGEIKSLKKELEKLEelkKKLAELEKKLDELEEELAELLKELEEL 582
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626410 416 LSESNERLQVHLKERMHALDEKNALT---QELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQLLQQEIAYN 487
Cdd:PRK03918 583 GFESVEELEERLKELEPFYNEYLELKdaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS 657
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
37-368 |
3.39e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 64.70 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 37 SMLDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINAnLPQEFATLTKELTQARETLLERDEEIGELKAErnnt 116
Cdd:TIGR02169 685 GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ-LEQEEEKLKERLEELEEDLSSLEQEIENVKSE---- 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 117 rllLEHLECLVSRHERSLrmtvVKRQAA--------AQSGVSsevEVLKALKSLFEHHKALDEKVRErLRLSIEKNNMME 188
Cdd:TIGR02169 760 ---LKELEARIEELEEDL----HKLEEAlndlearlSHSRIP---EIQAELSKLEEEVSRIEARLRE-IEQKLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 189 EELSSAKEELAQYKagvvpagvgsgsgagsaattaggggaeNGLKEKMAgvggsggvnGEANELNDYAAKTHELQTIIEK 268
Cdd:TIGR02169 829 EYLEKEIQELQEQR---------------------------IDLKEQIK---------SIEKEIENLNGKKEELEEELEE 872
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 269 QTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQRESTSLHD 348
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS 952
|
330 340
....*....|....*....|
gi 442626410 349 LnEKLEQELRHKEAQLKAQE 368
Cdd:TIGR02169 953 L-EDVQAELQRVEEEIRALE 971
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
39-455 |
4.77e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.63 E-value: 4.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 39 LDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINA-NLPQEFATLTKELTQARETLLERDEEIGELKAERNNTR 117
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKlEKLLQLLPLYQELEALEAELAELPERLEELEERLEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 118 LLLEHLECLVSRHERslrmtvvKRQAAAQSGVSSEVEVLKALKSLFEHHKALDEKVRErLRLSIEKNnmmEEELSSAKEE 197
Cdd:COG4717 160 ELEEELEELEAELAE-------LQEELEELLEQLSLATEEELQDLAEELEELQQRLAE-LEEELEEA---QEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 198 LAQYKAGVVPAGVGSGSGAGS--------------AATTAGGGGAENGLKEKMAGVGGSGGVNGEANELNDYAAKTHELQ 263
Cdd:COG4717 229 LEQLENELEAAALEERLKEARlllliaaallallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 264 TIIEKQTSELSQWQRRVSDL----NNKISELEENMSRVQkEHCKAQDQCAKLQRDLRENVAQKE----------DQEERI 329
Cdd:COG4717 309 ALPALEELEEEELEELLAALglppDLSPEELLELLDRIE-ELQELLREAEELEEELQLEELEQEiaallaeagvEDEEEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 330 TTLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQLKAQERHgSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLS 409
Cdd:COG4717 388 RAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE-ELEEELEELEEELEELEEELEELREELAELEAELEQLE 466
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 442626410 410 StvDKLLSESNERLQvHLKERMHALDEK----NALTQELEKARKVAEELH 455
Cdd:COG4717 467 E--DGELAELLQELE-ELKAELRELAEEwaalKLALELLEEAREEYREER 513
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
269-513 |
1.60e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.32 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 269 QTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQRESTSLHD 348
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 349 LNEKLEQELRhkeAQLKAQERHGSAEdrirglETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKlLSESNERLQVHLK 428
Cdd:COG4942 98 ELEAQKEELA---ELLRALYRLGRQP------PLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE-LRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 429 ERMHALDEKNALTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQLLQQEIAYNiQQTEALTRSLSPSSVVDPSG 508
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE-ALIARLEAEAAAAAERTPAA 246
|
....*
gi 442626410 509 AFSRS 513
Cdd:COG4942 247 GFAAL 251
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
257-634 |
1.95e-09 |
|
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: 62.00 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 257 AKTHELQTIIEkQTSELSQWQRRVSDLNNKISELEENMSRV---------QKEHCKAQDQCAKLQRDLREnvaQKEDQEE 327
Cdd:TIGR02168 152 AKPEERRAIFE-EAAGISKYKERRKETERKLERTRENLDRLedilnelerQLKSLERQAEKAERYKELKA---ELRELEL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 328 RITTLEKRYLNAQREST-----SLHDLNEKLEQELRHKEAQLKAQE-RHGSAEDRIRGLETNLDEKTNEVVRLNQRLkmn 401
Cdd:TIGR02168 228 ALLVLRLEELREELEELqeelkEAEEELEELTAELQELEEKLEELRlEVSELEEEIEELQKELYALANEISRLEQQK--- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 402 EEHNLRLSSTVDKLlSESNERLQVHLKERMHALDEKNALTQELEKARKVAEEL--HHEKSEIMKELSKTRL-----EIEN 474
Cdd:TIGR02168 305 QILRERLANLERQL-EELEAQLEELESKLDELAEELAELEEKLEELKEELESLeaELEELEAELEELESRLeeleeQLET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 475 FKR---QLLQQEIAYNIQQTEALTRslspssvvdpsgafsrsnshasfeTHSLRRQSKQRLSEENALVRSMAEQEWEKLQ 551
Cdd:TIGR02168 384 LRSkvaQLELQIASLNNEIERLEAR------------------------LERLEDRRERLQQEIEELLKKLEEAELKELQ 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 552 QAAHAQQQayELASAADCDDSdvlyaaatdmmspsghtdaqtlammLQEQLDAINNEIRLIQEEKQSTEARAEELESRVG 631
Cdd:TIGR02168 440 AELEELEE--ELEELQEELER-------------------------LEEALEELREELEEAEQALDAAERELAQLQARLD 492
|
...
gi 442626410 632 SLE 634
Cdd:TIGR02168 493 SLE 495
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
251-473 |
2.00e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 251 ELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHC---KAQDQCAKLQRDLRENVAQKEDQEE 327
Cdd:PRK03918 180 RLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKeleELKEEIEELEKELESLEGSKRKLEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 328 RITTLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQLKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLR 407
Cdd:PRK03918 260 KIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEER 339
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442626410 408 LSSTvDKLLSESNERLQVhLKERMHALDEKNALTQELEKARKVAEELHHEKSEIM-KELSKTRLEIE 473
Cdd:PRK03918 340 LEEL-KKKLKELEKRLEE-LEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKElEELEKAKEEIE 404
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
37-369 |
2.76e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.54 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 37 SMLDERDKLMDSL---REAQERLNETENKLRDVE-----KERDSLQRQInANLPQEFATLTKELTQARETLLERDEEIGE 108
Cdd:TIGR02169 191 LIIDEKRQQLERLrreREKAERYQALLKEKREYEgyellKEKEALERQK-EAIERQLASLEEELEKLTEEISELEKRLEE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 109 LKAERNNtrlLLEHLECLVSRHERSLRMTVVKRQAAAQSGVSSEVEVLKALKSLFEHHKALDEKvRERLRLSIEKnnmME 188
Cdd:TIGR02169 270 IEQLLEE---LNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE-IDKLLAEIEE---LE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 189 EELSSAKEELAQYKAGVvpagvgsgsgagsAATTAGGGGAENGLKEKMAGVGGSGGVNGEANE-LNDYAAKTHELQTIIE 267
Cdd:TIGR02169 343 REIEEERKRRDKLTEEY-------------AELKEELEDLRAELEEVDKEFAETRDELKDYREkLEKLKREINELKRELD 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 268 KQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQRESTslh 347
Cdd:TIGR02169 410 RLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELS--- 486
|
330 340
....*....|....*....|..
gi 442626410 348 dlneKLEQELRHKEAQLKAQER 369
Cdd:TIGR02169 487 ----KLQRELAEAEAQARASEE 504
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
40-474 |
5.49e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 5.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 40 DERDKLMDSLREAQERLNETENK---LRDVEKERDSLQRQInANLPQEFATLTKELTQARETLLERDEEIGELKAERNNT 116
Cdd:PRK02224 227 EQREQARETRDEADEVLEEHEERreeLETLEAEIEDLRETI-AETEREREELAEEVRDLRERLEELEEERDDLLAEAGLD 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 117 RL----LLEHLECLVSRHErSLRMTVVKRQAAAQsgvssevEVLKALKSLFEHHKALDEKVRErLRlsiEKNNMMEEELS 192
Cdd:PRK02224 306 DAdaeaVEARREELEDRDE-ELRDRLEECRVAAQ-------AHNEEAESLREDADDLEERAEE-LR---EEAAELESELE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 193 SAKEELAQYKA----------------GVVPAGVGSGSGAGSAATTAGGGGAENgLKEKMAGVGGSGGVNGEANELNDyA 256
Cdd:PRK02224 374 EAREAVEDRREeieeleeeieelrerfGDAPVDLGNAEDFLEELREERDELRER-EAELEATLRTARERVEEAEALLE-A 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 257 AKTHELQTIIEKQ--TSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDqCAKLQRDLRENVAQKEDQEERITTLEK 334
Cdd:PRK02224 452 GKCPECGQPVEGSphVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIERLEERREDLEELIAERRE 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 335 RyLNAQRES-TSLHDLNEKLEQELRHKEAQlkAQERHGSAED---RIRGLETNLDEKTNEVVRLNQ---RLKMNEEHNLR 407
Cdd:PRK02224 531 T-IEEKRERaEELRERAAELEAEAEEKREA--AAEAEEEAEEareEVAELNSKLAELKERIESLERirtLLAAIADAEDE 607
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442626410 408 LSSTVDKL--LSESNERLQVHLK---ERMHALDEK--NALTQELEKARKVAEELHHEKSEIMKELSKTRLEIEN 474
Cdd:PRK02224 608 IERLREKReaLAELNDERRERLAekrERKRELEAEfdEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQA 681
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
250-483 |
5.72e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.95 E-value: 5.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 250 NELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERI 329
Cdd:TIGR04523 61 KNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 330 TTLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQLKaqerhgSAEDRIRGLETNLDEKTNEVVRLNQRL----KMNEEHN 405
Cdd:TIGR04523 141 DKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELN------LLEKEKLNIQKNIDKIKNKLLKLELLLsnlkKKIQKNK 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442626410 406 LrLSSTVDKLLSESNErLQVHLKERMhalDEKNALTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQLLQQE 483
Cdd:TIGR04523 215 S-LESQISELKKQNNQ-LKDNIEKKQ---QEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELE 287
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
32-465 |
9.32e-08 |
|
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: 56.37 E-value: 9.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 32 EQLMVSMLDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINaNLPQ-------EFATLTKELTQARETLLERDE 104
Cdd:pfam10174 337 EQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIR-DLKDmldvkerKINVLQKKIENLQEQLRDKDK 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 105 EIGELK-------AERNNTRLLLEHLECLVSRHERslrmtvvkrqaaaqsgvsseveVLKALKslfEHHKALDEKVRERL 177
Cdd:pfam10174 416 QLAGLKervkslqTDSSNTDTALTTLEEALSEKER----------------------IIERLK---EQREREDRERLEEL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 178 RLSIEKNNMMEEELSSAKEELAQYKAGVVPAGVGSGSGAGSAATTAGGGGAENGLKEKmagvggsggVNGEANELNDYAA 257
Cdd:pfam10174 471 ESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQ---------KKEECSKLENQLK 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 258 KTHELQtiIEKQTSElsqwqrrvsDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYL 337
Cdd:pfam10174 542 KAHNAE--EAVRTNP---------EINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTL 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 338 NAQRESTSLHDLNEKLEQELRHKEAQLKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLkmnEEHNLRLSSTVDKLLS 417
Cdd:pfam10174 611 RQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQEL---DATKARLSSTQQSLAE 687
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442626410 418 ES--------------NERLQVHLKERMHALDEKNALTQELE----KARKVAEE---LHHEKSEIMKEL 465
Cdd:pfam10174 688 KDghltnlraerrkqlEEILEMKQEALLAAISEKDANIALLElsssKKKKTQEEvmaLKREKDRLVHQL 756
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
29-479 |
9.88e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 9.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 29 ANFEQLMVSMLDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQinANLPQEFATLTKELTQARETLLERDEEIGE 108
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKEL--KEKAEEYIKLSEFYEEYLDELREIEKRLSR 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 109 LKAERNNTRLLLEHLECLVSRherslrmtvVKRQAAAQSGVSSEVEVLKALKSLFEHHKALD---EKVRERLR-LSIEKN 184
Cdd:PRK03918 319 LEEEINGIEERIKELEEKEER---------LEELKKKLKELEKRLEELEERHELYEEAKAKKeelERLKKRLTgLTPEKL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 185 NMMEEELSSAKEELaqykagvvpagvgsgsgagsaattaggGGAENGLKEKMAGVGGSGGVNGEA-NELNDYAAKT---- 259
Cdd:PRK03918 390 EKELEELEKAKEEI---------------------------EEEISKITARIGELKKEIKELKKAiEELKKAKGKCpvcg 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 260 -----HELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQ---------DQCAKLQRDLRENVAQK--- 322
Cdd:PRK03918 443 relteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESeliklkelaEQLKELEEKLKKYNLEElek 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 323 -----EDQEERITTLEKRYLNAQRESTSLHDLN---EKLEQELRHKEAQLKAQERHGSA---------EDRIRGLE---- 381
Cdd:PRK03918 523 kaeeyEKLKEKLIKLKGEIKSLKKELEKLEELKkklAELEKKLDELEEELAELLKELEElgfesveelEERLKELEpfyn 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 382 ---------TNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESNERLQVHLKERMHAL-DEKNALTQELEKARKVA 451
Cdd:PRK03918 603 eylelkdaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELrEEYLELSRELAGLRAEL 682
|
490 500 510
....*....|....*....|....*....|....*...
