|
Name |
Accession |
Description |
Interval |
E-value |
| 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 ... |
1023-1094 |
2.40e-44 |
|
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: 154.40 E-value: 2.40e-44
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958790272 1023 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1094
Cdd:cd09568 1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
|
|
| 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 ... |
820-890 |
5.60e-44 |
|
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.
Pssm-ID: 188961 Cd Length: 71 Bit Score: 153.49 E-value: 5.60e-44
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958790272 820 FAQWDGPTVVAWLELWLGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 890
Cdd:cd09562 1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
|
|
| SAM_liprin-alpha1,2,3,4_repeat2 |
cd09565 |
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ... |
938-1003 |
1.09e-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: 1.09e-43
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958790272 938 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 1003
Cdd:cd09565 1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
|
|
| SAM_liprin-kazrin_repeat2 |
cd09495 |
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ... |
942-1001 |
1.94e-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: 117.25 E-value: 1.94e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 942 WIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1001
Cdd:cd09495 1 WWVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLVHLKVTSQLHHLSLKCGIHVLH 60
|
|
| SAM_liprin-kazrin_repeat1 |
cd09494 |
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
827-885 |
3.36e-27 |
|
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: 105.00 E-value: 3.36e-27
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958790272 827 TVVAWLELWLGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 885
Cdd:cd09494 1 RVCAWLEDFGLMP-MYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
|
|
| SAM_liprin-kazrin_repeat3 |
cd09496 |
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of ... |
1031-1092 |
6.75e-25 |
|
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: 98.77 E-value: 6.75e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958790272 1031 RVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNN 1092
Cdd:cd09496 1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETEFNN 62
|
|
| SAM_kazrin_repeat3 |
cd09570 |
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin ... |
1023-1094 |
1.34e-18 |
|
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: 80.95 E-value: 1.34e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958790272 1023 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1094
Cdd:cd09570 1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
|
|
| SAM_kazrin_repeat1 |
cd09564 |
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ... |
821-885 |
4.63e-17 |
|
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: 76.72 E-value: 4.63e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958790272 821 AQWDGPTVVAWLELWLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 885
Cdd:cd09564 2 SRWKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
195-515 |
1.24e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 85.37 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 195 QIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYL 274
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 275 SAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERH- 353
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAl 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 354 ---GNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERmAALEEKNVLIQESETF 430
Cdd:COG1196 393 raaAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE-EEEEALLELLAELLEE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 431 RKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSLIEPTISRTHLDTSAELRYSVGSLVDSQSDYRTTKVIRRPRRGRMG 510
Cdd:COG1196 472 AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNI 551
|
....*
gi 1958790272 511 VRRDE 515
Cdd:COG1196 552 VVEDD 556
|
|
| SAM_liprin-beta1,2_repeat2 |
cd09566 |
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ... |
937-1001 |
1.47e-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: 75.04 E-value: 1.47e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958790272 937 DMNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLrVHLKMVDSFHRTSLQYGIMCLK 1001
Cdd:cd09566 1 KLDTHWV-LRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDL-LHLKVTSALHHASIRRGIQVLR 63
|
|
| SAM_kazrin_repeat2 |
cd09567 |
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ... |
937-1001 |
1.72e-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: 74.75 E-value: 1.72e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958790272 937 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1001
Cdd:cd09567 1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
198-457 |
1.26e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 82.29 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 198 ELQEllEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQ 277
Cdd:COG1196 217 ELKE--ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 278 RESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQqtmRKAETLPEVEAELAQRIAALTKAEERHGNIE 357
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE---ELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 358 ERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEES 437
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
250 260
....*....|....*....|
gi 1958790272 438 LHDKERLAEEIEKLRSELDQ 457
Cdd:COG1196 452 AELEEEEEALLELLAELLEE 471
|
|
| SAM_liprin-beta1,2_repeat3 |
cd09569 |
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ... |
1023-1094 |
2.10e-15 |
|
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.
Pssm-ID: 188968 Cd Length: 72 Bit Score: 72.10 E-value: 2.10e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958790272 1023 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1094
Cdd:cd09569 1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
216-467 |
5.73e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 80.10 E-value: 5.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 216 RLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELA 295
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 296 NKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpevEAELAQRIAALTKAEERH-------GNIEERMRHLEGQLE 368
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL---KEELKALREALDELRAELtllneeaANLRERLESLERRIA 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 369 EKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLHLKER-------MAALEEKNVLIQESETFRKNLEESL 438
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEIEELeelIEELESELEALLNERasleealALLRSELEELSEELRELESKRSELR 914
|
250 260
....*....|....*....|....*....
gi 1958790272 439 HDKERLAEEIEKLRSELDQMKMRTGSLIE 467
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLEVRIDNLQE 943
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
27-407 |
7.91e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 79.72 E-value: 7.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 27 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRmTVVKRQAQspsgvsSEVEVLKALKSL 106
Cdd:TIGR02168 691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE-QLEERIAQ------LSKELTELEAEI 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 107 FEHHKALdEKVRERLRVSLERVSALEEELAAANQEIVALREqnvhiQRKMVSSEGSTESEHLDGMEPGQKVHEKRlsngs 186
Cdd:TIGR02168 764 EELEERL-EEAEEELAEAEAEIEELEAQIEQLKEELKALRE-----ALDELRAELTLLNEEAANLRERLESLERR----- 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 187 idstddtsqIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERI 266
Cdd:TIGR02168 833 ---------IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 267 TTLEKRYLSAQRESTSIHDMNDKLENELAnkeailrQMEEKNRQLQERL-ELAEQKLQQTMRKAETLPEVEAELAQRIAA 345
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLE-------GLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958790272 346 LTKAEERHGNI-----------EERMRHLEGQLEeknqELQRARQR-----EKMNEEHNKRLSDTVDRLltesNERLQ 407
Cdd:TIGR02168 977 LENKIKELGPVnlaaieeyeelKERYDFLTAQKE----DLTEAKETleeaiEEIDREARERFKDTFDQV----NENFQ 1046
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
174-461 |
8.32e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 79.72 E-value: 8.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 174 GQKVHEKRLSNGSIDSTDdtSQIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIR 253
Cdd:TIGR02168 652 GDLVRPGGVITGGSAKTN--SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIS 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 254 EAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTmrkAETLP 333
Cdd:TIGR02168 730 ALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL---REALD 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 334 EVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRAR-QREKMNEEHNKrlsdtVDRLLTESNERLQLHLKE 412
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSeDIESLAAEIEE-----LEELIEELESELEALLNE 881
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1958790272 413 RMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQMKMR 461
Cdd:TIGR02168 882 RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELR 930
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
40-459 |
1.51e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 78.96 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 40 REQLLEKEEEISELKAERNNTRLLLEHLECLVsrHERSLRMTVVKRQAqspSGVSSEVEVLKAlkslfEHhkaldEKVRE 119
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRL--DELSQELSDASRKI---GEIEKEIEQLEQ-----EE-----EKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 120 RLRVSLERVSALEEELAAANQEIVALREQnvhiqrkmvssegstesehLDGMEpgQKVHEKRLSNGSIDSTDDTSQIVEL 199
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELEAR-------------------IEELE--EDLHKLEEALNDLEARLSHSRIPEI 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 200 QELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARkdliktEEMNTKyQRDIREAMAQKEDMEERITTLEKRYlsaqre 279
Cdd:TIGR02169 797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE------KEIQEL-QEQRIDLKEQIKSIEKEIENLNGKK------ 863
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 280 stsihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpEVEAELAQRIAALTKAeeRHGNIEER 359
Cdd:TIGR02169 864 --------EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL-EAQIEKKRKRLSELKA--KLEALEEE 932
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 360 MRHLE---GQLEEKNQELQRARQREKMNEEhnkrlsdtvdrlltesnerlqlhLKERMAALEEKNVL-IQESETFRKNLE 435
Cdd:TIGR02169 933 LSEIEdpkGEDEEIPEEELSLEDVQAELQR-----------------------VEEEIRALEPVNMLaIQEYEEVLKRLD 989
|
410 420
....*....|....*....|....*..
gi 1958790272 436 ESLHDKERLAEE---IEKLRSELDQMK 459
Cdd:TIGR02169 990 ELKEKRAKLEEErkaILERIEEYEKKK 1016
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
100-458 |
1.53e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 78.95 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 100 LKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEHLDGMEPGQKVHE 179
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 180 KRlsngsidstddtSQIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQK 259
Cdd:TIGR02168 780 AE------------AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 260 EDMEERITTLEKRYLSAQREStsihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQqtmrkaetlpEVEAEL 339
Cdd:TIGR02168 848 EELSEDIESLAAEIEELEELI-------EELESELEALLNERASLEEALALLRSELEELSEELR----------ELESKR 910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 340 AQRIAALTKAEERHGNIEERMRHLEGQLEEKnqeLQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLhLKERMAALEE 419
Cdd:TIGR02168 911 SELRRELEELREKLAQLELRLEGLEVRIDNL---QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR-LENKIKELGP 986
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1958790272 420 KNVL-IQESETFRKNLEESLHDKERLAEEIEKLRSELDQM 458
Cdd:TIGR02168 987 VNLAaIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
215-457 |
1.64e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.83 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 215 DRLAALSSRVGEVEQEAETARKDLIKTEEMNtkyQRDIREAMAQKEDMEERITTLEKRYLSAQREStsihdmnDKLENEL 294
Cdd:COG1196 193 DILGELERQLEPLERQAEKAERYRELKEELK---ELEAELLLLKLRELEAELEELEAELEELEAEL-------EELEAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 295 ANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERhgnIEERMRHLEGQLEEKNQEL 374
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE---LEEELAELEEELEELEEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 375 QRARQREKMNEEH----NKRLSDTVDRLLTESNERLQL------HLKERMAALEEKNVLIQESETFRKNLEESLHDKERL 444
Cdd:COG1196 340 EELEEELEEAEEEleeaEAELAEAEEALLEAEAELAEAeeeleeLAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
250
....*....|...
gi 1958790272 445 AEEIEKLRSELDQ 457
Cdd:COG1196 420 EEELEELEEALAE 432
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
28-515 |
3.17e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 77.77 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 28 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLrmtvvkrqaqspsgvsSEVEVLKALKSLF 107
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERR----------------EELETLEAEIEDL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 108 EHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREqnvhiqrkMVSSEGSTESEHLDGMEPGQKVHEKRLSNGSI 187
Cdd:PRK02224 264 RETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG--------LDDADAEAVEARREELEDRDEELRDRLEECRV 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 188 DSTDDTSQIVELQEllekqnyemaqmkdRLAALSSRVGEVEQEAETARKDLIKTEEmntkyqrDIREAMAQKEDMEERIT 267
Cdd:PRK02224 336 AAQAHNEEAESLRE--------------DADDLEERAEELREEAAELESELEEARE-------AVEDRREEIEELEEEIE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 268 TLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQklqqtMRKAETLPEVEAEL--AQRIAA 345
Cdd:PRK02224 395 ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA-----LLEAGKCPECGQPVegSPHVET 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 346 LTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLS--DTVDRLLTESNERLQlHLKERMAAL-EEKNV 422
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIE-EKRERAEELrERAAE 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 423 LIQESETFRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSLiePTIsRTHLDTSAELRYSVGSLVDSQSDYRTTKVIR 502
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL--ERI-RTLLAAIADAEDEIERLREKREALAELNDER 625
|
490
....*....|...
gi 1958790272 503 RPRRGRMGVRRDE 515
Cdd:PRK02224 626 RERLAEKRERKRE 638
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
937-1001 |
5.56e-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: 5.56e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958790272 937 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1001
Cdd:pfam00536 1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
216-457 |
2.76e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 74.71 E-value: 2.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 216 RLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELA 295
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 296 NKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRI----AALTKAEERHGNIEERMRHLEGQLEEKN 371
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELesleAELEELEAELEELESRLEELEEQLETLR 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 372 QELQRARQREKMNEEHNKRLSDTVDRlLTESNERLQLHLKERMAALEEKNV--LIQESETFRKNLEESLHDKERLAEEIE 449
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEARLER-LEDRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQEELERLEEALE 464
|
....*...
gi 1958790272 450 KLRSELDQ 457
Cdd:TIGR02168 465 ELREELEE 472
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
94-386 |
3.44e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.20 E-value: 3.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 94 SSEVEVLKALKSL--FEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQnvhIQRKMVSSEGSTESEHLDGM 171
Cdd:COG1196 219 KEELKELEAELLLlkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE---LEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 172 EPGQKVHEKRLsngsidstdDTSQIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRD 251
Cdd:COG1196 296 ELARLEQDIAR---------LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 252 IREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEt 331
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE- 445
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1958790272 332 lpEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEE 386
Cdd:COG1196 446 --EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
195-459 |
7.14e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.55 E-value: 7.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 195 QIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYL 274
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 275 SAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLqqtmrkaETLPEVEAELAQRIAALtkaEERHG 354
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL-------EELEAELEELESRLEEL---EEQLE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 355 NIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNErlqLHLKERMAALEEKNVLIQESETFRKNL 434
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE---AELKELQAELEELEEELEELQEELERL 459
|
250 260
....*....|....*....|....*
gi 1958790272 435 EESLhdkERLAEEIEKLRSELDQMK 459
Cdd:TIGR02168 460 EEAL---EELREELEEAEQALDAAE 481
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
194-423 |
7.27e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.43 E-value: 7.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 194 SQIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRY 273
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 274 LSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERh 353
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE- 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 354 gnIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVL 423
Cdd:COG1196 426 --LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
|
| SAM_liprin-beta1,2_repeat1 |
cd09563 |
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
820-884 |
1.37e-12 |
|
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: 63.79 E-value: 1.37e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958790272 820 FAQWDGPTVVAWL-ELWLGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQ 884
Cdd:cd09563 1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
181-465 |
1.84e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 72.02 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 181 RLSNGSIDSTDDTSQIVELQELLEKqnyemaqMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKE 260
Cdd:TIGR02169 661 APRGGILFSRSEPAELQRLRERLEG-------LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 261 DMEERITTLEKRYLSAQRESTSIHDMNDKLENELAnkeailrQMEEKNRQLQERLELAEQKLQQtmrkaETLPEVEAEla 340
Cdd:TIGR02169 734 KLKERLEELEEDLSSLEQEIENVKSELKELEARIE-------ELEEDLHKLEEALNDLEARLSH-----SRIPEIQAE-- 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 341 qriaaLTKAEERHGNIEERMRHLEGQLEEKNQELQRArqREKMNEEHNKRlsdtvdRLLTESNERLQLHLKERMAALEEK 420
Cdd:TIGR02169 800 -----LSKLEEEVSRIEARLREIEQKLNRLTLEKEYL--EKEIQELQEQR------IDLKEQIKSIEKEIENLNGKKEEL 866
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1958790272 421 NVLIQESETFRKNLEESLHDkerLAEEIEKLRSELDQMKMRTGSL 465
Cdd:TIGR02169 867 EEELEELEAALRDLESRLGD---LKKERDELEAQLRELERKIEEL 908
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
27-455 |
2.89e-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: 71.24 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 27 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEvevLKALKSL 106
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE---LKELQAE 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 107 FEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEgsTESEHLDGMEPGQK--VHEKRLSN 184
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE--RLQENLEGFSEGVKalLKNQSGLS 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 185 GSIDS---------------------------TDDTSQIVELQELLEKQNYEMAQM----KDRLAALSSRVGEVEQEAET 233
Cdd:TIGR02168 520 GILGVlselisvdegyeaaieaalggrlqavvVENLNAAKKAIAFLKQNELGRVTFlpldSIKGTEIQGNDREILKNIEG 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 234 ARKDLIKTEEMNTKYQR-------------DIREAMAQ--KEDMEERITTLE-----KRYLSAQRESTSIHDMNDKlENE 293
Cdd:TIGR02168 600 FLGVAKDLVKFDPKLRKalsyllggvlvvdDLDNALELakKLRPGYRIVTLDgdlvrPGGVITGGSAKTNSSILER-RRE 678
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 294 LANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAA----LTKAEERHGNIEERMRHLEGQLEE 369
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAlrkdLARLEAEVEQLEERIAQLSKELTE 758
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 370 KNQELQRARQREKMNEEHNKRLSD---TVDRLLTESNERLQLhLKERMAALEEK----NVLIQESETFRKNLEESLHDKE 442
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAeieELEAQIEQLKEELKA-LREALDELRAEltllNEEAANLRERLESLERRIAATE 837
|
490
....*....|...
gi 1958790272 443 RLAEEIEKLRSEL 455
Cdd:TIGR02168 838 RRLEDLEEQIEEL 850
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
30-457 |
7.57e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.71 E-value: 7.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 30 AALTKELNACREQL---LEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVvkrqaqspSGVSSEVEVLKALKSL 106
Cdd:PRK03918 168 GEVIKEIKRRIERLekfIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL--------EKLEKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 107 FEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQR-KMVSSEGSTESEHLDGMEPGQKVHEKRLSNG 185
Cdd:PRK03918 240 IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElKEKAEEYIKLSEFYEEYLDELREIEKRLSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 186 SidstddtSQIVELQEL---LEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNT-----------KYQRD 251
Cdd:PRK03918 320 E-------EEINGIEERikeLEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERlkkrltgltpeKLEKE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 252 IREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLEN--------------------------ELANKEAILRQME 305
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelteehrkelleeytaELKRIEKELKEIE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 306 EKNRQLQERLELAEQKLQQ-----TMRK-AETLPEVEAELAQ-RIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRAR 378
Cdd:PRK03918 473 EKERKLRKELRELEKVLKKeseliKLKElAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 379 QREKMNEEHNKRLsDTVDRLLTESNERLQLHLKERMAALEEKnvlIQESETFRK---NLEESLHDKERLAEEIEKLRSEL 455
Cdd:PRK03918 553 ELKKKLAELEKKL-DELEEELAELLKELEELGFESVEELEER---LKELEPFYNeylELKDAEKELEREEKELKKLEEEL 628
|
..
gi 1958790272 456 DQ 457
Cdd:PRK03918 629 DK 630
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
193-467 |
2.60e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.16 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 193 TSQIVELQELLEKQNYEMAQMKDRLA-------ALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEER 265
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEelqkelyALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 266 ITTLEKRYLSAQRESTSihdmndkLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpevEAELAQRIAA 345
Cdd:TIGR02168 339 LAELEEKLEELKEELES-------LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL---NNEIERLEAR 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 346 LTKAEERHGNIEERMRHLEGQLEEKNQELQRAR--QREKMNEEHNKRLSDTVDRLLTESNERLQlhLKERMAALEEKNVL 423
Cdd:TIGR02168 409 LERLEDRRERLQQEIEELLKKLEEAELKELQAEleELEEELEELQEELERLEEALEELREELEE--AEQALDAAERELAQ 486
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1958790272 424 IQESETFRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSLIE 467
Cdd:TIGR02168 487 LQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIS 530
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
95-386 |
5.28e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.40 E-value: 5.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 95 SEVEVLKALKSLFEHHKALDEKVRERLrvslERVSALEEELAAANQEIVAL-REQNVHIQRKMVSSEGSTES--EHLDGM 171
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELE----KRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASleRSIAEK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 172 EPGQKVHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRD 251
Cdd:TIGR02169 314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 252 IREAmaqKEDMEERITTLEKRYLSAQRESTSIHDMNdkleNELANKEAILRQMEEKNRQLQERLELAEQKLQQTmrkaet 331
Cdd:TIGR02169 394 LEKL---KREINELKRELDRLQEELQRLSEELADLN----AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL------ 460
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1958790272 332 lpeveaelaqrIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEE 386
Cdd:TIGR02169 461 -----------AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
194-456 |
1.83e-10 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 64.32 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 194 SQIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRY 273
Cdd:pfam19220 48 SRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 274 LSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERH 353
Cdd:pfam19220 128 AAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDAT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 354 gniEERMRHLEGQLEEKNQELQRA-RQREKMNEEHNKRLSD-------------TVDRLLTESNERLQlHLKERMAALEE 419
Cdd:pfam19220 208 ---RARLRALEGQLAAEQAERERAeAQLEEAVEAHRAERASlrmklealtaraaATEQLLAEARNQLR-DRDEAIRAAER 283
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1958790272 420 KNV-LIQESETFRKNLEESLHDKERLAE---EIEKLRSELD 456
Cdd:pfam19220 284 RLKeASIERDTLERRLAGLEADLERRTQqfqEMQRARAELE 324
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
27-383 |
3.54e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.02 E-value: 3.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 27 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHE------------RSLRMTVVKRQAQSPSGVS 94
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAleaelaelperlEELEERLEELRELEEELEE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 95 SEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEHLDgmepg 174
Cdd:COG4717 168 LEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE----- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 175 QKVHEKRLSN----------GSIDSTDDTSQIVE------------LQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAE 232
Cdd:COG4717 243 ERLKEARLLLliaaallallGLGGSLLSLILTIAgvlflvlgllalLFLLLAREKASLGKEAEELQALPALEELEEEELE 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 233 TARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKnRQLQ 312
Cdd:COG4717 323 ELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEY-QELK 401
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958790272 313 ERLELAEQKLQQ------TMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLE--EKNQELQRARQREKM 383
Cdd:COG4717 402 EELEELEEQLEEllgeleELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEqlEEDGELAELLQELEE 480
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
199-465 |
3.79e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.31 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 199 LQELLEKQNYEMAQMKDRLaalsSRVGEVEQEAETARKDLIKTEemntkyqRDIREAMAQKEDMEERITTLEKRYlsaqR 278
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFI----KRTENIEELIKEKEKELEEVL-------REINEISSELPELREELEKLEKEV----K 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 279 ESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVE--AELAQRIAAL-TKAEERHGN 355
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKekAEEYIKLSEFyEEYLDELRE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 356 IEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL--LTESNERLQ--LHLKERMAALEEKnVLIQESETFR 431
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLeeLEERHELYEeaKAKKEELERLKKR-LTGLTPEKLE 390
|
250 260 270
....*....|....*....|....*....|....
