|
Name |
Accession |
Description |
Interval |
E-value |
| SAM_liprin-alpha1,2,3,4_repeat2 |
cd09565 |
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ... |
920-985 |
1.36e-43 |
|
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.
Pssm-ID: 188964 Cd Length: 66 Bit Score: 152.24 E-value: 1.36e-43
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017363542 920 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 985
Cdd:cd09565 1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
|
|
| SAM_liprin-alpha1,2,3,4_repeat1 |
cd09562 |
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 ... |
803-873 |
2.54e-42 |
|
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.
Pssm-ID: 188961 Cd Length: 71 Bit Score: 148.48 E-value: 2.54e-42
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017363542 803 FAQWDGPTVVSWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEMVSLT 873
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 ... |
1005-1076 |
4.39e-41 |
|
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: 145.15 E-value: 4.39e-41
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363542 1005 DVLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALILQIPTQNTQARQVMEREFNNLL 1076
Cdd:cd09568 1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
|
|
| SAM_liprin-kazrin_repeat2 |
cd09495 |
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ... |
924-983 |
9.70e-31 |
|
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: 115.32 E-value: 9.70e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 924 WIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 983
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 ... |
1013-1074 |
1.09e-26 |
|
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: 103.77 E-value: 1.09e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363542 1013 QVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALILQIPTQNTQARQVMEREFNN 1074
Cdd:cd09496 1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETEFNN 62
|
|
| SAM_liprin-kazrin_repeat1 |
cd09494 |
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
810-868 |
3.24e-25 |
|
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: 99.22 E-value: 3.24e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2017363542 810 TVVSWLELWVGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQE 868
Cdd:cd09494 1 RVCAWLEDFGLMP-MYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
|
|
| SAM_kazrin_repeat3 |
cd09570 |
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin ... |
1005-1076 |
2.38e-19 |
|
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188969 Cd Length: 72 Bit Score: 83.26 E-value: 2.38e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363542 1005 DVLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALILQIPTQNTQARQVMEREFNNLL 1076
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 ... |
1005-1076 |
1.98e-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: 74.80 E-value: 1.98e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363542 1005 DVLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALILQIPTQNTQARQVMEREFNNLL 1076
Cdd:cd09569 1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
|
|
| SAM_kazrin_repeat2 |
cd09567 |
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ... |
919-983 |
3.71e-16 |
|
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: 73.98 E-value: 3.71e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363542 919 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 983
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 ... |
919-983 |
4.36e-16 |
|
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: 73.50 E-value: 4.36e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363542 919 DMNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLrVHLKMVDSFHRTSLQYGIMCLK 983
Cdd:cd09566 1 KLDTHWV-LRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDL-LHLKVTSALHHASIRRGIQVLR 63
|
|
| SAM_kazrin_repeat1 |
cd09564 |
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ... |
804-868 |
1.07e-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: 72.87 E-value: 1.07e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363542 804 AQWDGPTVVSWLELWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQE 868
Cdd:cd09564 2 SRWKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
919-983 |
5.49e-14 |
|
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: 67.68 E-value: 5.49e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363542 919 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 983
Cdd:pfam00536 1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
159-446 |
2.12e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.97 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 159 EHHKALDEKVRER-LRAALERVTTLEEQLAGAHQQVSALQqgagvrdgAAEEEGTVELgpkrlwKEDTGRVEELQELLEK 237
Cdd:COG1196 213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELE--------AELEELEAEL------AELEAELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 238 QNFELSQARERLVTltttvteleedlgtARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHD 317
Cdd:COG1196 279 LELELEEAQAEEYE--------------LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 318 LNDKLENELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLsdtvDRLLSESNERLQLHL 397
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL----EEAEEALLERLERLE 420
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2017363542 398 KERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 446
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-448 |
5.51e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.47 E-value: 5.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 101 ISELKAERNNTRLLLEH-------LECLVSRHERSLRMtvVKRQAQSpsgvsseVEVLKALKS-LFEHHKALDEKVRERL 172
Cdd:TIGR02168 167 ISKYKERRKETERKLERtrenldrLEDILNELERQLKS--LERQAEK-------AERYKELKAeLRELELALLVLRLEEL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 173 RAALERvttLEEQLAGAHQQVSALQQGAGVRDGAAEEegtvelgpKRLWKedtGRVEELQELLEKQNFELSQARERLVTL 252
Cdd:TIGR02168 238 REELEE---LQEELKEAEEELEELTAELQELEEKLEE--------LRLEV---SELEEEIEELQKELYALANEISRLEQQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 253 TTTVTELEEDLgtaRRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQreatsihDLNDKLENELANKESL 332
Cdd:TIGR02168 304 KQILRERLANL---ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE-------AELEELEAELEELESR 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 333 HRQAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNErlqLHLKERMAALEEKNTLIQ 412
Cdd:TIGR02168 374 LEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE---AELKELQAELEELEEELE 450
|
330 340 350
....*....|....*....|....*....|....*.
gi 2017363542 413 ELESSQRQIEEQhhhKGRLSEEIEKLRQEVDQLKGR 448
Cdd:TIGR02168 451 ELQEELERLEEA---LEELREELEEAEQALDAAERE 483
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
147-424 |
1.03e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.70 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 147 EVEVLKALKSLFEHHKALDEkVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVElgpkrlwKEDTG 226
Cdd:TIGR02168 711 EEELEQLRKELEELSRQISA-LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL-------AEAEA 782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 227 RVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYL 306
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 307 AAQREATSIHDLNDKLENELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQELArvRQREKMNEDHNK--RLSDTVDR 384
Cdd:TIGR02168 863 ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE--ELREKLAQLELRleGLEVRIDN 940
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2017363542 385 LLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQ 424
Cdd:TIGR02168 941 LQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
147-430 |
7.21e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 7.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 147 EVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKRLWKEdtg 226
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE--- 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 227 RVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYL 306
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 307 AAQREATSIHDLNDKLENELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLL 386
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2017363542 387 SESNERLQLHLKERMAALEEKNtliqeLESSQRQIEEQHHHKGR 430
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAA-----RLLLLLEAEADYEGFLE 508
|
|
| SAM_liprin-beta1,2_repeat1 |
cd09563 |
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
803-867 |
1.14e-10 |
|
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: 58.01 E-value: 1.14e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017363542 803 FAQWDGPTVVSWL-ELWVGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQ 867
Cdd:cd09563 1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
21-615 |
2.66e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 65.14 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 21 DADANFEQLMVNMLDErEKLLESLREsqeTLAATQSRLQDAIHERDQLQ----RHLNSALPQEFATLTRELSMCREQLLE 96
Cdd:pfam15921 167 DSNTQIEQLRKMMLSH-EGVLQEIRS---ILVDFEEASGKKIYEHDSMStmhfRSLGSAISKILRELDTEISYLKGRIFP 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 97 REEEISELKAE-RNNTRLLLEH----LECLVSRHERSL-----RMTVVKRQAQSpsgVSSEVEV------------LKAL 154
Cdd:pfam15921 243 VEDQLEALKSEsQNKIELLLQQhqdrIEQLISEHEVEItglteKASSARSQANS---IQSQLEIiqeqarnqnsmyMRQL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 155 KSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHqqvSALQQGAGVRDGAAEEEGTV----------------ELG-- 216
Cdd:pfam15921 320 SDLESTVSQLRSELREAKRMYEDKIEELEKQLVLAN---SELTEARTERDQFSQESGNLddqlqklladlhkrekELSle 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 217 ---PKRLWKEDTG-----------------RVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLG--TARRDLIKS- 273
Cdd:pfam15921 397 keqNKRLWDRDTGnsitidhlrrelddrnmEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSslTAQLESTKEm 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 274 -----EELSSKHQ---------RDLREALAQKEDMEE----RITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQ 335
Cdd:pfam15921 477 lrkvvEELTAKKMtlessertvSDLTASLQEKERAIEatnaEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQ 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 336 AEERHGNIEEHLRQLEG--QLEEKNQELARVRQREKMnedhnkrlsdtvdRLLSESNERlQLHLKERMAALEEKNTLIQE 413
Cdd:pfam15921 557 MAEKDKVIEILRQQIENmtQLVGQHGRTAGAMQVEKA-------------QLEKEINDR-RLELQEFKILKDKKDAKIRE 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 414 LESSQRQIEEQHHHKGRLSEE----IEKLRQEVDQLkgrggpfvdgvhsrshMGSAADVRFSLGTTTHAPPGVHRRYSAL 489
Cdd:pfam15921 623 LEARVSDLELEKVKLVNAGSErlraVKDIKQERDQL----------------LNEVKTSRNELNSLSEDYEVLKRNFRNK 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 490 REEsaKDWETSPLPGMLAPAAGPAFDSDPEISDVdEDEPGGLVGSA-----DVVSPSGHSDA-QTLAMMLQEQLDAINEE 563
Cdd:pfam15921 687 SEE--METTTNKLKMQLKSAQSELEQTRNTLKSM-EGSDGHAMKVAmgmqkQITAKRGQIDAlQSKIQFLEEAMTNANKE 763
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 2017363542 564 IRMIQEEKE--STELRAEEIETRVTSGSMEALNLKQLRKRGSIPTSLTALSLAS 615
Cdd:pfam15921 764 KHFLKEEKNklSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKAS 817
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
20-445 |
1.24e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 20 ADADANFEQLMVNMLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLN--SALPQEFATLTRELSMCREQLLER 97
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAqlEELEEAEEALLERLERLEEELEEL 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 98 EEEISELKAERNNTRLLLEHLECLVSRHE---RSLRMTVVKRQAQSPSGVSSEVEVLKAL---KSLFEHHKALDEKVRER 171