gi 442626410 452 EELHHEKSEIMK----------ELSKTRLEIENFKRQL 479
Cdd:PRK03918 683 EELEKRREEIKKtleklkeeleEREKAKKELEKLEKAL 720
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
248-632 |
1.55e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.84 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 248 EANELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQdQCAKLQRDLRE-----NVAQK 322
Cdd:TIGR02169 154 ERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREyegyeLLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 323 EDQEERITTLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQLKAQERHGSA--EDRIRGLETNLDEKTNEVVRLNQRLKM 400
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlgEEEQLRVKEKIGELEAEIASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 401 NEEHNLRLSSTVDKLLSESNErlqvhLKERMHALD--------EKNALTQELEKARKVAEELHHEKSEIMKELSKTRLEI 472
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDK-----LLAEIEELEreieeerkRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 473 ENFKRQLlqqeiayniqqtEALTRSLSPSsvvdpsgafsrsNSHASFETHSLRRQSKQRLSEENALVRSMAEQ---EWEK 549
Cdd:TIGR02169 388 KDYREKL------------EKLKREINEL------------KRELDRLQEELQRLSEELADLNAAIAGIEAKInelEEEK 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 550 LQQAAHAQQQAYELASAADcddsdvlyaaatdMMSpsghtDAQTLAMMLQEQLDAINNEIRLIQEEKQSTEARAEELESR 629
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAA-------------DLS-----KYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
...
gi 442626410 630 VGS 632
Cdd:TIGR02169 506 VRG 508
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
320-464 |
1.64e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 55.17 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 320 AQKEDQEERittlEKRYLNAQREstsLHDLNEKLEQELRHKEAQLKAQERhgsaedRIRGLETNLDEKTNEVVRLNQRLK 399
Cdd:PRK12704 47 AKKEAEAIK----KEALLEAKEE---IHKLRNEFEKELRERRNELQKLEK------RLLQKEENLDRKLELLEKREEELE 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442626410 400 MNEEHNLRLSSTVDKLLSESNERLQVHLKErmhaLDEKNALTQELEKAR---KVAEELHHEKSEIMKE 464
Cdd:PRK12704 114 KKEKELEQKQQELEKKEEELEELIEEQLQE----LERISGLTAEEAKEIlleKVEEEARHEAAVLIKE 177
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
36-454 |
1.75e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 36 VSMLDERDKLMDSLREAQERLNETENKLRDVEKERdslqrqinanLPQEFATLTKELTQARETLLERDEEIGELKAERNN 115
Cdd:PRK03918 354 LEELEERHELYEEAKAKKEELERLKKRLTGLTPEK----------LEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 116 TRLLLEHLE-----CLVSRHERSL--RMTVVKRQAAAQSGVSSEVEVLKALKSLFEHHKALDEKVRERLRlSIEKNNMME 188
Cdd:PRK03918 424 LKKAIEELKkakgkCPVCGRELTEehRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES-ELIKLKELA 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 189 EELSSAKEELAQYKAgvvpagvgsgsgagsaATTAGGGGAENGLKEKMAG-VGGSGGVNGEANELNDYAAKTHELQTIIE 267
Cdd:PRK03918 503 EQLKELEEKLKKYNL----------------EELEKKAEEYEKLKEKLIKlKGEIKSLKKELEKLEELKKKLAELEKKLD 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 268 KQTSELSQWQRRVSDLNNK-ISELEENMSRVQKEHckaqdqcaklqrdlRENVAQKeDQEERITTLEKRYLNAQRESTSL 346
Cdd:PRK03918 567 ELEEELAELLKELEELGFEsVEELEERLKELEPFY--------------NEYLELK-DAEKELEREEKELKKLEEELDKA 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 347 HDLNEKLEQELRHKEAQLKAQERHGSaEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKllsesnerlqvh 426
Cdd:PRK03918 632 FEELAETEKRLEELRKELEELEKKYS-EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK------------ 698
|
410 420
....*....|....*....|....*...
gi 442626410 427 LKERMHALDEKNALTQELEKARKVAEEL 454
Cdd:PRK03918 699 LKEELEEREKAKKELEKLEKALERVEEL 726
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
279-644 |
1.89e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 279 RVSDLnnkISELEENMSRVQKEHCKAQD----QCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQREStslhdlnEKLE 354
Cdd:COG1196 190 RLEDI---LGELERQLEPLERQAEKAERyrelKEELKELEAELLLLKLRELEAELEELEAELEELEAEL-------EELE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 355 QELRHKEAQL-KAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLlsesNERLQVHLKERMHA 433
Cdd:COG1196 260 AELAELEAELeELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL----EEELAELEEELEEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 434 LDEKNALTQELEKARKVAEELhhekSEIMKELSKTRLEIENFKRQLLQQEIAYNIQQTEALTRSLSpssvvdpsgafsrs 513
Cdd:COG1196 336 EEELEELEEELEEAEEELEEA----EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE-------------- 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 514 nshasfetHSLRRQSKQRLSEENALVRSMAEQEWEKLQQAAHAQQQAYELASAADCDDSdvlyaaatdmmspSGHTDAQT 593
Cdd:COG1196 398 --------LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA-------------EEEAELEE 456
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 442626410 594 LAMMLQEQLDAINNEIRLIQEEKQSTEARAEELESRVGSLEHVNLLARGRS 644
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL 507
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
40-494 |
2.05e-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: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 40 DERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINaNLPQEFATLTKELTQARETLLERDEEIGELKAERNNTRLL 119
Cdd:TIGR04523 124 VELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYN-DLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 120 LEHLECLVSRHeRSLRMTVVKrqaaAQSGVSSEVEVLKALKSLFEHHKALDEKVRERLRLSIEKNNMMEEELSSAKEELA 199
Cdd:TIGR04523 203 LSNLKKKIQKN-KSLESQISE----LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 200 QYKAgvvpagvgsgsgagsaattaGGGGAENGLKEkmagvggsggVNGEANELNDYAAK--THELQTIIEKQ-------T 270
Cdd:TIGR04523 278 QNNK--------------------KIKELEKQLNQ----------LKSEISDLNNQKEQdwNKELKSELKNQekkleeiQ 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 271 SELSQWQRRVSDLNNKISELEE-------NMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQRES 343
Cdd:TIGR04523 328 NQISQNNKIISQLNEQISQLKKeltnsesENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLN 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 344 TSLHDLNEKLEQELRHKEAQ---LKAQERhgSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESn 420
Cdd:TIGR04523 408 QQKDEQIKKLQQEKELLEKEierLKETII--KNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNL- 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 421 ERLQVHLKERMHALDEKNALTQELEKARKV-----------AEELHHEKSEIMKELSKTRLEIE----NFKRQLLQQEIA 485
Cdd:TIGR04523 485 EQKQKELKSKEKELKKLNEEKKELEEKVKDltkkisslkekIEKLESEKKEKESKISDLEDELNkddfELKKENLEKEID 564
|
....*....
gi 442626410 486 YNIQQTEAL 494
Cdd:TIGR04523 565 EKNKEIEEL 573
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
14-464 |
2.39e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 14 EDSISQRSSQFSGEDANFEQL--MVSMLDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINAnlpqefatLTKE 91
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELeeKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING--------IEER 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 92 LtqarETLLERDEEIGELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAAAQSGVSSEVEVLKALKSLFEHHKALDE 171
Cdd:PRK03918 330 I----KELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEE 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 172 KVRE------RLRLSIEKNNMMEEELSSAK----------------EELAQYKAGVVPAGVGSGSGAGSAATTAGGGGA- 228
Cdd:PRK03918 406 EISKitarigELKKEIKELKKAIEELKKAKgkcpvcgrelteehrkELLEEYTAELKRIEKELKEIEEKERKLRKELREl 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 229 ENGLKE--------KMAGVGGSGGVNGEANELNDYAAKTHELQTIIEKqTSELSQWQRRVSDLNNKISELEENMSRVQKE 300
Cdd:PRK03918 486 EKVLKKeseliklkELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEK-LIKLKGEIKSLKKELEKLEELKKKLAELEKK 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 301 HCKAQDQCAKLQRDLRE-NVAQKEDQEERITTLEKRY------LNAQRESTSLHDLNEKLEQELRHKEAQL-KAQERHGS 372
Cdd:PRK03918 565 LDELEEELAELLKELEElGFESVEELEERLKELEPFYneylelKDAEKELEREEKELKKLEEELDKAFEELaETEKRLEE 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 373 AEDRIRGLETNLDEKTNEVVRlnqrlkmnEEHnLRLSSTVDKLLSESnERLQVHLKERMHALDEknaLTQELEKARKVAE 452
Cdd:PRK03918 645 LRKELEELEKKYSEEEYEELR--------EEY-LELSRELAGLRAEL-EELEKRREEIKKTLEK---LKEELEEREKAKK 711
|
490
....*....|..