gi 1958790272 432 KNLEESLHDKERLAEEIEKLRSELDQMKMRTGSL 465
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKEL 424
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
25-455 |
3.95e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.31 E-value: 3.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 25 TFQEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLEclvsrhERSLRMTVVKRQAQspsgvssEVEVLKALK 104
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE------EKVKELKELKEKAE-------EYIKLSEFY 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 105 SLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTES-EHLDGMEPGQKVHEKRLS 183
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyEEAKAKKEELERLKKRLT 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 184 NGSIDSTDDTSQIV-----ELQELLEKQNYEMAQMKDRLAALSSRVGEVEQE-----------AETARKDLIK--TEEMN 245
Cdd:PRK03918 383 GLTPEKLEKELEELekakeEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgrelTEEHRKELLEeyTAELK 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 246 tKYQRDIREAMAQKEDMEERITTLEKrYLSAQRESTSIHDMNDKLEN-ELANKEAILRQMEEKNRQ---LQERLELAEQK 321
Cdd:PRK03918 463 -RIEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQLKElEEKLKKYNLEELEKKAEEyekLKEKLIKLKGE 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 322 LQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHL----EGQLEEKNQELqrarqrEKMNEEHNkRLSDTVDR 397
Cdd:PRK03918 541 IKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesVEELEERLKEL------EPFYNEYL-ELKDAEKE 613
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958790272 398 L--LTESNERLQLHLKERMAALEEKNvliQESETFRKNLEE-----SLHDKERLAEEIEKLRSEL 455
Cdd:PRK03918 614 LerEEKELKKLEEELDKAFEELAETE---KRLEELRKELEElekkySEEEYEELREEYLELSREL 675
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
41-459 |
4.45e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.31 E-value: 4.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 41 EQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRmtVVKRQAQSPSGVSSEV-EVLKALKSLFEHHKALDEKVR- 118
Cdd:PRK03918 286 KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN--GIEERIKELEEKEERLeELKKKLKELEKRLEELEERHEl 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 119 -ERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEHLDGMEpgQKVHEKRLSNGSIDSTDDTSQIV 197
Cdd:PRK03918 364 yEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELK--KEIKELKKAIEELKKAKGKCPVC 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 198 -------ELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQ-----------------RDIR 253
Cdd:PRK03918 442 grelteeHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKElaeqlkeleeklkkynlEELE 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 254 EAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDK---LENELANKEA----ILRQMEEKNRQLQERLELAEQKLQQTM 326
Cdd:PRK03918 522 KKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKlaeLEKKLDELEEelaeLLKELEELGFESVEELEERLKELEPFY 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 327 RKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQreKMNEEHNKRLSDTVDRLltesnERL 406
Cdd:PRK03918 602 NEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK--KYSEEEYEELREEYLEL-----SRE 674
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1958790272 407 QLHLKERMAALEEknvLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQMK 459
Cdd:PRK03918 675 LAGLRAELEELEK---RREEIKKTLEKLKEELEEREKAKKELEKLEKALERVE 724
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
246-457 |
6.39e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 6.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 246 TKYQRDIREAMAQKEDMEERIT-------TLEKRY--LSAQRESTSIHDmndKLENELANKEAILRQMEEknRQLQERLE 316
Cdd:COG1196 168 SKYKERKEEAERKLEATEENLErledilgELERQLepLERQAEKAERYR---ELKEELKELEAELLLLKL--RELEAELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 317 LAEQKLQqtmrkaetlpEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQ-------RARQREKMNEEHNK 389
Cdd:COG1196 243 ELEAELE----------ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYellaelaRLEQDIARLEERRR 312
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958790272 390 RLSDTVDRLLTEsNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQ 457
Cdd:COG1196 313 ELEERLEELEEE-LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
35-380 |
6.89e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.42 E-value: 6.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 35 ELNACREQLLEKEEEISELKAERNNTRLLLEHLEclvSRHERslrmtvvKRQAQSpsgvSSEVEVLKALKSLFEHHKALd 114
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELE---AELEE-------LRLELE----ELELELEEAQAEEYELLAEL- 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 115 EKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEgstesehldgmepgqkvhekrlsngsidstddtS 194
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE---------------------------------E 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 195 QIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYL 274
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 275 SAQREstsihdmndkLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHG 354
Cdd:COG1196 425 ELEEA----------LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
330 340
....*....|....*....|....*.
gi 1958790272 355 NIEERMRHLEGQLEEKNQELQRARQR 380
Cdd:COG1196 495 LLLEAEADYEGFLEGVKAALLLAGLR 520
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
27-461 |
6.92e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.54 E-value: 6.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 27 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLEclvsRHERSLRMTVvkRQAQSPSGVSSEVEVLKALKSL 106
Cdd:PRK03918 231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK----KEIEELEEKV--KELKELKEKAEEYIKLSEFYEE 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 107 FEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTES-EHLDGMEPGQKVHEKRLSNG 185
Cdd:PRK03918 305 YLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyEEAKAKKEELERLKKRLTGL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 186 SIDstddtsQIVELQELLEKQNYEMaqmKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTK------------YQRDIR 253
Cdd:PRK03918 385 TPE------KLEKELEELEKAKEEI---EEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrelteehRKELLE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 254 EAMAQKEDMEERITTLEKRYLSAQRESTsihdmndKLENELANKEAI--LRQMEEKNRQLQERLE-LAEQKLQQTMRKAE 330
Cdd:PRK03918 456 EYTAELKRIEKELKEIEEKERKLRKELR-------ELEKVLKKESELikLKELAEQLKELEEKLKkYNLEELEKKAEEYE 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 331 TLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRA-RQREKMNEEHNKRLSDTVDRLLTESNERLQLH 409
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELlKELEELGFESVEELEERLKELEPFYNEYLELK 608
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1958790272 410 LKERMAALEEKNVLIQESEtfrknLEESLHDKERLAEEIEKLRSELDQMKMR 461
Cdd:PRK03918 609 DAEKELEREEKELKKLEEE-----LDKAFEELAETEKRLEELRKELEELEKK 655
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
118-453 |
7.63e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 63.44 E-value: 7.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 118 RERLRVSLERVSALEEELAAANQEIVALREQNVHIQRK---MVSSEGSTESEHLDGMEPGQKVHEKRLSNGSIDSTDDts 194
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARElaeLNEAESDLEQDYQAASDHLNLVQTALRQQEKIERYQA-- 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 195 QIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLikteemntkyqrdireamaqkEDMEERITTLEKR-- 272
Cdd:PRK04863 356 DLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQL---------------------ADYQQALDVQQTRai 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 273 -YLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQ-------------QTMRKAetLPEVEAE 338
Cdd:PRK04863 415 qYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSvaqaahsqfeqayQLVRKI--AGEVSRS 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 339 LAQRIA--ALTKAEErHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDrllteSNERLQLHLKERMAA 416
Cdd:PRK04863 493 EAWDVAreLLRRLRE-QRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLD-----DEDELEQLQEELEAR 566
|
330 340 350
....*....|....*....|....*....|....*..
gi 1958790272 417 LEEknvLIQESETFRKNLEESLHDKERLAEEIEKLRS 453
Cdd:PRK04863 567 LES---LSESVSEARERRMALRQQLEQLQARIQRLAA 600
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
25-353 |
9.13e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.15 E-value: 9.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 25 TFQEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLEclvsrherslrmtvvkrqaqspsgvsSEVEVLKALK 104
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ--------------------------KELYALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 105 SLFEHHKaldekvrERLRVSLERvsaLEEELAAANQEIVALREQNVHIQRKMVSSEgstesehldgmepgqkvhekrlsn 184
Cdd:TIGR02168 298 SRLEQQK-------QILRERLAN---LERQLEELEAQLEELESKLDELAEELAELE------------------------ 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 185 gsidstddtSQIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEE 264
Cdd:TIGR02168 344 ---------EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 265 RITTLEKRyLSAQRESTSIHDMnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIA 344
Cdd:TIGR02168 415 RRERLQQE-IEELLKKLEEAEL-KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
|
....*....
gi 1958790272 345 ALTKAEERH 353
Cdd:TIGR02168 493 SLERLQENL 501
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
194-386 |
1.32e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 61.38 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 194 SQIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAmaqKEDMEERITTLEKRY 273
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA---EAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 274 LSAQR------------ESTSIHDMNDKLEN----ELANKEAILRQMEEKNR--QLQERLELAEQKLQQTMRKAET-LPE 334
Cdd:COG3883 93 RALYRsggsvsyldvllGSESFSDFLDRLSAlskiADADADLLEELKADKAEleAKKAELEAKLAELEALKAELEAaKAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958790272 335 VEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEE 386
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
249-464 |
1.36e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.32 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 249 QRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK 328
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 329 AETLpevEAELAQRIAALTK------------------AEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKR 390
Cdd:COG4942 99 LEAQ---KEELAELLRALYRlgrqpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958790272 391 LSDTVDRLLTEsNERLQLHLKERMAALEEKNvliQESETFRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGS 464
Cdd:COG4942 176 LEALLAELEEE-RAALEALKAERQKLLARLE---KELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
27-377 |
4.06e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 4.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 27 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMtVVKRQAQSPSGVSSEVEVLKALKSL 106
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE-LLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 107 FE-------HHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEHLDGMEPGQKVHE 179
Cdd:COG1196 318 LEeleeelaELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 180 KRlsngsidstddtSQIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEmntkyqrDIREAMAQK 259
Cdd:COG1196 398 LA------------AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE-------EEAELEEEE 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 260 EDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQtmRKAETLPEVEAEL 339
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA--GAVAVLIGVEAAY 536
|
330 340 350
....*....|....*....|....*....|....*...
gi 1958790272 340 AQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRA 377
Cdd:COG1196 537 EAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRA 574
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
820-886 |
4.39e-09 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 53.84 E-value: 4.39e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958790272 820 FAQWDGPTVVAWLELwLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 886
Cdd:smart00454 1 VSQWSPESVADWLES-IGLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
41-478 |
4.46e-09 |
|
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: 61.22 E-value: 4.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 41 EQLLEKEEEISELKAERNNTRLL----LEHLECLVSRHERSLRMTVVKRQAQSpsgvsSEVE-VLKALKSLFEHHKALDE 115
Cdd:TIGR00606 684 QRVFQTEAELQEFISDLQSKLRLapdkLKSTESELKKKEKRRDEMLGLAPGRQ-----SIIDlKEKEIPELRNKLQKVNR 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 116 KVrERLRVSLERVSAL------EEELAAANQEIVALREQnVHIQRKMVSSEGSTESEHLDGMEPGQKVHEKRLSNGSIDS 189
Cdd:TIGR00606 759 DI-QRLKNDIEEQETLlgtimpEEESAKVCLTDVTIMER-FQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQH 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 190 TDDT--SQIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERIT 267
Cdd:TIGR00606 837 ELDTvvSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLET 916
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 268 TLEKrylSAQRESTSIHDMNDklENELANKEaiLRQMEEKNRQLQERLELAEQKLQQTmrKAETLPEVEAELAQRIAALT 347
Cdd:TIGR00606 917 FLEK---DQQEKEELISSKET--SNKKAQDK--VNDIKEKVKNIHGYMKDIENKIQDG--KDDYLKQKETELNTVNAQLE 987
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 348 KAEERHGNIEERMRHLEGQLEEKNQE---LQRARQREKMNEEHnKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLI 424
Cdd:TIGR00606 988 ECEKHQEKINEDMRLMRQDIDTQKIQerwLQDNLTLRKRENEL-KEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLI 1066
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958790272 425 QESETF-----RKNLEESLHDKERLAEEI-----EKLRSELDQMKMRTGSLIEPTISRTHLDTS 478
Cdd:TIGR00606 1067 KRNHVLalgrqKGYEKEIKHFKKELREPQfrdaeEKYREMMIVMRTTELVNKDLDIYYKTLDQA 1130
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
34-458 |
8.15e-09 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 59.98 E-value: 8.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 34 KELNACREQLLEKEEEISELKAERNNtrlLLEHLECLVsrhERSLRMTVVKRQAQSPSGVSSEvEVLKALKSLFEHHKAL 113
Cdd:TIGR00618 472 EQQLQTKEQIHLQETRKKAVVLARLL---ELQEEPCPL---CGSCIHPNPARQDIDNPGPLTR-RMQRGEQTYAQLETSE 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 114 dEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKM---------VSSEGSTESEHLDGMEPGQKVHEKRL-- 182
Cdd:TIGR00618 545 -EDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIpnlqnitvrLQDLTEKLSEAEDMLACEQHALLRKLqp 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 183 --SNGSIDSTDDTSQIVELQELLEKQNYE--MAQMKDRLAALSSRvgevEQEAETARKDLIKTEEMNTKYQR--DIREAM 256
Cdd:TIGR00618 624 eqDLQDVRLHLQQCSQELALKLTALHALQltLTQERVREHALSIR----VLPKELLASRQLALQKMQSEKEQltYWKEML 699
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 257 AQKEDMEERITTLEKRYlsaqrestsihdmnDKLENELANKEAILRQmeeknrQLQERLELAEQKLQQTMRKAET-LPEV 335
Cdd:TIGR00618 700 AQCQTLLRELETHIEEY--------------DREFNEIENASSSLGS------DLAAREDALNQSLKELMHQARTvLKAR 759
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 336 EAELAQRIAALTKAEERhgniEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMA 415
Cdd:TIGR00618 760 TEAHFNNNEEVTAALQT----GAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLS 835
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1958790272 416 ALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQM 458
Cdd:TIGR00618 836 RLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
35-440 |
9.55e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.15 E-value: 9.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 35 ELNACREQLLEKEEEISELKAERNNTRLLLEHLEcLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALD 114
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAE-EKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 115 E--KVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKmvSSEGSTESEHLDGMEPGQKVHEKRLSNgSIDSTDD 192
Cdd:PTZ00121 1474 EakKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAK--KAEEAKKADEAKKAEEAKKADEAKKAE-EKKKADE 1550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 193 TSQIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDliktEEMNTKYQRDIREAMAQKEDMEERITTLEKR 272
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIE----EVMKLYEEEKKMKAEEAKKAEEAKIKAEELK 1626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 273 ylSAQRESTSIHDMNDKLENEL--------ANKEAILRQMEEKNRQLQERLELAE-QKLQQTMRKAETLPEVEAELAQRI 343
Cdd:PTZ00121 1627 --KAEEEKKKVEQLKKKEAEEKkkaeelkkAEEENKIKAAEEAKKAEEDKKKAEEaKKAEEDEKKAAEALKKEAEEAKKA 1704
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 344 AALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKR---LSDTVDRLLTESNERLQLHLKERMAALEEK 420
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKdeeEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE 1784
|
410 420
....*....|....*....|
gi 1958790272 421 nvLIQESETFRKNLEESLHD 440
Cdd:PTZ00121 1785 --LDEEDEKRRMEVDKKIKD 1802
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
27-458 |
1.26e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 27 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSL 106
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 107 FEHHKALDEKVRERLRVsLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEHLDGMEPGQKVHEKRLSNGS 186
Cdd:COG1196 403 EELEEAEEALLERLERL-EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 187 IDSTDDTSQIVELQELLEKQNYE-------MAQMKDRLAALSSRVGE---VEQEAETARKDLIKTEEMNTKYQRDIREAM 256
Cdd:COG1196 482 LLEELAEAAARLLLLLEAEADYEgflegvkAALLLAGLRGLAGAVAVligVEAAYEAALEAALAAALQNIVVEDDEVAAA 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 257 A---QKEDMEERITTLEKRyLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLP 333
Cdd:COG1196 562 AieyLKAAKAGRATFLPLD-KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV 640
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 334 EVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQRE-KMNEEHNKRLSDTVDRLLTESNERLQLHLKE 412
Cdd:COG1196 641 TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLaEEELELEEALLAEEEEERELAEAEEERLEEE 720
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958790272 413 RMAALEEKNVLIQESETFRKNLEESLHDKERLAE-------------EIEKLRSELDQM 458
Cdd:COG1196 721 LEEEALEEQLEAEREELLEELLEEEELLEEEALEelpeppdleelerELERLEREIEAL 779
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
217-458 |
1.33e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 217 LAALSSRVGEVEQ--EAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKrYLSAQREstsIHDMNDKLENEL 294
Cdd:PRK03918 127 LNAIYIRQGEIDAilESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEK-FIKRTEN---IEELIKEKEKEL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 295 ANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQ---LEEKN 371
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEieeLEEKV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 372 QELQRARQREKMNEEHNKRLSDTVDRL-----LTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAE 446
Cdd:PRK03918 283 KELKELKEKAEEYIKLSEFYEEYLDELreiekRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHE 362
|
250
....*....|..
gi 1958790272 447 EIEKLRSELDQM 458
Cdd:PRK03918 363 LYEEAKAKKEEL 374
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
101-465 |
1.39e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 101 KALKSLFEHHKALDEKvRERLRVSLERVSALEEELAAANQEIVA-LREQNvhiqrkMVSSEGSTESEHLDGMEPGQKVHE 179
Cdd:PRK03918 162 NAYKNLGEVIKEIKRR-IERLEKFIKRTENIEELIKEKEKELEEvLREIN------EISSELPELREELEKLEKEVKELE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 180 KRlsngsidstddTSQIVELQELLEKQNYEMAQMKDRLAALSSRVGEVE---QEAETARKDLIKTEEMNTKYQRDIR--- 253
Cdd:PRK03918 235 EL-----------KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKkeiEELEEKVKELKELKEKAEEYIKLSEfye 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 254 EAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQME---------EKNRQLQERLELAEQKLqq 324
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEeleerhelyEEAKAKKEELERLKKRL-- 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 325 tmrKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ---ELQRARQR-----EKMNEEHNKRLSDTVD 396
Cdd:PRK03918 382 ---TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKaieELKKAKGKcpvcgRELTEEHRKELLEEYT 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 397 RLLTESNERLQ-LHLKERMAALEEKNV---LIQESETFR--------KNLEESL--HDKERL---AEEIEKLRSELDQMK 459
Cdd:PRK03918 459 AELKRIEKELKeIEEKERKLRKELRELekvLKKESELIKlkelaeqlKELEEKLkkYNLEELekkAEEYEKLKEKLIKLK 538
|
....*.