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEeeeEALLELLAELLEEAALLEAALAELLEELaeaAARLLLLLEAEADYEGF 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 172 LRAALERvtTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKRLwkEDTGRVEELQELLEKQN------FELSQA 245
Cdd:COG1196 507 LEGVKAA--LLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVV--EDDEVAAAAIEYLKAAKagratfLPLDKI 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 246 RERLVTLTTTVTELEEDL-GTARRDLIKSEELSSKHQRDLREALAQKEDME---ERITTLEKRYLAAQREATSIHDLNDK 321
Cdd:COG1196 583 RARAALAAALARGAIGAAvDLVASDLREADARYYVLGDTLLGRTLVAARLEaalRRAVTLAGRLREVTLEGEGGSAGGSL 662
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 322 LENELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERM 401
Cdd:COG1196 663 TGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELL 742
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2017363542 402 AALEEKNTLIQELESSQRQIEEqhhhkgrLSEEIEKLRQEVDQL 445
Cdd:COG1196 743 EEEELLEEEALEELPEPPDLEE-------LERELERLEREIEAL 779
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
9-448 |
2.61e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 9 NEGDRLGPPHGADADANFEQL--MVNMLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNS--------ALPQ 78
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELkeLEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKlekllqllPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 79 EFATLTRELSMCREQLLEREEEISELKAERNNTRLLLEHLEclvsRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLF 158
Cdd:COG4717 133 ELEALEAELAELPERLEELEERLEELRELEEELEELEAELA----ELQEELEELLEQLSLATEEELQDLAEELEELQQRL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 159 EHHKALDEKVRERLRAALERVTTLEEQLAGAH--QQVSALQQGAGVRDGAAEEEGTVELGPKRLWKED------TGRVEE 230
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQLENELEAAAleERLKEARLLLLIAAALLALLGLGGSLLSLILTIAgvlflvLGLLAL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 231 LQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQR 310
Cdd:COG4717 289 LFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEEL 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 311 EATSIHDLNDKLENELANKESLHRQAEERHgNIEEHLRQLEGQLEEKNQELARVRQREKmNEDHNKRLSDTVDRLLSESN 390
Cdd:COG4717 369 EQEIAALLAEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQLEELLGELEELLEALD-EEELEEELEELEEELEELEE 446
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2017363542 391 ERLQLHlkERMAALEEKntlIQELESSqrqieeqhhhkgrlsEEIEKLRQEVDQLKGR 448
Cdd:COG4717 447 ELEELR--EELAELEAE---LEQLEED---------------GELAELLQELEELKAE 484
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
262-448 |
9.92e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 9.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 262 DLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQAEERHG 341
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 342 NIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSD-------------------TVDRLLSESNERLQlHLKERMA 402
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEleekvkelkelkekaeeyiKLSEFYEEYLDELR-EIEKRLS 317
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2017363542 403 ALEEKntlIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGR 448
Cdd:PRK03918 318 RLEEE---INGIEERIKELEEKEERLEELKKKLKELEKRLEELEER 360
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
33-445 |
1.36e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.28 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 33 MLDEREKLLESL-------RESQETLAATQsRLQDAIHERDQLQRHLNSALPQEFATLTRELSMCREQLLEREEEISELK 105
Cdd:PRK02224 242 VLEEHEERREELetleaeiEDLRETIAETE-REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 106 AERNNTRLLLEHLECLVSRHER---SLRMTVVKRQAQSPSGVSS----EVEVLKALKSLFEHHKALDEkVRERLRAALER 178
Cdd:PRK02224 321 DRDEELRDRLEECRVAAQAHNEeaeSLREDADDLEERAEELREEaaelESELEEAREAVEDRREEIEE-LEEEIEELRER 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 179 VTTLEEQLAGAHQQVSALQQGagvRDGAAEEEGTVELGpkrlWKEDTGRVEELQELLEK-------QNFELSQARERLVT 251
Cdd:PRK02224 400 FGDAPVDLGNAEDFLEELREE---RDELREREAELEAT----LRTARERVEEAEALLEAgkcpecgQPVEGSPHVETIEE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 252 LTTTVTELEEDLGTARRDLiksEELSSKHQR--DLREALAQKEDMEERITTLEKRY------LAAQRE-ATSIHDLNDKL 322
Cdd:PRK02224 473 DRERVEELEAELEDLEEEV---EEVEERLERaeDLVEAEDRIERLEERREDLEELIaerretIEEKRErAEELRERAAEL 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 323 ENELANKESlhrQAEERHGNIEEHLRQLeGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRL--LSESNERLQLHLKER 400
Cdd:PRK02224 550 EAEAEEKRE---AAAEAEEEAEEAREEV-AELNSKLAELKERIESLERIRTLLAAIADAEDEIerLREKREALAELNDER 625
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2017363542 401 MAALEEKNTLIQELESS--QRQIEEQHHHKGRLSEEIEKLRQEVDQL 445
Cdd:PRK02224 626 RERLAEKRERKRELEAEfdEARIEEAREDKERAEEYLEQVEEKLDEL 672
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
218-448 |
2.32e-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: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 218 KRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEE----LSSKHQRDLREALAQKED 293
Cdd:TIGR02169 155 RRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERyqalLKEKREYEGYELLKEKEA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 294 MEERITTLEKRYlaaqreatsihdlnDKLENELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQELARvRQREKMNED 373
Cdd:TIGR02169 235 LERQKEAIERQL--------------ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL-RVKEKIGEL 299
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363542 374 HNKRLSdtVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGR 448
Cdd:TIGR02169 300 EAEIAS--LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE 372
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
32-435 |
2.46e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 58.59 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 32 NMLDEREKLLesLRESQETLaatQSRLQDAIHERDQLqrhlnsalpqefATLTRELSMCReqllereeeiSELKAERNNT 111
Cdd:pfam15921 98 NELHEKQKFY--LRQSVIDL---QTKLQEMQMERDAM------------ADIRRRESQSQ----------EDLRNQLQNT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 112 RLLLEHLECLVSR--HERSLRMTVVKRQAQSPSGVSSEVEVL------KALKSLFEHH-------KALDEKVRERLRAAL 176
Cdd:pfam15921 151 VHELEAAKCLKEDmlEDSNTQIEQLRKMMLSHEGVLQEIRSIlvdfeeASGKKIYEHDsmstmhfRSLGSAISKILRELD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 177 ERVTTLEEQLAGAHQQVSALQqgagvrdgaAEEEGTVELgpkrLWKEDTGRVE--------ELQELLEKQNFELSQARER 248
Cdd:pfam15921 231 TEISYLKGRIFPVEDQLEALK---------SESQNKIEL----LLQQHQDRIEqlisehevEITGLTEKASSARSQANSI 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 249 LVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREAlaqKEDMEERITTLEKRYLAAQREATSIHDLNDKLENElan 328
Cdd:pfam15921 298 QSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREA---KRMYEDKIEELEKQLVLANSELTEARTERDQFSQE--- 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 329 keslhrqaeerHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNER---------------- 392
Cdd:pfam15921 372 -----------SGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRnmevqrleallkamks 440
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2017363542 393 -LQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEI 435
Cdd:pfam15921 441 eCQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEEL 484
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
229-446 |
2.72e-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: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 229 EELQELL-EKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTL-EKRYL 306
Cdd:TIGR02169 211 ERYQALLkEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 307 AAQREATSIHDLNDKLENELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLL 386
Cdd:TIGR02169 291 RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLR 370
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 387 SesneRLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 446
Cdd:TIGR02169 371 A----ELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN 426
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
164-441 |
3.46e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 164 LDEK-VRERLRAALERVTTL---EEQLAGAHQQVSALQQgagVRDGAAEeegtvelgpkrlWKEDTGRVEELQELLEKQN 239
Cdd:COG4913 218 LEEPdTFEAADALVEHFDDLeraHEALEDAREQIELLEP---IRELAER------------YAAARERLAELEYLRAALR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 240 FELSQARerlvtltttvteleedLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATsihdln 319
Cdd:COG4913 283 LWFAQRR----------------LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRL------ 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 320 DKLENELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQELARVRQRekmnedhnkrlsdtVDRLLSESNERLQLHLKE 399
Cdd:COG4913 341 EQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE--------------AAALLEALEEELEALEEA 406
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2017363542 400 RMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQE 441
Cdd:COG4913 407 LAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDA 448
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
803-869 |
4.12e-08 |
|
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: 51.14 E-value: 4.12e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017363542 803 FAQWDGPTVVSWLELWvGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEM 869
Cdd:smart00454 1 VSQWSPESVADWLESI-GLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
31-444 |
5.67e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 57.04 E-value: 5.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 31 VNMLDEREKLL-ESLRESQETLAATQSRLQDAiheRDQLQRHLNS--ALPQEFATLTRELSMCREQLLEREEE------- 100
Cdd:pfam05483 270 ANQLEEKTKLQdENLKELIEKKDHLTKELEDI---KMSLQRSMSTqkALEEDLQIATKTICQLTEEKEAQMEElnkakaa 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 101 ----ISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgvsSEVEVLKALKS-----LFEHHKALDEKvrER 171
Cdd:pfam05483 347 hsfvVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS-----SELEEMTKFKNnkeveLEELKKILAED--EK 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 172 LRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKRLWKEDtgrVEELQELLEKQ---NFELSQARER 248
Cdd:pfam05483 420 LLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKE---VEDLKTELEKEklkNIELTAHCDK 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 249 LVTLTTTVTELEEDLgtarrdlikSEELSsKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHD----------- 317
Cdd:pfam05483 497 LLLENKELTQEASDM---------TLELK-KHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREefiqkgdevkc 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 318 LNDKLENELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNeRLQLHL 397
Cdd:pfam05483 567 KLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVN-KLELEL 645
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2017363542 398 KERMAALEEKntliqeLESSQRQIEEQHHHKGRLSEEIEKLRQEVDQ 444
Cdd:pfam05483 646 ASAKQKFEEI------IDNYQKEIEDKKISEEKLLEEVEKAKAIADE 686
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
281-446 |
5.98e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.31 E-value: 5.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 281 QRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQE 360
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 361 LARVRQR--EKMNEDHNKRLSDTVDRLLSESN--------ERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGR 430
Cdd:COG4942 99 LEAQKEElaELLRALYRLGRQPPLALLLSPEDfldavrrlQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170
....*....|....*.
