|
Name |
Accession |
Description |
Interval |
E-value |
| SAM_liprin-alpha1,2,3,4_repeat2 |
cd09565 |
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ... |
958-1023 |
3.20e-44 |
|
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: 154.17 E-value: 3.20e-44
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1926975374 958 MNHEWIGNEWLPSLGLPQYRSHFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 1023
Cdd:cd09565 1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
|
|
| SAM_liprin-alpha1,2,3,4_repeat1 |
cd09562 |
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 ... |
841-911 |
6.06e-42 |
|
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.
Pssm-ID: 188961 Cd Length: 71 Bit Score: 147.71 E-value: 6.06e-42
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1926975374 841 FAQWDGPTVVSWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEMVSLT 911
Cdd:cd09562 1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
|
|
| SAM_liprin-alpha1,2,3,4_repeat3 |
cd09568 |
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ... |
1043-1114 |
6.84e-41 |
|
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.
Pssm-ID: 188967 Cd Length: 72 Bit Score: 144.77 E-value: 6.84e-41
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1926975374 1043 DVLVWTNEQVVRWVQSVGLRDYAGNLQESGVHGALLALDENFDHSALALALQIPTQNTQARQVMEREFSNLL 1114
Cdd:cd09568 1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
|
|
| SAM_liprin-kazrin_repeat2 |
cd09495 |
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ... |
962-1021 |
1.51e-30 |
|
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: 114.94 E-value: 1.51e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 962 WIGNEWLPSLGLPQYRSHFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1021
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 ... |
848-906 |
2.30e-25 |
|
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of the SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and adherens junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188893 Cd Length: 58 Bit Score: 99.99 E-value: 2.30e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1926975374 848 TVVSWLELWVGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQE 906
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 ... |
1051-1112 |
1.25e-24 |
|
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and in adherens junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188895 Cd Length: 62 Bit Score: 98.00 E-value: 1.25e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1926975374 1051 QVVRWVQSVGLRDYAGNLQESGVHGALLALDENFDHSALALALQIPTQNTQARQVMEREFSN 1112
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 ... |
1043-1114 |
1.85e-20 |
|
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: 86.34 E-value: 1.85e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1926975374 1043 DVLVWTNEQVVRWVQSVGLRDYAGNLQESGVHGALLALDENFDHSALALALQIPTQNTQARQVMEREFSNLL 1114
Cdd:cd09570 1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
|
|
| SAM_kazrin_repeat2 |
cd09567 |
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ... |
957-1021 |
3.33e-16 |
|
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188966 Cd Length: 65 Bit Score: 73.98 E-value: 3.33e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1926975374 957 DMNHEWIGNEWLPSLGLPQYRSHFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1021
Cdd:cd09567 1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
|
|
| SAM_liprin-beta1,2_repeat2 |
cd09566 |
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ... |
957-1021 |
9.04e-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: 72.73 E-value: 9.04e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1926975374 957 DMNHEWIgNEWLPSLGLPQYRSHFMECLVDARMLDHLTKKDLrVHLKMVDSFHRTSLQYGIMCLK 1021
Cdd:cd09566 1 KLDTHWV-LRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDL-LHLKVTSALHHASIRRGIQVLR 63
|
|
| SAM_kazrin_repeat1 |
cd09564 |
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ... |
842-906 |
9.93e-16 |
|
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrin contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved into interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188963 Cd Length: 70 Bit Score: 72.87 E-value: 9.93e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1926975374 842 AQWDGPTVVSWLELWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQE 906
Cdd:cd09564 2 SRWKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
170-493 |
1.05e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 82.80 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 170 ERLRAALQRV----STLEEQLAGAHQQVSALQQAAGVRdgaaEEEGSVDLglkRLWKDDVVRLEELQElleKQNLELGQA 245
Cdd:TIGR02168 182 ERTRENLDRLedilNELERQLKSLERQAEKAERYKELK----AELRELEL---ALLVLRLEELREELE---ELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 246 RERLATLTAAVAELEEDLGTARRDLIKSEERSSRHQRDLREALAQKEDMEERIATLEKRylaaqreatsihdlndkLENE 325
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER-----------------LANL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 326 LANKESLHRQCEEKARHLQELLDVAEQKLQQTLRRAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQE 405
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 406 LARVRQREKMNEDHNKRLSDTVDRLLSESNERLQ-LHLKERMAALEEKNSLMQELESSQRQIEEQQNHKGRLSEEIEKLR 484
Cdd:TIGR02168 395 IASLNNEIERLEARLERLEDRRERLQQEIEELLKkLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAE 474
|
....*....
gi 1926975374 485 QEVDQLKGR 493
Cdd:TIGR02168 475 QALDAAERE 483
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
957-1021 |
4.51e-15 |
|
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: 70.76 E-value: 4.51e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1926975374 957 DMNHEWIGNEWLPSLGLPQYRSHFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1021
Cdd:pfam00536 1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
233-495 |
4.92e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 80.37 E-value: 4.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 233 ELLEKQNLELGQARERLATLTAAVAELEEDLGTARRDLIKSEERSSRHQRDLREALAQKEDMEERIATLEKRYLAAQREA 312
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 313 TSIHDLNDKLENELANKESLHRQCEEKARHLQELLDVAEQKLQQTLRRAetlpevEAELAQRIAALTKAEERHGNIEEHL 392
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL------EELAEELLEALRAAAELAAQLEELE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 393 RQLEGQLEEKNQELARVRQREKmNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNSLMQELESSQRQIEEQQNH 472
Cdd:COG1196 407 EAEEALLERLERLEEELEELEE-ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
250 260
....*....|....*....|...