gi 1958790272 460 MRTGSL 465
Cdd:PRK03918 539 GEIKSL 544
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
191-611 |
1.78e-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: 58.93 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 191 DDTSQIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEemntKYQrdirEAMAQKEDMEERITTLE 270
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE----RYQ----ALLKEKREYEGYELLKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 271 KRYLSAQREstsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAelaqrIAALTKAE 350
Cdd:TIGR02169 232 KEALERQKE---------AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ-----LRVKEKIG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 351 ERHGNIEErmrhLEGQLEEKNQELQRA-RQREKMNEEHNKrlsdtvdrlltesnerlqlhLKERMAALEEKnvliqeset 429
Cdd:TIGR02169 298 ELEAEIAS----LERSIAEKERELEDAeERLAKLEAEIDK--------------------LLAEIEELERE--------- 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 430 frknLEESLHDKERLAEEIEKLRSELDQMKMRTGSliEPTISRTHLDTSAELRYSVGSLVDSQSDYRTTkvirRPRRGRM 509
Cdd:TIGR02169 345 ----IEEERKRRDKLTEEYAELKEELEDLRAELEE--VDKEFAETRDELKDYREKLEKLKREINELKRE----LDRLQEE 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 510 GVRRDEpkvkSLGDHEwnrtQQIGVLGSHPFESDTEMSDIDDDDRETIFSSMDLLSPSGHSDAQTLAmmLQEQLDAINKE 589
Cdd:TIGR02169 415 LQRLSE----ELADLN----AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD--LKEEYDRVEKE 484
|
410 420
....*....|....*....|..
gi 1958790272 590 IRLIQEEKESTELRAEEIENRV 611
Cdd:TIGR02169 485 LSKLQRELAEAEAQARASEERV 506
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
126-497 |
1.85e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 126 ERVSALEEELAAANQEIVALREQNVHIQRKMvssegstesEHLDGmepgQKVHEKRLSNGS---IDSTDDTSQIVELQ-- 200
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAEL---------DALQE----RREALQRLAEYSwdeIDVASAEREIAELEae 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 201 -ELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRE 279
Cdd:COG4913 677 lERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFA 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 280 STSIhdmnDKLENELAnkeailRQMEEKNRQLQERLELAEQKLQQTMRKA-ETLPEVEAELAQRIAALTKAEERHGNIEE 358
Cdd:COG4913 757 AALG----DAVERELR------ENLEERIDALRARLNRAEEELERAMRAFnREWPAETADLDADLESLPEYLALLDRLEE 826
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 359 RmrhlegQLEEKNQELQRARQR----------EKMNEEHN---KRLsDTVDRLLTESN----ERLQLHLKERmaALEEKN 421
Cdd:COG4913 827 D------GLPEYEERFKELLNEnsiefvadllSKLRRAIReikERI-DPLNDSLKRIPfgpgRYLRLEARPR--PDPEVR 897
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 422 VLIQE-----SETFRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSLIepTISRTHLDTSAELRYSV-GSLVDSQSDY 495
Cdd:COG4913 898 EFRQElravtSGASLFDEELSEARFAALKRLIERLRSEEEESDRRWRARV--LDVRNHLEFDAEEIDREdGEEVETYSSS 975
|
..
gi 1958790272 496 RT 497
Cdd:COG4913 976 GG 977
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
194-405 |
2.11e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.85 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 194 SQIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRY 273
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 274 ----LSAQREST--------SIHDMNDkLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQ 341
Cdd:COG4942 107 aellRALYRLGRqpplalllSPEDFLD-AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958790272 342 RIAALTKAEERHgniEERMRHLEGQLEEKNQELQRARQREkmneehnKRLSDTVDRLLTESNER 405
Cdd:COG4942 186 ERAALEALKAER---QKLLARLEKELAELAAELAELQQEA-------EELEALIARLEAEAAAA 239
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
27-397 |
2.88e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 27 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSL 106
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAA 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 107 FEHH--KALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNvhiqrKMVSSEGSTESEHLDGMEPGQKVHEKRLSN 184
Cdd:COG1196 536 YEAAleAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLD-----KIRARAALAAALARGAIGAAVDLVASDLRE 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 185 GSIDSTDDTSQIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEE 264
Cdd:COG1196 611 ADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAE 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 265 RITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIA 344
Cdd:COG1196 691 EELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELE 770
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958790272 345 ALTKAEERHGNI-----------EERMRHLEGQLEeknqELQRARQR-----EKMNEEHNKRLSDTVDR 397
Cdd:COG1196 771 RLEREIEALGPVnllaieeyeelEERYDFLSEQRE----DLEEARETleeaiEEIDRETRERFLETFDA 835
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
112-456 |
3.93e-08 |
|
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: 58.04 E-value: 3.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 112 ALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQ------RKMVSSEGSTESEHLdgmepGQKVHEKRlsng 185
Cdd:COG3096 829 AFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKeqlqllNKLLPQANLLADETL-----ADRLEELR---- 899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 186 sidstddtsqiVELQELLEKQNYeMAQMKDRLAalssrvgEVEQEAETARKDLIKTEEMNTKYQRdireAMAQKEDMEER 265
Cdd:COG3096 900 -----------EELDAAQEAQAF-IQQHGKALA-------QLEPLVAVLQSDPEQFEQLQADYLQ----AKEQQRRLKQQ 956
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 266 ITTLEkrYLSAQRESTSIHD----------MNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEV 335
Cdd:COG3096 957 IFALS--EVVQRRPHFSYEDavgllgensdLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQT 1034
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 336 EAELAQRIAAL-----TKAEERhgnIEERMRHLEGQL----EEKNQ-ELQRARQREKMnEEHNKRLSDtVDRLLTESNER 405
Cdd:COG3096 1035 LQELEQELEELgvqadAEAEER---ARIRRDELHEELsqnrSRRSQlEKQLTRCEAEM-DSLQKRLRK-AERDYKQEREQ 1109
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1958790272 406 LQLHLKERMAALEeknvLIQESetfrkNLEESLHDKERLAEEIEKLRSELD 456
Cdd:COG3096 1110 VVQAKAGWCAVLR----LARDN-----DVERRLHRRELAYLSADELRSMSD 1151
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
230-482 |
4.23e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 230 EAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNR 309
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 310 QLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALtkaeerhgniEERMRHLEGQLEEKNQELQRARQREKMNEEHnk 389
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEEL----------KEELESLEAELEELEAELEELESRLEELEEQ-- 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 390 rlsdtvdrLLTESNERLQLhlkermaaLEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSLIEPT 469
Cdd:TIGR02168 381 --------LETLRSKVAQL--------ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEE 444
|
250
....*....|...
gi 1958790272 470 ISRTHLDTSAELR 482
Cdd:TIGR02168 445 LEEELEELQEELE 457
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
32-466 |
4.37e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 57.72 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 32 LTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHeRSLrmtvvkrqaqspsgvSSEVEVLKALKSLFEhhK 111
Cdd:TIGR04523 171 LENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKN-KSL---------------ESQISELKKQNNQLK--D 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 112 ALDEKVRErlrvslerVSALEEELAAANQEIVALREQNVHIQRKMV--SSEGSTESEHLDGMEPGQKVHEKRLSNGSIDS 189
Cdd:TIGR04523 233 NIEKKQQE--------INEKTTEISNTQTQLNQLKDEQNKIKKQLSekQKELEQNNKKIKELEKQLNQLKSEISDLNNQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 190 TDDTSQivELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREamaqKEDMEERIttl 269
Cdd:TIGR04523 305 EQDWNK--ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE----KQNEIEKL--- 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 270 ekrylsaQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKA 349
Cdd:TIGR04523 376 -------KKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQ 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 350 ----EERHGNIEERMRHLEGQ--------------LEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNErlqlhLK 411
Cdd:TIGR04523 449 dsvkELIIKNLDNTRESLETQlkvlsrsinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS-----LK 523
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958790272 412 ERMAALE----EKNVLIQESETFRKNLEESLhDKERLAEEIEKLRSELDQMKMRTGSLI 466
Cdd:TIGR04523 524 EKIEKLEsekkEKESKISDLEDELNKDDFEL-KKENLEKEIDEKNKEIEELKQTQKSLK 581
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
194-369 |
5.27e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 54.93 E-value: 5.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 194 SQIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLikteemnTKYQRDIREAMAQKEDMEERITTL--EK 271
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEI-------KRLELEIEEVEARIKKYEEQLGNVrnNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 272 RYLSAQRESTSIHDMNDKLEnelankEAILRQMEEKNrQLQERLELAEQKLQQtmrKAETLPEVEAELAQRIAALTKAEE 351
Cdd:COG1579 90 EYEALQKEIESLKRRISDLE------DEILELMERIE-ELEEELAELEAELAE---LEAELEEKKAELDEELAELEAELE 159
|
170
....*....|....*...
gi 1958790272 352 RhgnIEERMRHLEGQLEE 369
Cdd:COG1579 160 E---LEAEREELAAKIPP 174
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
45-470 |
5.48e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.46 E-value: 5.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 45 EKEEEISELKAERNNTRLllehlECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVR--ERLR 122
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKA-----DAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKkaDEAK 1437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 123 VSLERVSAlEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEHLDGMEPGQKVHE--KRLSNGSIDSTDDTSQIVELQ 200
Cdd:PTZ00121 1438 KKAEEAKK-ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEeaKKKADEAKKAAEAKKKADEAK 1516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 201 ELLEKQNYEMAQmkdrlAALSSRVGEVEQEAETARK--DLIKTEEMntKYQRDIREAMAQKEDMEERITTLEKRYLSAQR 278
Cdd:PTZ00121 1517 KAEEAKKADEAK-----KAEEAKKADEAKKAEEKKKadELKKAEEL--KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA 1589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 279 ESTSIHDMNDKLENELANKEAILRQMEE---------KNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKA 349
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEKKMKAEEAKKAEEakikaeelkKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK 1669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 350 EERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLltesnERLQLHLKERMAALEEknvLIQESET 429
Cdd:PTZ00121 1670 AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA-----EELKKAEEENKIKAEE---AKKEAEE 1741
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1958790272 430 FRKNLEESLHDKERlAEEIEKLRSELDQMKMRTGSLIEPTI 470
Cdd:PTZ00121 1742 DKKKAEEAKKDEEE-KKKIAHLKKEEEKKAEEIRKEKEAVI 1781
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
250-459 |
6.74e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 6.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 250 RDIREAMAQKED----MEERITTLEKRYLSAQRestsIHDMNDKLENelANKEAILRQMEEKNRQLqERLELAEQKLQQT 325
Cdd:TIGR02168 182 ERTRENLDRLEDilneLERQLKSLERQAEKAER----YKELKAELRE--LELALLVLRLEELREEL-EELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 326 MRKAET-LPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL------ 398
Cdd:TIGR02168 255 LEELTAeLQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELesklde 334
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958790272 399 ----LTESNERLQLhLKERMAALEEKnvlIQESETFRKNLEESLHDKErlaEEIEKLRSELDQMK 459
Cdd:TIGR02168 335 laeeLAELEEKLEE-LKEELESLEAE---LEELEAELEELESRLEELE---EQLETLRSKVAQLE 392
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
95-459 |
7.13e-08 |
|
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: 56.67 E-value: 7.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 95 SEVEVLKALKSLFEHHKALDEKVR---------ERLRVS-------LERVSALEEELAAANQEIValREQNVHIQRKMVS 158
Cdd:pfam17380 266 TENEFLNQLLHIVQHQKAVSERQQqekfekmeqERLRQEkeekareVERRRKLEEAEKARQAEMD--RQAAIYAEQERMA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 159 SEGSTESEHLdgmepgqKVHEKRLSNGSIDSTDDTSQIVELQELlEKQNYEMAQMKDRlaalssrvgeVEQEAETARKDL 238
Cdd:pfam17380 344 MERERELERI-------RQEERKRELERIRQEEIAMEISRMREL-ERLQMERQQKNER----------VRQELEAARKVK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 239 IKTEEMntkyQRDIREAMAQKEDMeerittlekrylsaqrestsihdmndKLENELANKEAILRQMEEKNRQLqERLELA 318
Cdd:pfam17380 406 ILEEER----QRKIQQQKVEMEQI--------------------------RAEQEEARQREVRRLEEERAREM-ERVRLE 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 319 EQKLQQTMrkaETLPEVEAELAQRIAALTKAEERHGNIEERMRH-LEGQLEEKnqelqrarqREKMNEEHNKRlsdtvdr 397
Cdd:pfam17380 455 EQERQQQV---ERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKiLEKELEER---------KQAMIEEERKR------- 515
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958790272 398 lltesnERLQLHLKERMAALEEKNVLIQESETFRKNLEesLHDKERLAEEIEKL---RSELDQMK 459
Cdd:pfam17380 516 ------KLLEKEMEERQKAIYEEERRREAEEERRKQQE--MEERRRIQEQMRKAteeRSRLEAME 572
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
50-465 |
7.90e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 57.05 E-value: 7.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 50 ISELKAERNNTRLLLEHLECLVsRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERL---RVSLE 126
Cdd:pfam15921 414 IDHLRRELDDRNMEVQRLEALL-KAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELtakKMTLE 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 127 R----VSAL-------EEELAAANQEIVALREQ-NVHIQrkmvssegstESEHLdgmepgqKVHEKRLSNGSIDSTDDTS 194
Cdd:pfam15921 493 SsertVSDLtaslqekERAIEATNAEITKLRSRvDLKLQ----------ELQHL-------KNEGDHLRNVQTECEALKL 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 195 QIVE---LQELLEKQNYEMAQM---KDRLA-ALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERIT 267
Cdd:pfam15921 556 QMAEkdkVIEILRQQIENMTQLvgqHGRTAgAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKV 635
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 268 TLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAET-LPEVEAELAQRIAAL 346
Cdd:pfam15921 636 KLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMqLKSAQSELEQTRNTL 715
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 347 TKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEhnkrlsdtvdrLLTESNerlqlhlKERMAALEEKNVLIQE 426
Cdd:pfam15921 716 KSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEE-----------AMTNAN-------KEKHFLKEEKNKLSQE 777
|
410 420 430
....*....|....*....|....*....|....*....
gi 1958790272 427 SETFRKnleeslhDKERLAEEIEKLRSELDQMKMRTGSL 465
Cdd:pfam15921 778 LSTVAT-------EKNKMAGELEVLRSQERRLKEKVANM 809
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
946-1001 |
9.77e-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: 49.99 E-value: 9.77e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958790272 946 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1001
Cdd:smart00454 11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
194-484 |
1.26e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 55.29 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 194 SQIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRY 273
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 274 LSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMrkaetlpevEAELAQRIAALTKAEERH 353
Cdd:COG4372 125 QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS---------EAEAEQALDELLKEANRN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 354 GNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKN 433
Cdd:COG4372 196 AEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEE 275
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1958790272 434 LEESLHDKERLAEEIEKLRSELDQMKMRTGSLIEPTISRTHLDTSAELRYS 484
Cdd:COG4372 276 EELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAK 326
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
100-621 |
1.60e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 55.89 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 100 LKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEhldgMEPGQKVHE 179
Cdd:pfam15921 87 VKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHE----LEAAKCLKE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 180 KRLSNGSidstddtSQIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKdlIKTEEMNTKYQRDIREAMAQK 259
Cdd:pfam15921 163 DMLEDSN-------TQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMST--MHFRSLGSAISKILRELDTEI 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 260 EDMEERITTLEKRYLSAQRESTS-----IHDMNDKLENELANKEAILRQMEEKN-------RQLQERLEL-AEQKLQQTM 326
Cdd:pfam15921 234 SYLKGRIFPVEDQLEALKSESQNkiellLQQHQDRIEQLISEHEVEITGLTEKAssarsqaNSIQSQLEIiQEQARNQNS 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 327 RKAETLPEVEAELAQRIAALTKAEERHgniEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTEsnerl 406
Cdd:pfam15921 314 MYMRQLSDLESTVSQLRSELREAKRMY---EDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLAD----- 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 407 qLHLKERMAALE-EKNVLIQESET--------FRKNLEESLHDKERLAEEIEKLRSELD-QMKMRTGSL------IEPTI 470
Cdd:pfam15921 386 -LHKREKELSLEkEQNKRLWDRDTgnsitidhLRRELDDRNMEVQRLEALLKAMKSECQgQMERQMAAIqgknesLEKVS 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 471 SRT-HLDTSAE-LRYSVGSLVDS----QSDYRT----TKVIRRPRRGRMGVRRDEPKVKSLGDHEWNRTQQIGVLGSHPF 540
Cdd:pfam15921 465 SLTaQLESTKEmLRKVVEELTAKkmtlESSERTvsdlTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 541 ESDTE-------MSDID---DDDRETIFSSMDLLSPSGHSDA--QTLAMMLQEQLDAINKEIRLIQEEKESTELRAEEIE 608
Cdd:pfam15921 545 NVQTEcealklqMAEKDkviEILRQQIENMTQLVGQHGRTAGamQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELE 624
|
570
....*....|...
gi 1958790272 609 NRVASVSLEGLNL 621
Cdd:pfam15921 625 ARVSDLELEKVKL 637
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
146-456 |
1.84e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 55.57 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 146 REQNVHIQRKMVSSEGSTESEHLDGMEPG-QKVH-EKRLSNGSIDSTDDTSQIVELQEllEKQNYEMAQMKDRLAALSSR 223
Cdd:pfam01576 90 RSQQLQNEKKKMQQHIQDLEEQLDEEEAArQKLQlEKVTTEAKIKKLEEDILLLEDQN--SKLSKERKLLEERISEFTSN 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 224 VGEVEQEAETARKDLIKTEEMNTkyqrDIREAMAQKEDMEERittLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQ 303
Cdd:pfam01576 168 LAEEEEKAKSLSKLKNKHEAMIS----DLEERLKKEEKGRQE---LEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 304 MEEKNRQLQERLE---LAEQKLQQTMRKAET-LPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEK------NQE 373
Cdd:pfam01576 241 KEEELQAALARLEeetAQKNNALKKIRELEAqISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTldttaaQQE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 374 LQRARQRE--------------------KMNEEHNKRLSDTVDRLltESNERLQLHLKERMAALEEKNVLI--------- 424
Cdd:pfam01576 321 LRSKREQEvtelkkaleeetrsheaqlqEMRQKHTQALEELTEQL--EQAKRNKANLEKAKQALESENAELqaelrtlqq 398
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1958790272 425 --QESETFRKNLEESLHD-----------KERLAEEIEKLRSELD 456
Cdd:pfam01576 399 akQDSEHKRKKLEGQLQElqarlseserqRAELAEKLSKLQSELE 443
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
235-458 |
2.17e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 55.36 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 235 RKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRY----LSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQ 310
Cdd:TIGR00618 165 KKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSqlltLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAY 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 311 LQERLELAEQK------LQQTMRKAETLPEVEAELAQRIAALTKA--EERHGNIEERMRHLEGQLEEKNQELQ-RARQRE 381
Cdd:TIGR00618 245 LTQKREAQEEQlkkqqlLKQLRARIEELRAQEAVLEETQERINRArkAAPLAAHIKAVTQIEQQAQRIHTELQsKMRSRA 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 382 KMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLH----DKERLAEEIEKLRSELDQ 457
Cdd:TIGR00618 325 KLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHtlqqQKTTLTQKLQSLCKELDI 404
|
.
gi 1958790272 458 M 458
Cdd:TIGR00618 405 L 405
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
32-450 |
3.15e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 54.64 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 32 LTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTvvKRQAQSpsgVSSEVEVLKALKSlfehhK 111
Cdd:TIGR04523 237 KQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKEL--EKQLNQ---LKSEISDLNNQKE-----Q 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 112 ALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIqrkmvssegstesehldgmepgqkvhEKRLSNGSIDSTD 191
Cdd:TIGR04523 307 DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQL--------------------------KKELTNSESENSE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 192 DTSQIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAEtarkdliKTEEMNTKYQRDIREAMAQKEDMEERITTLEK 271
Cdd:TIGR04523 361 KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ-------NQEKLNQQKDEQIKKLQQEKELLEKEIERLKE 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 272 RYLSAQREstsIHDmndkLENELANKEAILRQMEEKNRQLQERLEL-------AEQKLQQTMR-------KAETLPEVEA 337
Cdd:TIGR04523 434 TIIKNNSE---IKD----LTNQDSVKELIIKNLDNTRESLETQLKVlsrsinkIKQNLEQKQKelkskekELKKLNEEKK 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 338 ELAQRIAALTKaeeRHGNIEERMRHLEGQLEEKNQEL-QRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAA 416
Cdd:TIGR04523 507 ELEEKVKDLTK---KISSLKEKIEKLESEKKEKESKIsDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKK 583
|
410 420 430
....*....|....*....|....*....|....