gi 2017363542 431 LSEEIEKLRQEVDQLK 446
Cdd:COG4942 179 LLAELEEERAALEALK 194
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
149-367 |
6.06e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 6.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 149 EVLKALKSLFEH----HKALdEKVRERLRAaLERVTTLEEQLAGAHQQVSALQQ-GAGVRDGAAEEEgtvelgpKRLWKE 223
Cdd:COG4913 225 EAADALVEHFDDleraHEAL-EDAREQIEL-LEPIRELAERYAAARERLAELEYlRAALRLWFAQRR-------LELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 224 DTGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKsEELSSKhQRDLREALAQKEDMEERITTLEk 303
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLE-REIERL-ERELEERERRRARLEALLAALG- 372
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2017363542 304 ryLAAQREATSIHDLNDKLENELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQELARVRQR 367
Cdd:COG4913 373 --LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
227-449 |
7.36e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 7.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 227 RVEELQELLEkqnfELSQARERlvtltttvteleedLGTARRDLIKSEELSSKHQR--DLREALAQKEDMEERIT--TLE 302
Cdd:COG4913 226 AADALVEHFD----DLERAHEA--------------LEDAREQIELLEPIRELAERyaAARERLAELEYLRAALRlwFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 303 KRYLAAQREATSIHDLNDKLENELANKESLHRQAEERHGNIEEHLRQ--------LEGQLEEKNQELARVRQREKmnedh 374
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdrleqLEREIERLERELEERERRRA----- 362
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017363542 375 nkRLSDTVDRL---LSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHhkgRLSEEIEKLRQEVDQLKGRG 449
Cdd:COG4913 363 --RLEALLAALglpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR---DLRRELRELEAEIASLERRK 435
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
928-983 |
8.42e-08 |
|
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: 50.37 E-value: 8.42e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2017363542 928 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 983
Cdd:smart00454 11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
22-448 |
1.52e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 22 ADANFEQLMVNMLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQrhlnsALPQEFATLTRELSMCREQLLEREEEI 101
Cdd:PRK03918 187 RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE-----ELKEEIEELEKELESLEGSKRKLEEKI 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 102 SELKAERNNTRLLLEHLECLVSRHE--RSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRErLRAALERV 179
Cdd:PRK03918 262 RELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE-LEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 180 TTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTEL 259
Cdd:PRK03918 341 EELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 260 EEDLGTARRDLIKS----------------EELSSKHQRDLREALAQKEDMEERITTLEKR------YLAAQREATSIHD 317
Cdd:PRK03918 421 IKELKKAIEELKKAkgkcpvcgrelteehrKELLEEYTAELKRIEKELKEIEEKERKLRKElrelekVLKKESELIKLKE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 318 LNDKL---ENELA--NKESLHRQAEErHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLsDTVDRLLSESNER 392
Cdd:PRK03918 501 LAEQLkelEEKLKkyNLEELEKKAEE-YEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKL-DELEEELAELLKE 578
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017363542 393 LQL-------HLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGR 448
Cdd:PRK03918 579 LEElgfesveELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKR 641
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
35-442 |
1.65e-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: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 35 DEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSALpQEFATLTRELSMCREQLLEREEEISELKAERNNTRLL 114
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL-AELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 115 LEHLECLVSRHERSLRMTVVKRQAqspsgvsSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVS 194
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEE-------AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 195 ALQQGAGVRDGAAEEEGTVELGPKRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSE 274
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 275 ELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQAEERHGNIEEHLRQLEGQL 354
Cdd:COG1196 485 ELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIE 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 355 EEKNQELARVRqREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERmaALEEKNTLIQELESSQRQIEEQHHHKGRLSEE 434
Cdd:COG1196 565 YLKAAKAGRAT-FLPLDKIRARAALAAALARGAIGAAVDLVASDLR--EADARYYVLGDTLLGRTLVAARLEAALRRAVT 641
|
....*...
gi 2017363542 435 IEKLRQEV 442
Cdd:COG1196 642 LAGRLREV 649
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
42-334 |
1.91e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 42 ESLRESQETLAATqsRLQDAIHERDQLQRHLNsALPQEFATLTRELSMCREQLLEREEEISELKAERNNTRLLLEHLECL 121
Cdd:TIGR02168 220 AELRELELALLVL--RLEELREELEELQEELK-EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 122 VSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLfEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAG 201
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKL-DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 202 VRDGAAEEEGTVELGPKRLWKEDTGRVEELQELLEKQnfELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQ 281
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL--EDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQ 453
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2017363542 282 RDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHR 334
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE 506
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
267-446 |
2.07e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 267 RRDLIksEELS--SKHQRDLREALAQKEDMEERITTLE--------------------KRYLAAQREATsIHDLN----- 319
Cdd:COG1196 157 RRAII--EEAAgiSKYKERKEEAERKLEATEENLERLEdilgelerqleplerqaekaERYRELKEELK-ELEAEllllk 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 320 -DKLENELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQELARVRQR-EKMNEDHNKRLSDtvdrlLSESNERLQLHL 397
Cdd:COG1196 234 lRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELElEEAQAEEYELLAE-----LARLEQDIARLE 308
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2017363542 398 KERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 446
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
34-442 |
2.86e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 55.23 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 34 LDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSALPQEFATLTRELSmcrEQLLEREEEISELKAERNNTRl 113
Cdd:pfam12128 246 LQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWK---EKRDELNGELSAADAAVAKDR- 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 114 llEHLECLVSRHERSLRMTVVKR---QAQSPSgVSSEVEVL-KALKSLFEHHK-------ALDEKVRERLRAALERVT-- 180
Cdd:pfam12128 322 --SELEALEDQHGAFLDADIETAaadQEQLPS-WQSELENLeERLKALTGKHQdvtakynRRRSKIKEQNNRDIAGIKdk 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 181 ------TLEEQLAGAHQQVSAL------QQGAGVRDGAAEEEGTVE-LGPKRLWKEDTGRVEELQELLEKQNFELSQARE 247
Cdd:pfam12128 399 lakireARDRQLAVAEDDLQALeselreQLEAGKLEFNEEEYRLKSrLGELKLRLNQATATPELLLQLENFDERIERARE 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 248 RLVTLTTTVTELEEDLGTARRdliKSEELSSKHQR------DLREALAQKEDM-------------------EERITTLE 302
Cdd:pfam12128 479 EQEAANAEVERLQSELRQARK---RRDQASEALRQasrrleERQSALDELELQlfpqagtllhflrkeapdwEQSIGKVI 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 303 KRYL---------------------------AAQREATSIHDLNDKLENELANKESLHRQAEERHGNIEEHLRQLEGQLE 355
Cdd:pfam12128 556 SPELlhrtdldpevwdgsvggelnlygvkldLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELE 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 356 EKNQELARVRQREKMNEDHNKRLSDtvdrllSESNERLQLHlKERMAALEEKNTLIQELESSQRQIEEQH-----HHKGR 430
Cdd:pfam12128 636 KASREETFARTALKNARLDLRRLFD------EKQSEKDKKN-KALAERKDSANERLNSLEAQLKQLDKKHqawleEQKEQ 708
|
490
....*....|....*
gi 2017363542 431 LSE---EIEKLRQEV 442
Cdd:pfam12128 709 KREartEKQAYWQVV 723
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
227-450 |
3.93e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 227 RVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSK---HQRDLREALAQKEDMEERITTLEK 303
Cdd:PRK03918 187 RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEieeLEKELESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 304 RYLAAQREatsIHDLNDKLE--NELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDT 381
Cdd:PRK03918 267 RIEELKKE---IEELEEKVKelKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 382 VDRL------LSESNERLQLH-----LKERMAALEEKNTlIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGRGG 450
Cdd:PRK03918 344 KKKLkelekrLEELEERHELYeeakaKKEELERLKKRLT-GLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIK 422
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
281-441 |
7.97e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 7.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 281 QRDLREALAQKEDMEERITTLEKRYLAAQREATS-------------IHDLNDKLENELANKESLhRQAEERHGNIEEHL 347
Cdd:COG4913 623 EEELAEAEERLEALEAELDALQERREALQRLAEYswdeidvasaereIAELEAELERLDASSDDL-AALEEQLEELEAEL 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 348 RQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHH 427
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRAR 781
|
170
....*....|....
gi 2017363542 428 KGRLSEEIEKLRQE 441
Cdd:COG4913 782 LNRAEEELERAMRA 795
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
320-448 |
1.26e-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: 51.08 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 320 DKLENELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQELARVRqrEKMNEDHNKRLSDTVDR---LLSESNERLQLH 396
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE--EQLGNVRNNKEYEALQKeieSLKRRISDLEDE 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2017363542 397 LKERMAALEEKNTLIQELESSQRQIEEQHHH-KGRLSEEIEKLRQEVDQLKGR 448
Cdd:COG1579 112 ILELMERIEELEEELAELEAELAELEAELEEkKAELDEELAELEAELEELEAE 164
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
222-448 |
1.57e-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: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 222 KEDTGRVEELQELLEKQNFELSQARERLVTLTTTvteleedLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTL 301
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENR-------LDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 302 EKRYLAAQREATSIHDLNDKLENELANKESLHRQAEERHGNIEEHLRQleGQLEEKNQELARVRQREKMNEdhnKRLSDt 381
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIE---ARLRE- 816
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017363542 382 VDRLLSESNERLQLhLKERMAALEEKNTLIQELESS-QRQIEEQHHHKGRLSEEIEKLRQEVDQLKGR 448
Cdd:TIGR02169 817 IEQKLNRLTLEKEY-LEKEIQELQEQRIDLKEQIKSiEKEIENLNGKKEELEEELEELEAALRDLESR 883
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
229-406 |
1.88e-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: 50.31 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 229 EELQELLEKQNF--ELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRyl 306
Cdd:COG1579 4 EDLRALLDLQELdsELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 307 aaQREATSIHDLNDkLENELAnkeslhrQAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLL 386
Cdd:COG1579 82 --LGNVRNNKEYEA-LQKEIE-------SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL 151
|
170 180
....*....|....*....|
gi 2017363542 387 SESNERLQLHLKERMAALEE 406
Cdd:COG1579 152 AELEAELEELEAEREELAAK 171
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
229-441 |
4.14e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 229 EELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYlAA 308
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL-AE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 309 QREATSIHDLNDKLENELANKESLhrQAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRlLSE 388
Cdd:COG4942 109 LLRALYRLGRQPPLALLLSPEDFL--DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE-LEE 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2017363542 389 SNERLQLHLKERMAALEEKNtliQELESSQRQIEEQHHHKGRLSEEIEKLRQE 441
Cdd:COG4942 186 ERAALEALKAERQKLLARLE---KELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
159-444 |
5.54e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 5.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 159 EHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDgaAEEEGTVElgPKRLWKEDTG----RVEELQEL 234
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKK--AEEKKKAE--EAKKAEEDKNmalrKAEEAKKA 1589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 235 LEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEE-------LSSKHQRDLREALAQKEDMEERITTLEKRYLA 307
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEekkkveqLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK 1669
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 308 AQREATSIHDLNDKLENELANKESLHRQAEERhgnieehlRQLEgQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLS 387
Cdd:PTZ00121 1670 AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA--------KKAE-ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE 1740
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363542 388 ESNERLQLHLKERmaalEEKNTLIQELESSQRQIEEQHHHKGR-----LSEEIEKLRQEVDQ 444
Cdd:PTZ00121 1741 EDKKKAEEAKKDE----EEKKKIAHLKKEEEKKAEEIRKEKEAvieeeLDEEDEKRRMEVDK 1798
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
34-448 |
5.56e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 34 LDEREKLLESLRESQETLaatqSRLqdaIHERDQLQRHLNSaLPQEFATLTRELSMCREQLLEREEEISELKAERNNTRL 113
Cdd:PRK03918 278 LEEKVKELKELKEKAEEY----IKL---SEFYEEYLDELRE-IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 114 LLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKAlDEKVRERLRAALERVTTLEEQLAGAHQQV 193
Cdd:PRK03918 350 LEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKA-KEEIEEEISKITARIGELKKEIKELKKAI 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 194 SALQQGAGV-----RDGAAEEEgtvelgpKRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEdLGTARR 268
Cdd:PRK03918 429 EELKKAKGKcpvcgRELTEEHR-------KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESE-LIKLKE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 269 --DLIKS--EELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQAEERHGNIE 344
Cdd:PRK03918 501 laEQLKEleEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELE 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 345 EHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQL--HLKERMAALEEKNTLIQELES--SQRQ 420
Cdd:PRK03918 581 ELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAfeELAETEKRLEELRKELEELEKkySEEE 660
|
410 420
....*....|....*....|....*...