gi 1926975374 473 KGRLSEEIEKLRQEVDQLKGRGG 495
Cdd:COG1196 486 LAEAAARLLLLLEAEADYEGFLE 508
|
|
| SAM_liprin-beta1,2_repeat3 |
cd09569 |
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ... |
1043-1114 |
6.42e-14 |
|
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: 67.87 E-value: 6.42e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1926975374 1043 DVLVWTNEQVVRWVQSVGLRDYAGNLQESGVHGALLALDENFDHSALALALQIPTQNTQARQVMEREFSNLL 1114
Cdd:cd09569 1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
241-491 |
9.22e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 76.65 E-value: 9.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 241 ELGQARERLATLTAAVAELEEDLGTARRDLIKSEE----RSSRHQRDLREALAQKEDMEERIATLEKRYLAAQREATSIH 316
Cdd:TIGR02169 178 ELEEVEENIERLDLIIDEKRQQLERLRREREKAERyqalLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLT 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 317 DLNDKLENELANKESLHRQCEEKARHL--QELLDVAEQ--KLQQTLRRAE-TLPEVEAELAQRIAALTKAEERHGNIEEH 391
Cdd:TIGR02169 258 EEISELEKRLEEIEQLLEELNKKIKDLgeEEQLRVKEKigELEAEIASLErSIAEKERELEDAEERLAKLEAEIDKLLAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 392 LRQLEGQLEEKNQELARVRQREKMNEDhnkRLSDTVDRLLSESnerlqlhlKERMAALEEKNSLMQELESSQRQIEEQQN 471
Cdd:TIGR02169 338 IEELEREIEEERKRRDKLTEEYAELKE---ELEDLRAELEEVD--------KEFAETRDELKDYREKLEKLKREINELKR 406
|
250 260
....*....|....*....|
gi 1926975374 472 HKGRLSEEIEKLRQEVDQLK 491
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLN 426
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
147-490 |
8.24e-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: 8.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 147 EVEVLKALKSLFEHHKALDEkVRERLRAALQRVSTLEEQLAGAHQQVSALQQaagVRDGAAEEEGSVDLGLKRLwkddVV 226
Cdd:TIGR02168 711 EEELEQLRKELEELSRQISA-LRKDLARLEAEVEQLEERIAQLSKELTELEA---EIEELEERLEEAEEELAEA----EA 782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 227 RLEELQELLEKQNLELGQARERLATLTAAVAELEEDLGTARRDLIKSEERSSRHQRDLREALAQKEDMEERIATLEKRYL 306
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 307 AAQREATSIHDLNDKLENELANKEslhrqceekaRHLQELLDvAEQKLQQTLRraetlpEVEAELAQRIAALTKAEERHG 386
Cdd:TIGR02168 863 ELEELIEELESELEALLNERASLE----------EALALLRS-ELEELSEELR------ELESKRSELRRELEELREKLA 925
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 387 NIEEHLRQLEGQLEEKNQelaRVRQREKMNEDHNKRLSDTVDRLLSESNERLQLhLKERMAALEEKNSL-MQELESSQRQ 465
Cdd:TIGR02168 926 QLELRLEGLEVRIDNLQE---RLSEEYSLTLEEAEALENKIEDDEEEARRRLKR-LENKIKELGPVNLAaIEEYEELKER 1001
|
330 340
....*....|....*....|....*
gi 1926975374 466 IEEQQNHKGRLSEEIEKLRQEVDQL 490
Cdd:TIGR02168 1002 YDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
24-493 |
1.02e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.05 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 24 ANFEQLMVNMLDEREKLLESLRESQETLVATQGRLQDALHERDQLQRHLNSALPQEFATLTRELSLcreqllerEEEISE 103
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL--------AAQLEE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 104 LKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgvSSEVEVLKALKSLFEHHKALDEKVRERLRAALQ---RVS 180
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEE----EALEEAAEEEAELEEEEEALLELLAELLEEAALleaALA 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 181 TLEEQLAGAHQQVSALQQAAGVRDGAAEEEGSVDL--GLKRLWKDDVVRLEELQELLEKQNLELGQARERLATLTAAVAE 258
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLlaGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 259 LEEDLGTARR---------DLIKSEERSSRHQRDLREALAQKEDMEERIATLEKRYLAAQREATSIHDlNDKLENELANK 329
Cdd:COG1196 561 AAIEYLKAAKagratflplDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLV-AARLEAALRRA 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 330 ESLHRQCEEKARHLQELLDVAEQKLQQTLRRAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARV 409
Cdd:COG1196 640 VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEE 719
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 410 RQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNSLMQELESSQRQI--------------EEQQNHKGR 475
Cdd:COG1196 720 ELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIealgpvnllaieeyEELEERYDF 799
|
490
....*....|....*...
gi 1926975374 476 LSEEIEKLRQEVDQLKGR 493
Cdd:COG1196 800 LSEQREDLEEARETLEEA 817
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
38-493 |
3.27e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.22 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 38 EKLLESLRESQETLVAT-QGRLQDALHERdqlqrhLNsALPQEFATLTRElslcreqllereeeISELKAERNNTRLLLE 116
Cdd:PRK02224 179 ERVLSDQRGSLDQLKAQiEEKEEKDLHER------LN-GLESELAELDEE--------------IERYEEQREQARETRD 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 117 HLECLVSRHERSLrmtvvkrqaqspsgvsSEVEVLKALKSLFEHHKALDEKVRERLRaalQRVSTLEEQLAGAHQQVSAL 196
Cdd:PRK02224 238 EADEVLEEHEERR----------------EELETLEAEIEDLRETIAETEREREELA---EEVRDLRERLEELEEERDDL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 197 QQAAGVRDGAAEeegSVDLGLKRLWKDDVvrleELQELLEKQNLELGQARERLATLTAAVAELEEDLGTARRDLIKSEER 276
Cdd:PRK02224 299 LAEAGLDDADAE---AVEARREELEDRDE----ELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 277 SSRHQRDLREALAQKEDMEERIATLEKRYLAAqreATSIHDLNDKLENELANKESLHRQCEEKARHLQELLDVAEQklQQ 356
Cdd:PRK02224 372 LEEAREAVEDRREEIEELEEEIEELRERFGDA---PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEE--AE 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 357 TLRRAETLPEVEAEL--AQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMnEDHNKRLSD---TVDRLL 431
Cdd:PRK02224 447 ALLEAGKCPECGQPVegSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEA-EDRIERLEErreDLEELI 525
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1926975374 432 SESNERLQlhlkERMAALEEKNSLMQELESSQRQIEEQQNHKgrlSEEIEKLRQEVDQLKGR 493
Cdd:PRK02224 526 AERRETIE----EKRERAEELRERAAELEAEAEEKREAAAEA---EEEAEEAREEVAELNSK 580
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
37-409 |
4.05e-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: 4.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 37 REKLLESLRESQETLVatqgRLQDALHERD-QLQR-HLNSALPQEFATLTRELSlcREQLLEREEEISELKAERNNTRLL 114
Cdd:TIGR02168 174 RKETERKLERTRENLD----RLEDILNELErQLKSlERQAEKAERYKELKAELR--ELELALLVLRLEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 115 LEHLECLVSRHERSLRMTvvkrqaqspsgvSSEVEVLKALKSlfEHHKALDEkVRERLRAALQRVSTLEEQLAGAHQQVS 194
Cdd:TIGR02168 248 LKEAEEELEELTAELQEL------------EEKLEELRLEVS--ELEEEIEE-LQKELYALANEISRLEQQKQILRERLA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 195 ALQQAAGVRDGAAEEEGSVDLGLKRLWKDDVVRLEELQELLEKQNLELGQARERLATLTAAVAELEEDLGTARRDLIKSE 274
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 275 ERSSRHQRDLREALAQKEDMEERIATLEKRYLAAQREATS-----IHDLNDKLENELANKESLHRQCEEKARHLQELLDV 349
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaelkeLQAELEELEEELEELQEELERLEEALEELREELEE 472
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 350 AEQKLQQTLRRaetlpevEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARV 409
Cdd:TIGR02168 473 AEQALDAAERE-------LAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVL 525
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
102-493 |
8.56e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.71 E-value: 8.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 102 SELKAERNNTRLLLEHLECLVSRHERSLRmtVVKRQAQSPSGVSSEV-EVLKALKSLFEHHKALDEKVR--ERLRAALQR 178
Cdd:PRK03918 296 IKLSEFYEEYLDELREIEKRLSRLEEEIN--GIEERIKELEEKEERLeELKKKLKELEKRLEELEERHElyEEAKAKKEE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 179 VSTLEEQLAGahqqvsalqqaagvrdgaaEEEGSVDLGLKRLWKddvvRLEELQELLEKQNLELGQARERLATLTAAVAE 258
Cdd:PRK03918 374 LERLKKRLTG-------------------LTPEKLEKELEELEK----AKEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 259 LEEDLG---TARRDLIKSEERS--SRHQRDLREALAQKEDMEERIATLEKR------YLAAQREATSIHDLNDKL---EN 324
Cdd:PRK03918 431 LKKAKGkcpVCGRELTEEHRKEllEEYTAELKRIEKELKEIEEKERKLRKElrelekVLKKESELIKLKELAEQLkelEE 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 325 ELA--NKESLHRQCEEkARHLQELLDVAEQKLQQTLRRAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQL----EGQ 398
Cdd:PRK03918 511 KLKkyNLEELEKKAEE-YEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesVEE 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 399 LEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQL--HLKERMAALEEKNSLMQELES--SQRQIEEQQNHKG 474
Cdd:PRK03918 590 LEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAfeELAETEKRLEELRKELEELEKkySEEEYEELREEYL 669
|
410
....*....|....*....