gi 442626410 453 ELhhEKSEIMKE 464
Cdd:PRK03918 712 EL--EKLEKALE 721
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
899-965 |
2.39e-07 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 48.83 E-value: 2.39e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442626410 899 FALWNGPTIVAWLELWvGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 965
Cdd:smart00454 1 VSQWSPESVADWLESI-GLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
1072-1142 |
3.01e-07 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 48.42 E-value: 3.01e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442626410 1072 VLVWSNERVIRWVGSIGLKEYANNLLESGVHGGLMALdeGFDANAMGlalQIPTQNAQARQILDTEFNNLL 1142
Cdd:pfam07647 1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK---RLGITSVGHRRKILKKIQELK 66
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
93-478 |
3.08e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.07 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 93 TQARETLLERDEEIGELKAERNNTRLLLEHLECLVsrHERSLRMTVVKRQAAAqsgVSSEVEVLKAlkslfEHhkaldEK 172
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRL--DELSQELSDASRKIGE---IEKEIEQLEQ-----EE-----EK 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 173 VRERLRLSIEKNNMMEEELSSAKEELAQYkAGVVPAGVGSGSGAGSAATTAGGGGAENGLKEKMAgvggsggvngEANEL 252
Cdd:TIGR02169 735 LKERLEELEEDLSSLEQEIENVKSELKEL-EARIEELEEDLHKLEEALNDLEARLSHSRIPEIQA----------ELSKL 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 253 NDYAAK----THELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEhckaqdqCAKLQRDLRENVAQKEDQEER 328
Cdd:TIGR02169 804 EEEVSRiearLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE-------IENLNGKKEELEEELEELEAA 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 329 ITTLEKRYlnaqrestslhdlnEKLEQELRHKEAQLKAQERhgsaedRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRL 408
Cdd:TIGR02169 877 LRDLESRL--------------GDLKKERDELEAQLRELER------KIEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442626410 409 SSTVDKLLSESNERLQV--------HLKERMHALDEKNALT-QELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQ 478
Cdd:TIGR02169 937 EDPKGEDEEIPEEELSLedvqaelqRVEEEIRALEPVNMLAiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
55-480 |
3.85e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 55 RLNETENKLRDVEkERDSLQRQI-------NA--NLpQEFATLTKELTQARETLLERDEEIGELKaeRNNTRLLLEHLec 125
Cdd:PRK03918 133 RQGEIDAILESDE-SREKVVRQIlglddyeNAykNL-GEVIKEIKRRIERLEKFIKRTENIEELI--KEKEKELEEVL-- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 126 lvsrHERSLRMTVVKRQAAAQSGVSSEVEVLKALKSLFEHHKALDEKVRERLRLSIEKNNMMEEELSSAKEELAQYKAGV 205
Cdd:PRK03918 207 ----REINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 206 vpagvgsgsgagsaattAGGGGAENGLKEKMAGVGGSGGVNGEANELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNN 285
Cdd:PRK03918 283 -----------------KELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKK 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 286 KISELEENMSRVQKEHckaqdqcaKLQRDLRENVAQKEDQEERITTLEKRYLNAQRESTslhdlnEKLEQELRHKEAQLK 365
Cdd:PRK03918 346 KLKELEKRLEELEERH--------ELYEEAKAKKEELERLKKRLTGLTPEKLEKELEEL------EKAKEEIEEEISKIT 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 366 aqERHGSAEDRIRGLETNLDE--KTNEVVRLNQRLkMNEEHNLRLSSTVDKLLSESNERLQV------HLKERMHALDEK 437
Cdd:PRK03918 412 --ARIGELKKEIKELKKAIEElkKAKGKCPVCGRE-LTEEHRKELLEEYTAELKRIEKELKEieekerKLRKELRELEKV 488
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 442626410 438 NALTQELEKARKVAEELHHEKSEI----MKELSKTRLEIENFKRQLL 480
Cdd:PRK03918 489 LKKESELIKLKELAEQLKELEEKLkkynLEELEKKAEEYEKLKEKLI 535
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
9-526 |
4.15e-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: 4.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 9 MPTISEDSISQRS---SQFSGEDANFEQLMVSMLDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQiNANLPQEF 85
Cdd:pfam15921 301 LEIIQEQARNQNSmymRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQE-SGNLDDQL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 86 ATL-------TKELTQARET---LLERDE----EIGELKAERNNTRLLLEHLECLVsRHERSLRMTVVKRQAAAQSGVSS 151
Cdd:pfam15921 380 QKLladlhkrEKELSLEKEQnkrLWDRDTgnsiTIDHLRRELDDRNMEVQRLEALL-KAMKSECQGQMERQMAAIQGKNE 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 152 EVEVLKALKSLFEHHKALDEKVRERL---RLSIEKN---------NMMEEE--LSSAKEELAQYKAGVVPAGVGSGSGAG 217
Cdd:pfam15921 459 SLEKVSSLTAQLESTKEMLRKVVEELtakKMTLESSertvsdltaSLQEKEraIEATNAEITKLRSRVDLKLQELQHLKN 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 218 SAATTAGGGGAENGLKEKMAGVGGSGGVNGEA--------------------------NELNDYAAKTHELQTIIEKQTS 271
Cdd:pfam15921 539 EGDHLRNVQTECEALKLQMAEKDKVIEILRQQienmtqlvgqhgrtagamqvekaqleKEINDRRLELQEFKILKDKKDA 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 272 ELSQWQRRVSDLNNKISELEENMS---RVQKEHCKAQDQcakLQRDLRENVAQKEDQEERITTLEKRYLNAQRE-STSLH 347
Cdd:pfam15921 619 KIRELEARVSDLELEKVKLVNAGSerlRAVKDIKQERDQ---LLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEmETTTN 695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 348 DLNEKL---EQELRHKEAQLKAQE-RHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESNERL 423
Cdd:pfam15921 696 KLKMQLksaQSELEQTRNTLKSMEgSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLS 775
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 424 QvhlkERMHALDEKNALTQELEKARKVAEELHHEKSEIMKELSKTRL---EIENFKRQLLQQEIAYNIQQTEALT----- 495
Cdd:pfam15921 776 Q----ELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLqfaECQDIIQRQEQESVRLKLQHTLDVKelqgp 851
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 442626410 496 ----------RSLSPSSVVDPSGAFSRSNSHASFETHSLRR 526
Cdd:pfam15921 852 gytsnssmkpRLLQPASFTRTHSNVPSSQSTASFLSHHSRK 892
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
38-620 |
1.11e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.20 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 38 MLDERDKLMDSLREA----QERLNETENKLRDVEK-------ERDSLQ----RQINANLPQEFATLTKELTQARETLLER 102
Cdd:pfam15921 164 MLEDSNTQIEQLRKMmlshEGVLQEIRSILVDFEEasgkkiyEHDSMStmhfRSLGSAISKILRELDTEISYLKGRIFPV 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 103 DEEIGELKAE-RNNTRLLLEH----LECLVSRHERSLRMTVVKRQAAAQ--SGVSSEVEV------------LKALKSLF 163
Cdd:pfam15921 244 EDQLEALKSEsQNKIELLLQQhqdrIEQLISEHEVEITGLTEKASSARSqaNSIQSQLEIiqeqarnqnsmyMRQLSDLE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 164 EHHKALDEKVRERLRLSIEKNNMMEEELSSAKEELAQYKAgvvpagvgsgsgaGSAATTAGGGGAENGLKEKMAGVGGSG 243
Cdd:pfam15921 324 STVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEART-------------ERDQFSQESGNLDDQLQKLLADLHKRE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 244 GVNGEANELNDYAAKTHELQTIIekqtseLSQWQRRVSDLNNKISELEEnMSRVQKEHCKAQ--DQCAKLQrdlrenvaQ 321
Cdd:pfam15921 391 KELSLEKEQNKRLWDRDTGNSIT------IDHLRRELDDRNMEVQRLEA-LLKAMKSECQGQmeRQMAAIQ--------G 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 322 KEDQEERITTLekrylNAQRESTSlhDLNEKLEQELRHKEAQLKAQERH-----GSAEDRIRGLETNLDEKTNEVVRLN- 395
Cdd:pfam15921 456 KNESLEKVSSL-----TAQLESTK--EMLRKVVEELTAKKMTLESSERTvsdltASLQEKERAIEATNAEITKLRSRVDl 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 396 -----QRLKMNEEHNLRLSSTVDKLlsesneRLQVHLKERMHAL--DEKNALTQELEKARKVAEELHHEKSEIMKELSKT 468
Cdd:pfam15921 529 klqelQHLKNEGDHLRNVQTECEAL------KLQMAEKDKVIEIlrQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDR 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 469 RLEIENFKrqLLQQEIAYNIQQTEALTRSLSPSSV--VDPSGAFSRSNSHASFETHSLRRQSKQRLSEENALvrsmaEQE 546
Cdd:pfam15921 603 RLELQEFK--ILKDKKDAKIRELEARVSDLELEKVklVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSL-----SED 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 547 WEKLQQAAHAQQQAYE-----LASAADCDDSDVLYAAAT--DMMSPSGHtdAQTLAMMLQEQLDAINNEIRLIQEEKQST 619
Cdd:pfam15921 676 YEVLKRNFRNKSEEMEtttnkLKMQLKSAQSELEQTRNTlkSMEGSDGH--AMKVAMGMQKQITAKRGQIDALQSKIQFL 753
|
.
gi 442626410 620 E 620
Cdd:pfam15921 754 E 754
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
37-424 |
1.42e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 37 SMLDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQI------NANLPQEFATLTKELTQARETLLER-------D 103
Cdd:PRK02224 311 AVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDAddleerAEELREEAAELESELEEAREAVEDRreeieelE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 104 EEIGELKAERNNTRLLLE----HLECLVSRHERslrmtVVKRQAAAQSGVSSEVEVLKALKSLFE--------------- 164
Cdd:PRK02224 391 EEIEELRERFGDAPVDLGnaedFLEELREERDE-----LREREAELEATLRTARERVEEAEALLEagkcpecgqpvegsp 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 165 HHKALDEKVRERLRLSIEKNNmMEEELSSAKEELAQYKAGVVPAGVGSGSGAGSAATTAGGGGAENGLKEKmagVGGSGG 244
Cdd:PRK02224 466 HVETIEEDRERVEELEAELED-LEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEK---RERAEE 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 245 VNGEANELNDYAAKTHELQTiieKQTSELSQWQRRVSDLNNKISELEENMSRVqkehckaqdqcaklqRDLRENVAQKED 324
Cdd:PRK02224 542 LRERAAELEAEAEEKREAAA---EAEEEAEEAREEVAELNSKLAELKERIESL---------------ERIRTLLAAIAD 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 325 QEERITTL-EKRYLNAQRESTSLHDLNEKLE--QELR--HKEAQL-KAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRL 398
Cdd:PRK02224 604 AEDEIERLrEKREALAELNDERRERLAEKRErkRELEaeFDEARIeEAREDKERAEEYLEQVEEKLDELREERDDLQAEI 683
|
410 420
....*....|....*....|....*...
gi 442626410 399 KMNEEHNLRLSSTVDKL--LSESNERLQ 424
Cdd:PRK02224 684 GAVENELEELEELRERReaLENRVEALE 711
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
255-488 |
1.45e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.76 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 255 YAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVaqkedqeERITTLEK 334
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK-------ERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 335 RYLNAQRESTSLHDLNEKLEQELRHKEAQL-KAQERHGSAEDRIRG-----LETNLDEKTNEVVRLNQRL-----KMNEE 403
Cdd:TIGR02169 745 DLSSLEQEIENVKSELKELEARIEELEEDLhKLEEALNDLEARLSHsripeIQAELSKLEEEVSRIEARLreieqKLNRL 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 404 HNLR--LSSTVDKLLSESNErLQVHLKERMHALDEKNA----LTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKR 477
Cdd:TIGR02169 825 TLEKeyLEKEIQELQEQRID-LKEQIKSIEKEIENLNGkkeeLEEELEELEAALRDLESRLGDLKKERDELEAQLRELER 903
|
250
....*....|.
gi 442626410 478 QLLQQEIAYNI 488
Cdd:TIGR02169 904 KIEELEAQIEK 914
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
261-430 |
1.57e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.69 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 261 ELQTIIEKQT--SELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLN 338
Cdd:COG1579 5 DLRALLDLQEldSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 339 AQrestslhdlNEKLEQELRHKEAQLKaqERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSE 418
Cdd:COG1579 85 VR---------NNKEYEALQKEIESLK--RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
170
....*....|..
gi 442626410 419 SNERLQVHLKER 430
Cdd:COG1579 154 LEAELEELEAER 165
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
14-479 |
2.08e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.94 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 14 EDSISQRSSQFSGEDA---NFEQLMVSMLDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQI-----------NA 79
Cdd:TIGR04523 231 KDNIEKKQQEINEKTTeisNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEIsdlnnqkeqdwNK 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 80 NLPQEFATLTKELTQARETLLERDEEIGELKAERNNTRLLLEHLECLVSRHERSLRmtvvKRQaaaqsgvsSEVEVLKAL 159
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELE----EKQ--------NEIEKLKKE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 160 K-SLFEHHKALDEKVRErLRLSIEKNNMMEEELSSAKEELAQykagvvpagvgsgsgagsaattaggggaENGLKEKmag 238
Cdd:TIGR04523 379 NqSYKQEIKNLESQIND-LESKIQNQEKLNQQKDEQIKKLQQ----------------------------EKELLEK--- 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 239 vggsggvngeanELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLREN 318
Cdd:TIGR04523 427 ------------EIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSK 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 319 VAQKEDQEERITTLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQLKAQERHGSAED---RIRGLETNLDEKTNEVVRLN 395
Cdd:TIGR04523 495 EKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDfelKKENLEKEIDEKNKEIEELK 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 396 QRLKMNEEHNLRLSSTVDKLLSESNErlqvhLKERMHALDEKNA-LTQELEKARKVAEELHHEKSEIMKELSKTRLEIEN 474
Cdd:TIGR04523 575 QTQKSLKKKQEEKQELIDQKEKEKKD-----LIKEIEEKEKKISsLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
....*
gi 442626410 475 FKRQL 479
Cdd:TIGR04523 650 IKETI 654
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
30-634 |
2.20e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.04 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 30 NFEQLMVSMLDERDKLMDSLREAQERLNETENKLRDVEKERDSlQRQINANLPQEFATltkELTQARETLLERDEEIGEL 109
Cdd:pfam15921 114 DLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEA-AKCLKEDMLEDSNT---QIEQLRKMMLSHEGVLQEI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 110 KA-----ERNNTRLLLEHlECLVSRHERSLRMTVVKrqaaaqsgvsseveVLKALKSLFEHHKALDEKVRERLR-LSIEK 183