gi 2017363542 421 IEEQHHHKGRLSEEIEKLRQEVDQLKGR 448
Cdd:PRK03918 661 YEELREEYLELSRELAGLRAELEELEKR 688
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
343-448 |
5.87e-06 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 48.67 E-value: 5.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 343 IEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLlsesNERLQLHLK---ERMA--ALEEKNTLIQELESS 417
Cdd:COG1842 28 LDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKW----EEKARLALEkgrEDLAreALERKAELEAQAEAL 103
|
90 100 110
....*....|....*....|....*....|.
gi 2017363542 418 QRQIEEQHHHKGRLSEEIEKLRQEVDQLKGR 448
Cdd:COG1842 104 EAQLAQLEEQVEKLKEALRQLESKLEELKAK 134
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
34-407 |
5.91e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 5.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 34 LDEREKLLESLRESQETLAATQSRLQDAIherDQLQRHLNSALPQEFATLTRELSMCREQLLEREEEISELKAERNNTRL 113
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEEL---EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 114 LLEHLECLVSRHER--------------SLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERV 179
Cdd:COG4717 228 ELEQLENELEAAALeerlkearlllliaAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEEL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 180 TTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKRLWKEDTGRVEELQEllekqnfELSQARERLVTLTTTVTEL 259
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE-------ELQLEELEQEIAALLAEAG 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 260 EEDLGTARRDLIKSEElsskhQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDkLENELANKESLHRQAEER 339
Cdd:COG4717 381 VEDEEELRAALEQAEE-----YQELKEELEELEEQLEELLGELEELLEALDEEELEEELEE-LEEELEELEEELEELREE 454
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 340 HGNIEEHLRQLE--GQLEEKNQELARVRQREKMNEDHNKRLsDTVDRLLSESNERLQlhlKERMAALEEK 407
Cdd:COG4717 455 LAELEAELEQLEedGELAELLQELEELKAELRELAEEWAAL-KLALELLEEAREEYR---EERLPPVLER 520
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
272-446 |
6.16e-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: 50.40 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 272 KSEELSSKHQrDLREALAQKEDMEERITTLEKrylaaqrEATSIHDLNDKLENELANKESLHRQAEERHGNIEEHLR--Q 349
Cdd:TIGR04523 487 KQKELKSKEK-ELKKLNEEKKELEEKVKDLTK-------KISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKkeN 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 350 LEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNErlqlhLKERmaaLEEKNTLIQELESSQRQIEEQHHhkg 429
Cdd:TIGR04523 559 LEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKD-----LIKE---IEEKEKKISSLEKELEKAKKENE--- 627
|
170 180
....*....|....*....|....
gi 2017363542 430 RLSEEI-------EKLRQEVDQLK 446
Cdd:TIGR04523 628 KLSSIIknikskkNKLKQEVKQIK 651
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
163-448 |
6.22e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.72 E-value: 6.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 163 ALDEKVRERLRAALERVTTLEEQLAgahQQVSALQQGAGVRDGAAEEEGTVE--LGPKRLWKEDT--GRVEELQELLEkq 238
Cdd:COG3096 829 AFAPDPEAELAALRQRRSELERELA---QHRAQEQQLRQQLDQLKEQLQLLNklLPQANLLADETlaDRLEELREELD-- 903
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 239 nfELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELsskhQRDLREALAQKEDMEERITTLEkrYLAAQREATSIHD- 317
Cdd:COG3096 904 --AAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQL----QADYLQAKEQQRRLKQQIFALS--EVVQRRPHFSYEDa 975
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 318 ---------LNDKLENELANKESLHRQAEERhgnieehLRQLEGQLEEKNQELA----RVRQREKMNEDHNKRLSDTVDR 384
Cdd:COG3096 976 vgllgensdLNEKLRARLEQAEEARREAREQ-------LRQAQAQYSQYNQVLAslksSRDAKQQTLQELEQELEELGVQ 1048
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017363542 385 LLSESNERLQLHLKERMAAL----EEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGR 448
Cdd:COG3096 1049 ADAEAEERARIRRDELHEELsqnrSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKAG 1116
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
1006-1077 |
6.86e-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: 44.98 E-value: 6.86e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363542 1006 VLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHntlalILQIPTQNTQARQVMEREFNNLLA 1077
Cdd:smart00454 1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEED-----LKELGITKLGHRKKILKAIQKLKE 67
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
38-445 |
7.48e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 7.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 38 EKLLESLRESQETLAATQSRLQDA-IHERdqlqrhLNsALPQEFATLTRElsmcreqllereeeISELKAERNNTRLLLE 116
Cdd:PRK02224 179 ERVLSDQRGSLDQLKAQIEEKEEKdLHER------LN-GLESELAELDEE--------------IERYEEQREQARETRD 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 117 HLECLVSRHERSLrmtvvkrqaqspsgvsSEVEVLKALKSLFEHHKALDEKVRERLRaalERVTTLEEQLAGAHQQVSAL 196
Cdd:PRK02224 238 EADEVLEEHEERR----------------EELETLEAEIEDLRETIAETEREREELA---EEVRDLRERLEELEEERDDL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 197 QQGAGVRDGAAEeegTVELGPKRLWKEDtgrvEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEEL 276
Cdd:PRK02224 299 LAEAGLDDADAE---AVEARREELEDRD----EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 277 SSKHQRDLREALAQKEDMEERITTLEKRYLAAqreATSIHDLNDKLENELANKESLHrqaeERHGNIEEHLRQLEGQLEE 356
Cdd:PRK02224 372 LEEAREAVEDRREEIEELEEEIEELRERFGDA---PVDLGNAEDFLEELREERDELR----EREAELEATLRTARERVEE 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 357 KNQELA------------------RVRQREKMNEDHNKRLSDTVDRLlSESNERLQlHLKERMAALEEKNTLIQELESSQ 418
Cdd:PRK02224 445 AEALLEagkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEV-EEVEERLE-RAEDLVEAEDRIERLEERREDLE 522
|
410 420
....*....|....*....|....*..
gi 2017363542 419 RQIEEQHHHKGRLSEEIEKLRQEVDQL 445
Cdd:PRK02224 523 ELIAERRETIEEKRERAEELRERAAEL 549
|
|
| SAM_superfamily |
cd09487 |
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
928-979 |
8.04e-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: 8.04e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2017363542 928 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGI 979
Cdd:cd09487 4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
1006-1076 |
1.07e-05 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 44.18 E-value: 1.07e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017363542 1006 VLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALdeNFDHNTLAlilQIPTQNTQARQVMEREFNNLL 1076
Cdd:pfam07647 1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK---RLGITSVGHRRKILKKIQELK 66
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
228-446 |
1.53e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 228 VEELQELLEKQNFE-LSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKhqrdLREALAQKEDMEERITTLEKRYL 306
Cdd:PRK03918 505 LKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKK----LAELEKKLDELEEELAELLKELE 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 307 aaQREATSIHDLNDKLE---------NELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQELARVRQREkmnEDHNKR 377
Cdd:PRK03918 581 --ELGFESVEELEERLKelepfyneyLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL---EELEKK 655
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2017363542 378 LSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 446
Cdd:PRK03918 656 YSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVE 724
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
229-448 |
1.93e-05 |
|
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: 48.91 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 229 EELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRyLAA 308
Cdd:TIGR02169 691 SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR-IEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 309 QREAtsIHDLNDKLEN--------ELANKESLHRQAEERHGNIEEHLRQLEG----------QLEEKNQELARVRQREKM 370
Cdd:TIGR02169 770 LEED--LHKLEEALNDlearlshsRIPEIQAELSKLEEEVSRIEARLREIEQklnrltlekeYLEKEIQELQEQRIDLKE 847
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017363542 371 NEDHNKRLSDTVDRLLSESNERlqlhLKERMAALEEkntLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGR 448
Cdd:TIGR02169 848 QIKSIEKEIENLNGKKEELEEE----LEELEAALRD---LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKR 918
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
285-424 |
2.36e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 285 REALAQKEDMEerittlekryLAAQREatsIHDLNDKLENELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQELARV 364
Cdd:PRK12704 49 KEAEAIKKEAL----------LEAKEE---IHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKK 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017363542 365 RQREKMNEDHNKRLSDTVDRLLSESNERLqlhlkERMAAL---EEKNTLIQELESSQR--------QIEEQ 424
Cdd:PRK12704 116 EKELEQKQQELEKKEEELEELIEEQLQEL-----ERISGLtaeEAKEILLEKVEEEARheaavlikEIEEE 181
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
267-448 |
2.62e-05 |
|
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: 48.58 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 267 RRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQ---REATSIHDLNDKLENELAN----KESLHRQAEER 339
Cdd:pfam05557 26 KRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEealREQAELNRLKKKYLEALNKklneKESQLADAREV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 340 HGNIEEHLRQLEGQLEEKNQELARVR-QREKMNEDHN---KRLSDtvdrlLSESNERLQLHLKERMAALEEKNTLIQELE 415
Cdd:pfam05557 106 ISCLKNELSELRRQIQRAELELQSTNsELEELQERLDllkAKASE-----AEQLRQNLEKQQSSLAEAEQRIKELEFEIQ 180
|
170 180 190
....*....|....*....|....*....|...