gi 1926975374 475 RLSEEIEKLRQEVDQLKGR 493
Cdd:PRK03918 670 ELSRELAGLRAELEELEKR 688
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
20-429 |
1.20e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 20 ADTDANFEQLMVNMLDEREKLLESLRESQETLVATQGRLQDALHERDQLQRHLNSALpQEFATLTRELSLCREQLLEREE 99
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL-ELLAELLEEAALLEAALAELLE 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 100 EISELKAERNNTRLLLEHLEclvSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKA--LDEKVRERLRAALQ 177
Cdd:COG1196 485 ELAEAAARLLLLLEAEADYE---GFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAaaLQNIVVEDDEVAAA 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 178 RVSTLEEQLAG----------AHQQVSALQQAAGVRDGAAEEEGSVDLGLKRLWKDDVVRLEELQELLEKQNLELGQARE 247
Cdd:COG1196 562 AIEYLKAAKAGratflpldkiRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVT 641
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 248 RLATLTAAVAELEEDLGTARRDLIKSEERSSRHQRDLREALAQKEDMEERIATLEKRYLAAQREATSIHDLNDKLENELA 327
Cdd:COG1196 642 LAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEEL 721
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 328 NKESLHRQCEEKARHLQELLDVAEQKLQQTLRRAETLPEVEAELAQRIAALTKAEERHGN-----IEEH------LRQLE 396
Cdd:COG1196 722 EEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPvnllaIEEYeeleerYDFLS 801
|
410 420 430
....*....|....*....|....*....|....
gi 1926975374 397 GQLEEKNQELARVRQR-EKMNEDHNKRLSDTVDR 429
Cdd:COG1196 802 EQREDLEEARETLEEAiEEIDRETRERFLETFDA 835
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
261-495 |
1.22e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.32 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 261 EDLGTARRDLIKSEERSSRHQRDLREALAQKEDMEERIATLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKA 340
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 341 RHLQEL----------LDVAEQKLQQTLRRAETLPEVEAELAQRIAALTKAEER----------HGNIEEHLRQLEGQLE 400
Cdd:PRK03918 238 EEIEELekeleslegsKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKaeeyiklsefYEEYLDELREIEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 401 EKNQELARVRQREKMNEDHNKRLSDTVDRLlSESNERLQlHLKERMAALEEKNSLMQELES------------SQRQIEE 468
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKL-KELEKRLE-ELEERHELYEEAKAKKEELERlkkrltgltpekLEKELEE 395
|
250 260
....*....|....*....|....*..
gi 1926975374 469 QQNHKGRLSEEIEKLRQEVDQLKGRGG 495
Cdd:PRK03918 396 LEKAKEEIEEEISKITARIGELKKEIK 422
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
34-491 |
1.26e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.32 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 34 LDEREKLLESLRESQETLVATQGRLQDALHERDQLQRHLnSALPQEFATLTRELSlcreQLLEREEEISELKAERNNTRL 113
Cdd:PRK03918 278 LEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRL-SRLEEEINGIEERIK----ELEEKEERLEELKKKLKELEK 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 114 LLEHLEclvSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKAlDEKVRERLRAALQRVSTLEEQLAGAHQQV 193
Cdd:PRK03918 353 RLEELE---ERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKA-KEEIEEEISKITARIGELKKEIKELKKAI 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 194 SALQQAAGV-----RDGAAEEEGsvdlGLKRLWKDDVVRLEElqellekqnlELGQARERLATLTAAVAELEEDLGTARR 268
Cdd:PRK03918 429 EELKKAKGKcpvcgRELTEEHRK----ELLEEYTAELKRIEK----------ELKEIEEKERKLRKELRELEKVLKKESE 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 269 --------DLIKS--EERSSRHQRDLREALAQKEDMEERIATLEKRYLAAQREATSIHDLNDK---LENELANKES---- 331
Cdd:PRK03918 495 liklkelaEQLKEleEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKlaeLEKKLDELEEelae 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 332 LHRQCEEKARHLQELLDVAEQKLQQTLRRAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQ 411
Cdd:PRK03918 575 LLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 412 reKMNEDHNKRLSDtvdRLLSESNErlqlhLKERMAALEEKNSLMQELESSQRQIEEQQNHKGRLSEEIEKLRQEVDQLK 491
Cdd:PRK03918 655 --KYSEEEYEELRE---EYLELSRE-----LAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVE 724
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
21-491 |
2.68e-11 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 68.22 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 21 DTDANFEQLMVNMLDErEKLLESLREsqeTLVATQGRLQDALHERDQLQ----RHLNSALPQEFATLTRELSLCREQLLE 96
Cdd:pfam15921 167 DSNTQIEQLRKMMLSH-EGVLQEIRS---ILVDFEEASGKKIYEHDSMStmhfRSLGSAISKILRELDTEISYLKGRIFP 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 97 REEEISELKAE-RNNTRLLLEH----LECLVSRHERSL-----RMTVVKRQAQSpsgVSSEVEV------------LKAL 154
Cdd:pfam15921 243 VEDQLEALKSEsQNKIELLLQQhqdrIEQLISEHEVEItglteKASSARSQANS---IQSQLEIiqeqarnqnsmyMRQL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 155 KSLFEHHKALDEKVRERLRAALQRVSTLEEQLAGAHqqvSALQQAAGVRDGAAEEEGSVDLGLKRLWKDdvvrleelqel 234
Cdd:pfam15921 320 SDLESTVSQLRSELREAKRMYEDKIEELEKQLVLAN---SELTEARTERDQFSQESGNLDDQLQKLLAD----------- 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 235 LEKQNLELGQARERLATLtaavaeLEEDLGTA------RRDLiksEERSSRHQRdlREAL--AQKEDMEERIatlekryl 306
Cdd:pfam15921 386 LHKREKELSLEKEQNKRL------WDRDTGNSitidhlRREL---DDRNMEVQR--LEALlkAMKSECQGQM-------- 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 307 aaQREATSIHDLNDKLENelanKESLHRQCEEKArhlqelldvaeqklqqtlrraETLPEVEAELAQRIAALTKAEERHG 386
Cdd:pfam15921 447 --ERQMAAIQGKNESLEK----VSSLTAQLESTK---------------------EMLRKVVEELTAKKMTLESSERTVS 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 387 NIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNE----RLQLHLKERMAAL--EEKNSLMQELE 460
Cdd:pfam15921 500 DLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTEcealKLQMAEKDKVIEIlrQQIENMTQLVG 579
|
490 500 510
....*....|....*....|....*....|.