Cdd:pfam15921 190 RSilvdfEEASGKKIYEH-DSMSTMHFRSLGSAISK--------------ILRELDTEISYLKGRIFPVEDQLEaLKSES 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 184 NNMMEEELSSAKEELAQYKAgvvpagvgsgsgagsaattaGGGGAENGLKEKMAGVGGsggvngEANELNDyaakthELQ 263
Cdd:pfam15921 255 QNKIELLLQQHQDRIEQLIS--------------------EHEVEITGLTEKASSARS------QANSIQS------QLE 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 264 TIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHckaQDQCAKLQRDLRenVAQKEDQEERitTLEKRYlnaQRES 343
Cdd:pfam15921 303 IIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMY---EDKIEELEKQLV--LANSELTEAR--TERDQF---SQES 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 344 TSLHDLNEKLEQELRHKEAQLK-AQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKmneehnlRLSSTVDKLLSESner 422
Cdd:pfam15921 373 GNLDDQLQKLLADLHKREKELSlEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQ-------RLEALLKAMKSEC--- 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 423 lQVHLKERMHALDEKNaltQELEKARKVAEELHHEKS---EIMKELSKTRLEIENFKRQLlqQEIAYNIQQTEaltRSLS 499
Cdd:pfam15921 443 -QGQMERQMAAIQGKN---ESLEKVSSLTAQLESTKEmlrKVVEELTAKKMTLESSERTV--SDLTASLQEKE---RAIE 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 500 PSSvVDPSGAFSRSNshasfethsLRRQSKQRLSEENALVRSmAEQEWEKLQQAAHAQQQAYElasaadcddsdVLYAAA 579
Cdd:pfam15921 514 ATN-AEITKLRSRVD---------LKLQELQHLKNEGDHLRN-VQTECEALKLQMAEKDKVIE-----------ILRQQI 571
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 580 TDMMSPSGHTDAQTLAMMLQE-QLDAINNEIRLIQEE----KQSTEARAEELESRVGSLE 634
Cdd:pfam15921 572 ENMTQLVGQHGRTAGAMQVEKaQLEKEINDRRLELQEfkilKDKKDAKIRELEARVSDLE 631
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
43-479 |
2.37e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 43 DKLMDSLREAQERLNETENKLRDVEKERDSLQRQINanlpqEFATLTKELTQARETLLERDEEIGELKAERNNTRLLLEH 122
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREIN-----EISSELPELREELEKLEKEVKELEELKEEIEELEKELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 123 LECLVSRHERSLRMTvvkrqaaaQSGVSSEVEVLKALKSLFEHHKALDEKVRERLRLSIEKNNMmEEELSSAKEELAQYK 202
Cdd:PRK03918 250 LEGSKRKLEEKIREL--------EERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEY-LDELREIEKRLSRLE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 203 AGVvpagvgsgsgagsaattaggggaeNGLKEKMAgvggsggvngEANELNDYAAKTHELQTIIEKQTSELSQWQRrvsd 282
Cdd:PRK03918 321 EEI------------------------NGIEERIK----------ELEEKEERLEELKKKLKELEKRLEELEERHE---- 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 283 LNNKISELEENMSRVQKEhcKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQRESTSLHDLNEKLE-------- 354
Cdd:PRK03918 363 LYEEAKAKKEELERLKKR--LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkcpv 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 355 --QEL-RHKEAQLKAQ--ERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKmNEEHNLRLSSTVDkLLSESNERLQVHLKE 429
Cdd:PRK03918 441 cgRELtEEHRKELLEEytAELKRIEKELKEIEEKERKLRKELRELEKVLK-KESELIKLKELAE-QLKELEEKLKKYNLE 518
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 442626410 430 RmhaLDEKNALTQEL-EKARKVAEELHHEKSEI--MKELSKTRLEIENFKRQL 479
Cdd:PRK03918 519 E---LEKKAEEYEKLkEKLIKLKGEIKSLKKELekLEELKKKLAELEKKLDEL 568
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
995-1049 |
3.31e-06 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 45.75 E-value: 3.31e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 442626410 995 WLPGLGLPQYRTTFMECLVDARMLDHLTKKDLRGQLKMVDSFHRTSLQYGISMLK 1049
Cdd:smart00454 12 WLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
49-499 |
3.38e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 49 LREAQERLNETENKLRDVEKERDSLQRQINANLPQ-EFATLTKELTQARETLLERDEEIGELKAERNNTRLLLEHLECLV 127
Cdd:PRK02224 164 LEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEkEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 128 SRHERSLrmtvvkrqaaaqsgvsSEVEVLKALKSLFEHHKALDEKVRERLRLSIEKNNMMEEELSSAKEELAqykagvvp 207
Cdd:PRK02224 244 EEHEERR----------------EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLL-------- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 208 agvgsgsgagsaattaggggAENGLkekmagvggsggvngEANELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKI 287
Cdd:PRK02224 300 --------------------AEAGL---------------DDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEA 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 288 SELEENMSRVQKEHCKAQDQCAKLQ-------RDLRENVAQKEDQEERITTLEKRYLNAQRESTSLHDLNEKLEQE---L 357
Cdd:PRK02224 345 ESLREDADDLEERAEELREEAAELEseleearEAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREErdeL 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 358 RHKEAQLKA-------------------------QERHGS--------AEDRIRGLETNLDEKTNEVVRLNQRLKMNEEH 404
Cdd:PRK02224 425 REREAELEAtlrtarerveeaealleagkcpecgQPVEGSphvetieeDRERVEELEAELEDLEEEVEEVEERLERAEDL 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 405 nLRLSSTVDKLL---SESNERLQVH---LKERMHALDEKNALTQELEKArkvAEELHHEKSEIMKELSKTRLEIENFKRQ 478
Cdd:PRK02224 505 -VEAEDRIERLEerrEDLEELIAERretIEEKRERAEELRERAAELEAE---AEEKREAAAEAEEEAEEAREEVAELNSK 580
|
490 500
....*....|....*....|.
gi 442626410 479 LlqQEIAYNIQQTEALTRSLS 499
Cdd:PRK02224 581 L--AELKERIESLERIRTLLA 599
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
44-635 |
3.67e-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: 51.51 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 44 KLMDSLREAQERLNETENKLRDVEK---ERDSLQRQINANLP--QEFATLTKELTQARETL------------LERDEEI 106
Cdd:TIGR00618 226 KELKHLREALQQTQQSHAYLTQKREaqeEQLKKQQLLKQLRAriEELRAQEAVLEETQERInrarkaaplaahIKAVTQI 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 107 gELKAERNNTRLLLEHLECLVSRHERSlrmTVVKRQAAAQSGVSSEVEVLKA---------LKSLFEHHKALDEKVRERL 177
Cdd:TIGR00618 306 -EQQAQRIHTELQSKMRSRAKLLMKRA---AHVKQQSSIEEQRRLLQTLHSQeihirdaheVATSIREISCQQHTLTQHI 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 178 RLSIEKNNMMEEELSSAKEELAQYKAgvvpagvgsgsgagSAATTAGGGGAENGLKEKMAGVGGSGGVNGEANELND-YA 256
Cdd:TIGR00618 382 HTLQQQKTTLTQKLQSLCKELDILQR--------------EQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAaAI 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 257 AKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQ----------E 326
Cdd:TIGR00618 448 TCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPArqdidnpgplT 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 327 ERITTLEKRYLNAQRESTSL-HDLNEKLEQELRHKEAQLKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHN 405
Cdd:TIGR00618 528 RRMQRGEQTYAQLETSEEDVyHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAE 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 406 LRLSSTVDKLLSESNERL---QVHLKERMHALDEKNALTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQLLQQ 482
Cdd:TIGR00618 608 DMLACEQHALLRKLQPEQdlqDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQS 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 483 EIAYNIQQTEALTRSLS-PSSVVDPSGAFSRSNSHASFETHSLRRQSKQRLSEENALVRSMAEQEWEKLQQAAHAQQQAY 561
Cdd:TIGR00618 688 EKEQLTYWKEMLAQCQTlLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNN 767
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 562 ELASAADCDDSDVLYAAAT-----DMMSPSGHTDAQTLAMMLQ---EQLDAINNEIRLIQEEKQSTEARAEELESRVGSL 633
Cdd:TIGR00618 768 EEVTAALQTGAELSHLAAEiqffnRLREEDTHLLKTLEAEIGQeipSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEI 847
|
..
gi 442626410 634 EH 635
Cdd:TIGR00618 848 TH 849
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
333-492 |
3.84e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.93 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 333 EKRYLNAQRESTSLHDlNEKLEQELRHKEAQLKAQERhgsAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEhnlrlssTV 412
Cdd:PRK12704 30 EAKIKEAEEEAKRILE-EAKKEAEAIKKEALLEAKEE---IHKLRNEFEKELRERRNELQKLEKRLLQKEE-------NL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 413 DKLLsESNERLQVHLKERMHALDEKnalTQELEKARKVAEELHHEKSEIMKELSKtrLEIENFKRQLLQQ-------EIA 485
Cdd:PRK12704 99 DRKL-ELLEKREEELEKKEKELEQK---QQELEKKEEELEELIEEQLQELERISG--LTAEEAKEILLEKveeearhEAA 172
|
....*..
gi 442626410 486 YNIQQTE 492
Cdd:PRK12704 173 VLIKEIE 179
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
272-399 |
7.62e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 7.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 272 ELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQ-EERITTLEKRYLNAQRESTSLHDLN 350
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQlEREIERLERELEERERRRARLEALL 368
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 442626410 351 EKLEQELRH-----KEAQLKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLK 399
Cdd:COG4913 369 AALGLPLPAsaeefAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
|
|
| SAM_superfamily |
cd09487 |
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
995-1045 |
8.66e-06 |
|
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.
Pssm-ID: 188886 [Multi-domain] Cd Length: 56 Bit Score: 44.15 E-value: 8.66e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 442626410 995 WLPGLGLPQYRTTFMECLVDARMLDHLTKKDLRgQLKMVDSFHRTSLQYGI 1045
Cdd:cd09487 5 WLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
262-488 |
1.11e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 262 LQTIIEKQTSELSQWQRRVSDLN-NKISELEENMSRVQKEHckaqDQCAKLQRDLRENVAQKEDQEERITTLEKRY--LN 338
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNlKELKELEEELKEAEEKE----EEYAELQEELEELEEELEELEAELEELREELekLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 339 AQRESTSLHDLNEKLEQELRHKEAQLKAQERHgsaEDRIRGLETNLDEKTNEVVRLNQRLkmnEEHNLRLSSTVDKLLSE 418
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELPERLEELEER---LEELRELEEELEELEAELAELQEEL---EELLEQLSLATEEELQD 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 419 SNERLQvhlkermHALDEKNALTQELEKARKVAEELHHEKSEImkelsKTRLEIENFKRQLLQQEIAYNI 488
Cdd:COG4717 197 LAEELE-------ELQQRLAELEEELEEAQEELEELEEELEQL-----ENELEAAALEERLKEARLLLLI 254
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
50-203 |
1.67e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.61 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 50 REAQERLNEtenkLRDVEKERDSLQRQInANLPQEFATLTKELTQARETLLERDEEIGELKAERNNTRLLLEHLECLVSR 129
Cdd:COG1579 3 PEDLRALLD----LQELDSELDRLEHRL-KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442626410 130 HERslRMTVVK--RQAAAqsgVSSEVEVLKALKSLFEHH-KALDEKVrERLRLSIEKnnmMEEELSSAKEELAQYKA 203
Cdd:COG1579 78 YEE--QLGNVRnnKEYEA---LQKEIESLKRRISDLEDEiLELMERI-EELEEELAE---LEAELAELEAELEEKKA 145
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
256-498 |
1.78e-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: 49.02 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 256 AAKTHELQTI---IEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCaklqRDLRENV-AQKEDQEERI-T 330
Cdd:pfam01576 239 AKKEEELQAAlarLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQR----RDLGEELeALKTELEDTLdT 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 331 TLEKRYLNAQREsTSLHDLNEKLEQELRHKEAQLKA-QERHGSA------------------EDRIRGLETNLDEKTNEV 391
Cdd:pfam01576 315 TAAQQELRSKRE-QEVTELKKALEEETRSHEAQLQEmRQKHTQAleelteqleqakrnkanlEKAKQALESENAELQAEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 392 VRLNQRLKMNEEHNLRLSSTVDKLLSESN--ERLQVHLKERMHALD-EKNALTQELEKARKVAEELHHEKSEIMKELSKT 468
Cdd:pfam01576 394 RTLQQAKQDSEHKRKKLEGQLQELQARLSesERQRAELAEKLSKLQsELESVSSLLNEAEGKNIKLSKDVSSLESQLQDT 473
|
250 260 270
....*....|....*....|....*....|
gi 442626410 469 RLEIENFKRQLLQqeIAYNIQQTEALTRSL 498
Cdd:pfam01576 474 QELLQEETRQKLN--LSTRLRQLEDERNSL 501
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
346-464 |
2.57e-05 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 46.42 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 346 LHDLNEKLEQELRHKEAQLKAQERhgsaedRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESNERLQv 425
Cdd:pfam12072 62 IHKLRAEAERELKERRNELQRQER------RLLQKEETLDRKDESLEKKEESLEKKEKELEAQQQQLEEKEEELEELIE- 134
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 442626410 426 hlkERMHALDEKNALTQELEKAR---KVAEELHHEKSEIMKE 464
Cdd:pfam12072 135 ---EQRQELERISGLTSEEAKEIlldEVEEELRHEAAVMIKE 173
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
257-499 |
2.70e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.63 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 257 AKTHELQTIIEKQTselsQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRY 336
Cdd:pfam01576 9 AKEEELQKVKERQQ----KAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 337 LNAQRESTSLHDLNEKLEQELRHKEAQLKAQErhgSAEDRIRGLETNLDEKtneVVRLNQRLKMNEEHNLRLSSTvDKLL 416
Cdd:pfam01576 85 EEEEERSQQLQNEKKKMQQHIQDLEEQLDEEE---AARQKLQLEKVTTEAK---IKKLEEDILLLEDQNSKLSKE-RKLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 417 SESNERLQVHLKERmhalDEKnalTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQL------LQQEIAYNIQQ 490
Cdd:pfam01576 158 EERISEFTSNLAEE----EEK---AKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLegestdLQEQIAELQAQ 230
|
....*....