gi 2017363542 416 SSQRQIEEQHHHKGRLsEEIEKLRQEVDQLKGR 448
Cdd:pfam05557 181 SQEQDSEIVKNSKSEL-ARIPELEKELERLREH 212
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
149-370 |
3.48e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 149 EVLKALKSLFEHHKALDEkVRERLRAALERVTTLEEQLAGAHQQVSALQQgagvrdgaaeeegtvelgpkrlwkedtgRV 228
Cdd:COG1579 4 EDLRALLDLQELDSELDR-LEHRLKELPAELAELEDELAALEARLEAAKT----------------------------EL 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 229 EELQELLEKQNFELSQARERLVtltttvteleedlgtarrdliKSEEL--SSKHQRDLREALAQKEDMEERITTLEKRYL 306
Cdd:COG1579 55 EDLEKEIKRLELEIEEVEARIK---------------------KYEEQlgNVRNNKEYEALQKEIESLKRRISDLEDEIL 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363542 307 AAQREAtsihdlnDKLENELANKESLHRQAEERhgnIEEHLRQLEGQLEEKNQELARVR-QREKM 370
Cdd:COG1579 114 ELMERI-------EELEEELAELEAELAELEAE---LEEKKAELDEELAELEAELEELEaEREEL 168
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
39-445 |
4.03e-05 |
|
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: 48.14 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 39 KLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSalpqefatLTRELSMCREQLLEREEEISELKAERNNTRLLLEHL 118
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDE--------LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 119 EclvsrherslrmtvvkrqaqspsgvssevEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAG--AHQQVSAL 196
Cdd:TIGR02169 743 E-----------------------------EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDleARLSHSRI 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 197 QQgagVRDGAAEEEGTVelgpkrlwKEDTGRVEELQELLEKQNFELSQARErlvtLTTTVTELEEDLGTARRDLIKSEEL 276
Cdd:TIGR02169 794 PE---IQAELSKLEEEV--------SRIEARLREIEQKLNRLTLEKEYLEK----EIQELQEQRIDLKEQIKSIEKEIEN 858
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 277 SSKHQRDLREALAQKE----DMEERITTLEKrylaaQReatsihdlnDKLENELANKESLHRQAEERHGNIEEHLRQLEG 352
Cdd:TIGR02169 859 LNGKKEELEEELEELEaalrDLESRLGDLKK-----ER---------DELEAQLRELERKIEELEAQIEKKRKRLSELKA 924
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 353 QLEEKNQELARVrqrekmnEDHNKRLSDTVDRLLSEsnERLQLHLK---ERMAALEEKNTL-IQELESSQRQIEEQHHHK 428
Cdd:TIGR02169 925 KLEALEEELSEI-------EDPKGEDEEIPEEELSL--EDVQAELQrveEEIRALEPVNMLaIQEYEEVLKRLDELKEKR 995
|
410
....*....|....*..
gi 2017363542 429 GRLSEEIEKLRQEVDQL 445
Cdd:TIGR02169 996 AKLEEERKAILERIEEY 1012
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
32-446 |
4.30e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.04 E-value: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 32 NMLDEREKLLESLRESQETLAATQsRLQDAIHERDQLQRHLNSALPQEfATLTRELSmcreqllereeEISELKAERNNT 111
Cdd:TIGR00618 223 VLEKELKHLREALQQTQQSHAYLT-QKREAQEEQLKKQQLLKQLRARI-EELRAQEA-----------VLEETQERINRA 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 112 RllleHLECLVsrhERSLRMTVVKRQAQspsgvssevevlkalkslfEHHKALDEKVRERLRAALERVTTLEEQLAGAHQ 191
Cdd:TIGR00618 290 R----KAAPLA---AHIKAVTQIEQQAQ-------------------RIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 192 QVSA---LQQGAGVRDGAAEEEGTVELGPKRlwKEDTGRVEELQELLEKQNfELSQARERLVTLTTTVTELEEDLGTARR 268
Cdd:TIGR00618 344 RRLLqtlHSQEIHIRDAHEVATSIREISCQQ--HTLTQHIHTLQQQKTTLT-QKLQSLCKELDILQREQATIDTRTSAFR 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 269 DLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHdlnDKLENELANKESLHRQAEERHGNIEEHL- 347
Cdd:TIGR00618 421 DLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSL---KEREQQLQTKEQIHLQETRKKAVVLARLl 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 348 ------RQLEGQLEEKNQEL----------ARVRQREKMNEDHNKRLSDTVDRLLSEsnerlqlhlKERMAALEEKNTLI 411
Cdd:TIGR00618 498 elqeepCPLCGSCIHPNPARqdidnpgpltRRMQRGEQTYAQLETSEEDVYHQLTSE---------RKQRASLKEQMQEI 568
|
410 420 430
....*....|....*....|....*....|....*
gi 2017363542 412 QELESSQRQIEEqhhhkgRLSEEIEKLRQEVDQLK 446
Cdd:TIGR00618 569 QQSFSILTQCDN------RSKEDIPNLQNITVRLQ 597
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
263-445 |
4.33e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.71 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 263 LGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYlaaQREATSIHDLNDKLENELaNKEsLHRQAEerhgN 342
Cdd:TIGR04523 248 ISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQL---NQLKSEISDLNNQKEQDW-NKE-LKSELK----N 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 343 IEEHLRQLEGQLEEKNQELARVRQ------REKMNEDHNKRlsdTVDRLLSESNERLQLHLKERMAALEEKNTLIQELES 416
Cdd:TIGR04523 319 QEKKLEEIQNQISQNNKIISQLNEqisqlkKELTNSESENS---EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIND 395
|
170 180
....*....|....*....|....*....
gi 2017363542 417 SQRQIEEQHHHKGRLSEEIEKLRQEVDQL 445
Cdd:TIGR04523 396 LESKIQNQEKLNQQKDEQIKKLQQEKELL 424
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
235-441 |
4.41e-05 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 47.11 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 235 LEKQNFELSQARErlvtlttTVTELEEDLGTARRDLIKSEEL-SSKHQRD--LREALAQKEDME--------------ER 297
Cdd:pfam15905 127 LEKQLLELTRVNE-------LLKAKFSEDGTQKKMSSLSMELmKLRNKLEakMKEVMAKQEGMEgklqvtqknlehskGK 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 298 ITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQAEErhgnIEEHLRQLEGQLEEKNQELARVRQREKMNEDHnkr 377
Cdd:pfam15905 200 VAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEK----YKLDIAQLEELLKEKNDEIESLKQSLEEKEQE--- 272
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017363542 378 LSDTVDRLlsesNERLQL--HLKERMAALEE--KNTLIQELESSQRQIEEQhhhkgrlSEEIEKLRQE 441
Cdd:pfam15905 273 LSKQIKDL----NEKCKLleSEKEELLREYEekEQTLNAELEELKEKLTLE-------EQEHQKLQQK 329
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
104-448 |
8.11e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 46.74 E-value: 8.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 104 LKAERNNTRLLLEHLECLVSRHERSLRmtvvkRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLraaLERVTTLE 183
Cdd:pfam10174 343 LQTEVDALRLRLEEKESFLNKKTKQLQ-----DLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENL---QEQLRDKD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 184 EQLAGAHQQVSALQQGAGVRDGA--------AEEEGTVELGPKRLWKEDTGRVEELqELLEKQNFELSQARERLVTLTTT 255
Cdd:pfam10174 415 KQLAGLKERVKSLQTDSSNTDTAlttleealSEKERIIERLKEQREREDRERLEEL-ESLKKENKDLKEKVSALQPELTE 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 256 VTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDK---LENELANK--E 330
Cdd:pfam10174 494 KESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRirlLEQEVARYkeE 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 331 SLHRQAE-ERHGNIeehLRQLEgqlEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNT 409
Cdd:pfam10174 574 SGKAQAEvERLLGI---LREVE---NEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDN 647
|
330 340 350
....*....|....*....|....*....|....*....
gi 2017363542 410 LIQEleSSQRQIEEqhhhkgrLSEEIEKLRQEVDQLKGR 448
Cdd:pfam10174 648 LADN--SQQLQLEE-------LMGALEKTRQELDATKAR 677
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
227-421 |
8.90e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 8.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 227 RVEELQELLEKQNFELSQARERlvtltttVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYL 306
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREE-------LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 307 AAQREATSIHDLNDKLENELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQELARVRQreKMNEDHNKRLSDTVDRLL 386
Cdd:COG4372 112 ELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ--ELQALSEAEAEQALDELL 189
|
170 180 190
....*....|....*....|....*....|....*
gi 2017363542 387 SESNERLQLHLKERMAALEEKNTLIQELESSQRQI 421
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAK 224
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
154-444 |
1.19e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 154 LKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQgagvrdgaaeeegtvelgpkrlwkedtgRVEELQE 233
Cdd:COG4372 15 LFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQARE----------------------------ELEQLEE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 234 LLEKQNFELSQARERlvtltttvteleedLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREAT 313
Cdd:COG4372 67 ELEQARSELEQLEEE--------------LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 314 SIHDLNDKLENELANKESLHRQAEERHGNIEEHLRQLEGQLE-----EKNQELARVRQREKMNEDHNKRLSDTVDRLLSE 388
Cdd:COG4372 133 QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQalseaEAEQALDELLKEANRNAEKEEELAEAEKLIESL 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2017363542 389 SNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQ 444
Cdd:COG4372 213 PRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
28-373 |
1.40e-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: 46.21 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 28 QLMVNMLDEREKLLESLRESQETLAATQSRLQDAihERDQLQRHLNSALPQEfATLTRELSMCREQLLEREEEISELKAE 107
Cdd:TIGR02169 190 DLIIDEKRQQLERLRREREKAERYQALLKEKREY--EGYELLKEKEALERQK-EAIERQLASLEEELEKLTEEISELEKR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 108 RNNTRLLLEHLECLVSRhERSLRMTVVKRQAQSpsgVSSEVEVLK-ALKSLFEHHKALDEKVR---ERLRAALERVTTLE 183
Cdd:TIGR02169 267 LEEIEQLLEELNKKIKD-LGEEEQLRVKEKIGE---LEAEIASLErSIAEKERELEDAEERLAkleAEIDKLLAEIEELE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 184 EQLAGAHQQVSALQqgAGVRDGAAEEEGTVElgpkrlwkedtgRVEELQELLEKQNFELSQARERlvtltttVTELEEDL 263
Cdd:TIGR02169 343 REIEEERKRRDKLT--EEYAELKEELEDLRA------------ELEEVDKEFAETRDELKDYREK-------LEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 264 GTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREatsIHDLNDKLENELANKESlhrqAEERHGNI 343
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE---IKKQEWKLEQLAADLSK----YEQELYDL 474
|
330 340 350
....*....|....*....|....*....|
gi 2017363542 344 EEHLRQLEGQLEEKNQELARVRQREKMNED 373
Cdd:TIGR02169 475 KEEYDRVEKELSKLQRELAEAEAQARASEE 504
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
280-448 |
1.64e-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: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 280 HQRDLREALAQK----EDMEERITTLEKRYLAAQREatsIHDLNDKLEnELANKESLHRQAEERHGNIEEH------LRQ 349
Cdd:COG4913 590 HEKDDRRRIRSRyvlgFDNRAKLAALEAELAELEEE---LAEAEERLE-ALEAELDALQERREALQRLAEYswdeidVAS 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 350 LEGQLEEKNQELARvrqrekmnedhnkrlsdtvdrlLSESNERLQlHLKERMAALEEkntliqELESSQRQIEEQHHHKG 429
Cdd:COG4913 666 AEREIAELEAELER----------------------LDASSDDLA-ALEEQLEELEA------ELEELEEELDELKGEIG 716
|
170
....*....|....*....