gi 1926975374 461 SSQRQIEEQQNHKGRLSEEIEKLRQEVDQLK 491
Cdd:pfam15921 580 QHGRTAGAMQVEKAQLEKEINDRRLELQEFK 610
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
26-486 |
2.85e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.40 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 26 FEQLMVNMLDER-EKLLESLRESQETLVATQGRLQDALHERDQLQRHLNSA-------LPQEFATLTREL---------- 87
Cdd:COG4913 285 FAQRRLELLEAElEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrleqLEREIERLERELeererrrarl 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 88 -SLCREQLLEREEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSP--SGVSSEVEVLKALKSLFEHHkal 164
Cdd:COG4913 365 eALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRelRELEAEIASLERRKSNIPAR--- 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 165 DEKVRERLRAAL---------------------------------QRVSTL--EEQLAGAHQQVSALQQAAGVRdGAAEE 209
Cdd:COG4913 442 LLALRDALAEALgldeaelpfvgelievrpeeerwrgaiervlggFALTLLvpPEHYAAALRWVNRLHLRGRLV-YERVR 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 210 EGSVDLGLKRLWKDDVVRleelqelleKQNLELGQARERLATLTAAVAEL-----EEDLGTARRD-----LIKSeeRSSR 279
Cdd:COG4913 521 TGLPDPERPRLDPDSLAG---------KLDFKPHPFRAWLEAELGRRFDYvcvdsPEELRRHPRAitragQVKG--NGTR 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 280 HQRDLREALAQK----EDMEERIATLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLDVAE---- 351
Cdd:COG4913 590 HEKDDRRRIRSRyvlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASaere 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 352 -QKLQQTLRRAETLPEVEAELAQRIAALTKAEERhgnIEEHLRQLEGQLEEKNQELARVRQREkmnedhnKRLSDTVDRL 430
Cdd:COG4913 670 iAELEAELERLDASSDDLAALEEQLEELEAELEE---LEEELDELKGEIGRLEKELEQAEEEL-------DELQDRLEAA 739
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1926975374 431 LSESNERLQLHLKERMAALEEKNSLMQELESSQRQIEEQQNHKGRLSEEIEKLRQE 486
Cdd:COG4913 740 EDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
240-407 |
6.49e-11 |
|
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: 63.79 E-value: 6.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 240 LELGQARERLATLTAAVAELEEDLGTARRDLIKSEERSSRHQRDLREALAQKEDMEERIATLEKRylaaQREATSIHDLN 319
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ----LGNVRNNKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 320 DkLENELANKESLHRQCEEKARHLQELLDVAEQKLQqtlrraetlpEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQL 399
Cdd:COG1579 93 A-LQKEIESLKRRISDLEDEILELMERIEELEEELA----------ELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
....*...
gi 1926975374 400 EEKNQELA 407
Cdd:COG1579 162 EAEREELA 169
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
243-493 |
7.96e-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: 67.02 E-value: 7.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 243 GQARERLATLTAAVAELEEDLGTARRDLIKSEERSSRHQRDLREALAQKEDMEERIATLEkRYLAAQREatsihdlndKL 322
Cdd:TIGR02169 152 PVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKE---------KR 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 323 ENE----LANKESLHRQCEEKARHLQELldvaeqklqqtlrraetlpevEAELAQRIAALTKAEERHGNIEEHLRQLEGQ 398
Cdd:TIGR02169 222 EYEgyelLKEKEALERQKEAIERQLASL---------------------EEELEKLTEEISELEKRLEEIEQLLEELNKK 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 399 LEEKNQELARvRQREKMNEDHNKRLSdtVDRLLSESNERLQLHLKERMAALEEKNSLMQELESSQRQIEEQQNHKGRLSE 478
Cdd:TIGR02169 281 IKDLGEEEQL-RVKEKIGELEAEIAS--LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTE 357
|
250
....*....|....*
gi 1926975374 479 EIEKLRQEVDQLKGR 493
Cdd:TIGR02169 358 EYAELKEELEDLRAE 372
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
34-539 |
8.12e-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: 67.00 E-value: 8.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 34 LDEREKLLESLRESQETLVATQGRLQDALHERDQLQRHLNSalpqEFATLTRELSLCREQLLEREEEISELKAERNNTRL 113
Cdd:TIGR02168 346 LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS----KVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 114 LLEHLECLVSRHERS-LRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRE------RLRAALQRVSTLEEQL 186
Cdd:TIGR02168 422 EIEELLKKLEEAELKeLQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAaerelaQLQARLDSLERLQENL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 187 AGAHQQVSALQQAAGVRDG-----------AAEEEGSVDLGLKRLWKDDVVRLEELQELL---EKQN-------LELGQA 245
Cdd:TIGR02168 502 EGFSEGVKALLKNQSGLSGilgvlselisvDEGYEAAIEAALGGRLQAVVVENLNAAKKAiafLKQNelgrvtfLPLDSI 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 246 RERL--ATLTAAVAELEEDLGTARrDLIKSEER-----SSRHQR-----DLREALAQ--KEDMEERIATLE-----KRYL 306
Cdd:TIGR02168 582 KGTEiqGNDREILKNIEGFLGVAK-DLVKFDPKlrkalSYLLGGvlvvdDLDNALELakKLRPGYRIVTLDgdlvrPGGV 660
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 307 AAQREATSIHDLNDKlENELANKESLHRQCEEKARHLQELLDVAEQKLQQTLRRAETLPEVEAELAQRIAA----LTKAE 382
Cdd:TIGR02168 661 ITGGSAKTNSSILER-RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAlrkdLARLE 739
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 383 ERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRL-----------------LSESNERLQLHLKER 445
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELeaqieqlkeelkalreaLDELRAELTLLNEEA 819
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 446 MAALEEKNSLMQELESSQRQIEEQQNHKGRLSEEIEKLRQEVDQLKgrggpfVDGVHLRSHTGSAVDLRFSLSTAAPGLR 525
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE------ELIEELESELEALLNERASLEEALALLR 893
|
570
....*....|....