gi 442626410 491 TEALTRSLS 499
Cdd:pfam01576 231 IAELRAQLA 239
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
27-634 |
3.88e-05 |
|
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: 48.13 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 27 EDANFEQLMVSMLDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINA------NLPQEFATLTKELTQARETLL 100
Cdd:TIGR02168 310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEleaeleELESRLEELEEQLETLRSKVA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 101 ERDEEIGELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAAAQSGVSSEVEVLKA-LKSLFEHHKALDEKVrERLRL 179
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEeLEELQEELERLEEAL-EELRE 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 180 SIEKNnmmEEELSSAKEELAQYKAGVVPAGVGSGSGAGSAATTAGGGGAENGLKEKMAGVGGSGGVNGE---ANE----- 251
Cdd:TIGR02168 469 ELEEA---EQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGyeaAIEaalgg 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 252 -LNDYAAKTHELQ-TIIE--KQTS-------ELSQWQRRVSDLNNK-ISELEENMSRVQKEHCKAQDQCAKLQRDLRENV 319
Cdd:TIGR02168 546 rLQAVVVENLNAAkKAIAflKQNElgrvtflPLDSIKGTEIQGNDReILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGV 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 320 ------------AQKEDQEERITTLEKRYLNAQ------RESTSLHDLNEKleQELRHKEAQLKAQERH-GSAEDRIRGL 380
Cdd:TIGR02168 626 lvvddldnalelAKKLRPGYRIVTLDGDLVRPGgvitggSAKTNSSILERR--REIEELEEKIEELEEKiAELEKALAEL 703
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 381 ETNLDEKTNEVVRLNQRlkmnEEHNLRLSSTVDKLLSESNERLQVHLKERMHALDEKNALTQELEKARKVAEELHHEKSE 460
Cdd:TIGR02168 704 RKELEELEEELEQLRKE----LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 461 IMKELSKTRLEIENFKRQLLQQEIAYNIQQTEAltrslspssvvdpsgafsrSNSHASFETHSLRRQSKQRLSEENALVR 540
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREALDELRAEL-------------------TLLNEEAANLRERLESLERRIAATERRL 840
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 541 SMAEQEWEKLQQAAHAQQQAYELASAADCDDSDVLYAAATDMMSpsghtdAQTLAMMLQEQLDAINNEIRLIQEEKQSTE 620
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS------LEEALALLRSELEELSEELRELESKRSELR 914
|
650
....*....|....
gi 442626410 621 ARAEELESRVGSLE 634
Cdd:TIGR02168 915 RELEELREKLAQLE 928
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
251-453 |
4.67e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 4.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 251 ELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLREnvaQKEDQEERIT 330
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE---RREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 331 TLEKR-----YLNAQRESTSLHDLNEKLEQELRHKEAQLKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKmneehn 405
Cdd:COG3883 94 ALYRSggsvsYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELE------ 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 442626410 406 lRLSSTVDKLLSESNERLQVHLKERMHALDEKNALTQELEKARKVAEE 453
Cdd:COG3883 168 -AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
22-162 |
4.97e-05 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 45.66 E-value: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 22 SQFSGEDANFEQLMVSMLDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINA--------NLPqEFATLTKELT 93
Cdd:pfam15619 49 GKYEGTESELPQLIARHNEEVRVLRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRleklsedkNLA-EREELQKKLE 127
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442626410 94 QARETLLERDEEIGELkaERnntrllleHLECLVSRHERSLRMTVVKrQAAAQSGVSSEVEVLKALKSL 162
Cdd:pfam15619 128 QLEAKLEDKDEKIQDL--ER--------KLELENKSFRRQLAAEKKK-HKEAQEEVKILQEEIERLQQK 185
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
248-499 |
5.54e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.66 E-value: 5.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 248 EANELNDYAAKTHELQTIIEKQTSELsqwqrrvsDLNNKISELEENMSRVQKEHCKAQdqcaklqrDLRENVAQKEDQEE 327
Cdd:pfam02463 161 EAAGSRLKRKKKEALKKLIEETENLA--------ELIIDLEELKLQELKLKEQAKKAL--------EYYQLKEKLELEEE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 328 RITTLEKRYLNAQREsTSLHDLNEKLEQELRHKEAQLKAQERHGSAEDRIRGLETNLDEKTNEVvrlnQRLKMNEEHNLR 407
Cdd:pfam02463 225 YLLYLDYLKLNEERI-DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEE----LKLLAKEEEELK 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 408 LSSTVDKLLSESNERLQVHLKERMHALDEKNALTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQLLQQEIAYN 487
Cdd:pfam02463 300 SELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKK 379
|
250
....*....|..
gi 442626410 488 IQQTEALTRSLS 499
Cdd:pfam02463 380 KLESERLSSAAK 391
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
248-472 |
6.38e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 6.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 248 EANELNDYAAKTHELQTIIEKQTSELSQW--QRRVSDLNNKISELEEnmsrvqkehckaqdQCAKLQRDLRENVAQKEDQ 325
Cdd:COG4913 256 PIRELAERYAAARERLAELEYLRAALRLWfaQRRLELLEAELEELRA--------------ELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 326 EERITTLEKRYLNA--QREstslhdlnEKLEQELRHKEAQLKAQER-HGSAEDRIRGLETNLDEKTNEVVRLNQRLKmne 402
Cdd:COG4913 322 REELDELEAQIRGNggDRL--------EQLEREIERLERELEERERrRARLEALLAALGLPLPASAEEFAALRAEAA--- 390
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442626410 403 ehnlRLSSTVDKLLSESNERLQVHLKERMHALDEKNALTQELE--KARK--VAEELHHEKSEIMKELSKTRLEI 472
Cdd:COG4913 391 ----ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAslERRKsnIPARLLALRDALAEALGLDEAEL 460
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
31-178 |
6.49e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 6.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 31 FEQLMVSMLDER-DKLMDSLREAQERLNETENKLRDVEKERDSLQRQINAN-------LPQEFATLTKELTQARETL--- 99
Cdd:COG4913 285 FAQRRLELLEAElEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrleqLEREIERLERELEERERRRarl 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 100 --------LERDEEIGELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAA--AQSGVSSEVEVLKALKSLFEHHkal 169
Cdd:COG4913 365 eallaalgLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLrrELRELEAEIASLERRKSNIPAR--- 441
|
....*....
gi 442626410 170 DEKVRERLR 178
Cdd:COG4913 442 LLALRDALA 450
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
266-498 |
7.54e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.99 E-value: 7.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 266 IEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEhckaqdqcakLQRDLRENVaqkEDQEERITTLEKRYLNAqrests 345
Cdd:COG5022 880 AERQLQELKIDVKSISSLKLVNLELESEIIELKKS----------LSSDLIENL---EFKTELIARLKKLLNNI------ 940
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 346 lhDLNEKLEQELRHKEAQLKAQERHGSAEDRIRGLETNLDEKTNEVVRLNqrlKMNEEhnlrLSSTVDKL--LSESNERL 423
Cdd:COG5022 941 --DLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGN---KANSE----LKNFKKELaeLSKQYGAL 1011
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 424 QVH---LKERMHALDEKNALTQELEKAR---KVAEELHHEKSEIMKELSKTRLEIENFK----RQLLQQEIAYNIQQTEA 493
Cdd:COG5022 1012 QEStkqLKELPVEVAELQSASKIISSEStelSILKPLQKLKGLLLLENNQLQARYKALKlrreNSLLDDKQLYQLESTEN 1091
|
....*
gi 442626410 494 LTRSL 498
Cdd:COG5022 1092 LLKTI 1096
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
1072-1143 |
1.03e-04 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 41.51 E-value: 1.03e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626410 1072 VLVWSNERVIRWVGSIGLKEYANNLLESGVHGGLMALDEGFDanamgLALQIPTQNAQARQILDTEFNNLLQ 1143
Cdd:smart00454 1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEE-----DLKELGITKLGHRKKILKAIQKLKE 67
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
286-448 |
1.20e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 286 KISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKE----------------DQEERITTLEKRYLNAQRESTSLhdl 349
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREalqrlaeyswdeidvaSAEREIAELEAELERLDASSDDL--- 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 350 nEKLEQELRHKEAQLK-AQERHGSAEDRIRGLETNLDEKTNEVVRLNQRL-----KMNEEHNLRLSSTVDKLLSESNER- 422
Cdd:COG4913 688 -AALEEQLEELEAELEeLEEELDELKGEIGRLEKELEQAEEELDELQDRLeaaedLARLELRALLEERFAAALGDAVERe 766
|
170 180
....*....|....*....|....*..
gi 442626410 423 LQVHLKERMHALDEK-NALTQELEKAR 448
Cdd:COG4913 767 LRENLEERIDALRARlNRAEEELERAM 793
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
41-464 |
1.23e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 41 ERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQinanlpQEFATLTKELTQARETLLERDEEIGELKAERNNTRLLL 120
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK------AEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAK 1424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 121 EHLEcLVSRHERSLRMTVVKRQAAAQSGVSSEVEVLKALKSLFEHHKALDE--KVRERLRLSIEKNNMMEEELSSAKEEL 198
Cdd:PTZ00121 1425 KKAE-EKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEakKKAEEAKKADEAKKKAEEAKKKADEAK 1503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 199 AQYKAGVVPAGVGSGSGAGSAATTAGGGGAENGLKEKMAGVGGSGGVNGEANELNdyaaKTHELQTIIEKQTSELSQ-WQ 277
Cdd:PTZ00121 1504 KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK----KAEEKKKAEEAKKAEEDKnMA 1579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 278 RRVSDLNNKISE--LEENMSRVQKEHCKAQDQCAKLQ--RDLRENVAQKEDQEERITTLEKRYLNAQRESTSLHDLNE-- 351
Cdd:PTZ00121 1580 LRKAEEAKKAEEarIEEVMKLYEEEKKMKAEEAKKAEeaKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEen 1659
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 352 --KLEQELRHKEAQLKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEE-----HNLRLSSTVDKLLSESNERLQ 424
Cdd:PTZ00121 1660 kiKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEekkkaEELKKAEEENKIKAEEAKKEA 1739
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 442626410 425 VHLKERMHAL----DEKNALTQELEKARKVAEELHHEKSEIMKE 464
Cdd:PTZ00121 1740 EEDKKKAEEAkkdeEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| SAM_STIM-1,2-like |
cd09504 |
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ... |
902-960 |
1.27e-04 |
|
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like (Stromal interaction molecule) proteins is a putative protein-protein interaction domain. STIM1 and STIM2 human proteins are type I transmembrane proteins. The N-terminal part of them includes "hidden" EF-hand and SAM domains. This region is responsible for sensing changes in store-operated and basal cytoplasmic Ca2+ levels and initiates oligomerization. "Hidden" EF hand and SAM domains have a stable intramolecular association, and the SAM domain is a component that regulates stability within STIM proteins. Destabilization of the EF-SAM association during Ca2+ depletion leads to partial unfolding and aggregation (homooligomerization), thus activating the store-operated Ca2+ entry. Immunoprecipitation analysis indicates that STIM1 and STIM2 can form co-precipitable oligomeric associations in vivo. It was suggested that STIM1 and STIM2 are involved in opposite regulation of store operated channels in plasma membrane.
Pssm-ID: 188903 Cd Length: 74 Bit Score: 41.55 E-value: 1.27e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626410 902 WNGPTIVAWLELWVGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNPLHRLKLRL 960
Cdd:cd09504 5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
272-394 |
1.48e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 272 ELSQWQRRVSDL---NNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQRESTSLH- 347
Cdd:COG4913 669 EIAELEAELERLdasSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELr 748
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 442626410 348 -DLNEKLEQEL-RHKEAQLKAQerhgsAEDRIRGLETNLDEKTNEVVRL 394
Cdd:COG4913 749 aLLEERFAAALgDAVERELREN-----LEERIDALRARLNRAEEELERA 792
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
41-203 |
1.68e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 41 ERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINAnlpqefatLTKELTQARETLLERDEEIGEL-----KAERNN 115
Cdd:COG4942 49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAE--------LEKEIAELRAELEAQKEELAELlralyRLGRQP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 116 TRLLLEHLEcLVSRHERSLRM--TVVKRQAAAQSGVSSEVEVLKALKSLFEHHKA-----LDEKVRERLRLSIEKNNmME 188
Cdd:COG4942 121 PLALLLSPE-DFLDAVRRLQYlkYLAPARREQAEELRADLAELAALRAELEAERAelealLAELEEERAALEALKAE-RQ 198
|
170
....*....|....*
gi 442626410 189 EELSSAKEELAQYKA 203
Cdd:COG4942 199 KLLARLEKELAELAA 213
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
266-461 |
2.31e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 266 IEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQRESTS 345
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 346 LHDLNEKLEQELRhkeaqlKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKL-LSESNERLQ 424
Cdd:COG4372 113 LQEELEELQKERQ------DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALsEAEAEQALD 186
|
170 180 190
....*....|....*....|....*....|....*..
gi 442626410 425 VHLKERMHALDEKNALTQELEKARKVAEELHHEKSEI 461
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEA 223
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
313-485 |
2.83e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 313 RDLRENVAQKEDQEERITTLE------KRYLNAQRESTSLHDLNEKLEQELRHKEAQLkAQERHGSAEDRIRGLETNLDE 386
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEpirelaERYAAARERLAELEYLRAALRLWFAQRRLEL-LEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 387 KTNEVVRLNQRLkmNEEHNLRLSSTVDKL--LSESNERLQVHLKERMHALDEKNALTQELE---------------KARK 449
Cdd:COG4913 314 LEARLDALREEL--DELEAQIRGNGGDRLeqLEREIERLERELEERERRRARLEALLAALGlplpasaeefaalraEAAA 391
|
170 180 190
....*....|....*....|....*....|....*...