gi 2017363542 430 RLSEEIEKLRQEVDQLKGR 448
Cdd:COG4913 717 RLEKELEQAEEELDELQDR 735
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
284-448 |
2.00e-04 |
|
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: 45.73 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 284 LREALAQKEDMEERITTLEKRylaaqREATSIHDLNDKLENELANKESLHRQAEErhgniEEHLRQLEGQLEEKNQELAR 363
Cdd:pfam02463 159 EEEAAGSRLKRKKKEALKKLI-----EETENLAELIIDLEELKLQELKLKEQAKK-----ALEYYQLKEKLELEEEYLLY 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 364 VRQREkmnedHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVD 443
Cdd:pfam02463 229 LDYLK-----LNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELL 303
|
....*
gi 2017363542 444 QLKGR 448
Cdd:pfam02463 304 KLERR 308
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
290-446 |
2.05e-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: 45.40 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 290 QKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQAEERHGNIEEHLRQLEGQLE----EKNQELAR-- 363
Cdd:TIGR04523 233 NIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdlnnQKEQDWNKel 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 364 ---VRQREKMNEDHNKRLSDTvDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQ 440
Cdd:TIGR04523 313 kseLKNQEKKLEEIQNQISQN-NKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLES 391
|
....*.
gi 2017363542 441 EVDQLK 446
Cdd:TIGR04523 392 QINDLE 397
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
291-446 |
2.13e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 44.62 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 291 KEDMEERITTLEKRYLAAQREATSIHDLNDKLEnelankeslhrqaeERHGNIEEHLRQLEGQLEEKNQ----ELArvRQ 366
Cdd:smart00787 146 KEGLDENLEGLKEDYKLLMKELELLNSIKPKLR--------------DRKDALEEELRQLKQLEDELEDcdptELD--RA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 367 REKMnedhnKRLSDTVDRLLSESNErLQLHLKERMAALEEKNTLIQELESS----QRQIEEQHHHKGRlseEIEKLRQEV 442
Cdd:smart00787 210 KEKL-----KKLLQEIMIKVKKLEE-LEEELQELESKIEDLTNKKSELNTEiaeaEKKLEQCRGFTFK---EIEKLKEQL 280
|
....
gi 2017363542 443 DQLK 446
Cdd:smart00787 281 KLLQ 284
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
310-448 |
2.19e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 310 REATSIHDLNDKLENELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDhnkrlsdtvdRLLSES 389
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE----------QLGNVR 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2017363542 390 NERLQLHLKERMAALEEKntlIQELESSQRQIEEQHHHKgrlSEEIEKLRQEVDQLKGR 448
Cdd:COG1579 87 NNKEYEALQKEIESLKRR---ISDLEDEILELMERIEEL---EEELAELEAELAELEAE 139
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
147-447 |
2.26e-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: 45.73 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 147 EVEVLKALKSLFEHHKALDEKVRERLRaalervttlEEQLAGAHQQVSALQQGAGVRDGAAEE--EGTVELGPKRLWKED 224
Cdd:TIGR00618 593 TVRLQDLTEKLSEAEDMLACEQHALLR---------KLQPEQDLQDVRLHLQQCSQELALKLTalHALQLTLTQERVREH 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 225 TGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREAL-AQKEDMEERITTLEK 303
Cdd:TIGR00618 664 ALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASsSLGSDLAAREDALNQ 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 304 RYLAAQREATSI--HDLNDKLENELANKESLHRQAEERH--GNIEEHLRQLEgqleEKNQELArvrqrEKMNEDHNKRLS 379
Cdd:TIGR00618 744 SLKELMHQARTVlkARTEAHFNNNEEVTAALQTGAELSHlaAEIQFFNRLRE----EDTHLLK-----TLEAEIGQEIPS 814
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017363542 380 DTVDRLLSEsnERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKG 447
Cdd:TIGR00618 815 DEDILNLQC--ETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNG 880
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
18-446 |
2.88e-04 |
|
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: 45.11 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 18 HGADADANFEQLMVNMLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQR---HLNSALPQEFATL---TRELSMCR 91
Cdd:pfam15921 318 QLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQesgNLDDQLQKLLADLhkrEKELSLEK 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 92 EQLLE-------REEEISELKAERNNTRLLLEHLECLVsRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKAL 164
Cdd:pfam15921 398 EQNKRlwdrdtgNSITIDHLRRELDDRNMEVQRLEALL-KAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEM 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 165 DEKVRERL-----------RAALERVTTLEEQ---LAGAHQQVSALQQGAGVR---------DGAAEEEGTVELGPKRLW 221
Cdd:pfam15921 477 LRKVVEELtakkmtlesseRTVSDLTASLQEKeraIEATNAEITKLRSRVDLKlqelqhlknEGDHLRNVQTECEALKLQ 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 222 KEDTGRVEE-LQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITT 300
Cdd:pfam15921 557 MAEKDKVIEiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVK 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 301 LEKRYLAAQREATSIHDLNDKLENELANK-----------ESLHRQAEERHGNIEEHLRQLEGQLEEKNQELARVRQREK 369
Cdd:pfam15921 637 LVNAGSERLRAVKDIKQERDQLLNEVKTSrnelnslsedyEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLK 716
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 370 MNEDHN-----------KRLS---DTVDRLLSESN---ERLQLHLKERMAALEEKNTLIQELESSQRQieeqhhhKGRLS 432
Cdd:pfam15921 717 SMEGSDghamkvamgmqKQITakrGQIDALQSKIQfleEAMTNANKEKHFLKEEKNKLSQELSTVATE-------KNKMA 789
|
490
....*....|....
gi 2017363542 433 EEIEKLRQEVDQLK 446
Cdd:pfam15921 790 GELEVLRSQERRLK 803
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
34-446 |
3.04e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 34 LDEREKLLESLRESQETLAATQSRL-QDAIHERDQLQRhlnsaLPQEFATLTRELSMCREQLLEREEEISELKAERNNTR 112
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLeQDIARLEERRRE-----LEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 113 LLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEkVRERLRAALERVTTLEEQLAGAHQQ 192
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE-LEEAEEALLERLERLEEELEELEEA 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 193 VSALQQgagVRDGAAEEEGTVELGPKRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIK 272
Cdd:COG1196 430 LAELEE---EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 273 SEELSSKHQRDLREALAQKEDmeeRITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQAEERHGNIE------EH 346
Cdd:COG1196 507 LEGVKAALLLAGLRGLAGAVA---VLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATflpldkIR 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 347 LRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQELE---SSQRQIEE 423
Cdd:COG1196 584 ARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEgegGSAGGSLT 663
|
410 420
....*....|....*....|...
gi 2017363542 424 QHHHKGRLSEEIEKLRQEVDQLK 446
Cdd:COG1196 664 GGSRRELLAALLEAEAELEELAE 686
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
42-445 |
3.81e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 42 ESLRESQETLAATQSRLQDAIHE-RDQLQRHLNSA----------------LPQEFATLTRELSMCREQLLEREEEISEL 104
Cdd:PRK02224 310 EAVEARREELEDRDEELRDRLEEcRVAAQAHNEEAeslredaddleeraeeLREEAAELESELEEAREAVEDRREEIEEL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 105 KAERNNTRL-----------LLEHLECLVSRHERslrmtVVKRQAQSPSGVSSEVEVLKALKSLFEHHKA-------LDE 166
Cdd:PRK02224 390 EEEIEELRErfgdapvdlgnAEDFLEELREERDE-----LREREAELEATLRTARERVEEAEALLEAGKCpecgqpvEGS 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 167 KVRERLRAALERVTTLEEQLAGAHQQVSALQQgagvRDGAAEEEGTVELGPKRLwKEdtgRVEELQELLEKQNFELSQAR 246
Cdd:PRK02224 465 PHVETIEEDRERVEELEAELEDLEEEVEEVEE----RLERAEDLVEAEDRIERL-EE---RREDLEELIAERRETIEEKR 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 247 ERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEK-RYLAAQRE--ATSIHDLNDKLE 323
Cdd:PRK02224 537 ERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERiRTLLAAIAdaEDEIERLREKRE 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 324 nELANKESLHRqaeERHGNIEEHLRQLEGQLEEKNQELArvRQREKMNEDHNKRLSDTVDRLLSESNErlqlhLKERMAA 403
Cdd:PRK02224 617 -ALAELNDERR---ERLAEKRERKRELEAEFDEARIEEA--REDKERAEEYLEQVEEKLDELREERDD-----LQAEIGA 685
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2017363542 404 LEEKntlIQELESsqrqIEEQHHHKGRLSEEIEKLRQEVDQL 445
Cdd:PRK02224 686 VENE---LEELEE----LRERREALENRVEALEALYDEAEEL 720
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
165-448 |
4.18e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.65 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 165 DEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEgtvelgpkRLWKEDTGRVEELQELLEKQNFELSQ 244
Cdd:TIGR00606 790 DVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQ--------HELDTVVSKIELNRKLIQDQQEQIQH 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 245 ARERLVTLTTTVTELEEDLGTARRDLIKSEELSS-----------KHQRDLREALAQKEDMEERITTLEKRYLAAQREAT 313
Cdd:TIGR00606 862 LKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTevqslireikdAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQD 941
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 314 SIHDLNDKLENELANKESLHRQAEErhgNIEEHLRQLEGQLEEKNQELARVRQR-EKMNEDHNKRLSDTVDRLLSESNER 392
Cdd:TIGR00606 942 KVNDIKEKVKNIHGYMKDIENKIQD---GKDDYLKQKETELNTVNAQLEECEKHqEKINEDMRLMRQDIDTQKIQERWLQ 1018
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2017363542 393 LQLHLKERMAALEE-KNTLIQEL-ESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGR 448
Cdd:TIGR00606 1019 DNLTLRKRENELKEvEEELKQHLkEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGR 1076
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
272-446 |
4.60e-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: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 272 KSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREatsIHDLNDK---LENELAN----KESLHRQAEERHG--- 341
Cdd:TIGR04523 402 NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE---IKDLTNQdsvKELIIKNldntRESLETQLKVLSRsin 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 342 NIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSE----SNERLQLH--LKERMAALEEKNT------ 409
Cdd:TIGR04523 479 KIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKieklESEKKEKEskISDLEDELNKDDFelkken 558
|
170 180 190
....*....|....*....|....*....|....*..