gi 1926975374 526 RRYSLREEPAKDWE 539
Cdd:TIGR02168 894 SELEELSEELRELE 907
|
|
| SAM_liprin-beta1,2_repeat1 |
cd09563 |
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
841-905 |
8.48e-11 |
|
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta protein contain three copies (repeats) of SAM domain. They may form heterodimers with liprins-alpha through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta is potentially able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.
Pssm-ID: 188962 Cd Length: 64 Bit Score: 58.78 E-value: 8.48e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1926975374 841 FAQWDGPTVVSWL-ELWVGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQ 905
Cdd:cd09563 1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
34-452 |
2.10e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.17 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 34 LDEREKLLESLRESQETLVATQGRLQDALHERDQLQRHL-NSALPQEFATLTRELSLCREQLLEREEEISELKAERNNTR 112
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLqLLPLYQELEALEAELAELPERLEELEERLEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 113 LLLEHLEclvsRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALQRVSTLEEQLAGAH-- 190
Cdd:COG4717 167 ELEAELA----ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAle 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 191 QQVSALQQAAGVRDGAAEEEGSVDLGLKRLWK-------------DDVVRLEELQELLEKQNLELGQARERLATLTAAVA 257
Cdd:COG4717 243 ERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELE 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 258 ELEEDLGTARRDLIKSEERSSRHQRDLREALAQKEDMEERIATL----EKRYLAAQREATSIHDLNDKLEnELANKESLH 333
Cdd:COG4717 323 ELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEeleqEIAALLAEAGVEDEEELRAALE-QAEEYQELK 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 334 RQCEEKARHLQELLDVAEQKLQQTLRRA--ETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLE--GQLEEKNQELARV 409
Cdd:COG4717 402 EELEELEEQLEELLGELEELLEALDEEEleEELEELEEELEELEEELEELREELAELEAELEQLEedGELAELLQELEEL 481
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1926975374 410 RQREKMNEDHNKRLsDTVDRLLSESNERLQlhlKERMAALEEK 452
Cdd:COG4717 482 KAELRELAEEWAAL-KLALELLEEAREEYR---EERLPPVLER 520
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
241-471 |
2.23e-10 |
|
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: 64.01 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 241 ELGQARERLATLTAAVAELEEDLGTARRDLIKSEERSSRHQRDLREALAQKEDMEERIATLEKRYLAAQREatsIHDLND 320
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE---LEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 321 KLENELANKESLHRQCEEKarhlqelLDVAEQKLQQTLRRAETLPEVEAELAQRIAALTKAEERhgnieehLRQLEGQLE 400
Cdd:COG4942 105 ELAELLRALYRLGRQPPLA-------LLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE-------LAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1926975374 401 EKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNSLMQELESSQRQIEEQQN 471
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
246-491 |
3.14e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.09 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 246 RERLATLTAAVAELEEDLGTARRDLIKSEERSSRHQRDLREALAQKEDMEERIATLEKRYLAAQREATSIHDLNDKLENE 325
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 326 LANKESLHRQCEEKARHLQELL---DVAEQKLQQTLRRaETLPEVEAELaqriaalTKAEERHGNIEEHLRQLEG----- 397
Cdd:TIGR02169 753 IENVKSELKELEARIEELEEDLhklEEALNDLEARLSH-SRIPEIQAEL-------SKLEEEVSRIEARLREIEQklnrl 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 398 -----QLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNSLMQELESSQRQIEEQQNH 472
Cdd:TIGR02169 825 tlekeYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK 904
|
250
....*....|....*....
gi 1926975374 473 KGRLSEEIEKLRQEVDQLK 491
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELK 923
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
58-400 |
5.49e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 5.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 58 LQDALHERDQLQRHLN-SALPQEFATLTRELSLCREQLLEREEEISELKAERNNTRLLLEHLECLVSRHERSLRMtVVKR 136
Cdd:COG1196 218 LKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE-LLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 137 QAQSPSGVSSEVEVLKALkslfehhkaldekvRERLRAALQRVSTLEEQLAGAHQQVSALQQAAgvrdgAAEEEgsvdlg 216
Cdd:COG1196 297 LARLEQDIARLEERRREL--------------EERLEELEEELAELEEELEELEEELEELEEEL-----EEAEE------ 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 217 lkrlwkddvvrleelqellekqnlELGQARERLATLTAAVAELEEDLGTARRDLIKSEERSSRHQRDLREALAQKEDMEE 296
Cdd:COG1196 352 ------------------------ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 297 RIATLEKRYLAAQREATSihdLNDKLENELANKESLHRQCEEKARHLQELLDVAEQKLQQTLRRAETLPEVEAELAQRIA 376
Cdd:COG1196 408 AEEALLERLERLEEELEE---LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
330 340
....*....|....*....|....
gi 1926975374 377 ALTKAEERHGNIEEHLRQLEGQLE 400
Cdd:COG1196 485 ELAEAAARLLLLLEAEADYEGFLE 508
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
241-493 |
6.66e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.93 E-value: 6.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 241 ELGQARERLATLTAAVAELEEDLGTARRDLIKSEERSSRHQRDLREALAQKEDMEERIATLEKRYLAAQREATSIHDLND 320
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 321 KLENELANKeslhrqcEEKARHLQELLDVAEQKLQQtlrraETLPEVEAELAQriaaltkaeerhgnIEEHLRQLEGQLE 400
Cdd:TIGR02169 762 ELEARIEEL-------EEDLHKLEEALNDLEARLSH-----SRIPEIQAELSK--------------LEEEVSRIEARLR 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 401 EKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNER------LQLHLKERMAALEEKNSLMQELESS----QRQIEEQQ 470
Cdd:TIGR02169 816 EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIekeienLNGKKEELEEELEELEAALRDLESRlgdlKKERDELE 895
|
250 260
....*....|....*....|...