gi 1958790272 417 LEEKNVLIQESETFRKNLEESLHDKERLAEEIEK 450
Cdd:TIGR04523 584 QEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEK 617
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
31-460 |
3.17e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 54.80 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 31 ALTKELNACREQLLEKEEEISELKAERNNTRlllEHLECLVSR--HERSLRMTVVKRQAQSPSGVSSevevlkaLKSLFE 108
Cdd:pfam01576 212 KLEGESTDLQEQIAELQAQIAELRAQLAKKE---EELQAALARleEETAQKNNALKKIRELEAQISE-------LQEDLE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 109 HHKALDEKVRERLRVSLERVSALEEEL------AAANQEIVALREQNVHIQRKMVSSEGstesehldgmepgqKVHEKRL 182
Cdd:pfam01576 282 SERAARNKAEKQRRDLGEELEALKTELedtldtTAAQQELRSKREQEVTELKKALEEET--------------RSHEAQL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 183 SNGSIDSTddtSQIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETarkdlIKTEEMNTKYQRDIREAMAQKedm 262
Cdd:pfam01576 348 QEMRQKHT---QALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRT-----LQQAKQDSEHKRKKLEGQLQE--- 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 263 eerittLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMrkaETLPEveaELAQR 342
Cdd:pfam01576 417 ------LQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQ---ELLQE---ETRQK 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 343 IAALTKAEErhgnIEERMRHLEGQLEEknqELQRARQREKMNEEHNKRLSDTVDRLLTESnerlqlhlkERMAALEE-KN 421
Cdd:pfam01576 485 LNLSTRLRQ----LEDERNSLQEQLEE---EEEAKRNVERQLSTLQAQLSDMKKKLEEDA---------GTLEALEEgKK 548
|
410 420 430
....*....|....*....|....*....|....*....
gi 1958790272 422 VLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQMKM 460
Cdd:pfam01576 549 RLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLV 587
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
203-379 |
3.40e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 203 LEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEmntkyQRDIREAMAQKEDMEERITTLEKRYLSAQRESTS 282
Cdd:COG4717 83 AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK-----LLQLLPLYQELEALEAELAELPERLEELEERLEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 283 IHDmndkLENELANKEAILRQMEEKNRQLQERLELA-EQKLQQTMRKAEtlpEVEAELAQRIAALTKAEERHGNIEERMR 361
Cdd:COG4717 158 LRE----LEEELEELEAELAELQEELEELLEQLSLAtEEELQDLAEELE---ELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180
....*....|....*....|
gi 1958790272 362 HLEGQLE--EKNQELQRARQ 379
Cdd:COG4717 231 QLENELEaaALEERLKEARL 250
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
119-467 |
3.83e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.59 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 119 ERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEHLDGMepgQKVHEKRLSNgsidstddtsQIVE 198
Cdd:TIGR00618 212 CMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQ---LRARIEELRA----------QEAV 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 199 LQELLEKQNYemAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEkrylSAQR 278
Cdd:TIGR00618 279 LEETQERINR--ARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQ----TLHS 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 279 ESTSIHDMNDKlenELANKEAILRQMEEKN--RQLQERLELAEQKLQQTMRKAETLPE----VEAELAQRIAALTKAEER 352
Cdd:TIGR00618 353 QEIHIRDAHEV---ATSIREISCQQHTLTQhiHTLQQQKTTLTQKLQSLCKELDILQReqatIDTRTSAFRDLQGQLAHA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 353 HGNIEERMRHLEGQ----------LEEKNQELQRARQR---EKMNEEHNKRLSDTVDRLLTESNERLQLH------LKER 413
Cdd:TIGR00618 430 KKQQELQQRYAELCaaaitctaqcEKLEKIHLQESAQSlkeREQQLQTKEQIHLQETRKKAVVLARLLELqeepcpLCGS 509
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1958790272 414 MAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSLIE 467
Cdd:TIGR00618 510 CIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKE 563
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
269-461 |
4.21e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 4.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 269 LEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTK 348
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 349 AEERHgNIEERMRHLEGQLEE---KNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKErmaaleeknvLIQ 425
Cdd:COG4717 131 YQELE-ALEAELAELPERLEEleeRLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD----------LAE 199
|
170 180 190
....*....|....*....|....*....|....*.
gi 1958790272 426 ESETFRKNLEESLHDKERLAEEIEKLRSELDQMKMR 461
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
276-456 |
4.41e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 276 AQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGN 355
Cdd:PRK02224 197 EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 356 IEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNErlqlhLKERmaaLEEKNVLIQESETFRKNLE 435
Cdd:PRK02224 277 LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEE-----LRDR---LEECRVAAQAHNEEAESLR 348
|
170 180
....*....|....*....|.
gi 1958790272 436 ESLHDKERLAEEIEKLRSELD 456
Cdd:PRK02224 349 EDADDLEERAEELREEAAELE 369
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
210-418 |
4.55e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 210 MAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQREStsihdmnDK 289
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREEL-------EK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 290 LENELANKEAI--LRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGN-IEERMRHLEGQ 366
Cdd:COG4717 121 LEKLLQLLPLYqeLEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLaTEEELQDLAEE 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958790272 367 LEEKNQELQRARQREKMNEEHNKRLSDTVDRLlteSNERLQLHLKERMAALE 418
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQL---ENELEAAALEERLKEAR 249
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
195-379 |
5.52e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 5.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 195 QIVELQELLEKQNyEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEmnTKYQRDIREAMAQKEDMEERITTLEKRYL 274
Cdd:COG4913 250 QIELLEPIRELAE-RYAAARERLAELEYLRAALRLWFAQRRLELLEAEL--EELRAELARLEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 275 SAQREstsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQkLQQTMRKAE-TLPEVEAELAQRI----AALTKA 349
Cdd:COG4913 327 ELEAQ---------IRGNGGDRLEQLEREIERLERELEERERRRAR-LEALLAALGlPLPASAEEFAALRaeaaALLEAL 396
|
170 180 190
....*....|....*....|....*....|
gi 1958790272 350 EERHGNIEERMRHLEGQLEEKNQELQRARQ 379
Cdd:COG4913 397 EEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
1024-1095 |
5.70e-07 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 48.06 E-value: 5.70e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958790272 1024 VLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDEnfdysSLALLLQIPTQNTQARQILEREYNNLLA 1095
Cdd:smart00454 1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLT-----SEEDLKELGITKLGHRKKILKAIQKLKE 67
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
118-453 |
7.38e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 53.80 E-value: 7.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 118 RERLRVSLERVSALEEELAAANQEIVALREQNVHIQR---KMVSSEGSTE------SEHLDGMEPGQKVHEKrlsngsID 188
Cdd:COG3096 277 ANERRELSERALELRRELFGARRQLAEEQYRLVEMAReleELSARESDLEqdyqaaSDHLNLVQTALRQQEK------IE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 189 STDDtsQIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLikteemnTKYQRDIREAMAQKEDMEERITT 268
Cdd:COG3096 351 RYQE--DLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQL-------ADYQQALDVQQTRAIQYQQAVQA 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 269 LEKrylsaQRESTSIHDMN-DKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETL----PEVEAELA-QR 342
Cdd:COG3096 422 LEK-----ARALCGLPDLTpENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVckiaGEVERSQAwQT 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 343 IAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDrllteSNERLQLHLKERMAALEEknv 422
Cdd:COG3096 497 ARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLD-----AAEELEELLAELEAQLEE--- 568
|
330 340 350
....*....|....*....|....*....|.
gi 1958790272 423 LIQESETFRKNLEESLHDKERLAEEIEKLRS 453
Cdd:COG3096 569 LEEQAAEAVEQRSELRQQLEQLRARIKELAA 599
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
27-530 |
8.17e-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: 53.69 E-value: 8.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 27 QEFAALTKELNacrEQLLEKEEEISELKAERNNTRLLL--------EHLECLVSRHERSLRMTVVKR---QAQSPSgVSS 95
Cdd:pfam12128 279 EERQETSAELN---QLLRTLDDQWKEKRDELNGELSAAdaavakdrSELEALEDQHGAFLDADIETAaadQEQLPS-WQS 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 96 EVEVL-KALKSLFEHHKALDEKV-RERLRVSLE---RVSALEEELAAANQEIVALREqnvhiqrkmvssegsTESEHLDG 170
Cdd:pfam12128 355 ELENLeERLKALTGKHQDVTAKYnRRRSKIKEQnnrDIAGIKDKLAKIREARDRQLA---------------VAEDDLQA 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 171 ME-PGQKVHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEmAQMKDRLAALSSRVGEVEQEAETARKDLikteemnTKYQ 249
Cdd:pfam12128 420 LEsELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATAT-PELLLQLENFDERIERAREEQEAANAEV-------ERLQ 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 250 RDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMND----KLENELANKEAILRQMEEK--NRQLQERLELAEQKLQ 323
Cdd:pfam12128 492 SELRQARKRRDQASEALRQASRRLEERQSALDELELQLFpqagTLLHFLRKEAPDWEQSIGKviSPELLHRTDLDPEVWD 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 324 QTMRKAETL-------------------PEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMN 384
Cdd:pfam12128 572 GSVGGELNLygvkldlkridvpewaaseEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNA 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 385 EEHNKRLSDTVDRL---LTESNERLQLHLKERMAALE-EKNVLIQESETF-----RKNLEESLHDKERLAEEIEKLRSEL 455
Cdd:pfam12128 652 RLDLRRLFDEKQSEkdkKNKALAERKDSANERLNSLEaQLKQLDKKHQAWleeqkEQKREARTEKQAYWQVVEGALDAQL 731
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958790272 456 DQMKmrTGSLIEPTISRTHLDTSAELRY-SVGSL-VDSQSDYRTTKVIRRPRRGRMGVRRDEPKVKSLgdHEWNRTQ 530
Cdd:pfam12128 732 ALLK--AAIAARRSGAKAELKALETWYKrDLASLgVDPDVIAKLKREIRTLERKIERIAVRRQEVLRY--FDWYQET 804
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
188-462 |
8.91e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 53.26 E-value: 8.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 188 DSTDDTSQIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIR-------EAMAQKE 260
Cdd:pfam01576 216 ESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLEseraarnKAEKQRR 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 261 DMEERI------------TTLEKRYLSAQREsTSIHDMNDKLENELANKEAILRQMEEKNRQ----LQERLELAEQKLQQ 324
Cdd:pfam01576 296 DLGEELealkteledtldTTAAQQELRSKRE-QEVTELKKALEEETRSHEAQLQEMRQKHTQaleeLTEQLEQAKRNKAN 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 325 TMRKAETLPEVEAELAQRIAALTKAEerhGNIEERMRHLEGQLEEKNQELQRA-RQREKMNEEHNK-------------- 389
Cdd:pfam01576 375 LEKAKQALESENAELQAELRTLQQAK---QDSEHKRKKLEGQLQELQARLSESeRQRAELAEKLSKlqselesvssllne 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 390 ------RLSDTVDRL---LTESNERLQ------LHLKERMAALEEknvliqESETFRKNLEESLHDKERLAEEIEKLRSE 454
Cdd:pfam01576 452 aegkniKLSKDVSSLesqLQDTQELLQeetrqkLNLSTRLRQLED------ERNSLQEQLEEEEEAKRNVERQLSTLQAQ 525
|
....*...
gi 1958790272 455 LDQMKMRT 462
Cdd:pfam01576 526 LSDMKKKL 533
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
27-467 |
1.07e-06 |
|
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: 53.14 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 27 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQA--QSPSGVSSEVEVLKA-- 102
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANleRQLEELEAQLEELESkl 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 103 -------------LKSLFEHHKALDEKV---RERLRVSLERVSALEEELAAANQEIVALREQ----NVHIQR---KMVSS 159
Cdd:TIGR02168 333 delaeelaeleekLEELKEELESLEAELeelEAELEELESRLEELEEQLETLRSKVAQLELQiaslNNEIERleaRLERL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 160 EGSTESEHLDGMEPGQKVHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLI 239
Cdd:TIGR02168 413 EDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 240 KTEEM---NTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIH-----DMNDKL-ENELANKEAI--LRQMEE-- 306
Cdd:TIGR02168 493 SLERLqenLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEaalggRLQAVVvENLNAAKKAIafLKQNELgr 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 307 ---------KNRQLQERLELAEQKLQQTMRKAETLPEVEAEL-------------------AQRIAALTKAEER------ 352
Cdd:TIGR02168 573 vtflpldsiKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLrkalsyllggvlvvddldnALELAKKLRPGYRivtldg 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 353 -----HG---------------------NIEERMRHLEGQLEEKNQELQRAR-QREKMNEEHNK--RLSDTVDRLLTESN 403
Cdd:TIGR02168 653 dlvrpGGvitggsaktnssilerrreieELEEKIEELEEKIAELEKALAELRkELEELEEELEQlrKELEELSRQISALR 732
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958790272 404 ERLQLHLKERMAALE-------EKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSLIE 467
Cdd:TIGR02168 733 KDLARLEAEVEQLEEriaqlskELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE 803
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
293-450 |
1.19e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.47 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 293 ELANKEAIlRQMEEKNRQLQERLELAEQKLQQTMRKAETlpEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ 372
Cdd:PRK12704 34 KEAEEEAK-RILEEAKKEAEAIKKEALLEAKEEIHKLRN--EFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 373 ELQRARQREKMNEEHNKRLSDTVDRLLTESNERLqlhlkERMAAL---EEKNVLIQESEtfrknlEESLHDKERLAEEIE 449
Cdd:PRK12704 111 ELEKKEKELEQKQQELEKKEEELEELIEEQLQEL-----ERISGLtaeEAKEILLEKVE------EEARHEAAVLIKEIE 179
|
.
gi 1958790272 450 K 450
Cdd:PRK12704 180 E 180
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
170-459 |
1.27e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.21 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 170 GMEPGQKVHEKRLSNGSIdSTDDTSQIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQ 249
Cdd:COG4372 1 GDRLGEKVGKARLSLFGL-RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 250 RDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKA 329
Cdd:COG4372 80 EELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 330 ETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLH 409
Cdd:COG4372 160 ESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1958790272 410 LKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQMK 459
Cdd:COG4372 240 DALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALE 289
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
35-407 |
1.68e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.60 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 35 ELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHErSLRMtvvKRQAQSPSGVSSEVEVLKALKSLFEHHKALD 114
Cdd:PRK01156 333 VLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIE-SLKK---KIEEYSKNIERMSAFISEILKIQEIDPDAIK 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 115 eKVRERLRVSLERVSAleeELAAANQEIVALREQNVHIQRKMVSSEGST------------ESEHL--DGMEPGQKVHEK 180
Cdd:PRK01156 409 -KELNEINVKLQDISS---KVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgttlgeeKSNHIinHYNEKKSRLEEK 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 181 --RLSNGSIDSTDDTSQIVELQELLEKQNYEMA-----QMKDRLAALS------SRVGEVEQEAETARKDL--IKTEEMN 245
Cdd:PRK01156 485 irEIEIEVKDIDEKIVDLKKRKEYLESEEINKSineynKIESARADLEdikikiNELKDKHDKYEEIKNRYksLKLEDLD 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 246 TKYQrDIREAMAQKEDMEerITTLEKRYLSAQRESTSIHDMNDKLENELANKEA----ILRQMEEKNRQLQERLELAEQK 321
Cdd:PRK01156 565 SKRT-SWLNALAVISLID--IETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSyidkSIREIENEANNLNNKYNEIQEN 641
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 322 --LQQTMR-KAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVdrl 398
Cdd:PRK01156 642 kiLIEKLRgKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRI--- 718
|
....*....
gi 1958790272 399 lTESNERLQ 407
Cdd:PRK01156 719 -NDINETLE 726
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
131-361 |
1.70e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 131 LEEELAAANQEIVALREQNVHIQRKMVSSEgstesehldgmepgQKVHEKRLSNGSIDSTDDT----SQIVELQELLEKQ 206
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAE--------------AALEEFRQKNGLVDLSEEAklllQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 207 NYEMAQMKDRLAALSSRVGEVEQEAETARKDlikteEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQREstsIHDM 286
Cdd:COG3206 232 RAELAEAEARLAALRAQLGSGPDALPELLQS-----PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ---IAAL 303
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958790272 287 NDKLENELankEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMR 361
Cdd:COG3206 304 RAQLQQEA---QRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
27-348 |
1.72e-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: 52.38 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 27 QEFAALTKELNACREQLLEKEEEISELKAErnntrllLEHLECLVSRHERSLrmtvvkrqaqspSGVSSEVEVLKA--LK 104
Cdd:TIGR02169 730 QEEEKLKERLEELEEDLSSLEQEIENVKSE-------LKELEARIEELEEDL------------HKLEEALNDLEArlSH 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 105 SLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEhldgmepGQKVHEKRLsn 184
Cdd:TIGR02169 791 SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI-------EKEIENLNG-- 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 185 gsidstddtsQIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKdliKTEEMNTKYQRD---IREAMAQKED 261
Cdd:TIGR02169 862 ----------KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELER---KIEELEAQIEKKrkrLSELKAKLEA 928
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 262 MEERITTLEKRYLSAQRESTSIHDMnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQ 341
Cdd:TIGR02169 929 LEEELSEIEDPKGEDEEIPEEELSL-EDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILE 1007
|
....*..
gi 1958790272 342 RIAALTK 348
Cdd:TIGR02169 1008 RIEEYEK 1014
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
29-383 |
2.24e-06 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 51.61 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 29 FAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHER---SLRMTVVKRQAQSPS---GVSSEVEVLKA 102
Cdd:pfam19220 57 LAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAakeELRIELRDKTAQAEAlerQLAAETEQNRA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 103 LKslfEHHKALdekvRERLRVSLERVSALEEELAAAnQEIVALREQNVHIQRKMVSSEGSTESEHLDGMEPgqkvHEKRL 182
Cdd:pfam19220 137 LE---EENKAL----REEAQAAEKALQRAEGELATA-RERLALLEQENRRLQALSEEQAAELAELTRRLAE----LETQL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 183 SNGSIDSTDDTSQIVELQELLEK----QNYEMAQMKDRLAALSSRVgeveqEAETARkdLIKTEEMNTkyqrdirEAMAQ 258
Cdd:pfam19220 205 DATRARLRALEGQLAAEQAERERaeaqLEEAVEAHRAERASLRMKL-----EALTAR--AAATEQLLA-------EARNQ 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 259 KEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLElaeqklqqTMRKAetlpeveae 338
Cdd:pfam19220 271 LRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAE--------MLTKA--------- 333
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1958790272 339 LAQRIAALTKAEERHGNIEERMRHLEGQ-------LEEKNQELQRARQREKM 383
Cdd:pfam19220 334 LAAKDAALERAEERIASLSDRIAELTKRfeveraaLEQANRRLKEELQRERA 385
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
107-450 |
2.50e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 107 FEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSteseHLDGMEPGQKVHEKRLSNgS 186
Cdd:PTZ00121 1208 AEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMA----HFARRQAAIKAEEARKAD-E 1282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 187 IDSTDDTSQIVELQELLEKQNYEMAQMKdrlAALSSRVGEVEQEAETARKdliKTEEMNTKYQRDIREAMAQKEDMEERI 266
Cdd:PTZ00121 1283 LKKAEEKKKADEAKKAEEKKKADEAKKK---AEEAKKADEAKKKAEEAKK---KADAAKKKAEEAKKAAEAAKAEAEAAA 1356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 267 TTLEKRYLSAQRESTSIHDMNDKLEnELANKEAILRQMEEKNRQLQE---------RLELAEQKLQQTMRKAETLPEVEa 337
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKAD-AAKKKAEEKKKADEAKKKAEEdkkkadelkKAAAAKKKADEAKKKAEEKKKAD- 1434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 338 ELAQRIAALTKAEERHGNIEERMRHLEgqLEEKNQELQRARQREKMNEEhnKRLSDTVDRLLTESNERLQlhlkERMAAL 417
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKKKAEEAKKAEE--AKKKAEEAKKADEAKKKAEE--AKKADEAKKKAEEAKKKAD----EAKKAA 1506
|
330 340 350
....*....|....*....|....*....|...