gi 442626410 450 VAEELHHEKSEIMKELSKTRLEIENFKRQL--LQQEIA 485
Cdd:COG4913 392 LLEALEEELEALEEALAEAEAALRDLRRELreLEAEIA 429
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
251-486 |
5.08e-04 |
|
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: 44.29 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 251 ELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERIT 330
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 331 TLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQLKaqerhgSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEhnlRLSS 410
Cdd:TIGR02169 396 KLKREINELKRELDRLQEELQRLSEELADLNAAIA------GIEAKINELEEEKEDKALEIKKQEWKLEQLAA---DLSK 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442626410 411 TVDKLLSESNERLQVhlKERMHALDEKNAltqELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQLLQQEIAY 486
Cdd:TIGR02169 467 YEQELYDLKEEYDRV--EKELSKLQRELA---EAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERY 537
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
41-502 |
5.25e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 44.35 E-value: 5.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 41 ERDK---LMDSLREAQERLNETENKLRDvEKERDSLQRQINANLPQEFATLTKELTQARETLLERDEEIGELKAERNNTR 117
Cdd:pfam05557 46 ESDRnqeLQKRIRLLEKREAEAEEALRE-QAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 118 LLLEHLECLVSRHERSLRMTVVKRQAAAQSGVSSEvevlKALKSLFEHhkalDEKVRErLRLSIEKNNMMEEELSSAKEE 197
Cdd:pfam05557 125 LELQSTNSELEELQERLDLLKAKASEAEQLRQNLE----KQQSSLAEA----EQRIKE-LEFEIQSQEQDSEIVKNSKSE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 198 LAQykagvVPAGVGSGSGAGSAATTAGGGGAENGLKEKMAGVGGSGGVNGEanelnDYAAKTHELQTIIEKQTSELSQWQ 277
Cdd:pfam05557 196 LAR-----IPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREE-----KYREEAATLELEKEKLEQELQSWV 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 278 ----------RRVSDLNNKISEL-EENMSRVQKEHCKAQD--QCAKLQRDLRENVAQ-----------KEDQEERITTLE 333
Cdd:pfam05557 266 klaqdtglnlRSPEDLSRRIEQLqQREIVLKEENSSLTSSarQLEKARRELEQELAQylkkiedlnkkLKRHKALVRRLQ 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 334 KRYLNAQRESTSLHDLNEKLEQELRHKEAQLKAQERHGSAEDRIRGLETNLDEKTnevVRLNQRLKMNEEHNLRLSSTVD 413
Cdd:pfam05557 346 RRVLLLTKERDGYRAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEME---AQLSVAEEELGGYKQQAQTLER 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 414 KLLSesnERLQVHLKERMHALDEKNALTQELEKARKVAEELHHEKSEImkelsktRLEIEnfkRQLLQQEiaYNIQQTEA 493
Cdd:pfam05557 423 ELQA---LRQQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNEL-------EMELE---RRCLQGD--YDPKKTKV 487
|
....*....
gi 442626410 494 LTRSLSPSS 502
Cdd:pfam05557 488 LHLSMNPAA 496
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
41-392 |
5.48e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.24 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 41 ERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINaNLPQEFATLTKELTQARETLLERDEEIGELKAERNNTRLLL 120
Cdd:TIGR04523 378 ENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIK-KLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELII 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 121 EHLECLVSRHERSLRMTvvkrqaaaqsgvssEVEVLKALKSLFEHHKALDEKVRERLRLSIEKNNMmEEELSSAKEELAQ 200
Cdd:TIGR04523 457 KNLDNTRESLETQLKVL--------------SRSINKIKQNLEQKQKELKSKEKELKKLNEEKKEL-EEKVKDLTKKISS 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 201 YKagvvpagvgsgsgAGSAATTAGGGGAENGLKEKmagvggsggvNGEANELnDYAAKTHELQTIIEKQTSELSQWQRRV 280
Cdd:TIGR04523 522 LK-------------EKIEKLESEKKEKESKISDL----------EDELNKD-DFELKKENLEKEIDEKNKEIEELKQTQ 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 281 SDLNNKISELEENMsrvqkehckaqDQCAKLQRDLRENVAQKEDQ----EERITTLEKRYLNAQRESTSLHDLNEKLEQE 356
Cdd:TIGR04523 578 KSLKKKQEEKQELI-----------DQKEKEKKDLIKEIEEKEKKisslEKELEKAKKENEKLSSIIKNIKSKKNKLKQE 646
|
330 340 350
....*....|....*....|....*....|....*.
gi 442626410 357 LRHKEAQLkaqerhgsaeDRIRGLETNLDEKTNEVV 392
Cdd:TIGR04523 647 VKQIKETI----------KEIRNKWPEIIKKIKESK 672
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
251-545 |
7.03e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.94 E-value: 7.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 251 ELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISE-LEENMSRVQ------------KEHCKAQDQCAKLQRDLRE 317
Cdd:pfam05483 100 ELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEeIQENKDLIKennatrhlcnllKETCARSAEKTKKYEYERE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 318 NVAQ-----KEDQEERITTLEKRYLNAQRESTSLH-----------DLNEKLEQELRHKEAQ-----LKAQERhgsaEDR 376
Cdd:pfam05483 180 ETRQvymdlNNNIEKMILAFEELRVQAENARLEMHfklkedhekiqHLEEEYKKEINDKEKQvslllIQITEK----ENK 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 377 IRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESN-----------------ERLQVHLKERMHALDEKNA 439
Cdd:pfam05483 256 MKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEdikmslqrsmstqkaleEDLQIATKTICQLTEEKEA 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 440 LTQELEKARKVaeelhheKSEIMKELSKTRLEIENFKRQlLQQEIAYNIQQTEALTRSLSPSSVVDPSGAFSRSNSHASF 519
Cdd:pfam05483 336 QMEELNKAKAA-------HSFVVTEFEATTCSLEELLRT-EQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVEL 407
|
330 340
....*....|....*....|....*.
gi 442626410 520 ETHSLRRQSKQRLSEENALVRSMAEQ 545
Cdd:pfam05483 408 EELKKILAEDEKLLDEKKQFEKIAEE 433
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
294-502 |
7.26e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.80 E-value: 7.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 294 MSRVQKEHCKAQDQCAKLQRDLRENVA--QKEDQEERITTLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQLKAQERHG 371
Cdd:TIGR00618 184 MEFAKKKSLHGKAELLTLRSQLLTLCTpcMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLK 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 372 SAEDRIRGLETNLDEKTNEVVRLNQRLKMNE--EHNLRLSStVDKLLSESNERLQVHLKERMHALDEKNAL---TQELEK 446
Cdd:TIGR00618 264 QLRARIEELRAQEAVLEETQERINRARKAAPlaAHIKAVTQ-IEQQAQRIHTELQSKMRSRAKLLMKRAAHvkqQSSIEE 342
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 442626410 447 ARKVAEELHHEKSEIMKELSKTRLEIENFKRQL-LQQEIAYNIQQTEALTRSLSPSS 502
Cdd:TIGR00618 343 QRRLLQTLHSQEIHIRDAHEVATSIREISCQQHtLTQHIHTLQQQKTTLTQKLQSLC 399
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
29-496 |
7.61e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 7.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 29 ANFEQLMVSMLDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQinanlpQEFATLTKELTQARETLLERDEEIGE 108
Cdd:PTZ00121 1263 AHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKK------AEEAKKADEAKKKAEEAKKKADAAKK 1336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 109 lKAERNNTRLLLEHLECLVSRHERSlrmTVVKRQAAAQSGVSSEVEVLKALKSlfehhKALDEKVRERLRLSIEKNNMME 188
Cdd:PTZ00121 1337 -KAEEAKKAAEAAKAEAEAAADEAE---AAEEKAEAAEKKKEEAKKKADAAKK-----KAEEKKKADEAKKKAEEDKKKA 1407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 189 EELSSAKEElaQYKAGVVPAGVGSGSGAGSAATTAGGGGAENGLKEKMAGVGGSGGVNGEANElndyAAKTHELQTIIEK 268
Cdd:PTZ00121 1408 DELKKAAAA--KKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEE----AKKADEAKKKAEE 1481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 269 QtselsqwqRRVSDLNNKISELEENMSRVQKehcKAQdqcAKLQRDLRENVAQKEDQEERITTLEKRYLNAQRESTSLHD 348
Cdd:PTZ00121 1482 A--------KKADEAKKKAEEAKKKADEAKK---AAE---AKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK 1547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 349 LNE-KLEQELRHKEAQLKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESN--ERLQV 425
Cdd:PTZ00121 1548 ADElKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIkaEELKK 1627
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442626410 426 HLKERMHALDEKNALTQELEKARKVAEElhHEKSEIMKELSKTRLEIENFKRQLLQQEIAYNIQQTEALTR 496
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAEELKKA--EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
275-485 |
7.89e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.35 E-value: 7.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 275 QWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQRESTSLHDLNEKLE 354
Cdd:pfam07888 70 QWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 355 QEL-RHKEAQLKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLK-------MNEEHNLRLSSTVDKL---LSESNERL 423
Cdd:pfam07888 150 TELeRMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQelrnslaQRDTQVLQLQDTITTLtqkLTTAHRKE 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626410 424 QVH--LKERMHALDEK-NALTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQLLQQEIA 485
Cdd:pfam07888 230 AENeaLLEELRSLQERlNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLA 294
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
248-498 |
1.09e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.42 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 248 EANELNDYAAKTHELQTIIEKQT--SELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQ 325
Cdd:pfam02463 205 QAKKALEYYQLKEKLELEEEYLLylDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQ 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 326 EERITTLEKRYLNAQRESTSL----HDLNEKLEQELRHKEAQLKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMN 401
Cdd:pfam02463 285 EEELKLLAKEEEELKSELLKLerrkVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 402 EEHNLRLSSTVDKLLSESNERLQVHLKERMHALDEKNALTQELEKARKVAEELHHEKSEIMKELSKTRLEIEnfKRQLLQ 481
Cdd:pfam02463 365 QEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEE--ESIELK 442
|
250
....*....|....*..