gi 1926975374 471 NHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:TIGR02169 896 AQLRELERKIEELEAQIEKKRKR 918
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
274-493 |
1.21e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.16 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 274 EERSSRHQRDLREALAQKEDMEERIATLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLDVAEQK 353
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 354 LqqTLRRAEtLPEVEAELAQRIAALTKAEERHGNIEEHLRQleGQLEEKNQELARVRQREKMNEdhnKRLSDtVDRLLSE 433
Cdd:TIGR02169 753 I--ENVKSE-LKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIE---ARLRE-IEQKLNR 823
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 434 SNERLQLHLKERMAALEEKNSLMQELESSQRQIEEQQNHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:TIGR02169 824 LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
40-494 |
1.38e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 40 LLESLRESQETLVATQGRL-QDALHERDQLQRHLNSA--LPQEFATLTRELSlcreqllEREEEISELKAERNNTRLLLE 116
Cdd:COG4717 47 LLERLEKEADELFKPQGRKpELNLKELKELEEELKEAeeKEEEYAELQEELE-------ELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 117 HLECLVSRHErslrmtvvkrqaqspsgvsseveVLKALKSLFEHHKALDEKVrERLRAALQRVSTLEEQLAGAHQQVSAL 196
Cdd:COG4717 120 KLEKLLQLLP-----------------------LYQELEALEAELAELPERL-EELEERLEELRELEEELEELEAELAEL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 197 QQAAgvrdgaAEEEGSVDLGLKRLWKDDVVRLEELQELLEKQNLELGQARERLATLTAAVAELEEDLGTArrdliKSEER 276
Cdd:COG4717 176 QEEL------EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA-----ALEER 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 277 SSRHQRDLRE--ALAQKEDMEERIATLEKRYLAAQREATSIHDLndkLENELANKESLHRQCEEKARHLQELLDVAEQKL 354
Cdd:COG4717 245 LKEARLLLLIaaALLALLGLGGSLLSLILTIAGVLFLVLGLLAL---LFLLLAREKASLGKEAEELQALPALEELEEEEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 355 QQTLRRAETLPEVEAELAQR-IAALTKAEERHGNIEEHLRQLE-GQLEEKNQEL---ARVRQREKMNE--DHNKRLSDTV 427
Cdd:COG4717 322 EELLAALGLPPDLSPEELLElLDRIEELQELLREAEELEEELQlEELEQEIAALlaeAGVEDEEELRAalEQAEEYQELK 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1926975374 428 DRLlSESNERLQLHLKERMAALE--EKNSLMQELESSQRQIEEQQNHKGRLSEEIEKLRQEVDQLKGRG 494
Cdd:COG4717 402 EEL-EELEEQLEELLGELEELLEalDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDG 469
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
259-486 |
1.61e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.63 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 259 LEE-DLGTARRDLIKSEERSSRHQRDLREALAQKEDMEeRIATLEKRYLAAQREATSIHDLNDKLENELAnkeslhrqcE 337
Cdd:COG4913 218 LEEpDTFEAADALVEHFDDLERAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFA---------Q 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 338 EKARHLQELLDVAEQKLQQTLRRAETLPEVEAELAQRIAALTKAEERHG-----NIEEHLRQLEGQLEEKNQELARVRQR 412
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgdrleQLEREIERLERELEERERRRARLEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 413 EKM-------NEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNSLMQELESSQRQIEEQQNHKGRLSEEIEKLRQ 485
Cdd:COG4913 368 LAAlglplpaSAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
|
.
gi 1926975374 486 E 486
Cdd:COG4913 448 A 448
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
37-487 |
1.64e-09 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 62.55 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 37 REKLLESLRESQETLVATQGRLQDALHERDQLQRHLNsalpQEFATLTRELSlcrEQLLEREEEISELKAERNNTRlllE 116
Cdd:pfam12128 253 LESAELRLSHLHFGYKSDETLIASRQEERQETSAELN----QLLRTLDDQWK---EKRDELNGELSAADAAVAKDR---S 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 117 HLECLVSRHERSLRMTVVKR---QAQSPSgVSSEVEVL-KALKSLFEHHKALDEKVrERLRAAlqRVSTLEEQLAGAHQQ 192
Cdd:pfam12128 323 ELEALEDQHGAFLDADIETAaadQEQLPS-WQSELENLeERLKALTGKHQDVTAKY-NRRRSK--IKEQNNRDIAGIKDK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 193 VSALQQAAgVRdGAAEEEGSVDlGLKRLWKDDVVRLEELQELLEKQ-NLELGQARERLATLTAAVAELE------EDLGT 265
Cdd:pfam12128 399 LAKIREAR-DR-QLAVAEDDLQ-ALESELREQLEAGKLEFNEEEYRlKSRLGELKLRLNQATATPELLLqlenfdERIER 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 266 ARRDLIKSEERSSRHQRDLREALAQKEDMEERIATLEKRYLAAQREATSI--------HDLNDKLENE----------LA 327
Cdd:pfam12128 476 AREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELelqlfpqaGTLLHFLRKEapdweqsigkVI 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 328 NKESLHRQ----CEEKARHLQEL------LDVAEQKLQQTLRRAETLpevEAELAQRIAALTKAEERHGNIEEHLRQLEG 397
Cdd:pfam12128 556 SPELLHRTdldpEVWDGSVGGELnlygvkLDLKRIDVPEWAASEEEL---RERLDKAEEALQSAREKQAAAEEQLVQANG 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 398 QLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKErmaALEEKNSLMQELESSQRQI----EEQQNHK 473
Cdd:pfam12128 633 ELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDS---ANERLNSLEAQLKQLDKKHqawlEEQKEQK 709
|
490
....*....|....
gi 1926975374 474 GRLSEEIEKLRQEV 487
Cdd:pfam12128 710 REARTEKQAYWQVV 723
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
169-489 |
1.64e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.63 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 169 RERLRAALQRVSTLEEQLAGAHQQVSALQQAAGVRDGAAEEEGSVDlglKRLWKDDVVRLEELQELLEKQ--------NL 240
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLA---EYSWDEIDVASAEREIAELEAelerldasSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 241 ELGQARERLATLTAAVAELEEDLGTARRDLIKSEERSSRHQRDLREALAQKEDMEERIATLEKRYLAAQREATSIhdlnD 320
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALG----D 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 321 KLENELAnkeslhRQCEEKARHLQELLDVAEQKLQQTLRRA-ETLPEVEAELAQRIAALTKAEERHGNIE-----EHLRQ 394
Cdd:COG4913 762 AVERELR------ENLEERIDALRARLNRAEEELERAMRAFnREWPAETADLDADLESLPEYLALLDRLEedglpEYEER 835
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 395 LEGQLEEKN-QELARVRQREKMNEDHNKRLSDTVDRLLSESN----ERLQLHLKERMAA--LEEKNSLMQELESSQRQIE 467
Cdd:COG4913 836 FKELLNENSiEFVADLLSKLRRAIREIKERIDPLNDSLKRIPfgpgRYLRLEARPRPDPevREFRQELRAVTSGASLFDE 915
|
330 340
....*....|....*....|...