gi 1958790272 418 EEKnvliQESETFRKNLEESLHDKERLAEEIEK 450
Cdd:PTZ00121 1507 EAK----KKADEAKKAEEAKKADEAKKAEEAKK 1535
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
250-461 |
2.56e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 250 RDIREAMaqkEDMEERITTLE------KRYLSAQRESTSIHDMNDKLEnelankeaiLRQMEEKNRQLQERLELAEQKLQ 323
Cdd:COG4913 238 ERAHEAL---EDAREQIELLEpirelaERYAAARERLAELEYLRAALR---------LWFAQRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 324 QTMRKAETLPEVEAELAQRIAALTKAEERHGNIEErmrhleGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESN 403
Cdd:COG4913 306 RLEAELERLEARLDALREELDELEAQIRGNGGDRL------EQLEREIERLERELEERERRRARLEALLAALGLPLPASA 379
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958790272 404 ERLQLHLKERMAALEEknvLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQMKMR 461
Cdd:COG4913 380 EEFAALRAEAAALLEA---LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
252-419 |
3.52e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.54 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 252 IREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAeqklqQTMRKAET 331
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-----RNNKEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 332 LpevEAELAQriaaltkAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLK 411
Cdd:COG1579 94 L---QKEIES-------LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
....*...
gi 1958790272 412 ERMAALEE 419
Cdd:COG1579 164 EREELAAK 171
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
251-437 |
3.64e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 251 DIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKA- 329
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALy 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 330 ---ETLPEVEA--------ELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL 398
Cdd:COG3883 97 rsgGSVSYLDVllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 1958790272 399 LTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEES 437
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
26-431 |
4.05e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 26 FQEFAALTKELNACR---EQLLEKEEEISELKAErnntrllLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKA 102
Cdd:COG4717 131 YQELEALEAELAELPerlEELEERLEELRELEEE-------LEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 103 LKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEHLDGMEPGQKVHEKRL 182
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVL 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 183 SNGSIDSTDDTSQIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDM 262
Cdd:COG4717 284 GLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 263 EERITTLEKRYLSAQRESTSIHDMNDKLEnELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKA--ETLPEVEAELA 340
Cdd:COG4717 364 QLEELEQEIAALLAEAGVEDEEELRAALE-QAEEYQELKEELEELEEQLEELLGELEELLEALDEEEleEELEELEEELE 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 341 QRIAALTKAEERHGNIEERMRHLE--GQLEEKNQELQRARQREKMNEEHNKRL---SDTVDRLLTESNERLQLHLKERMA 415
Cdd:COG4717 443 ELEEELEELREELAELEAELEQLEedGELAELLQELEELKAELRELAEEWAALklaLELLEEAREEYREERLPPVLERAS 522
|
410 420
....*....|....*....|...
gi 1958790272 416 AL-------EEKNVLIQESETFR 431
Cdd:COG4717 523 EYfsrltdgRYRLIRIDEDLSLK 545
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
25-418 |
4.45e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 51.27 E-value: 4.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 25 TFQEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKrQAQSPSGVSSEVEVLKALK 104
Cdd:pfam15921 459 SLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAE-ITKLRSRVDLKLQELQHLK 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 105 SLFEHhkaldekvrerLRVSLERVSALEEELAAANQEIVALREQnVHIQRKMVSSEGSTESE-HLDGMEPGQKVHEKRLS 183
Cdd:pfam15921 538 NEGDH-----------LRNVQTECEALKLQMAEKDKVIEILRQQ-IENMTQLVGQHGRTAGAmQVEKAQLEKEINDRRLE 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 184 NGSIDSTDDT--SQIVELQELLEKQNYEMAQM----KDRLAALSSRVGEVEQ---EAETARKDLIKTEEMNTKYQRDIRE 254
Cdd:pfam15921 606 LQEFKILKDKkdAKIRELEARVSDLELEKVKLvnagSERLRAVKDIKQERDQllnEVKTSRNELNSLSEDYEVLKRNFRN 685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 255 amaQKEDMEERITTLEKRYLSAQRE----STSIHDMNDKLENELANKEAILRQMEEKNRQ---LQERLELAEQKLQQTMR 327
Cdd:pfam15921 686 ---KSEEMETTTNKLKMQLKSAQSEleqtRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQidaLQSKIQFLEEAMTNANK 762
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 328 KAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMneehnkRLSDTVDRLLTESNERLQ 407
Cdd:pfam15921 763 EKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASL------QFAECQDIIQRQEQESVR 836
|
410
....*....|.
gi 1958790272 408 LHLKERMAALE 418
Cdd:pfam15921 837 LKLQHTLDVKE 847
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
45-420 |
6.46e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.49 E-value: 6.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 45 EKEEEISELKAERNNTRLLLEHLECLVSRHERSLR------------MTVVKRQAQSPSgvsSEVEVLKALKS-----LF 107
Cdd:pfam05483 332 EKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRteqqrleknedqLKIITMELQKKS---SELEEMTKFKNnkeveLE 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 108 EHHKALDEKvrERLRVSLERVSALEEELAAANQEIVAL---REQNVHIQRKMVSSEGSTESEHLDGMEPGQKVHEK-RLS 183
Cdd:pfam05483 409 ELKKILAED--EKLLDEKKQFEKIAEELKGKEQELIFLlqaREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKeKLK 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 184 NGSI----------------DSTDDTSQIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLI-------- 239
Cdd:pfam05483 487 NIELtahcdklllenkeltqEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIqkgdevkc 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 240 ---KTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMN---------------------DKLENELA 295
Cdd:pfam05483 567 kldKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENkalkkkgsaenkqlnayeikvNKLELELA 646
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 296 NKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETL--------PEVEAELAQRIAALTKAEERHGN-----IEERMRH 362
Cdd:pfam05483 647 SAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIadeavklqKEIDKRCQHKIAEMVALMEKHKHqydkiIEERDSE 726
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958790272 363 LeGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLL---TESNERLQLHLKERMAALEEK 420
Cdd:pfam05483 727 L-GLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLeieKEEKEKLKMEAKENTAILKDK 786
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
27-459 |
6.94e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 50.35 E-value: 6.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 27 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAqSPSGVSSEVEVLKALKSL 106
Cdd:TIGR00618 386 QQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAA-ITCTAQCEKLEKIHLQES 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 107 FEHHKALDEKV--RERLRVSLERVSALEEELAAANQEI-VALREQNVHIQRKMVSS-EGSTESEHLDGMEPGQKVHEKRL 182
Cdd:TIGR00618 465 AQSLKEREQQLqtKEQIHLQETRKKAVVLARLLELQEEpCPLCGSCIHPNPARQDIdNPGPLTRRMQRGEQTYAQLETSE 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 183 SNGSIDSTDDTSQIVELQEllekqnyEMAQMKDRLAALSSRVGEVEQEAETARK---DLIKTEEMNTKYQRDIREAM-AQ 258
Cdd:TIGR00618 545 EDVYHQLTSERKQRASLKE-------QMQEIQQSFSILTQCDNRSKEDIPNLQNitvRLQDLTEKLSEAEDMLACEQhAL 617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 259 KEDMEERITTLEKRYLS---AQRESTSIHDMNDKLENELANKEAI-LRQMEEKNRQLQERLELAEQKLQQtmrKAETLPE 334
Cdd:TIGR00618 618 LRKLQPEQDLQDVRLHLqqcSQELALKLTALHALQLTLTQERVREhALSIRVLPKELLASRQLALQKMQS---EKEQLTY 694
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 335 VEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRarQREKMNEEHNK--RLSDTVDRLLTESNERLQLHLKE 412
Cdd:TIGR00618 695 WKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAA--REDALNQSLKElmHQARTVLKARTEAHFNNNEEVTA 772
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1958790272 413 RMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQMK 459
Cdd:TIGR00618 773 ALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDIL 819
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
112-455 |
7.01e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.61 E-value: 7.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 112 ALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEHLD-GMEPGQKVHEKRLSNGSIDST 190
Cdd:pfam12128 597 ASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDlRRLFDEKQSEKDKKNKALAER 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 191 DDTSQI------VELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARK---DLIKTEEMNTKYQRDiREAMAQKED 261
Cdd:pfam12128 677 KDSANErlnsleAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDaqlALLKAAIAARRSGAK-AELKALETW 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 262 MEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQmeekNRQLQERLELAEQKLQQTMRKAET-LPEVEAELA 340
Cdd:pfam12128 756 YKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRY----FDWYQETWLQRRPRLATQLSNIERaISELQQQLA 831
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 341 QRIAaltKAEERHGNIEERMRHLEGQLEEKNQELQRARQR-EKMNEEHnkrlsdtvdrlLTESNERLQLHLKERMAALEE 419
Cdd:pfam12128 832 RLIA---DTKLRRAKLEMERKASEKQQVRLSENLRGLRCEmSKLATLK-----------EDANSEQAQGSIGERLAQLED 897
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1958790272 420 -KNVLIQESETFRKNLEE-----SLHDKERLAEEIEKLRSEL 455
Cdd:pfam12128 898 lKLKRDYLSESVKKYVEHfknviADHSGSGLAETWESLREED 939
|
|
| SAM_superfamily |
cd09487 |
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
946-997 |
7.02e-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: 44.54 E-value: 7.02e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1958790272 946 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGI 997
Cdd:cd09487 4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
84-459 |
9.03e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 9.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 84 KRQAQSPSGVSSEVEVL-KALKSLFEHHKALDEKVRERLRVSlERVSALEEELAAANQEIVALREQnvhIQRKMVSSEGS 162
Cdd:COG4717 60 KPQGRKPELNLKELKELeEELKEAEEKEEEYAELQEELEELE-EELEELEAELEELREELEKLEKL---LQLLPLYQELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 163 TESEHLDGMEPGQKVHEKRLSngsidstddtsQIVELQELLEKQNYEMAQMKDRLAALSSRVG-EVEQEAETARKDLIKT 241
Cdd:COG4717 136 ALEAELAELPERLEELEERLE-----------ELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 242 EEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQREST---------------SIHDMNDKLENELANKEAIL----- 301
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlkearlllliaaallALLGLGGSLLSLILTIAGVLflvlg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 302 ----------RQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKN 371
Cdd:COG4717 285 llallflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 372 QELQRARQREKMNE-------------EHNKRLSDTVDRLlTESNERLQLHLKERMAALE--EKNVLIQESETFRKNLEE 436
Cdd:COG4717 365 LEELEQEIAALLAEagvedeeelraalEQAEEYQELKEEL-EELEEQLEELLGELEELLEalDEEELEEELEELEEELEE 443
|
410 420
....*....|....*....|...
gi 1958790272 437 SLHDKERLAEEIEKLRSELDQMK 459
Cdd:COG4717 444 LEEELEELREELAELEAELEQLE 466
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
304-457 |
1.27e-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: 48.00 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 304 MEEKNRQLqERLELAEQKLQQTMRKAETLP----EVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQ 379
Cdd:COG1579 2 MPEDLRAL-LDLQELDSELDRLEHRLKELPaelaELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 380 R--------------------EKMNEEHNKRLSDTVDRLltESNERLQLHLKERMAALEEKnvLIQESETFRKNLEESLH 439
Cdd:COG1579 81 QlgnvrnnkeyealqkeieslKRRISDLEDEILELMERI--EELEEELAELEAELAELEAE--LEEKKAELDEELAELEA 156
|
170
....*....|....*...
gi 1958790272 440 DKERLAEEIEKLRSELDQ 457
Cdd:COG1579 157 ELEELEAEREELAAKIPP 174
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
27-374 |
1.30e-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: 49.44 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 27 QEFAALTKELNACREQLLEKEEEISELKAERNNtrlLLEHLEclvsrhERSLRMTVVKRQAQSPSGVSSEVEVlkALKSL 106
Cdd:pfam10174 373 EEKSTLAGEIRDLKDMLDVKERKINVLQKKIEN---LQEQLR------DKDKQLAGLKERVKSLQTDSSNTDT--ALTTL 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 107 FEhhkALDEKVR--ERLRVSLERVS-ALEEELAAANQEIVALREQNVHIQRKMVSSEGSTES--EHLDGMEPGQKVHEKR 181
Cdd:pfam10174 442 EE---ALSEKERiiERLKEQREREDrERLEELESLKKENKDLKEKVSALQPELTEKESSLIDlkEHASSLASSGLKKDSK 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 182 LSNGSIDSTDDTSQIVELQELLEK-QNYEMAQMKDrlAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKE 260
Cdd:pfam10174 519 LKSLEIAVEQKKEECSKLENQLKKaHNAEEAVRTN--PEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKN 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 261 DMEERITTLEKRYLSaQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELA 340
Cdd:pfam10174 597 DKDKKIAELESLTLR-QMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQELDATK 675
|
330 340 350
....*....|....*....|....*....|....*....
gi 1958790272 341 QRIAALTKA-EERHGNIE----ERMRHLEGQLEEKNQEL 374
Cdd:pfam10174 676 ARLSSTQQSlAEKDGHLTnlraERRKQLEEILEMKQEAL 714
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
191-455 |
1.40e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.58 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 191 DDTSQIVELQELLEKQNYEMAQMKDRLAALSSRVGEVE----QEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERI 266
Cdd:pfam02463 159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKlqelKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 267 TTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAA- 345
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKe 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 346 ----LTKAEERHGNIEERMRHLEGQLEEKN---QELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALE 418
Cdd:pfam02463 319 sekeKKKAEKELKKEKEEIEELEKELKELEikrEAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
|
250 260 270
....*....|....*....|....*....|....*..
gi 1958790272 419 EKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSEL 455
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEE 435
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
218-458 |
1.75e-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: 48.97 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 218 AALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRylsaqrestsihdmndkleneLANK 297
Cdd:pfam05557 9 ARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKR---------------------EAEA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 298 EAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHgnieermrhlEGQLEEKNQELQRA 377
Cdd:pfam05557 68 EEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRA----------ELELQSTNSELEEL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 378 RQR-----------EKMNEEHNKRLSdtvdrLLTESNERLQ----------------LHLKERMAALEEKNVLIQESETF 430
Cdd:pfam05557 138 QERldllkakaseaEQLRQNLEKQQS-----SLAEAEQRIKelefeiqsqeqdseivKNSKSELARIPELEKELERLREH 212
|
250 260
....*....|....*....|....*...
gi 1958790272 431 RKNLEESLHDKERLAEEIEKLRSELDQM 458
Cdd:pfam05557 213 NKHLNENIENKLLLKEEVEDLKRKLERE 240
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
227-461 |
1.92e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 48.38 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 227 VEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEErittleKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEE 306
Cdd:pfam13868 107 VERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKE------LEKEEEREEDERILEYLKEKAEREEEREAEREEIEE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 307 KNRQLQERLElaeQKLQQTMRKAETLPEVEAELAQ-------RIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQ 379
Cdd:pfam13868 181 EKEREIARLR---AQQEKAQDEKAERDELRAKLYQeeqerkeRQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAE 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 380 REKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEknvLIQESE-TFRKNLEESLHDKERLAEEIEKLRSELDQM 458
Cdd:pfam13868 258 REEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEK---QIEEREeQRAAEREEELEEGERLREEEAERRERIEEE 334
|
...
gi 1958790272 459 KMR 461
Cdd:pfam13868 335 RQK 337
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
281-391 |
2.52e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.67 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 281 TSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAEL---AQRIA--ALTKAEERHGN 355
Cdd:PRK00409 509 KLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLleeAEKEAqqAIKEAKKEADE 588
|
90 100 110
....*....|....*....|....*....|....*....
gi 1958790272 356 IEERMRHLE--GQLEEKNQELQRARQR-EKMNEEHNKRL 391
Cdd:PRK00409 589 IIKELRQLQkgGYASVKAHELIEARKRlNKANEKKEKKK 627
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
111-467 |
2.88e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 111 KALDEKVRErLRVSLERVSALEEELAAANQEIVALREQNVHIQRKM-----------VSSEGSTESEHLDGMEPGQKVHE 179
Cdd:COG4717 74 KELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELeklekllqllpLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 180 KRLsngsidstddtSQIVELQELLEKQNYEMAQMKDRLAALSSRVG-EVEQEAETARKDLIKTEEMNTKYQRDIREAMAQ 258
Cdd:COG4717 153 ERL-----------EELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 259 KEDMEERITTLEKRYLSAQREST---------------SIHDMNDKLENELANKEAIL---------------RQMEEKN 308
Cdd:COG4717 222 LEELEEELEQLENELEAAALEERlkearlllliaaallALLGLGGSLLSLILTIAGVLflvlgllallflllaREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 309 RQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRhlegQLEEKNQELQRARQREKMNEEHN 388
Cdd:COG4717 302 KEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLR----EAEELEEELQLEELEQEIAALLA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 389 KRLSDTVDRLltesnERLQLHLKERMAALEEKNVLIQESETFRKNLEESL--HDKERLAEEIEKLRSELDQMKMRTGSLI 466
Cdd:COG4717 378 EAGVEDEEEL-----RAALEQAEEYQELKEELEELEEQLEELLGELEELLeaLDEEELEEELEELEEELEELEEELEELR 452
|
.
gi 1958790272 467 E 467
Cdd:COG4717 453 E 453
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
291-457 |
2.97e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 291 ENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlpEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEK 370
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN---ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 371 NQELQRARQREKMNEE--HNKRLSDTVDRL-----LTESNERLQLHLKERMAALEEKnvliqesetfRKNLEESLHDKER 443
Cdd:COG3883 92 ARALYRSGGSVSYLDVllGSESFSDFLDRLsalskIADADADLLEELKADKAELEAK----------KAELEAKLAELEA 161
|
170
....*....|....