gi 2017363542 410 LIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 446
Cdd:TIGR04523 559 LEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKE 595
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
269-447 |
4.63e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 269 DLIKSE-ELSSKHQRDLREALAQkedmeeRITTLEKRYLAAQREATSIHDLNDKLENELANkesLHRQAEERHGNIEEhL 347
Cdd:PHA02562 191 DHIQQQiKTYNKNIEEQRKKNGE------NIARKQNKYDELVEEAKTIKAEIEELTDELLN---LVMDIEDPSAALNK-L 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 348 RQLEGQLEEKNQELARVrqrEKMNEDHN------KRLSDTVDRL------LSESNERLQLhLKERMAALEEK----NTLI 411
Cdd:PHA02562 261 NTAAAKIKSKIEQFQKV---IKMYEKGGvcptctQQISEGPDRItkikdkLKELQHSLEK-LDTAIDELEEImdefNEQS 336
|
170 180 190
....*....|....*....|....*....|....*.
gi 2017363542 412 QELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKG 447
Cdd:PHA02562 337 KKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQA 372
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
262-418 |
5.42e-04 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 42.74 E-value: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 262 DLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERIT-TLEKRYLAAQREA-TSIHDLndklENELANKESLHRQAEER 339
Cdd:pfam04012 37 ELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQaALTKGNEELAREAlAEKKSL----EKQAEALETQLAQQRSA 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2017363542 340 HGNIEEHLRQLEGQLEEKNQELARVRQREKMNEdHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQ 418
Cdd:pfam04012 113 VEQLRKQLAALETKIQQLKAKKNLLKARLKAAK-AQEAVQTSLGSLSTSSATDSFERIEEKIEEREARADAAAELASAV 190
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
279-441 |
5.46e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.34 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 279 KHQRDLREALAQK--EDMEERITTLEKRYLAaqREATSIHDLNdklENELANKESLHRQAE---ERHGNIEEHLRQLEG- 352
Cdd:pfam17380 279 QHQKAVSERQQQEkfEKMEQERLRQEKEEKA--REVERRRKLE---EAEKARQAEMDRQAAiyaEQERMAMERERELERi 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 353 QLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKermAALEEKntlIQElESSQRQIEEQHHHKGRLS 432
Cdd:pfam17380 354 RQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELE---AARKVK---ILE-EERQRKIQQQKVEMEQIR 426
|
....*....
gi 2017363542 433 EEIEKLRQE 441
Cdd:pfam17380 427 AEQEEARQR 435
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
266-442 |
5.84e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.50 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 266 ARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKR---YLAAQREATSIHDLNDK--LENELANKESLHRQAEERH 340
Cdd:COG1842 35 MEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKarlALEKGREDLAREALERKaeLEAQAEALEAQLAQLEEQV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 341 GNIEEHLRQLEGQLEEKNQELARVRQREKMNEdHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQEL---ESS 417
Cdd:COG1842 115 EKLKEALRQLESKLEELKAKKDTLKARAKAAK-AQEKVNEALSGIDSDDATSALERMEEKIEEMEARAEAAAELaagDSL 193
|
170 180
....*....|....*....|....*
gi 2017363542 418 QRQIEEQhHHKGRLSEEIEKLRQEV 442
Cdd:COG1842 194 DDELAEL-EADSEVEDELAALKAKM 217
|
|
| SAM_STIM-1,2-like |
cd09504 |
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ... |
806-864 |
6.45e-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: 39.24 E-value: 6.45e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363542 806 WDGPTVVSWLELWVGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNALHRLKLRL 864
Cdd:cd09504 5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
343-446 |
7.21e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.69 E-value: 7.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 343 IEEHLRQLEGQLEEKNQELARVRQREK-MNEDHNKRLSDTVDRLLSEsNERLQLHLKERMAALEEkntLIQELESSQRQI 421
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELtEEEEEIRRLEEQVERLEAE-VEELEAELEEKDERIER---LERELSEARSEE 457
|
90 100
....*....|....*....|....*
gi 2017363542 422 EEQHhhkgRLSEEIEKLRQEVDQLK 446
Cdd:COG2433 458 RREI----RKDREISRLDREIERLE 478
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
36-407 |
1.35e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.79 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 36 EREKLLESLRESQETLAATQS--RLQDAIHERDQLQRHLNSALPQEFATLTRELSMCREQLLEREEEISELKAERNNTRL 113
Cdd:pfam05483 406 ELEELKKILAEDEKLLDEKKQfeKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKL 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 114 llEHLECLVSRHERSLRMtvvKRQAQSPSGVSSEvevLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQV 193
Cdd:pfam05483 486 --KNIELTAHCDKLLLEN---KELTQEASDMTLE---LKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEF 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 194 saLQQGAGVR---DGAAEEEGTVE---LGPKRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTAR 267
Cdd:pfam05483 558 --IQKGDEVKcklDKSEENARSIEyevLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYE 635
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 268 RDLIKSE-ELSSKHQRdLREALA--QKEDMEERITtlEKRYLAAQREATSIHDLNDKLENELaNKESLHRQAEeRHGNIE 344
Cdd:pfam05483 636 IKVNKLElELASAKQK-FEEIIDnyQKEIEDKKIS--EEKLLEEVEKAKAIADEAVKLQKEI-DKRCQHKIAE-MVALME 710
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017363542 345 EHLRQLEGQLEEKNQELARVRQREKMNEDHNK----RLSDTVDRLLS---------ESNERLQLHLKERMAALEEK 407
Cdd:pfam05483 711 KHKHQYDKIIEERDSELGLYKNKEQEQSSAKAaleiELSNIKAELLSlkkqleiekEEKEKLKMEAKENTAILKDK 786
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
805-869 |
1.65e-03 |
|
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.
Pssm-ID: 425739 Cd Length: 64 Bit Score: 38.02 E-value: 1.65e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363542 805 QWDGPTVVSWLElWVGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNALHRLKLRLAIQEM 869
Cdd:pfam00536 2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
274-438 |
1.73e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 41.63 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 274 EELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDK---------------LENELANKESLHRQAEE 338
Cdd:pfam06008 57 EELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKvatlgendfalpssdLSRMLAEAQRMLGEIRS 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 339 RhgNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQ---LHLKERMAALEEKNTLIQELE 415
Cdd:pfam06008 137 R--DFGTQLQNAEAELKAAQDLLSRIQTWFQSPQEENKALANALRDSLAEYEAKLSdlrELLREAAAKTRDANRLNLANQ 214
|
170 180
....*....|....*....|...
gi 2017363542 416 SSQRQIEEQHHHKGRLSEEIEKL 438
Cdd:pfam06008 215 ANLREFQRKKEEVSEQKNQLEET 237
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
928-983 |
1.92e-03 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 38.02 E-value: 1.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2017363542 928 EWLPSLGLPQYRSYFMECLVD-ARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 983
Cdd:pfam07647 11 DWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLK-RLGITSVGHRRKILKKIQELK 66
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
81-444 |
1.98e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 81 ATLTRELSMCREQLLEREEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgVSSEVE-------VLKA 153
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAE---LEAELErldassdDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 154 LKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKRLWKEDTGRVEELQE 233
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 234 LLEKQnfeLSQARERlvtltttvteleedLGTARRDLIKseeLSSKHQR-------DLREALAQKEDMEERITTLEKRYL 306
Cdd:COG4913 770 NLEER---IDALRAR--------------LNRAEEELER---AMRAFNRewpaetaDLDADLESLPEYLALLDRLEEDGL 829
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 307 AAQREAtsIHDLndKLENELANKESLHRQAEERHGNIEEhlrqlegQLEEKNQELARVRqrekMNEDHnkrlsdtvdrll 386
Cdd:COG4913 830 PEYEER--FKEL--LNENSIEFVADLLSKLRRAIREIKE-------RIDPLNDSLKRIP----FGPGR------------ 882
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017363542 387 sesneRLQLHLKERmaALEEKNTLIQELESSQRQI-----EEQHHHKGRLSEEIEKLRQEVDQ 444
Cdd:COG4913 883 -----YLRLEARPR--PDPEVREFRQELRAVTSGAslfdeELSEARFAALKRLIERLRSEEEE 938
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
306-443 |
2.03e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 40.64 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 306 LAAQREatsIHDLNDKLENELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRL 385
Cdd:pfam12072 56 LEAKEE---IHKLRAEAERELKERRNELQRQERRLLQKEETLDRKDESLEKKEESLEKKEKELEAQQQQLEEKEEELEEL 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363542 386 LSESNERLqlhlkERMAAL---EEKNTLIQELEssqrqiEEQHHHKGRLSEEIE-KLRQEVD 443
Cdd:pfam12072 133 IEEQRQEL-----ERISGLtseEAKEILLDEVE------EELRHEAAVMIKEIEeEAKEEAD 183
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
227-446 |
2.19e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 227 RVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYL 306
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 307 AAQREAtsihdlnDKLENELAnkeslhrQAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRL- 385
Cdd:COG4372 112 ELQEEL-------EELQKERQ-------DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALs 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017363542 386 LSESNERLQLHLKE--RMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 446
Cdd:COG4372 178 EAEAEQALDELLKEanRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLD 240
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
282-448 |
2.56e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.98 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 282 RDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLEN---------ELANKESLHRQA--EERHGNIEEhLRQL 350
Cdd:pfam05622 38 KKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETarddyrikcEELEKEVLELQHrnEELTSLAEE-AQAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 351 EGQLEEKNQELARVRQREKMNEDHNKRLSDTVD-----RLLSESNerlqLHLKERMAALEEK----NTLIQELESSQRQI 421
Cdd:pfam05622 117 KDEMDILRESSDKVKKLEATVETYKKKLEDLGDlrrqvKLLEERN----AEYMQRTLQLEEElkkaNALRGQLETYKRQV 192
|
170 180 190
....*....|....*....|....*....|
gi 2017363542 422 EEQHHhkgRLSEEI---EKLRQEVDQLKGR 448
Cdd:pfam05622 193 QELHG---KLSEESkkaDKLEFEYKKLEEK 219
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
59-395 |
2.61e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.03 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 59 QDAIHERDQ---LQRHLNSALPQEFATLTRELSMCREQLLEREEEISELKAER----NNTRLLLEHLECL--VSRHERSL 129
Cdd:pfam17380 281 QKAVSERQQqekFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAaiyaEQERMAMERERELerIRQEERKR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 130 RMTVVKRQAqspsgVSSEVEVLKALKSLFEHHKALDEKVRERLRAAlERVTTLEEQlagahQQVSALQQGAGVRDGAAEE 209
Cdd:pfam17380 361 ELERIRQEE-----IAMEISRMRELERLQMERQQKNERVRQELEAA-RKVKILEEE-----RQRKIQQQKVEMEQIRAEQ 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 210 EgtvelgpkrlwkedTGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEelssKHQRDlreala 289
Cdd:pfam17380 430 E--------------EARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELE----KEKRD------ 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 290 QKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQELARVRQREK 369
Cdd:pfam17380 486 RKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEER 565
|
330 340
....*....|....*....|....*.