gi 1926975374 468 EQQNHKG-RLSEEIEKLRQEVDQ 489
Cdd:COG4913 916 ELSEARFaALKRLIERLRSEEEE 938
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
9-445 |
2.56e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 9 NEGDPLGPPHGADTDANFEQLmvnmlDEREKLLESLRESQETLVATQGRLQDALHERDQLQRHLNSA------------- 75
Cdd:COG4717 53 KEADELFKPQGRKPELNLKEL-----KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELreeleklekllql 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 76 --LPQEFATLTRELSLCREQLLEREEEISELKAERNNTRLLLEHLEclvsRHERSLRMTVVKRQAQSPSGVSSEVEVLKA 153
Cdd:COG4717 128 lpLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELA----ELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 154 LKSLFEHHKALDEKVRERLRAALQRVSTLEEQLAGAH--QQVSALQQAAGVRDGAAEEEGSVDLGLKRLWK--------- 222
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAAleERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvl 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 223 ----DDVVRLEELQELLEKQNLELGQARERLATLTAAVAELEEDLGTARRDLIKSEERSSRHQRDLREALAQKEDMEERI 298
Cdd:COG4717 284 gllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 299 ATL----EKRYLAAQREATSIHDLNDKLEnELANKESLHRQCEEKARHLQELLDVAEQKLQQTlrraeTLPEVEAELAQR 374
Cdd:COG4717 364 QLEeleqEIAALLAEAGVEDEEELRAALE-QAEEYQELKEELEELEEQLEELLGELEELLEAL-----DEEELEEELEEL 437
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1926975374 375 IAALTKAEERHGNIEEHLRQLEGQLE--EKNQELARVRQREKMNEDHNKRLSD--TVDRLLSESNERLQLHLKER 445
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEqlEEDGELAELLQELEELKAELRELAEewAALKLALELLEEAREEYREE 512
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
166-497 |
4.63e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 61.13 E-value: 4.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 166 EKVRERLRAALQRVSTLEEQLAGAHQQVSALQQAAGVRDGA--AEEEGSVDLGLKRLWKDDVVRLEELQELLEKQ-NLEL 242
Cdd:PRK04863 379 EENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAvqALERAKQLCGLPDLTADNAEDWLEEFQAKEQEaTEEL 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 243 GQARERLATLTAAVAELEEDLGTARRdlIKSEERSSRHQRDLREALAQKEdmeeriatlEKRYLAAQREAtsihdlndkL 322
Cdd:PRK04863 459 LSLEQKLSVAQAAHSQFEQAYQLVRK--IAGEVSRSEAWDVARELLRRLR---------EQRHLAEQLQQ---------L 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 323 ENELANKESLHRQceekARHLQELLDVAEQKLQQTLRRAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEK 402
Cdd:PRK04863 519 RMRLSELEQRLRQ----QQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQAR 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 403 NQELARVRQREkmnedhnkrlsdtvdRLLSESNERLQLHLKErmaALEEKNSLMQELESSQRQIEEQQNHKGRLSEEIEK 482
Cdd:PRK04863 595 IQRLAARAPAW---------------LAAQDALARLREQSGE---EFEDSQDVTEYMQQLLERERELTVERDELAARKQA 656
|
330
....*....|....*
gi 1926975374 483 LRQEVDQLKGRGGPF 497
Cdd:PRK04863 657 LDEEIERLSQPGGSE 671
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
177-485 |
4.77e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.82 E-value: 4.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 177 QRVSTLEEQLAGAHQQVSALQQAAGVRDGAAEEEGSVDLGLKRlwKDDVVRLEELQELlekqnlELGQARERLATLTAAV 256
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEER--REDLEELIAERRE------TIEEKRERAEELRERA 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 257 AELEEDLGTARRDLIKSEERSSRHQRDLREALAQKEDMEERIATLEKrylaaqreatsIHDLNDKLENELANKESLhrqc 336
Cdd:PRK02224 547 AELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER-----------IRTLLAAIADAEDEIERL---- 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 337 EEKARHLQELLDVAEQKLQQtlrRAETLPEVEAELAQriAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMN 416
Cdd:PRK02224 612 REKREALAELNDERRERLAE---KRERKRELEAEFDE--ARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAV 686
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1926975374 417 EDHNKRLSDtvdrllsesnerlqlhLKERMAALEEKnslMQELESSQRQIEEQQNHKGRLSEEiekLRQ 485
Cdd:PRK02224 687 ENELEELEE----------------LRERREALENR---VEALEALYDEAEELESMYGDLRAE---LRQ 733
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
21-493 |
5.23e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.70 E-value: 5.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 21 DTDANFEQLMVNM--LDEREKLLESLRESQETL---VATQGRLQDALHERDQLQRhLNSALPQEFATltRELSLCREQLL 95
Cdd:COG4913 222 DTFEAADALVEHFddLERAHEALEDAREQIELLepiRELAERYAAARERLAELEY-LRAALRLWFAQ--RRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 96 EREEEISELKAERNNTRLLLEHLECLVSRHERSLRmtvvkrqaqspsgvSSEVEVLKALKSLFEHHKALDEKVRERLRAA 175
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEAQIR--------------GNGGDRLEQLEREIERLERELEERERRRARL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 176 LQRVSTLEEQLAGAHQQVSALQ-QAAGVRDGAAEEEGSVDlglKRLWKDDVVRLEELQELLEKQN-------------LE 241
Cdd:COG4913 365 EALLAALGLPLPASAEEFAALRaEAAALLEALEEELEALE---EALAEAEAALRDLRRELRELEAeiaslerrksnipAR 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 242 LGQARERLATLTAA-------VAEL----EED----------LGTARRDLIKSEERSSR-----HQRDLREAL----AQK 291
Cdd:COG4913 442 LLALRDALAEALGLdeaelpfVGELievrPEEerwrgaiervLGGFALTLLVPPEHYAAalrwvNRLHLRGRLvyerVRT 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 292 EDMEERIATLEKRYLAAQREaTSIHDLNDKLENELANKESLHR-------QCEEKA------------------RHL--- 343
Cdd:COG4913 522 GLPDPERPRLDPDSLAGKLD-FKPHPFRAWLEAELGRRFDYVCvdspeelRRHPRAitragqvkgngtrhekddRRRirs 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 344 --------QELLDVAEQKLQQTLRRAETLPEVEAELAQRIAALTKAEERHGNIEEH------LRQLEGQLEEKNQELARv 409
Cdd:COG4913 601 ryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYswdeidVASAEREIAELEAELER- 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 410 rqrekmnedhnkrlsdtvdrlLSESNERLQlHLKERMAALEEknslmqELESSQRQIEEQQNHKGRLSEEIEKLRQEVDQ 489
Cdd:COG4913 680 ---------------------LDASSDDLA-ALEEQLEELEA------ELEELEEELDELKGEIGRLEKELEQAEEELDE 731
|
....