gi 442626410 482 QEIAyNIQQTEALTRSL 498
Cdd:pfam02463 443 QGKL-TEEKEELEKQEL 458
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
86-365 |
1.37e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 86 ATLTKELTQARETLLERDEEIGELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAAAQSGVSSEVE----VLKALKS 161
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDassdDLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 162 LFEHHKALDEKVRERLRLSIEKNNMMEEELSSAKEELAQykagvvpagvgsgsgagsaattaggggaenglkekmAGVGG 241
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE------------------------------------LQDRL 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 242 SGGVNGEANELNDYAAKTHElQTIIEKQTSELSQW-QRRVSDLNNKISELEENMSRVQKEHCKAQDQCAklqRDLRENVA 320
Cdd:COG4913 737 EAAEDLARLELRALLEERFA-AALGDAVERELRENlEERIDALRARLNRAEEELERAMRAFNREWPAET---ADLDADLE 812
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 442626410 321 QKEDQEERITTLE-----------KRYLNAQrESTSLHDLNEKLEQELRHKEAQLK 365
Cdd:COG4913 813 SLPEYLALLDRLEedglpeyeerfKELLNEN-SIEFVADLLSKLRRAIREIKERID 867
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
350-494 |
1.37e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.02 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 350 NEKLEQELRHKEAQLKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHnLRLSSTVDKLlSESNERLQVHLKE 429
Cdd:COG3096 281 RELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDH-LNLVQTALRQ-QEKIERYQEDLEE 358
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442626410 430 rmhaldeknaLTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQL--LQQeiAYNIQQTEAL 494
Cdd:COG3096 359 ----------LTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLadYQQ--ALDVQQTRAI 413
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
43-634 |
1.54e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 43 DKLMDSLREAQ-----ERLNETENKLRDVEKERDSLQRQInANLPQEFATLTKELTQARETL---------------LER 102
Cdd:TIGR02169 214 QALLKEKREYEgyellKEKEALERQKEAIERQLASLEEEL-EKLTEEISELEKRLEEIEQLLeelnkkikdlgeeeqLRV 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 103 DEEIGELKAERNNTRLLLEHLECLVSRHERSLRMTVVK--RQAAAQSGVSSEVEVLKALKSLFEHHKALDEKVRERLRLS 180
Cdd:TIGR02169 293 KEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEidKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 181 IE----KNNMMEEELSSAKEELAQYKAGVVPAGVGSGSGAGSAATTAGGGGA-ENGLKEKMAGVGGSGGVNGEANElnDY 255
Cdd:TIGR02169 373 LEevdkEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADlNAAIAGIEAKINELEEEKEDKAL--EI 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 256 AAKTHELQTIIEKqtseLSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERIT----- 330
Cdd:TIGR02169 451 KKQEWKLEQLAAD----LSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgt 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 331 -----TLEKRYLNAQRESTSLHDLNEKLEQELRHKEA------------------QLKAQERHGS--AEDRIRGLETNL- 384
Cdd:TIGR02169 527 vaqlgSVGERYATAIEVAAGNRLNNVVVEDDAVAKEAiellkrrkagratflplnKMRDERRDLSilSEDGVIGFAVDLv 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 385 --DEKTNEVVR-------LNQRLKMNEEH--NLRLSSTVDKLLSES---------------------------NERLQVH 426
Cdd:TIGR02169 607 efDPKYEPAFKyvfgdtlVVEDIEAARRLmgKYRMVTLEGELFEKSgamtggsraprggilfsrsepaelqrlRERLEGL 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 427 LKERMHALDEKNALTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQL---------LQQEIAYNIQQTEALTRS 497
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLeeleedlssLEQEIENVKSELKELEAR 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 498 LSPssvvdpsgafsrsnshasfethsLRRQSKQRLSEENALVRSMAEQEWEKLQQAAHAQQQAYELASA------ADCDD 571
Cdd:TIGR02169 767 IEE-----------------------LEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEArlreieQKLNR 823
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442626410 572 SDVLYAAATDMMSpsghtDAQTLAMMLQEQLDAINNEIRLIQEEKQSTEARAEELESRVGSLE 634
Cdd:TIGR02169 824 LTLEKEYLEKEIQ-----ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLE 881
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
248-390 |
1.54e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 248 EANELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEH-----------CKAQ-----DQCAKL 311
Cdd:PHA02562 225 LVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIkmyekggvcptCTQQisegpDRITKI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 312 QRDLRENVAQKEDQEERITTLEKRYLNAQRESTSLHDLNEKLEQE-----------LRHKEAQLKAQERHGSAEDRIRGL 380
Cdd:PHA02562 305 KDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNkqslitlvdkaKKVKAAIEELQAEFVDNAEELAKL 384
|
170
....*....|
gi 442626410 381 ETNLDEKTNE 390
Cdd:PHA02562 385 QDELDKIVKT 394
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
355-483 |
1.63e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 355 QELRHKEAQLKAQERHgsAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHnlrlSSTVDKLLSESNERLQVHLKERmhal 434
Cdd:COG1579 20 DRLEHRLKELPAELAE--LEDELAALEARLEAAKTELEDLEKEIKRLELE----IEEVEARIKKYEEQLGNVRNNK---- 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 442626410 435 dEKNALTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQLLQQE 483
Cdd:COG1579 90 -EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE 137
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
154-342 |
1.72e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 154 EVLKALKSLFEHHKALD--EKVRERLRLSIEKnnmMEEELSSAKEELAQYKAGVvpagvgsgsgagsAATTAGGGGAENG 231
Cdd:COG1579 4 EDLRALLDLQELDSELDrlEHRLKELPAELAE---LEDELAALEARLEAAKTEL-------------EDLEKEIKRLELE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 232 LKEKMAGVGGSGGVNGEANELNDYAAKTHELQTIiekqtselsqwQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKL 311
Cdd:COG1579 68 IEEVEARIKKYEEQLGNVRNNKEYEALQKEIESL-----------KRRISDLEDEILELMERIEELEEELAELEAELAEL 136
|
170 180 190
....*....|....*....|....*....|.
gi 442626410 312 QRDLRENVAQKEDQEERITTLEKRyLNAQRE 342
Cdd:COG1579 137 EAELEEKKAELDEELAELEAELEE-LEAERE 166
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
303-448 |
1.77e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 42.14 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 303 KAQDQCAKLQRDLRENVAQKEDQEERITTL--EKRYLNAQRESTSLHDLNEKLEQELRHKEAQLKAQERHGS-------- 372
Cdd:COG3524 174 AREDAVRFAEEEVERAEERLRDAREALLAFrnRNGILDPEATAEALLQLIATLEGQLAELEAELAALRSYLSpnspqvrq 253
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442626410 373 AEDRIRGLETNLDEKTNEVVRLNQRLKMNEehnlrlsstvdklLSESNERLQVHLKERMHALdeKNALTQeLEKAR 448
Cdd:COG3524 254 LRRRIAALEKQIAAERARLTGASGGDSLAS-------------LLAEYERLELEREFAEKAY--TSALAA-LEQAR 313
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
251-548 |
2.06e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 251 ELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENmsrvqkehckaQDQCAKLQRDLRENVAQKEDQEERIT 330
Cdd:PRK01156 160 EINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENI-----------KKQIADDEKSHSITLKEIERLSIEYN 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 331 TLEKRYLNAQ---RESTSLHDLNEKLEQELRHKEAQLKAQERHgsaEDRIRGLETNLDEKTNEVVRLNqRLKMNEEHNLR 407
Cdd:PRK01156 229 NAMDDYNNLKsalNELSSLEDMKNRYESEIKTAESDLSMELEK---NNYYKELEERHMKIINDPVYKN-RNYINDYFKYK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 408 LS-STVDKLLSESNERLQVHlKERMHALDEKNALTQELEKARKVAEELHHEKSEI----MKELSKTRlEIENFKRQLLQQ 482
Cdd:PRK01156 305 NDiENKKQILSNIDAEINKY-HAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELegyeMDYNSYLK-SIESLKKKIEEY 382
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442626410 483 EIayNIQQTEALTRSLSPSSVVDPSGAFSRSNshasfETHSLRRQSKQRLSEENALVRSMAEQEWE 548
Cdd:PRK01156 383 SK--NIERMSAFISEILKIQEIDPDAIKKELN-----EINVKLQDISSKVSSLNQRIRALRENLDE 441
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
47-203 |
2.07e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 47 DSLREAQERLNETENKLRDVEKERDSLQRQINA-------------NLPQEFATLTKELTQARETLLERDEEIGELKAER 113
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEElneeynelqaeleALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 114 NNTRLLLEHLECLVSrhERSL-----RMTVVKRQAAAQsgvSSEVEVLKALKSLFEHHKALDEKVRERLRLSIEKNNMME 188
Cdd:COG3883 96 YRSGGSVSYLDVLLG--SESFsdfldRLSALSKIADAD---ADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170
....*....|....*
gi 442626410 189 EELSSAKEELAQYKA 203
Cdd:COG3883 171 AELEAQQAEQEALLA 185
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
32-179 |
2.09e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 32 EQLMVSMLDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQIN---------------ANLPQEFATLTKELTQAR 96
Cdd:COG3206 204 KNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGsgpdalpellqspviQQLRAQLAELEAELAELS 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 97 ETLLERDEEIGELKAERNNTRLLLehleclvsrhERSLRMTVVKRQAAAQSGVSSEVEVLKALKSLFEHHKALDEKVRER 176
Cdd:COG3206 284 ARYTPNHPDVIALRAQIAALRAQL----------QQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAEL 353
|
...
gi 442626410 177 LRL 179
Cdd:COG3206 354 RRL 356
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
49-183 |
2.16e-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: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 49 LREAQERLNETENKLRDVEKERDSLQRqinanLPQEFATLTKELTQARETLLERDEEIGELKAERNNTRLLLEHLECLVS 128
Cdd:COG4913 663 VASAEREIAELEAELERLDASSDDLAA-----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 129 RHERSLRMTVV-----KRQAAAQSGVSSEVEvlkalKSLFEHHKALDEKvRERLRLSIEK 183
Cdd:COG4913 738 AAEDLARLELRalleeRFAAALGDAVERELR-----ENLEERIDALRAR-LNRAEEELER 791
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
248-483 |
2.18e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.34 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 248 EANEL-NDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRE---NVAQKE 323
Cdd:TIGR00606 692 ELQEFiSDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRlknDIEEQE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 324 DQEERITTLEKRYLNAQRESTSLHDLNEKLEqELRHKEAQLKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEe 403
Cdd:TIGR00606 772 TLLGTIMPEEESAKVCLTDVTIMERFQMELK-DVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNR- 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 404 hnlrlsstvdKLLSESNERLQvHLKERMHAL-DEKNALTQELEKARKVAE---ELHHEKSEIMKELSKTRLEI---ENFK 476
Cdd:TIGR00606 850 ----------KLIQDQQEQIQ-HLKSKTNELkSEKLQIGTNLQRRQQFEEqlvELSTEVQSLIREIKDAKEQDsplETFL 918
|
....*..
gi 442626410 477 RQLLQQE 483
Cdd:TIGR00606 919 EKDQQEK 925
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
902-965 |
2.77e-03 |
|
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.
Pssm-ID: 425739 Cd Length: 64 Bit Score: 37.25 E-value: 2.77e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442626410 902 WNGPTIVAWLElWVGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQEM 965
Cdd:pfam00536 3 WSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
304-478 |
3.03e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 304 AQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQRESTSLHDLNEK---------LEQELRHKEAQLKA-------- 366
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYswdeidvasAEREIAELEAELERldassddl 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 367 ---QERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESNERLQVHLKERMHALDEKNAltqe 443
Cdd:COG4913 688 aalEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAV---- 763
|
170 180 190
....*....|....*....|....*....|....*....
gi 442626410 444 lekARKVAEELHHEKSEIMKELSKTRLEIEN----FKRQ 478
Cdd:COG4913 764 ---ERELRENLEERIDALRARLNRAEEELERamraFNRE 799
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
37-460 |
3.14e-03 |
|
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: 41.21 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 37 SMLDERDKLMDSLREAQERLNETENKLRD-------VEKERDSLQRQINAnLPQEFATLTKELTQARETLLERDEEIGEL 109
Cdd:pfam19220 31 QLIEPIEAILRELPQAKSRLLELEALLAQeraaygkLRRELAGLTRRLSA-AEGELEELVARLAKLEAALREAEAAKEEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 110 KAERNNTRLLLEHLEclvsrherslrmtvvkRQAAAQSGVSSEVEvlKALKSLFEHHKALDEKVRErlrlsieknnmMEE 189
Cdd:pfam19220 110 RIELRDKTAQAEALE----------------RQLAAETEQNRALE--EENKALREEAQAAEKALQR-----------AEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 190 ELSSAKEELAQYKAgvvpagvgsgsgagsaattaggggaENGLKEKMAGVGgsggvngeANELNDYAAKTHELQTIIEKQ 269
Cdd:pfam19220 161 ELATARERLALLEQ-------------------------ENRRLQALSEEQ--------AAELAELTRRLAELETQLDAT 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 270 TSELSQWQRRVSDLNNK----ISELEENMSRVQKEHCK-------AQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLN 338
Cdd:pfam19220 208 RARLRALEGQLAAEQAEreraEAQLEEAVEAHRAERASlrmkleaLTARAAATEQLLAEARNQLRDRDEAIRAAERRLKE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 339 AQRESTSLHDLNEKLEQELRHKEAQLKAQER-HGSAEDRIRGLETNLDEKTNEVVRLNQRlkmneehNLRLSSTVDklls 417
Cdd:pfam19220 288 ASIERDTLERRLAGLEADLERRTQQFQEMQRaRAELEERAEMLTKALAAKDAALERAEER-------IASLSDRIA---- 356
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 442626410 418 esnerlqvHLKERMHalDEKNALTQeleKARKVAEELHHEKSE 460
Cdd:pfam19220 357 --------ELTKRFE--VERAALEQ---ANRRLKEELQRERAE 386
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
266-505 |
3.19e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 266 IEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEhckaQDQCAKLQRDLRENVAQKEDQEERITTL----EKR----YL 337
Cdd:PRK04863 899 IREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSD----PEQFEQLKQDYQQAQQTQRDAKQQAFALtevvQRRahfsYE 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 338 NAQRESTSLHDLNEKLEQELRHKEAQlkaQERhgsAEDRIRGLETNLDEKtnevvrlNQRLkmneehnLRLSSTVDKLLS 417
Cdd:PRK04863 975 DAAEMLAKNSDLNEKLRQRLEQAEQE---RTR---AREQLRQAQAQLAQY-------NQVL-------ASLKSSYDAKRQ 1034
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 418 ESNErlqvhLKERMHALDeKNALTQELEKARKVAEELHHE-------KSEIMKELSKTRLEIENFKRQLLQQEIAYNIQQ 490
Cdd:PRK04863 1035 MLQE-----LKQELQDLG-VPADSGAEERARARRDELHARlsanrsrRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMR 1108
|
250
....*....|....*
gi 442626410 491 TEALTRSLSPSSVVD 505
Cdd:PRK04863 1109 EQVVNAKAGWCAVLR 1123
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
250-496 |
3.37e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.05 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 250 NELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQ---E 326
Cdd:COG1340 36 EELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIdklR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 327 ERITTLEKRYlnaQRESTSLHDLNEkLEQELRHKEAQLKAQERHGSAEDRIRGLETNLDEKtnevvrlnqRLKMNEEHnl 406
Cdd:COG1340 116 KEIERLEWRQ---QTEVLSPEEEKE-LVEKIKELEKELEKAKKALEKNEKLKELRAELKEL---------RKEAEEIH-- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 407 rlsstvdKLLSESNERLQVHLKERmhaldekNALTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQL--LQQEI 484
Cdd:COG1340 181 -------KKIKELAEEAQELHEEM-------IELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELreLRKEL 246
|
250
....*....|..