gi 1958790272 444 LAEEIEKLRSELDQ 457
Cdd:COG3883 162 LKAELEAAKAELEA 175
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
198-380 |
3.44e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 47.76 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 198 ELQELLEKQNyEMAQMKDRL-------AALSSRVGEVEQ-EAEtaRKDLIKTEEMNTKYQRdIREAMAQKED-MEERITT 268
Cdd:COG0497 173 ELEELRADEA-ERARELDLLrfqleelEAAALQPGEEEElEEE--RRRLSNAEKLREALQE-ALEALSGGEGgALDLLGQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 269 LEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQ---ERLELAEQKLQ---QTMRK----AETLPEVEAE 338
Cdd:COG0497 249 ALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEfdpERLEEVEERLAllrRLARKygvtVEELLAYAEE 328
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1958790272 339 LAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQR 380
Cdd:COG0497 329 LRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKK 370
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
28-309 |
4.33e-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: 47.76 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 28 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRhERSLRMTVVKRQAQSpsgVSSEVEVLK-ALKSL 106
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKD-LGEEEQLRVKEKIGE---LEAEIASLErSIAEK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 107 FEHHKALDEKVR---ERLRVSLERVSALEEELAAANQEIVALRE--QNVHIQRKMVSSEGSTESEHLDGMEPGQKVHEKR 181
Cdd:TIGR02169 314 ERELEDAEERLAkleAEIDKLLAEIEELEREIEEERKRRDKLTEeyAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 182 LSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKED 261
Cdd:TIGR02169 394 LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD 473
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1958790272 262 MEERITTLEKRYLSAQREstsihdmndkleneLANKEAILRQMEEKNR 309
Cdd:TIGR02169 474 LKEEYDRVEKELSKLQRE--------------LAEAEAQARASEERVR 507
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
24-455 |
4.40e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 24 YTFQEFAALTKELNACREQLLEKEEE----ISELKAERNNTRLLLEHLE-----CLVSRHErslrmtvvkrqaqspsgvs 94
Cdd:PRK03918 384 LTPEKLEKELEELEKAKEEIEEEISKitarIGELKKEIKELKKAIEELKkakgkCPVCGRE------------------- 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 95 sevevlkalksLFEHHKAldekvrERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMV-SSEGSTESEHLDgmep 173
Cdd:PRK03918 445 -----------LTEEHRK------ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkESELIKLKELAE---- 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 174 gqkvhekrlsngsidstddtsQIVELQELLEKQNYEMAQMKDRLA-ALSSRVGEVEQEAETARKDLIKTEEMNTKyqrdI 252
Cdd:PRK03918 504 ---------------------QLKELEEKLKKYNLEELEKKAEEYeKLKEKLIKLKGEIKSLKKELEKLEELKKK----L 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 253 REAMAQKEDMEERITTLEKRYLSAQREstSIHDMNDKLE---------NELANKEAILRQMEEKNRQLQERLELAEQKLQ 323
Cdd:PRK03918 559 AELEKKLDELEEELAELLKELEELGFE--SVEELEERLKelepfyneyLELKDAEKELEREEKELKKLEEELDKAFEELA 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 324 QTMRKAEtlpeveaELAQRIAALTK--AEERHGNIEERMRHLEGQLEEKNQELqrarqrekmneEHNKRLSDTVDRLLTE 401
Cdd:PRK03918 637 ETEKRLE-------ELRKELEELEKkySEEEYEELREEYLELSRELAGLRAEL-----------EELEKRREEIKKTLEK 698
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1958790272 402 snerlqlhLKERMAALEEKnvlIQESEtfrkNLEESLHDKERLAEEIEKLRSEL 455
Cdd:PRK03918 699 --------LKEELEEREKA---KKELE----KLEKALERVEELREKVKKYKALL 737
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
107-454 |
4.91e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 107 FEHHKALDEKVRERLRVSLERVSALEEELAAANQeivALREQNVHIQRKMVSSEGSTESEHLDGMEPGQKVHEKRLSNGS 186
Cdd:PTZ00121 1093 TEEAFGKAEEAKKTETGKAEEARKAEEAKKKAED---ARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEA 1169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 187 iDSTDDTSQIVELQELLE-KQNYEMAQMKDRLAALSSRVGEVEQEAETARK--DLIKTEEMNTKYQRDIREAMAQKEDmE 263
Cdd:PTZ00121 1170 -RKAEDAKKAEAARKAEEvRKAEELRKAEDARKAEAARKAEEERKAEEARKaeDAKKAEAVKKAEEAKKDAEEAKKAE-E 1247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 264 ERITTLEKRYLSAQRESTSIHDMNDKLENelANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRI 343
Cdd:PTZ00121 1248 ERNNEEIRKFEEARMAHFARRQAAIKAEE--ARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAE 1325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 344 AALTKAEERHGNIEERMRHLE---GQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNE-RLQLHLKERMAALEE 419
Cdd:PTZ00121 1326 EAKKKADAAKKKAEEAKKAAEaakAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkKKADEAKKKAEEDKK 1405
|
330 340 350
....*....|....*....|....*....|....*..
gi 1958790272 420 KNVLIQESETFRKNLEESLHDKE--RLAEEIEKLRSE 454
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKKAEekKKADEAKKKAEE 1442
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
124-328 |
6.04e-05 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 45.28 E-value: 6.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 124 SLERVSALEEELAAANQEIVALREQNVHIQRKmvssegstesehldgmepgQKVHEKRLSNgsIDSTDDtsqivELQELL 203
Cdd:pfam15619 9 RLHKIKELQNELAELQSKLEELRKENRLLKRL-------------------QKRQEKALGK--YEGTES-----ELPQLI 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 204 EKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREA-MAQKEDMEERITTLEKRYLSAQREsts 282
Cdd:pfam15619 63 ARHNEEVRVLRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKnLAEREELQKKLEQLEAKLEDKDEK--- 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958790272 283 IHDMNDKLEN-------ELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK 328
Cdd:pfam15619 140 IQDLERKLELenksfrrQLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKERE 192
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
199-461 |
6.49e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.81 E-value: 6.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 199 LQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLiktEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQR 278
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQW---ERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 279 ESTSIHdmndklenelANKEAILRQMEEKNRQLQErLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEE-RHGNIE 357
Cdd:pfam07888 109 SSEELS----------EEKDALLAQRAAHEARIRE-LEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEaERKQLQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 358 ERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLH--LKERMAALEEK-NVLIQESETFR 431
Cdd:pfam07888 178 AKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLtqkLTTAHRKEAENeaLLEELRSLQERlNASERKVEGLG 257
|
250 260 270
....*....|....*....|....*....|
gi 1958790272 432 KNLEESLHDKERLAEEIEKLRSELDQMKMR 461
Cdd:pfam07888 258 EELSSMAAQRDRTQAELHQARLQAAQLTLQ 287
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
309-506 |
6.53e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 47.01 E-value: 6.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 309 RQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERmrhlegqlEEKNQELQRARQREKMNEEHN 388
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRER--------EELQREEERLVQKEEQLDARA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 389 KRLSDTVDRLLTESN----ERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHD--KERLAEEIEKLRSELD-QMKMR 461
Cdd:PRK12705 98 EKLDNLENQLEEREKalsaRELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAelEEEKAQRVKKIEEEADlEAERK 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1958790272 462 TGSLIEPTISRTHLDTSAELRYSVgslVDSQSDYRTTKVIRRPRR 506
Cdd:PRK12705 178 AQNILAQAMQRIASETASDLSVSV---VPIPSDAMKGRIIGREGR 219
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
115-352 |
9.99e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 9.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 115 EKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEgstesEHLDGMEPGQKVHEKRLSngsidstDDTS 194
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA-----RRIRALEQELAALEAELA-------ELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 195 QIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRyL 274
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE-L 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958790272 275 SAQREstsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEER 352
Cdd:COG4942 170 EAERA---------ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
198-426 |
1.03e-04 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 45.48 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 198 ELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKryLSAQ 277
Cdd:pfam06008 27 QLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKE--INEK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 278 RESTSIHDM---NDKLENELANKEAILRQMeeKNRQLQERLELAEQKLqqtmRKAETLPEVEAELAQRIAALTKAeerhg 354
Cdd:pfam06008 105 VATLGENDFalpSSDLSRMLAEAQRMLGEI--RSRDFGTQLQNAEAEL----KAAQDLLSRIQTWFQSPQEENKA----- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 355 nIEERMRHLEGQLEEKNQELQ--------RARQREKMNEEHNKRLSDTVDRLLT--ESNERLQLHLKERMAALEEKNVLI 424
Cdd:pfam06008 174 -LANALRDSLAEYEAKLSDLRellreaaaKTRDANRLNLANQANLREFQRKKEEvsEQKNQLEETLKTARDSLDAANLLL 252
|
..
gi 1958790272 425 QE 426
Cdd:pfam06008 253 QE 254
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
822-886 |
1.09e-04 |
|
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.
Pssm-ID: 425739 Cd Length: 64 Bit Score: 41.49 E-value: 1.09e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958790272 822 QWDGPTVVAWLElWLGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQEM 886
Cdd:pfam00536 2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
195-464 |
1.15e-04 |
|
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: 46.35 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 195 QIVELQELLEKQNYEMAQMKDRLAALssrvgevEQEAETARKDLIKTEEmntkyqrdireAMAQKEDMEERITtlEKRYL 274
Cdd:pfam10174 402 KIENLQEQLRDKDKQLAGLKERVKSL-------QTDSSNTDTALTTLEE-----------ALSEKERIIERLK--EQRER 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 275 SAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERH- 353
Cdd:pfam10174 462 EDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLk 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 354 ------------GNIEERMRHLEGQLEEKNQELQRARQ---------REKMNEEHNK--RLSDTVDRLLTESNERLQLHL 410
Cdd:pfam10174 542 kahnaeeavrtnPEINDRIRLLEQEVARYKEESGKAQAeverllgilREVENEKNDKdkKIAELESLTLRQMKEQNKKVA 621
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958790272 411 KERMAALEEKNVLIQESETFRKNLEESLHDK-----ERLAEEIEKLRSELDQMKMRTGS 464
Cdd:pfam10174 622 NIKHGQQEMKKKGAQLLEEARRREDNLADNSqqlqlEELMGALEKTRQELDATKARLSS 680
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
1024-1094 |
1.28e-04 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 41.10 E-value: 1.28e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958790272 1024 VLVWSNDRVIRWIQAIGLREYANNILESGVHG--SLIALDENFdysslalLLQIPTQNTQARQILEREYNNLL 1094
Cdd:pfam07647 1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGaeLLLRLTLED-------LKRLGITSVGHRRKILKKIQELK 66
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
105-391 |
1.31e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 105 SLFEHHKALDEKVR--ERLRVSLERVSALEEELAAA---NQEIVALREQNVHIQRKMVSSEGSTE--SEHLDGMEPGQKV 177
Cdd:PRK04863 797 ELAERYATLSFDVQklQRLHQAFSRFIGSHLAVAFEadpEAELRQLNRRRVELERALADHESQEQqqRSQLEQAKEGLSA 876
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 178 HEKRLsnGSIDSTDDTSQIVELQELLEkQNYEMAQMKDRLAALSSRVGEVEQEAETARKDliktEEMNTKYQRDIREAMA 257
Cdd:PRK04863 877 LNRLL--PRLNLLADETLADRVEEIRE-QLDEAEEAKRFVQQHGNALAQLEPIVSVLQSD----PEQFEQLKQDYQQAQQ 949
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 258 QKEDMEERITTL----EKR----YLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKA 329
Cdd:PRK04863 950 TQRDAKQQAFALtevvQRRahfsYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSY 1029
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958790272 330 ETLPEVEAELAQRIAALT-----KAEERhgnIEERMRHLEGQL----EEKNQ-ELQRARQREKMNEEhNKRL 391
Cdd:PRK04863 1030 DAKRQMLQELKQELQDLGvpadsGAEER---ARARRDELHARLsanrSRRNQlEKQLTFCEAEMDNL-TKKL 1097
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
30-316 |
1.37e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 30 AALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgVSSEVE-------VLKA 102
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAE---LEAELErldassdDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 103 LKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQnvhiQRKMVSSEGSTESEHLDGMepgqkvhekrl 182
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR----LEAAEDLARLELRALLEER----------- 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 183 sngsidstddtsqiveLQELLEKQNYemaqmKDRLAALSSRVGEVEQEAETARKDLIKT-EEMNTKYQRDIREAMAQKED 261
Cdd:COG4913 755 ----------------FAAALGDAVE-----RELRENLEERIDALRARLNRAEEELERAmRAFNREWPAETADLDADLES 813
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958790272 262 MEE---RITTLEKRYLSAQREstsihDMNDKL-ENELANKEAILRQMEEKNRQLQERLE 316
Cdd:COG4913 814 LPEylaLLDRLEEDGLPEYEE-----RFKELLnENSIEFVADLLSKLRRAIREIKERID 867
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
116-459 |
1.44e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 46.00 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 116 KVRERLRVSLERVSALEEELAAANQEIVALREQNvHIQRKMVssegstesEHLDGM--EPGQKVHEKRLSNG-SIDSTDD 192
Cdd:pfam06160 83 KAKKALDEIEELLDDIEEDIKQILEELDELLESE-EKNREEV--------EELKDKyrELRKTLLANRFSYGpAIDELEK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 193 T-----SQIVELQELLEKQNYEMA-----QMKDRLAALSSRVGEVEQEAETARKDLikTEEMNtkyqrDIREAMAQkedM 262
Cdd:pfam06160 154 QlaeieEEFSQFEELTESGDYLEArevleKLEEETDALEELMEDIPPLYEELKTEL--PDQLE-----ELKEGYRE---M 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 263 EERITTLEkrYLSAQRESTSIHDMNDKLENELANKEaiLRQMEEKNRQLQERLElaeqKLQQTMRKaetlpEVEAELaqr 342
Cdd:pfam06160 224 EEEGYALE--HLNVDKEIQQLEEQLEENLALLENLE--LDEAEEALEEIEERID----QLYDLLEK-----EVDAKK--- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 343 iaaltKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEH-------NKRLsDTVDRLLTESNERLQLH------ 409
Cdd:pfam06160 288 -----YVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYTLNENElervrglEKQL-EELEKRYDEIVERLEEKevayse 361
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1958790272 410 LKERMAALEEKNVLIQES-ETFRKNLeESLHDKERLA-EEIEKLRSELDQMK 459
Cdd:pfam06160 362 LQEELEEILEQLEEIEEEqEEFKESL-QSLRKDELEArEKLDEFKLELREIK 412
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
344-467 |
1.59e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.00 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 344 AALTKAEERHGNIEErmrhlegqlEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTEsNERLQLHLKERMAALEEknvL 423
Cdd:COG2433 380 EALEELIEKELPEEE---------PEAEREKEHEERELTEEEEEIRRLEEQVERLEAE-VEELEAELEEKDERIER---L 446
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1958790272 424 IQESETFRKNLEESLH-DKE--RLAEEIEKLRSELDQMKMRTGSLIE 467
Cdd:COG2433 447 ERELSEARSEERREIRkDREisRLDREIERLERELEEERERIEELKR 493
|
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
119-534 |
2.16e-04 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 45.50 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 119 ERLRVSLERVsalEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEHLDGMEPGQKVHEK--RLSNGSID----STDD 192
Cdd:COG5192 363 EKMKMQLQEI---EQDPGVDGVGLQLFSNSDAIDTVDRESSEIDNVGRKTRRQPTGKAIAEEtsREDELSFDdsdvSTSD 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 193 TSQIVELQELLEKQNYEMAQMKDRLAALSSRVGEvEQEAETARKDLIKTEEMNTkyQRDIREAMAQKEDMEERITTlEKR 272
Cdd:COG5192 440 ENEDVDFTGKKGAINNEDESDNEEVAFDSDSQFD-ESEGNLRWKEGLASKLAYS--QSGKRGRNIQKIFYDESLSP-EEC 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 273 YLSAQRESTSIHDMNDKLENElanKEAILRQMEEKNRQLQERLE-LAEQKLQQTMRKAETLPEVEAELAQriAALTKAEE 351
Cdd:COG5192 516 IEEYKGESAKSSESDLVVQDE---PEDFFDVSKVANESISSNHEkLMESEFEELKKKWSSLAQLKSRFQK--DATLDSIE 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 352 RHgniEErmrhLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEK---NVLIQESE 428
Cdd:COG5192 591 GE---EE----LIQDDEKGNFEDLEDEENSSDNEMEESRGSSVTAENEESADEVDYETEREENARKKEElrgNFELEERG 663
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 429 TFRKN-LEESLHDKERLAEEIEKLRSELDQM---------KMRTGSLIEPTISRTHLDTSAELRYS----VGSLVDSQSD 494
Cdd:COG5192 664 DPEKKdVDWYTEEKRKIEEQLKINRSEFETMvpesrvvieGYRAGRYVRIVLSHVPLEFVDEFNSRypivLGGLLPAEKE 743
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1958790272 495 YRTTKV-IRRPRRGRMGVRRDEPKVKSLGdheWNRTQQIGV 534
Cdd:COG5192 744 MGIVQGrIKRHRWHKKILKTNDPLIFSVG---WRRFQSIPV 781
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
259-465 |
2.18e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 259 KEDMEERITTLEKRYLSAQRESTSIHDmndkLENELANKEAILRQmEEKNRQLQERLELAEQKLQQTMRKAETLPEVEA- 337
Cdd:PRK11281 38 EADVQAQLDALNKQKLLEAEDKLVQQD----LEQTLALLDKIDRQ-KEETEQLKQQLAQAPAKLRQAQAELEALKDDNDe 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 338 ELAQRIAALTkaeerhgnieerMRHLEGQLEEKNQELQRARqrekmneehnKRLSDTVDRLLTESN--ERLQlhlkermA 415
Cdd:PRK11281 113 ETRETLSTLS------------LRQLESRLAQTLDQLQNAQ----------NDLAEYNSQLVSLQTqpERAQ-------A 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958790272 416 ALEEKNVLIQESETFRKNLEESlhDKERLAEEIEKLRSELD----QMKMRTGSL 465
Cdd:PRK11281 164 ALYANSQRLQQIRNLLKGGKVG--GKALRPSQRVLLQAEQAllnaQNDLQRKSL 215
|
|
| pepcterm_ChnLen |
TIGR03007 |
polysaccharide chain length determinant protein, PEP-CTERM locus subfamily; Members of this ... |
126-341 |
2.35e-04 |
|
polysaccharide chain length determinant protein, PEP-CTERM locus subfamily; Members of this protein family belong to the family of polysaccharide chain length determinant proteins (pfam02706). All are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria, and are found near the epsH homolog that is the putative exosortase gene. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 274386 [Multi-domain] Cd Length: 498 Bit Score: 45.04 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 126 ERVSALEEELAAANQEIVALREQNVhiqrkmvssegstesehldGMEPGQkvhekrlsngsidSTDDTSQIVELQELLEK 205
Cdd:TIGR03007 168 EQIKTYEKKLEAAENRLKAFKQENG-------------------GILPDQ-------------EGDYYSEISEAQEELEA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 206 QNYEMAQMKDRLAALSSRVGEVEQEAETARKDLI-----KTEEMNTKYQR----------DIREAMAQKEDMEERITTLE 270
Cdd:TIGR03007 216 ARLELNEAIAQRDALKRQLGGEEPVLLAGSSVANseldgRIEALEKQLDAlrlrytdkhpDVIATKREIAQLEEQKEEEG 295
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958790272 271 KRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLElaeqklqQTMRKAETLPEVEAELAQ 341
Cdd:TIGR03007 296 SAKNGGPERGEIANPVYQQLQIELAEAEAEIASLEARVAELTARIE-------RLESLLRTIPEVEAELTQ 359
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
216-462 |
2.79e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 44.84 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 216 RLAALSSRVGEVEQEAET-----ARKDLIKTEEMNTKYQRDIR-------EAMAQKEDMEERITTLEKRY------LSAQ 277
Cdd:pfam06160 61 SLPDIEELLFEAEELNDKyrfkkAKKALDEIEELLDDIEEDIKqileeldELLESEEKNREEVEELKDKYrelrktLLAN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 278 RES--TSIhdmnDKLENELANKEAILRQMEEKN--------RQLQERLELAEQKLQQTMRK--------AETLPEVEAEL 339
Cdd:pfam06160 141 RFSygPAI----DELEKQLAEIEEEFSQFEELTesgdyleaREVLEKLEEETDALEELMEDipplyeelKTELPDQLEEL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 340 AQRIAALTKAEER--HGNIEERMRHLEGQLEE-----KNQELQRArqrEKMNEEHNKRLSDTVDRLLTESNERLQLH--- 409
Cdd:pfam06160 217 KEGYREMEEEGYAleHLNVDKEIQQLEEQLEEnlallENLELDEA---EEALEEIEERIDQLYDLLEKEVDAKKYVEknl 293
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 410 --LKERMAALEEKNVLIQE-----SETFRKNlEESLHDKERLAEEIEKLRSELDQMKMRT 462
Cdd:pfam06160 294 peIEDYLEHAEEQNKELKEelervQQSYTLN-ENELERVRGLEKQLEELEKRYDEIVERL 352
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
217-452 |
2.86e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.83 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 217 LAALSSRVGEVEQEAET-----ARKDLIKTEEMNTKYQRD---IREAMA----QKEDMEERITTLEKRYLSAQRE----S 280
Cdd:PRK04778 81 LPDIEEQLFEAEELNDKfrfrkAKHEINEIESLLDLIEEDieqILEELQelleSEEKNREEVEQLKDLYRELRKSllanR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 281 TSIHDMNDKLENELANKEAILRQMEEKN-----RQLQERLELAEQKLQQTMRKAETLPEVEAELAQRI-AALTKAEE--- 351
Cdd:PRK04778 161 FSFGPALDELEKQLENLEEEFSQFVELTesgdyVEAREILDQLEEELAALEQIMEEIPELLKELQTELpDQLQELKAgyr 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 352 ---------RHGNIEERMRHLEGQLEEKNQELQR---ARQREKmNEEHNKRLSDTVDRLLTEsnerlqlhlkerMAAlee 419
Cdd:PRK04778 241 elveegyhlDHLDIEKEIQDLKEQIDENLALLEEldlDEAEEK-NEEIQERIDQLYDILERE------------VKA--- 304
|
250 260 270
....*....|....*....|....*....|...