gi 2017363542 370 MNEDHNKRLSDTVDRLLSESNERLQL 395
Cdd:pfam17380 566 SRLEAMEREREMMRQIVESEKARAEY 591
|
|
| SAM_Neurabin-like |
cd09512 |
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ... |
1006-1045 |
2.64e-03 |
|
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like (Neural actin-binding) subfamily is a putative protein-protein interaction domain. This group currently includes the SAM domains of neurobin-I, SAMD14 and neurobin-I/SAMD14-like proteins. Most are multidomain proteins and in addition to SAM domain they contain other protein-binding domains such as PDZ and actin-binding domains. Members of this subfamily participate in signal transduction. Neurabin-I is involved in the regulation of Ca signaling intensity in alpha-adrenergic receptors; it forms a functional pair of opposing regulators with neurabin-II. Neurabins are expressed almost exclusively in neuronal cells. They are known to interact with protein phosphatase 1 and inhibit its activity; they also can bind actin filaments; however, the exact role of the SAM domain is unclear, since SAM doesn't participate in these interactions.
Pssm-ID: 188911 [Multi-domain] Cd Length: 70 Bit Score: 37.63 E-value: 2.64e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2017363542 1006 VLVWTNDQVVHWVQSIGLRDYAGNLHESGVHG-ALLALDEN 1045
Cdd:cd09512 4 VSEWSVQQVCQWLMGLGLEQYIPEFTANNIDGqQLLQLDSS 44
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
265-446 |
4.57e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 265 TARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKEslhRQAEERHGNIE 344
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE---AEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 345 EHLRQL--EGQ--------LEEKNQE--LARVRQREKMNEDHNKRLSDTVDrlLSESNERLQLHLKERMAALEE-KNTLI 411
Cdd:COG3883 90 ERARALyrSGGsvsyldvlLGSESFSdfLDRLSALSKIADADADLLEELKA--DKAELEAKKAELEAKLAELEAlKAELE 167
|
170 180 190
....*....|....*....|....*....|....*
gi 2017363542 412 QELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLK 446
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
222-445 |
5.41e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 40.71 E-value: 5.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 222 KEDTGRVEELQELLEKQNFELS-QARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQ----RDLREALAQ-KEDME 295
Cdd:COG5185 274 AESSKRLNENANNLIKQFENTKeKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETetgiQNLTAEIEQgQESLT 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 296 ERITTL---EKRYLAAQREATSIHDLNDKLENELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQELARVR-----QR 367
Cdd:COG5185 354 ENLEAIkeeIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQrqieqAT 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 368 EKMNEDHNK------RLSDTVDRLLSESNERLQLHLKERM----AALEEKNTLIQELESSQRQI-EEQHHHKGRLSEEIE 436
Cdd:COG5185 434 SSNEEVSKLlnelisELNKVMREADEESQSRLEEAYDEINrsvrSKKEDLNEELTQIESRVSTLkATLEKLRAKLERQLE 513
|
....*....
gi 2017363542 437 KLRQEVDQL 445
Cdd:COG5185 514 GVRSKLDQV 522
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
166-379 |
5.77e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 166 EKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAgvrdgaaeEEGTVELgpkrlwKEDTGRVEELQELLEKQNFELSQA 245
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEY--------NELQAEL------EALQAEIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 246 RERlvtltttvteleedLGTARRDLIKSEELSSkhqrdLREALAQKEDMEE---RITTLEKRYLAAQREATSIHDLNDKL 322
Cdd:COG3883 85 REE--------------LGERARALYRSGGSVS-----YLDVLLGSESFSDfldRLSALSKIADADADLLEELKADKAEL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2017363542 323 ENELANKESLHRQAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLS 379
Cdd:COG3883 146 EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
223-445 |
6.61e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 6.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 223 EDTGRVEE--LQELLEKQNF---ELSQARERLVTLTTTVTELEEDLGTARRDLikSEELSSKHQRDLrEALAQKEDMEER 297
Cdd:pfam01576 337 EEETRSHEaqLQEMRQKHTQaleELTEQLEQAKRNKANLEKAKQALESENAEL--QAELRTLQQAKQ-DSEHKRKKLEGQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 298 ITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQAEERHGNIEEHLRQLEGQL--------EEKNQELA---RVRQ 366
Cdd:pfam01576 414 LQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLqdtqellqEETRQKLNlstRLRQ 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 367 --------REKMNEDHNKRLS-----DTVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSE 433
Cdd:pfam01576 494 ledernslQEQLEEEEEAKRNverqlSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEK 573
|
250
....*....|..
gi 2017363542 434 EIEKLRQEVDQL 445
Cdd:pfam01576 574 TKNRLQQELDDL 585
|
|
| SAM_SARM1-like_repeat1 |
cd09501 |
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
928-972 |
6.72e-03 |
|
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of SARM1-like adaptor proteins is a protein-protein interaction domain. SARM1-like proteins contain two tandem SAM domains. SARM1-like proteins are involved in TLR (Toll-like receptor) signaling. They are responsible for targeted localization of the whole protein to post-synaptic regions of axons. In humans SARM1 expression is detected in kidney and liver.
Pssm-ID: 188900 [Multi-domain] Cd Length: 69 Bit Score: 36.51 E-value: 6.72e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2017363542 928 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHR 972
Cdd:cd09501 11 TWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLR 55
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
13-441 |
6.83e-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: 40.59 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 13 RLGPPHGADADANFEQLMVNMLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSALPQEFATLTRELSMCRE 92
Cdd:pfam12128 445 RLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDE 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 93 QLLEREEEISELKA-ERNNTRLLLEHLECLVSR---HERSLRMTVVKRQAQSPS---GVSSEVEVLKALKSLFeHHKALD 165
Cdd:pfam12128 525 LELQLFPQAGTLLHfLRKEAPDWEQSIGKVISPellHRTDLDPEVWDGSVGGELnlyGVKLDLKRIDVPEWAA-SEEELR 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 166 E---KVRERLRAALERVTTLEEQLAGAHQQVSALQqgAGVRDGAAEEEGTvELGPKRLWKEDTGRVEELQELLEKQNFEL 242
Cdd:pfam12128 604 ErldKAEEALQSAREKQAAAEEQLVQANGELEKAS--REETFARTALKNA-RLDLRRLFDEKQSEKDKKNKALAERKDSA 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 243 SQARERLVTLTTTVTELEEDLGTARRDliKSEELSSKHQRDLREALAQKEDMEERI-TTLEKRYLAAQRE---------- 311
Cdd:pfam12128 681 NERLNSLEAQLKQLDKKHQAWLEEQKE--QKREARTEKQAYWQVVEGALDAQLALLkAAIAARRSGAKAElkaletwykr 758
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 312 ---------------ATSIHDLNDKLENELANKE-------------SLHRQA-EERHGNIEEHLRQLEGQLEEKNQELA 362
Cdd:pfam12128 759 dlaslgvdpdviaklKREIRTLERKIERIAVRRQevlryfdwyqetwLQRRPRlATQLSNIERAISELQQQLARLIADTK 838
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 363 RVRQREKMNEDHNKRLSDTVDRLLSE---------------SNERLQLHLKERMAALEE-KNTLIQELESSQRQIEE--- 423
Cdd:pfam12128 839 LRRAKLEMERKASEKQQVRLSENLRGlrcemsklatlkedaNSEQAQGSIGERLAQLEDlKLKRDYLSESVKKYVEHfkn 918
|
490 500
....*....|....*....|
gi 2017363542 424 --QHHHKGRLSEEIEKLRQE 441
Cdd:pfam12128 919 viADHSGSGLAETWESLREE 938
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
282-446 |
8.08e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.51 E-value: 8.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 282 RDLREALAQKEDMEERITTLEKRYLAAQRE-ATSIHDLNDklENELANK-ESLHRQAEERhgnieEHLRQLEGQLEEKNQ 359
Cdd:COG1340 95 DELRKELAELNKAGGSIDKLRKEIERLEWRqQTEVLSPEE--EKELVEKiKELEKELEKA-----KKALEKNEKLKELRA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 360 ELARVRQREkmnEDHNKRLSDTVDRLLSESNERLQLhLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLR 439
Cdd:COG1340 168 ELKELRKEA---EEIHKKIKELAEEAQELHEEMIEL-YKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELR 243
|
....*..
gi 2017363542 440 QEVDQLK 446
Cdd:COG1340 244 KELKKLR 250
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
268-448 |
9.91e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 38.97 E-value: 9.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 268 RDLIKSEELSSKHQrDLREALAQKEDMEERITTLEKRYLAAQREATSihDLNDKLENELANKESLHRQAEERHGNIEEHL 347
Cdd:cd00176 30 DDLESVEALLKKHE-ALEAELAAHEERVEALNELGEQLIEEGHPDAE--EIQERLEELNQRWEELRELAEERRQRLEEAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363542 348 RQLegqleeknQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHH 427
Cdd:cd00176 107 DLQ--------QFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHP 178
|
170 180
....*....|....*....|...
gi 2017363542 428 KGR--LSEEIEKLRQEVDQLKGR 448
Cdd:cd00176 179 DADeeIEEKLEELNERWEELLEL 201
|
|
| |