gi 442626410 485 AYNIQQTEALTR 496
Cdd:COG1340 247 KKLRKKQRALKR 258
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
12-473 |
3.61e-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: 41.75 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 12 ISEDSISQRSSQFSGEDANF----EQLMVSMLDERDKLmDSLREAQERLNETENKLRDVEKERDSLQRQInANLPQEFAT 87
Cdd:pfam12128 206 LEDDGVVPPKSRLNRQQVEHwirdIQAIAGIMKIRPEF-TKLQQEFNTLESAELRLSHLHFGYKSDETLI-ASRQEERQE 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 88 LTKELTQARETLLE-----RDEEIGELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAAAQS--GVSSEVEVL-KAL 159
Cdd:pfam12128 284 TSAELNQLLRTLDDqwkekRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQlpSWQSELENLeERL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 160 KSLFEHHKALDEKVRERLRLSIEKNNM----MEEELSSAKEELAQYKAGV--VPAGVGSGSGAGSAATTAGGGGAENGLK 233
Cdd:pfam12128 364 KALTGKHQDVTAKYNRRRSKIKEQNNRdiagIKDKLAKIREARDRQLAVAedDLQALESELREQLEAGKLEFNEEEYRLK 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 234 EKMAGVG-GSGGVNGEANELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQ---CA 309
Cdd:pfam12128 444 SRLGELKlRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERqsaLD 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 310 KLQR------------------DLRENVAQ----------------KEDQEERITTLEKRYLNAQR-ESTSLHDLNEKLE 354
Cdd:pfam12128 524 ELELqlfpqagtllhflrkeapDWEQSIGKvispellhrtdldpevWDGSVGGELNLYGVKLDLKRiDVPEWAASEEELR 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 355 QELRHKEAQLK-AQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESNERLQVHLK---ER 430
Cdd:pfam12128 604 ERLDKAEEALQsAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDsanER 683
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 442626410 431 MHALD-EKNALTQELEKARkvaEELHHEKSEIMKELSKTRLEIE 473
Cdd:pfam12128 684 LNSLEaQLKQLDKKHQAWL---EEQKEQKREARTEKQAYWQVVE 724
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
250-493 |
4.08e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.48 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 250 NELNDYAAKTHELQTIIEKQTSELSQWQRRVS--------DLNNKISELEENMSRVQ------KEHCKA----QDQCAKL 311
Cdd:COG3096 850 RELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPqanlladeTLADRLEELREELDAAQeaqafiQQHGKAlaqlEPLVAVL 929
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 312 QRD------LRENVAQKEDQEERI-------TTLEKR-----YLNAQRESTSLHDLNEKLEQELRHKEAQL--------K 365
Cdd:COG3096 930 QSDpeqfeqLQADYLQAKEQQRRLkqqifalSEVVQRrphfsYEDAVGLLGENSDLNEKLRARLEQAEEARreareqlrQ 1009
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 366 AQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKmneehnlRLSSTVDkllSESNERlqvhlkermhALDEKNALTQELE 445
Cdd:COG3096 1010 AQAQYSQYNQVLASLKSSRDAKQQTLQELEQELE-------ELGVQAD---AEAEER----------ARIRRDELHEELS 1069
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 442626410 446 KARKvaeelhhEKSEIMKELSKTRLEIENFKRQLLQQEIAYNIQQTEA 493
Cdd:COG3096 1070 QNRS-------RRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQV 1110
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
39-193 |
4.29e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 39 LDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINanlPQEFATLTKELTQARETLLERDEEIGELKAERNNTRL 118
Cdd:PRK03918 618 EKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS---EEEYEELREEYLELSRELAGLRAELEELEKRREEIKK 694
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442626410 119 LLEHLeclvsrherslrmtvvKRQAAAQSGVSSEVEVL-KALKSLfehhKALDEKVReRLRLSIEKNNMME-EELSS 193
Cdd:PRK03918 695 TLEKL----------------KEELEEREKAKKELEKLeKALERV----EELREKVK-KYKALLKERALSKvGEIAS 750
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
37-377 |
4.34e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 37 SMLDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINAnLPQEFATLTKELTQARETLLERDEEIGELKAERNNT 116
Cdd:COG4372 35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQ-LEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 117 RLLLEHLECLVSRHERSlRMTVVKRQAAAQSGVSSEVEVLKALKSlfehhkALDEKVRERLRLSIEKNNMMEEELSSAKE 196
Cdd:COG4372 114 QEELEELQKERQDLEQQ-RKQLEAQIAELQSEIAEREEELKELEE------QLESLQEELAALEQELQALSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 197 ELAQYKAGVVPAGVGSGSGAGSAATTAGGGGAENGLKEKMAGVGGSGGVNGEANELNDYAAKTHELQTIIEKQTSELSQW 276
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 277 QRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQRESTSLHDLNEKLEQE 356
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLL 346
|
330 340
....*....|....*....|.
gi 442626410 357 LRHKEAQLKAQERHGSAEDRI 377
Cdd:COG4372 347 LVGLLDNDVLELLSKGAEAGV 367
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
261-434 |
4.70e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.05 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 261 ELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLREN-VAQKEDQEERITTL--EKRYL 337
Cdd:PRK11281 125 QLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGkVGGKALRPSQRVLLqaEQALL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 338 NAQRE--------STSLHDLNEK-----------LEQEL----------RHKEAQLKAQERHgSAEDRIRGLETNLDEKT 388
Cdd:PRK11281 205 NAQNDlqrkslegNTQLQDLLQKqrdyltariqrLEHQLqllqeainskRLTLSEKTVQEAQ-SQDEAARIQANPLVAQE 283
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 442626410 389 NEV-VRLNQRL-----KMNE--EHNLRLSSTVDKLL-SESNerlqvhLKERMHAL 434
Cdd:PRK11281 284 LEInLQLSQRLlkateKLNTltQQNLRVKNWLDRLTqSERN------IKEQISVL 332
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
40-203 |
5.04e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 40 DERDKLMDS---LREAQERLNETENKLRDVEKERDSLQRQINAnLPQEFATLTKELTQARETLLERDEEIGELKAERNNT 116
Cdd:COG4913 675 AELERLDASsddLAALEEQLEELEAELEELEEELDELKGEIGR-LEKELEQAEEELDELQDRLEAAEDLARLELRALLEE 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 117 RLLLEHLECLVSRHERSLRmtvvKRQAAAQSGVSSEVEvlkALKSLFEHHKALDEKVRERLRLSIEKNNMMEEELSS-AK 195
Cdd:COG4913 754 RFAAALGDAVERELRENLE----ERIDALRARLNRAEE---ELERAMRAFNREWPAETADLDADLESLPEYLALLDRlEE 826
|
....*...
gi 442626410 196 EELAQYKA 203
Cdd:COG4913 827 DGLPEYEE 834
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
17-549 |
5.16e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 17 ISQRSSQFSGEDANFeQLMVSMLDERDKLMDSLREAQERLNETENKLRD--VEKERDSLQRQINANLPQEFATLTKELTQ 94
Cdd:TIGR00606 338 LNQEKTELLVEQGRL-QLQADRHQEHIRARDSLIQSLATRLELDGFERGpfSERQIKNFHTLVIERQEDEAKTAAQLCAD 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 95 ARETLLERDEEIGELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAAAQSgvssevevlkaLKSLFEHHKALDEKVR 174
Cdd:TIGR00606 417 LQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGS-----------SDRILELDQELRKAER 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 175 ErlrLSIEKNNMMEEELSSAKEELAQYKAGVVPAGVGSGSGAGSAATTAGGGGAENGLKEKMAGVGGS-----GGVNGEA 249
Cdd:TIGR00606 486 E---LSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQirkikSRHSDEL 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 250 NELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLREnVAQKEDQEERI 329
Cdd:TIGR00606 563 TSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFD-VCGSQDEESDL 641
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 330 TTLEKRYLNAQRE------STSLHD--------------------------LNE---KLEQELRHKEAQLKAQERHGSAE 374
Cdd:TIGR00606 642 ERLKEEIEKSSKQramlagATAVYSqfitqltdenqsccpvcqrvfqteaeLQEfisDLQSKLRLAPDKLKSTESELKKK 721
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 375 DRIR--------GLETNLDEKTNEVVRLN----------QRLKMNEEHNLRLSSTVDKLLSESN---------ERLQVHL 427
Cdd:TIGR00606 722 EKRRdemlglapGRQSIIDLKEKEIPELRnklqkvnrdiQRLKNDIEEQETLLGTIMPEEESAKvcltdvtimERFQMEL 801
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 428 KERMHALDEKNALTQELEKARKVaEELHHEKSEIMKELSKTRLEIE-NFKRQLLQQEIAYNIQQT--EALTRSLSPSSVV 504
Cdd:TIGR00606 802 KDVERKIAQQAAKLQGSDLDRTV-QQVNQEKQEKQHELDTVVSKIElNRKLIQDQQEQIQHLKSKtnELKSEKLQIGTNL 880
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 442626410 505 DPSGAFSRSNSHASFETHSLRRQSKQRLSEENALVRSMAEQEWEK 549
Cdd:TIGR00606 881 QRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEK 925
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
351-500 |
6.01e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 351 EKLEQELRHKEAQL-KAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKM---NEEhnlrlsstVDKLLSE--SNERLQ 424
Cdd:COG1579 34 AELEDELAALEARLeAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnNKE--------YEALQKEieSLKRRI 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442626410 425 VHLKERMHALDEknaltqELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQlLQQEIAYNIQQTEALTRSLSP 500
Cdd:COG1579 106 SDLEDEILELME------RIEELEEELAELEAELAELEAELEEKKAELDEELAE-LEAELEELEAEREELAAKIPP 174
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
250-422 |
7.39e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 250 NELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKE------ 323
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSyldvll 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 324 ---------DQEERITTLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQLKAQERhgSAEDRIRGLETNLDEKTNEVVRL 394
Cdd:COG3883 110 gsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKA--ELEAAKAELEAQQAEQEALLAQL 187
|
170 180
....*....|....*....|....*...
gi 442626410 395 NQRLKMNEEHNLRLSSTVDKLLSESNER 422
Cdd:COG3883 188 SAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
324-550 |
8.10e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 8.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 324 DQEERITTLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQLKAQER---HGSAEDRIRGLETNLDEKTNEVVRLNqrlkm 400
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeYSWDEIDVASAEREIAELEAELERLD----- 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 401 neehnlrlsstvdkllsESNERLQvhlkermhaldeknALTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQll 480
Cdd:COG4913 682 -----------------ASSDDLA--------------ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE-- 728
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 481 qqeiaynIQQTEALTRSLSPSSVVDPSGAFSRSNSHASFETHslRRQSKQRLSEENALVRSMAEQEWEKL 550
Cdd:COG4913 729 -------LDELQDRLEAAEDLARLELRALLEERFAAALGDAV--ERELRENLEERIDALRARLNRAEEEL 789
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
309-496 |
8.30e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 8.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 309 AKLQRDLRENVAQKEDQEERITTLEKRYLNAQREStslhdlnEKLEQELRHKEAQLKAqerhgsAEDRIRGLETNLDEKT 388
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREEL-------EQLEEELEQARSELEQ------LEEELEELNEQLQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 389 NEVVRLNQRLKMNEEHNLRLSSTVDKLLSEsNERLQvhlkermhalDEKNALTQELEKARKVAEELHHEKSEIMKELSKT 468
Cdd:COG4372 94 AELAQAQEELESLQEEAEELQEELEELQKE-RQDLE----------QQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180
....*....|....*....|....*...
gi 442626410 469 RLEIENFKRQLLQQEIAYNIQQTEALTR 496
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLK 190
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
249-470 |
9.70e-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: 40.21 E-value: 9.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 249 ANELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAK-LQRDLR------ENVAQ 321
Cdd:pfam12128 693 QLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETwYKRDLAslgvdpDVIAK 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 322 -KEDQEERITTLEK---------RYLNAQRESTSLHDLN-----EKLEQELRHKEAQLKAQERhgSAEDRIRGLETNLDE 386
Cdd:pfam12128 773 lKREIRTLERKIERiavrrqevlRYFDWYQETWLQRRPRlatqlSNIERAISELQQQLARLIA--DTKLRRAKLEMERKA 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626410 387 KTNEVVRLNQRLKmneEHNLRLSSTVDKLLSESNERLQVHLKERMHALDE-KNALTQELEKARKvaeELHHEKSeIMKEL 465
Cdd:pfam12128 851 SEKQQVRLSENLR---GLRCEMSKLATLKEDANSEQAQGSIGERLAQLEDlKLKRDYLSESVKK---YVEHFKN-VIADH 923
|
....*
gi 442626410 466 SKTRL 470
Cdd:pfam12128 924 SGSGL 928
|
|
| |