gi 1958790272 420 KNVLIQESETFRKNLEESLHDKERLAEEIEKLR 452
Cdd:PRK04778 305 RKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVK 337
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
115-357 |
2.89e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 115 EKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEgstesehldgmepgqkvhekrlsngsidstddtS 194
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQ---------------------------------A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 195 QIVELQELLEKQNyemAQMKDRLAAL---SSRVGEVEQ--EAETARKDLIKTEEMNTKYQRD---IREAMAQKEDMEERI 266
Cdd:COG3883 73 EIAEAEAEIEERR---EELGERARALyrsGGSVSYLDVllGSESFSDFLDRLSALSKIADADadlLEELKADKAELEAKK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 267 TTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAAL 346
Cdd:COG3883 150 AELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
250
....*....|.
gi 1958790272 347 TKAEERHGNIE 357
Cdd:COG3883 230 AAAAAAAAAAA 240
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
30-299 |
3.01e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 30 AALTKELNACREQLLEKEEEISELKAERNNTRlllehleclvsrherslrmtvvkrqaqspsgvSSEVEVLKALKSLfeh 109
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALK--------------------------------KEEKALLKQLAAL--- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 110 hkaldekvRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTeSEHLDGMEPGQKVHEKRLsngsIDS 189
Cdd:COG4942 61 --------ERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL-AELLRALYRLGRQPPLAL----LLS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 190 TDDTSQIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDM----EER 265
Cdd:COG4942 128 PEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLlarlEKE 207
|
250 260 270
....*....|....*....|....*....|....
gi 1958790272 266 ITTLEKRYLSAQRESTSIHDMNDKLENELANKEA 299
Cdd:COG4942 208 LAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
206-436 |
3.07e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 206 QNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQR--DIREAMAQKEDMEERITTLEKRYLSAQREstsi 283
Cdd:COG3206 159 EAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQknGLVDLSEEAKLLLQQLSELESQLAEARAE---- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 284 hdmndklenelankeaiLRQMEEKNRQLQERLELAEQKLQQTMRkAETLPEVEAELAQRIAALTKAEERHGNIEERMRHL 363
Cdd:COG3206 235 -----------------LAEAEARLAALRAQLGSGPDALPELLQ-SPVIQQLRAQLAELEAELAELSARYTPNHPDVIAL 296
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958790272 364 EGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEE 436
Cdd:COG3206 297 RAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES 369
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
98-279 |
3.43e-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: 43.37 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 98 EVLKALKSLFEHHKALDEkVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEgstesEHLDGMEPGQKV 177
Cdd:COG1579 4 EDLRALLDLQELDSELDR-LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLE-----LEIEEVEARIKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 178 HEKRLsnGSIDSTDdtsqivELQELLEkqnyEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMA 257
Cdd:COG1579 78 YEEQL--GNVRNNK------EYEALQK----EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA 145
|
170 180
....*....|....*....|..
gi 1958790272 258 QKEDMEERITTLEKRyLSAQRE 279
Cdd:COG1579 146 ELDEELAELEAELEE-LEAERE 166
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
252-459 |
3.51e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 252 IREAMAQKEDMEERITTLEKRYlsaqresTSIHDMNDKLEnELANKEAILRQMEEKNRQLQE-RLELAEQKLQQTMRKAE 330
Cdd:COG4913 213 VREYMLEEPDTFEAADALVEHF-------DDLERAHEALE-DAREQIELLEPIRELAERYAAaRERLAELEYLRAALRLW 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 331 TLPEVEAELAQRIAALtkaEERHGNIEERMRHLEGQLEEKNQELQRARQRekmneehnkRLSDTVDRL--LTESNERLQL 408
Cdd:COG4913 285 FAQRRLELLEAELEEL---RAELARLEAELERLEARLDALREELDELEAQ---------IRGNGGDRLeqLEREIERLER 352
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958790272 409 HLKERMAALEEKNVLIQ--------ESETFRKNLEESLHDKERLAEEIEKLRSELDQMK 459
Cdd:COG4913 353 ELEERERRRARLEALLAalglplpaSAEEFAALRAEAAALLEALEEELEALEEALAEAE 411
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
289-459 |
4.88e-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: 42.99 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 289 KLENELANKEAILRQMEEKNRQLQERLELAEQKLQqtmrkaetlpEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLE 368
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLE----------AAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 369 E-KNQELQRARQREKmnEEHNKRLSDTVDRLLtesnerlqlhlkERMAALEEKNVLIQESETFRKNLEESL-HDKERLAE 446
Cdd:COG1579 84 NvRNNKEYEALQKEI--ESLKRRISDLEDEIL------------ELMERIEELEEELAELEAELAELEAELeEKKAELDE 149
|
170
....*....|...
gi 1958790272 447 EIEKLRSELDQMK 459
Cdd:COG1579 150 ELAELEAELEELE 162
|
|
| SAM_STIM-1,2-like |
cd09504 |
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ... |
823-881 |
5.01e-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: 39.62 E-value: 5.01e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958790272 823 WDGPTVVAWLELWLGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNPLHRLKLRL 881
Cdd:cd09504 5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
78-617 |
5.46e-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: 44.27 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 78 LRMTVVKRQAQspsgVSSEVEVLKALKSLFEHHKALDEKVRErlrvSLERVSALEEELAAANQEIVALREQNVHIQRKMV 157
Cdd:TIGR00606 222 IRDQITSKEAQ----LESSREIVKSYENELDPLKNRLKEIEH----NLSKIMKLDNEIKALKSRKKQMEKDNSELELKME 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 158 SSEGSTESEHLDgmepgqkVHEKRLSNGSidstDDTSQIVELQELLEKQNYEMAQMKDRLAALSSRVG------EVEQEA 231
Cdd:TIGR00606 294 KVFQGTDEQLND-------LYHNHQRTVR----EKERELVDCQRELEKLNKERRLLNQEKTELLVEQGrlqlqaDRHQEH 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 232 ETARKDLIKTEEMNTKY---------QRDIREAMA-QKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAIL 301
Cdd:TIGR00606 363 IRARDSLIQSLATRLELdgfergpfsERQIKNFHTlVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTI 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 302 RQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEErHGNIEERMRHLEGQLEEKNQELQRARQRE 381
Cdd:TIGR00606 443 ELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEK-NSLTETLKKEVKSLQNEKADLDRKLRKLD 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 382 KMNEEHNkRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETF--RKNLEESLH----DKERLAEEIEKLRSEL 455
Cdd:TIGR00606 522 QEMEQLN-HHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFpnKKQLEDWLHskskEINQTRDRLAKLNKEL 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 456 DQMKMRTGSLIEPTISRTHLDTSAELR-YSVGSLVDSQSDY-RTTKVIRRPRRGRMGVRRDEPKVKSLGDHEWNRTQQIG 533
Cdd:TIGR00606 601 ASLEQNKNHINNELESKEEQLSSYEDKlFDVCGSQDEESDLeRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCC 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 534 VLGSHPFESDTEMSDIDDDdretiFSSMDLLSPSGHSDAQTLAMMLQEQLDAINKEIRLIQEEKESTELRAEEIENRVAS 613
Cdd:TIGR00606 681 PVCQRVFQTEAELQEFISD-----LQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQK 755
|
....
gi 1958790272 614 VSLE 617
Cdd:TIGR00606 756 VNRD 759
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
103-487 |
5.55e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 5.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 103 LKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEgstesehldgmepgqkvhekrl 182
Cdd:COG4372 15 LFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQAR---------------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 183 sngsidstddtSQIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLikteemnTKYQRDIREAMAQKEDM 262
Cdd:COG4372 73 -----------SELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL-------EELQKERQDLEQQRKQL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 263 EERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQME--EKNRQLQERLELAEQKLQQTMRKAETLPEVEAELA 340
Cdd:COG4372 135 EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSeaEAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 341 QRIAALT--KAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALE 418
Cdd:COG4372 215 ELAEELLeaKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALE 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958790272 419 EKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSLIEPTISRTHLDTSAELRYSVGS 487
Cdd:COG4372 295 LKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGA 363
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
312-450 |
5.64e-04 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 41.52 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 312 QERLELAEQKLQQtmrkaetLPEVEAELAQRIAALTKaeeRHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRL 391
Cdd:pfam12718 13 QERAEELEEKVKE-------LEQENLEKEQEIKSLTH---KNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNENLTRKI 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958790272 392 sdtvdRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEK 450
Cdd:pfam12718 83 -----QLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEE 136
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
226-455 |
6.69e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.94 E-value: 6.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 226 EVEQEAETARKdlikteEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTsihdmndKLENELANKEAILRQME 305
Cdd:pfam05483 201 ELRVQAENARL------EMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQIT-------EKENKMKDLTFLLEESR 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 306 EKNRQLQERLELAEQKLQQTMRK----AETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQRE 381
Cdd:pfam05483 268 DKANQLEEKTKLQDENLKELIEKkdhlTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAH 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 382 KMNEEHNKRLSDTVDRLLTESNERLQ----------LHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEE---I 448
Cdd:pfam05483 348 SFVVTEFEATTCSLEELLRTEQQRLEknedqlkiitMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEkkqF 427
|
....*..
gi 1958790272 449 EKLRSEL 455
Cdd:pfam05483 428 EKIAEEL 434
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
55-374 |
7.17e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.06 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 55 AERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPsgvssevEVLKALKSLFehhKALDEKVRERLRVSLERVSALEEE 134
Cdd:pfam12128 247 QQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQ-------ETSAELNQLL---RTLDDQWKEKRDELNGELSAADAA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 135 LAAANQEIVALREQNVHIQRKMVSSEgSTESEHLDGMEPGQKVHEKRLSnGSIDSTDDTSQIVELQELLEKQ--NYEMAQ 212
Cdd:pfam12128 317 VAKDRSELEALEDQHGAFLDADIETA-AADQEQLPSWQSELENLEERLK-ALTGKHQDVTAKYNRRRSKIKEqnNRDIAG 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 213 MKDRLAAlsSRVGEVEQEAEtARKDLIKTE-EMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQREstsihdmndklE 291
Cdd:pfam12128 395 IKDKLAK--IREARDRQLAV-AEDDLQALEsELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATAT-----------P 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 292 NELANKEailrqmeeknrQLQERLELAEQKLQQTMRKAETLpevEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKN 371
Cdd:pfam12128 461 ELLLQLE-----------NFDERIERAREEQEAANAEVERL---QSELRQARKRRDQASEALRQASRRLEERQSALDELE 526
|
...
gi 1958790272 372 QEL 374
Cdd:pfam12128 527 LQL 529
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
298-451 |
9.23e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.79 E-value: 9.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 298 EAILRQMEEKNRQLQERLELAE---QKLQQTMRKAETLPEVEAELAQRIAALtkaEERHGNIEERMRHLEGQLEEKNQEL 374
Cdd:COG3096 518 RAQLAELEQRLRQQQNAERLLEefcQRIGQQLDAAEELEELLAELEAQLEEL---EEQAAEAVEQRSELRQQLEQLRARI 594
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958790272 375 QRARQREKMNEEHNKRLSdtvdRLLTESNERLQlHLKERMAALEekNVLIQESETFRKNlEESLHDKERLAEEIEKL 451
Cdd:COG3096 595 KELAARAPAWLAAQDALE----RLREQSGEALA-DSQEVTAAMQ--QLLEREREATVER-DELAARKQALESQIERL 663
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
246-467 |
9.53e-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: 43.42 E-value: 9.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 246 TKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIhDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQK---- 321
Cdd:pfam02463 165 SRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKL-KEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIdllq 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 322 -----LQQTMRKAETLPEVEAELAQRIAALTKAEER-HGNIEERMRHLEGQLEEKNQELQRARQREKMNEEhNKRLSDTV 395
Cdd:pfam02463 244 ellrdEQEEIESSKQEIEKEEEKLAQVLKENKEEEKeKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE-KLKESEKE 322
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958790272 396 DRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSLIE 467
Cdd:pfam02463 323 KKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE 394
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
282-459 |
1.21e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 41.73 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 282 SIHDMND---KLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK---------AETLPEVEAELAQRIAALTKA 349
Cdd:COG1842 31 AIRDMEEdlvEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKgredlareaLERKAELEAQAEALEAQLAQL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 350 EERHGNIEERMRHLEGQLEEKNQELQRARQREKMNeEHNKRLSDTVDRLLTESNErlqlhlkERMAALEEKnvliQESET 429
Cdd:COG1842 111 EEQVEKLKEALRQLESKLEELKAKKDTLKARAKAA-KAQEKVNEALSGIDSDDAT-------SALERMEEK----IEEME 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 1958790272 430 FRKNLEESLHDKERLAEEIEKLRS------ELDQMK 459
Cdd:COG1842 179 ARAEAAAELAAGDSLDDELAELEAdsevedELAALK 214
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
187-378 |
1.30e-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: 41.66 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 187 IDSTDDTSQIVELQELLEKQNyemaQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQ-KEDMEER 265
Cdd:cd00176 23 LSSTDYGDDLESVEALLKKHE----ALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEElRELAEER 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 266 ITTLEKRYLSAQRestsiHDMNDKLENELANKEAILRQME------------EKNRQLQERLELAEQKLQQTMRKAETLP 333
Cdd:cd00176 99 RQRLEEALDLQQF-----FRDADDLEQWLEEKEAALASEDlgkdlesveellKKHKELEEELEAHEPRLKSLNELAEELL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1958790272 334 EveaelAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRAR 378
Cdd:cd00176 174 E-----EGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
198-464 |
1.40e-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: 42.64 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 198 ELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETAR-----KDLIKTEEMNTKYQRDIREA----MAQKEDMEERITT 268
Cdd:COG5185 272 ENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKateslEEQLAAAEAEQELEESKRETetgiQNLTAEIEQGQES 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 269 LEKRYLSAQRESTSIHDMND------KLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPE-------- 334
Cdd:COG5185 352 LTENLEAIKEEIENIVGEVElsksseELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEelqrqieq 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 335 VEAELAQRIAALTKAEERhgnIEERMRHLEGQLEEKNQELQRARQRE--KMNEEHNKRLSDTVDRLLT--ESNERLQLHL 410
Cdd:COG5185 432 ATSSNEEVSKLLNELISE---LNKVMREADEESQSRLEEAYDEINRSvrSKKEDLNEELTQIESRVSTlkATLEKLRAKL 508
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1958790272 411 KERMAALEEKNVLIQESETFRKNLEESLHDKERlaEEIEKLRSELDQMKMRTGS 464
Cdd:COG5185 509 ERQLEGVRSKLDQVAESLKDFMRARGYAHILAL--ENLIPASELIQASNAKTDG 560
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
288-462 |
1.40e-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: 41.28 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 288 DKLENELANKEAILRQME------------EKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIaaltkaEERHGN 355
Cdd:cd00176 10 DELEAWLSEKEELLSSTDygddlesveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI------QERLEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 356 IEERMRHLEGQLEEKNQELQRARQREKMNEEH---NKRLSDTVDRLLTESN-------ERLQLHLKERMAALEEKNVLIQ 425
Cdd:cd00176 84 LNQRWEELRELAEERRQRLEEALDLQQFFRDAddlEQWLEEKEAALASEDLgkdlesvEELLKKHKELEEELEAHEPRLK 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 1958790272 426 ESETFRKNLEESLH--DKERLAEEIEKLRSELDQMKMRT 462
Cdd:cd00176 164 SLNELAEELLEEGHpdADEEIEEKLEELNERWEELLELA 202
|
|
| PRK03992 |
PRK03992 |
proteasome-activating nucleotidase; Provisional |
412-470 |
1.69e-03 |
|
proteasome-activating nucleotidase; Provisional
Pssm-ID: 179699 [Multi-domain] Cd Length: 389 Bit Score: 42.13 E-value: 1.69e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 412 ERMAALEEKNV-LIQESETFRKNLEESLHDKERLAEEIEKLRSELDqmKMRTGSLIEPTI 470
Cdd:PRK03992 1 ERLEALEERNSeLEEQIRQLELKLRDLEAENEKLERELERLKSELE--KLKSPPLIVATV 58
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
27-166 |
1.73e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 27 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgVSSEVEVLKALKSL 106
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEA---LQKEIESLKRRISD 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 107 FEhhkaldekvrERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTESE 166
Cdd:COG1579 108 LE----------DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
235-454 |
1.76e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.76 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 235 RKDLIKTEEMNTKYQRDIREAMAQKEdMEERITTLEkrylsaqreSTSIHdmNDKLENELANKEAILRQMEEKNRQLQER 314
Cdd:COG5022 809 RKEYRSYLACIIKLQKTIKREKKLRE-TEEVEFSLK---------AEVLI--QKFGRSLKAKKRFSLLKKETIYLQSAQR 876
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 315 LELAEQK---LQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIE-----ERMRHLEGQLEEKNQELQRARQREKmNEE 386
Cdd:COG5022 877 VELAERQlqeLKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENlefktELIARLKKLLNNIDLEEGPSIEYVK-LPE 955
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958790272 387 HNKRLsdTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSE 454
Cdd:COG5022 956 LNKLH--EVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKEL 1021
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
195-406 |
1.84e-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: 42.47 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 195 QIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTlekryl 274
Cdd:pfam01576 890 RIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKS------ 963
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 275 saqrestsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK-AETLPEVEAElaQRIAALTKAEERH 353
Cdd:pfam01576 964 --------------KFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKlKEVLLQVEDE--RRHADQYKDQAEK 1027
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958790272 354 GNIeeRMRHLEGQLEEKNQELQRAR-QREKMNEEhnkrLSDTvdrllTESNERL 406
Cdd:pfam01576 1028 GNS--RMKQLKRQLEEAEEEASRANaARRKLQRE----LDDA-----TESNESM 1070
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
244-459 |
2.02e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.37 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 244 MNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQREstsihdmndkLENELANKEAILRQMEEKNRQLQErleLAEQKLQ 323
Cdd:COG0497 138 LDPDAQRELLDAFAGLEELLEEYREAYRAWRALKKE----------LEELRADEAERARELDLLRFQLEE---LEAAALQ 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 324 qtmrkaetlPEVEAELAQRIAALTKAEERHGNIEERMRHLEGqlEEKN--QELQRARQR-EKMnEEHNKRLSDTVDRL-- 398
Cdd:COG0497 205 ---------PGEEEELEEERRRLSNAEKLREALQEALEALSG--GEGGalDLLGQALRAlERL-AEYDPSLAELAERLes 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 399 ----LTESNERLQLHLK------ERMAALEEK-----------NVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQ 457
Cdd:COG0497 273 alieLEEAASELRRYLDslefdpERLEEVEERlallrrlarkyGVTVEELLAYAEELRAELAELENSDERLEELEAELAE 352
|
..
gi 1958790272 458 MK 459
Cdd:COG0497 353 AE 354
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
118-454 |
2.05e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.16 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 118 RERLRVSLERVSAlEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEH----LDGMEPGQKVHEKRLSNGSIDSTDDT 193
Cdd:pfam02029 12 RRRAREERRRQKE-EEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEeeafLDRTAKREERRQKRLQEALERQKEFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 194 SQIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAmAQKEDMEERITTLEKRY 273
Cdd:pfam02029 91 PTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQA-EEEGEEEEDKSEEAEEV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 274 LSAQRESTSIHDMNDKLENELANKEAILRQMEEK--NRQLQERLELAEQKLQQTMRKAETLPEV---EAELAQRIAALTK 348
Cdd:pfam02029 170 PTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGhpEVKSQNGEEEVTKLKVTTKRRQGGLSQSqerEEEAEVFLEAEQK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 349 AEErhgnieERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLsdtvdrlltesnerlqlhlKERMAALEEKNVLIQESE 428
Cdd:pfam02029 250 LEE------LRRRRQEKESEEFEKLRQKQQEAELELEELKKKR-------------------EERRKLLEEEEQRRKQEE 304
|
330 340
....*....|....*....|....*.
gi 1958790272 429 TFRKNLEESlhDKERLAEEIEKLRSE 454
Cdd:pfam02029 305 AERKLREEE--EKRRMKEEIERRRAE 328
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
288-455 |
2.05e-03 |
|
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: 40.82 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 288 DKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlPEVEAELAQRIAALTKAEERHG-----------NI 356
Cdd:pfam04012 39 VKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGN--EELAREALAEKKSLEKQAEALEtqlaqqrsaveQL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 357 EERMRHLEGQLEEKNQE-------LQRARQREKMNEehnkrlsdTVDRLLTESNERLQLHLKERMAALEEKNVLIQESEt 429
Cdd:pfam04012 117 RKQLAALETKIQQLKAKknllkarLKAAKAQEAVQT--------SLGSLSTSSATDSFERIEEKIEEREARADAAAELA- 187
|
170 180
....*....|....*....|....*.
gi 1958790272 430 FRKNLEESLHDKERLAEEIEKLRSEL 455
Cdd:pfam04012 188 SAVDLDAKLEQAGIQMEVSEDVLARL 213
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
946-1001 |
2.27e-03 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 37.63 E-value: 2.27e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958790272 946 EWLPSLGLPQYRSYFMECLVD-ARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1001
Cdd:pfam07647 11 DWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLK-RLGITSVGHRRKILKKIQELK 66
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
185-368 |
2.30e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.59 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 185 GSIDSTDDTSQIVELQELLEKQNYEMAQM---------KDRLAALSSRVGEVEQEAETARKDLikteemnTKYQRDIrea 255
Cdd:cd22656 82 AQNAGGTIDSYYAEILELIDDLADATDDEeleeakktiKALLDDLLKEAKKYQDKAAKVVDKL-------TDFENQT--- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 256 MAQKEDMEERITTLEKRYlsaQRESTSIHDMN-DKLENELAN-KEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLP 333
Cdd:cd22656 152 EKDQTALETLEKALKDLL---TDEGGAIARKEiKDLQKELEKlNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLT 228
|
170 180 190
....*....|....*....|....*....|....*
gi 1958790272 334 EVEAELAQRIAALTKAEERHGNIEERMRHLEGQLE 368
Cdd:cd22656 229 AADTDLDNLLALIGPAIPALEKLQGAWQAIATDLD 263
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
301-414 |
2.95e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 301 LRQMEEKNRQLQ-ERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQ 379
Cdd:COG0542 413 LDELERRLEQLEiEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEK 492
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958790272 380 R----EKMNEEHNKRLSDTVD-----------------RLLTESNERLqLHLKERM 414
Cdd:COG0542 493 ElaelEEELAELAPLLREEVTeediaevvsrwtgipvgKLLEGEREKL-LNLEEEL 547
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
194-346 |
3.30e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 40.27 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 194 SQIVELQELLEKQNYEMA-------QMKDRLAALSSRVGEVEQEAETARKD---LIKTEEMNTKYQRDIREAMAQKEDME 263
Cdd:pfam13851 33 EEIAELKKKEERNEKLMSeiqqenkRLTEPLQKAQEEVEELRKQLENYEKDkqsLKNLKARLKVLEKELKDLKWEHEVLE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 264 ERITTLEKRY--LSAQREStSIHDMNDKLENE---LANK-EAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEA 337
Cdd:pfam13851 113 QRFEKVERERdeLYDKFEA-AIQDVQQKTGLKnllLEKKlQALGETLEKKEAQLNEVLAAANLDPDALQAVTEKLEDVLE 191
|
....*....
gi 1958790272 338 ELAQRIAAL 346
Cdd:pfam13851 192 SKNQLIKDL 200
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
229-386 |
3.79e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 229 QEAETARKDLIKTEEmntkyqrdiREAMAQKEDMEerittlekryLSAQREstsIHDMNDKLENELANKEAILRQMEEKN 308
Cdd:PRK12704 34 KEAEEEAKRILEEAK---------KEAEAIKKEAL----------LEAKEE---IHKLRNEFEKELRERRNELQKLEKRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 309 RQLQERLElaeqklqqtmRKAETLPEVEAELAQRIAALTKAEErhgNIEERmrhlEGQLEEK----NQELQR-------- 376
Cdd:PRK12704 92 LQKEENLD----------RKLELLEKREEELEKKEKELEQKQQ---ELEKK----EEELEELieeqLQELERisgltaee 154
|
170
....*....|..
gi 1958790272 377 ARQR--EKMNEE 386
Cdd:PRK12704 155 AKEIllEKVEEE 166
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
84-367 |
4.58e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 84 KRQAQSPSGVSSEVEVLKALKslfehhKALDEKVRERLR-VSLERVSA-----------LEEELAAANQEIVALREQNVH 151
Cdd:PRK11281 87 QQLAQAPAKLRQAQAELEALK------DDNDEETRETLStLSLRQLESrlaqtldqlqnAQNDLAEYNSQLVSLQTQPER 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 152 IQRKMvsSEGSTESEHLDgmepgqkvheKRLSNGSIDSTD-DTSQIVEL---QELLEKQNyemAQMKDRLAALSsrvgeV 227
Cdd:PRK11281 161 AQAAL--YANSQRLQQIR----------NLLKGGKVGGKAlRPSQRVLLqaeQALLNAQN---DLQRKSLEGNT-----Q 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 228 EQEAETARKDLiKTEEMN--TKYQRDIREAMAQKedmeeRITTLEKrylSAQrESTSIHDMNDKLENELANKEAilrqme 305
Cdd:PRK11281 221 LQDLLQKQRDY-LTARIQrlEHQLQLLQEAINSK-----RLTLSEK---TVQ-EAQSQDEAARIQANPLVAQEL------ 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958790272 306 EKNRQLQERLelaeqkLQQTmRKAETLPEVEAELAQRIAALTKAEErhgNIEERMRHLEGQL 367
Cdd:PRK11281 285 EINLQLSQRL------LKAT-EKLNTLTQQNLRVKNWLDRLTQSER---NIKEQISVLKGSL 336
|
|
| SAM_superfamily |
cd09487 |
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
828-885 |
4.77e-03 |
|
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.
Pssm-ID: 188886 [Multi-domain] Cd Length: 56 Bit Score: 36.45 E-value: 4.77e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958790272 828 VVAWLElWLGMPaWYVAACRANVKSGAIMSALSDTEIQrEIGISNPLHRLKLRLAIQE 885
Cdd:cd09487 2 VAEWLE-SLGLE-QYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAIQR 56
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
113-415 |
4.83e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 41.01 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 113 LDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEHLDGMEPGQKVHEKRLSNgsiDSTDD 192
Cdd:pfam02029 71 REERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQE---NKWST 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 193 TSQIVELQELLEKQNYEMAQMKDRlaalsSRVGEVEQEAETARKDLIKTEEMNTKYQRD---IREAMAQKEDMEERITTL 269
Cdd:pfam02029 148 EVRQAEEEGEEEEDKSEEAEEVPT-----ENFAKEEVKDEKIKKEKKVKYESKVFLDQKrghPEVKSQNGEEEVTKLKVT 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 270 EKRYLSAQRESTSIH-DMNDKLENELAnkeailrqMEEKNRQLQERLELAEQKLQQTMRKAEtlpeveAELaqriaaltk 348
Cdd:pfam02029 223 TKRRQGGLSQSQEREeEAEVFLEAEQK--------LEELRRRRQEKESEEFEKLRQKQQEAE------LEL--------- 279
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958790272 349 aEERHGNIEERMRHLEgqlEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMA 415
Cdd:pfam02029 280 -EELKKKREERRKLLE---EEEQRRKQEEAERKLREEEEKRRMKEEIERRRAEAAEKRQKLPEDSSS 342
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
309-449 |
4.93e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 39.48 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 309 RQLQERLELAEQKLQQTMRKAETLP----------------EVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ 372
Cdd:pfam12072 27 AKIGSAEELAKRIIEEAKKEAETKKkealleakeeihklraEAERELKERRNELQRQERRLLQKEETLDRKDESLEKKEE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 373 ELQRARQREKMNEEHNKRLSDTVDRLLTESNERLqlhlkERMAAL---EEKNVLIQESEtfrknlEESLHDKERLAEEIE 449
Cdd:pfam12072 107 SLEKKEKELEAQQQQLEEKEEELEELIEEQRQEL-----ERISGLtseEAKEILLDEVE------EELRHEAAVMIKEIE 175
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
115-459 |
5.51e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.88 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 115 EKVRERLRVSLERVSALEEELAAANQeivALREQNVHIQRKMVSSEGSTESEHldgmEPGQKVHEKRLSNGSI-DSTDDT 193
Cdd:pfam05557 44 DRESDRNQELQKRIRLLEKREAEAEE---ALREQAELNRLKKKYLEALNKKLN----EKESQLADAREVISCLkNELSEL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 194 SQIVELQEL-LEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEE-------- 264
Cdd:pfam05557 117 RRQIQRAELeLQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIvknsksel 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 265 -RITTLEKRyLSAQRE-----STSIHDmNDKLENELANKEAILRQME---EKNRQLQERLELAEQKLQQ----------T 325
Cdd:pfam05557 197 aRIPELEKE-LERLREhnkhlNENIEN-KLLLKEEVEDLKRKLEREEkyrEEAATLELEKEKLEQELQSwvklaqdtglN 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 326 MRKAETLPEVEAELAQRIAALTkaeERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLltesNER 405
Cdd:pfam05557 275 LRSPEDLSRRIEQLQQREIVLK---EENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRL----QRR 347
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1958790272 406 LQLHLKERmaaleekNVLIQESETFRKNLEESLHDkERLAEEIEKLRSELDQMK 459
Cdd:pfam05557 348 VLLLTKER-------DGYRAILESYDKELTMSNYS-PQLLERIEEAEDMTQKMQ 393
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
198-450 |
5.56e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 40.41 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 198 ELQELLEKQNYEMAQMKDRLAALSSRvgEVEQEAETARKDLIKTEEmntKYQRDIRE-AMAQKEDMEERITTLEKRYLSA 276
Cdd:pfam15558 35 EELRRRDQKRQETLERERRLLLQQSQ--EQWQAEKEQRKARLGREE---RRRADRREkQVIEKESRWREQAEDQENQRQE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 277 QRESTSIHDMNDKLENE--LANKEAILRQMEEKNR-QLQERLELAEQKLQQ--------------------TMRKAETLP 333
Cdd:pfam15558 110 KLERARQEAEQRKQCQEqrLKEKEEELQALREQNSlQLQERLEEACHKRQLkereeqkkvqennlsellnhQARKVLVDC 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 334 EVEAELAQRIAAL----TKAEERH-GNIEERMRHLEGQLEEKNQELQRARQR-EKMNEEHNKRLSDTV---DRLLTESNE 404
Cdd:pfam15558 190 QAKAEELLRRLSLeqslQRSQENYeQLVEERHRELREKAQKEEEQFQRAKWRaEEKEEERQEHKEALAelaDRKIQQARQ 269
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958790272 405 RLQLHLKERMAALEEKNVLIQ------------ESETFRKNLEESLHDKERLAEEIEK 450
Cdd:pfam15558 270 VAHKTVQDKAQRARELNLEREknhhilklkvekEEKCHREGIKEAIKKKEQRSEQISR 327
|
|
| BAR_SNX7 |
cd07666 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 7; BAR domains are dimerization, lipid ... |
203-394 |
5.73e-03 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 7; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. The specific function of SNX7 is still unknown. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153350 Cd Length: 243 Bit Score: 39.89 E-value: 5.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 203 LEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQrDIREAMAQK----EDMEERITTLEKRYLSAQR 278
Cdd:cd07666 14 LTAQAWELSSHKKQGPGLLSRMGQTVKAVASSVRGVKNRPEEFTEMN-EYVEAFSQKinvlDKISQRIYKEQREYFEELK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 279 ESTSIHDMNDKLENELANK--------EAILRQMEEKNRQLQERLE-------LAEQKLQQTMRKAEtlpEVEAELAQRI 343
Cdd:cd07666 93 EYGPIYTLWSASEEELADSlkgmasciDRCCKATDKRMKGLSEQLLpviheyvLYSETLMGVIKRRD---QIQAELDSKV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958790272 344 AALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDT 394
Cdd:cd07666 170 EALANKKADRDLLKEEIEKLEDKVECANNALKADWERWKQNMQTDLRSAFT 220
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
128-456 |
6.06e-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: 40.44 E-value: 6.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 128 VSALEEELAAANQEIVALREQNVHIQrKMVSSEGSTESEHLDGMEPGQKVHEK--RLSNGSID----STDDTSQIVELQ- 200
Cdd:pfam05622 23 VSLLQEEKNSLQQENKKLQERLDQLE-SGDDSGTPGGKKYLLLQKQLEQLQEEnfRLETARDDyrikCEELEKEVLELQh 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 201 --ELLEKQNYEMAQMKDRLAAL---SSRVGEVEQEAETARKdliKTEEMNtkyqrDIREAMAQkedMEERITTLEKRYLS 275
Cdd:pfam05622 102 rnEELTSLAEEAQALKDEMDILresSDKVKKLEATVETYKK---KLEDLG-----DLRRQVKL---LEERNAEYMQRTLQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 276 aqrestsihdmndkLENELANKEAILRQMEEKNRQLQErlelAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHgn 355
Cdd:pfam05622 171 --------------LEEELKKANALRGQLETYKRQVQE----LHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERL-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 356 IEERmrhleGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETfrKNLE 435
Cdd:pfam05622 231 IIER-----DTLRETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLGQE--GSYR 303
|
330 340
....*....|....*....|.
gi 1958790272 436 ESLHDKERLAEEIEKLRSELD 456
Cdd:pfam05622 304 ERLTELQQLLEDANRRKNELE 324
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
104-393 |
6.55e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 40.51 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 104 KSLFEHHKALDEKVRERLRvSLERVSALEEELAAANQEIVALREQNVH--IQRKMVSSEGSTESEHLDGMEPGQKVHEKR 181
Cdd:pfam09731 121 KSEQEKEKALEEVLKEAIS-KAESATAVAKEAKDDAIQAVKAHTDSLKeaSDTAEISREKATDSALQKAEALAEKLKEVI 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 182 LSNGSIDSTDDTSQIVELQELLE------KQNYEMAQMKDRLAALSSRVGE-VEQEAETARKDLIKTE------------ 242
Cdd:pfam09731 200 NLAKQSEEEAAPPLLDAAPETPPklpehlDNVEEKVEKAQSLAKLVDQYKElVASERIVFQQELVSIFpdiipvlkednl 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 243 EMNTKYQRDIREAMAQKEDMEERITTLEKR-YLSAQRESTSIHDMNDKLENELAnkEAILRQMEEKNRQLQERLELAEQK 321
Cdd:pfam09731 280 LSNDDLNSLIAHAHREIDQLSKKLAELKKReEKHIERALEKQKEELDKLAEELS--ARLEEVRAADEAQLRLEFEREREE 357
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958790272 322 LQQTMRKaetlpEVEAELAQRIAALTKaeerhgnieermrHLEGQLEEKNQELQRARQR---EKMNEEHNKRLSD 393
Cdd:pfam09731 358 IRESYEE-----KLRTELERQAEAHEE-------------HLKDVLVEQEIELQREFLQdikEKVEEERAGRLLK 414
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
348-614 |
6.65e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.82 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 348 KAEERHGNIEERMRHLEGQLEEKNQELQR-ARQREKMNEehnkrlsdtVDRLLTESNE-RLQLHLKERMAALEEKNVLIQ 425
Cdd:TIGR02169 174 KALEELEEVEENIERLDLIIDEKRQQLERlRREREKAER---------YQALLKEKREyEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 426 ESETFRKNLEES---LHDKERLAEEIEKLRSELDQMKMRTGSLIEPTISRTHLDTSAELRysvgSLVDSQSDYRTTKVIR 502
Cdd:TIGR02169 245 QLASLEEELEKLteeISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIA----SLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 503 RPRRGRMGVRRDepkvKSLGDHEWNRTQqigvLGSHPFESDTEMSDIDD--DDRETIFSSMDLLSPSG------HSDAQT 574
Cdd:TIGR02169 321 EERLAKLEAEID----KLLAEIEELERE----IEEERKRRDKLTEEYAElkEELEDLRAELEEVDKEFaetrdeLKDYRE 392
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1958790272 575 LAMMLQEQLDAINKEIRLIQEEKESTELRAEEIENRVASV 614
Cdd:TIGR02169 393 KLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
|
|
| SAM_SARM1-like_repeat1 |
cd09501 |
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
946-990 |
7.88e-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: 36.13 E-value: 7.88e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1958790272 946 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHR 990
Cdd:cd09501 11 TWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLR 55
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
257-378 |
8.18e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.95 E-value: 8.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 257 AQKEDMEERITTLEKRYLSAQREstsihdmNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVE 336
Cdd:PRK09039 74 QGNQDLQDSVANLRASLSAAEAE-------RSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQI 146
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1958790272 337 AELAQRIAAL--------TKAEERHGNIEERMRHLEGQLEEKNQELQRAR 378
Cdd:PRK09039 147 AALRRQLAALeaaldaseKRDRESQAKIADLGRRLNVALAQRVQELNRYR 196
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
193-353 |
8.80e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.00 E-value: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 193 TSQIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAE---------TARKDLIKTEEMNTKYQRDIREAMAQKEDME 263
Cdd:PHA02562 240 TDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyekggvcpTCTQQISEGPDRITKIKDKLKELQHSLEKLD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 264 ERITTLEKRYLSAQRESTSIHDMNDKLENelaNKEAILRqMEEKNRQLQERLELAEqklQQTMRKAETLPEVEAELAQRI 343
Cdd:PHA02562 320 TAIDELEEIMDEFNEQSKKLLELKNKIST---NKQSLIT-LVDKAKKVKAAIEELQ---AEFVDNAEELAKLQDELDKIV 392
|
170
....*....|.
gi 1958790272 344 AALTK-AEERH 353
Cdd:PHA02562 393 KTKSElVKEKY 403
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
293-605 |
9.57e-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: 40.11 E-value: 9.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 293 ELANKEAILRQMEEKNRQLQERLELAEQklqQTMRKAETlpeveaelaQRIAALTKAEERHGniEERMRHLEG-QLEEKN 371
Cdd:pfam17380 294 EKMEQERLRQEKEEKAREVERRRKLEEA---EKARQAEM---------DRQAAIYAEQERMA--MERERELERiRQEERK 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 372 QELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHL----------KERMAALEEKNVliqESETFRKNLEESLHDK 441
Cdd:pfam17380 360 RELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELeaarkvkileEERQRKIQQQKV---EMEQIRAEQEEARQRE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 442 -----ERLAEEIEKLRSEL--DQMKMRTGSLIEPTISRTHLDTSAELRYSVGS------LVDSQSDYRTTKVIRRPRRGR 508
Cdd:pfam17380 437 vrrleEERAREMERVRLEEqeRQQQVERLRQQEEERKRKKLELEKEKRDRKRAeeqrrkILEKELEERKQAMIEEERKRK 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 509 MGVRRDEPKVKSLGDHEWNRTQQigvlgshpfesDTEMSDIDDDDRETIFSSMDLLSPSghsdaqtlammlQEQLDAINK 588
Cdd:pfam17380 517 LLEKEMEERQKAIYEEERRREAE-----------EERRKQQEMEERRRIQEQMRKATEE------------RSRLEAMER 573
|
330
....*....|....*..
gi 1958790272 589 EIRLIQEEKESTELRAE 605
Cdd:pfam17380 574 EREMMRQIVESEKARAE 590
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
291-458 |
9.80e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 40.01 E-value: 9.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 291 ENELANKEAILRQMEEKNRQLQERLELAE--QKLQQTMRKAEtlpEVEAELAQRIAALTKAEErhgnieermrHLEgQLE 368
Cdd:pfam05667 311 EAPAATSSPPTKVETEEELQQQREEELEElqEQLEDLESSIQ---ELEKEIKKLESSIKQVEE----------ELE-ELK 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790272 369 EKNQELQRARQREKMneehnkrlsdTVDRLL-TESN-ERLQL---HLKERMAAL----EEKNV-LIQESETFRKNLEESL 438
Cdd:pfam05667 377 EQNEELEKQYKVKKK----------TLDLLPdAEENiAKLQAlvdASAQRLVELagqwEKHRVpLIEEYRALKEAKSNKE 446
|
170 180
....*....|....*....|
gi 1958790272 439 HDKERLAEEIEKLRSELDQM 458
Cdd:pfam05667 447 DESQRKLEEIKELREKIKEV 466
|
|
| |