gi 1926975374 490 LKGR 493
Cdd:COG4913 732 LQDR 735
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
36-436 |
6.02e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.85 E-value: 6.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 36 EREKLLESLRESQETLVATQGRLQDALHERDQLQRHLNSALpqEFATLTRELslcreqlleREEEISELKAERNNTRLLL 115
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE--RYQALLKEK---------REYEGYELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 116 EHLECLVSRHERSLRMTVVKRQAQspsgvssEVEVLKALKSLFEHHKALDEKVRERLRAALQRVSTLEEQLAGAHQQVSA 195
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISEL-------EKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 196 LQQAagVRDGAAEE-EGSVDLGLKRLWKDDVVRleelqellekqnlELGQARERLATLTAAVAELEEDLGTARRDLIKSE 274
Cdd:TIGR02169 313 KERE--LEDAEERLaKLEAEIDKLLAEIEELER-------------EIEEERKRRDKLTEEYAELKEELEDLRAELEEVD 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 275 ERSSRHQRDLREALAQKEDMEERIATLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLDVAEQKL 354
Cdd:TIGR02169 378 KEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 355 QQTlrraetlpeveaelaqrIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDrLLSES 434
Cdd:TIGR02169 458 EQL-----------------AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEE-VLKAS 519
|
..
gi 1926975374 435 NE 436
Cdd:TIGR02169 520 IQ 521
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
342-493 |
1.03e-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: 57.24 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 342 HLQELLDVAE--QKLQQTLRRAETLP----EVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRqrEKM 415
Cdd:COG1579 5 DLRALLDLQEldSELDRLEHRLKELPaelaELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE--EQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 416 NEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNSLMQELESSQRQIEEQQNH----KGRLSEEIEKLRQEVDQLK 491
Cdd:COG1579 83 GNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEleekKAELDEELAELEAELEELE 162
|
..
gi 1926975374 492 GR 493
Cdd:COG1579 163 AE 164
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
32-491 |
1.06e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 59.98 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 32 NMLDEREKLLESLRESQETLVATQgRLQDALHERDQLQRHLNSALPQEfATLTRELSlcreqllereeEISELKAERNNT 111
Cdd:TIGR00618 223 VLEKELKHLREALQQTQQSHAYLT-QKREAQEEQLKKQQLLKQLRARI-EELRAQEA-----------VLEETQERINRA 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 112 RllleHLECLVsrhERSLRMTVVKRQAQspsgvssevEVLKALKSlfehHKALDEKVRERLRAALQRVSTLEEQlagaHQ 191
Cdd:TIGR00618 290 R----KAAPLA---AHIKAVTQIEQQAQ---------RIHTELQS----KMRSRAKLLMKRAAHVKQQSSIEEQ----RR 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 192 QVSALQQAAGVRDGAAEEEgsvdlglkRLWKDDVVRLEELQELLEKQNLELGQARERLATLTAAVAELEEDLGT------ 265
Cdd:TIGR00618 346 LLQTLHSQEIHIRDAHEVA--------TSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATidtrts 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 266 ARRDLIKSEERSSRHQRDLREALAQKEDMEERIATLEKRYLAAQREATSIHdlnDKLENELANKESLHRQCEE-KARHLQ 344
Cdd:TIGR00618 418 AFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSL---KEREQQLQTKEQIHLQETRkKAVVLA 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 345 ELLDVAEQklQQTLRRAETLPEVEAELAQRIAALT----KAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHN 420
Cdd:TIGR00618 495 RLLELQEE--PCPLCGSCIHPNPARQDIDNPGPLTrrmqRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSF 572
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1926975374 421 KRLSDTVDRLLSESN---ERLQLHLKERMAALEEKNSLMQELESSQRQIEEQQnHKGRLSEEIEKLRQEVDQLK 491
Cdd:TIGR00618 573 SILTQCDNRSKEDIPnlqNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQ-DLQDVRLHLQQCSQELALKL 645
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
841-907 |
1.41e-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: 52.68 E-value: 1.41e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1926975374 841 FAQWDGPTVVSWLELWvGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEM 907
Cdd:smart00454 1 VSQWSPESVADWLESI-GLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
142-492 |
1.41e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 142 SGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALQRVSTLEEQLAGAHQQVSALQQAAGvRDGAAEEEGSVDLGLKRLW 221
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK-ELKELKEKAEEYIKLSEFY 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 222 KDDVVRleelqelleKQNLElgqarERLATLTAAVAELEEDLgtarrdliksEERSSRHQRdLREALAQKEDMEERIATL 301
Cdd:PRK03918 303 EEYLDE---------LREIE-----KRLSRLEEEINGIEERI----------KELEEKEER-LEELKKKLKELEKRLEEL 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 302 EKRylaaqreatsiHDLNDKLENELANKESLhrqceeKARHLQELLDVAEQKLQQTLRRAETLPEVEAELAQRIAAL-TK 380
Cdd:PRK03918 358 EER-----------HELYEEAKAKKEELERL------KKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELkKE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 381 AEERHGNIEEhLRQLEGQ----------------LEEKNQELARVRQREKMNEDHNKRLSD---TVDRLLSESNERLQLH 441
Cdd:PRK03918 421 IKELKKAIEE-LKKAKGKcpvcgrelteehrkelLEEYTAELKRIEKELKEIEEKERKLRKelrELEKVLKKESELIKLK 499
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1926975374 442 -LKERMAALEEKNSL--MQELESSQRQIEEQQNHKGRLSEEIEKLRQEVDQLKG 492
Cdd:PRK03918 500 eLAEQLKELEEKLKKynLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE 553
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
966-1021 |
1.47e-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: 52.30 E-value: 1.47e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1926975374 966 EWLPSLGLPQYRSHFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1021
Cdd:smart00454 11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
261-491 |
1.80e-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: 58.88 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 261 EDLGTARRDLIKSEERSsrhQRDLREALAQKEDMEERIATLEKRYLAAQREATSIHDLNDK---LE---NELANKES-LH 333
Cdd:TIGR04523 155 EKLNNKYNDLKKQKEEL---ENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKnksLEsqiSELKKQNNqLK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 334 RQCEEKARHLQEL---LDVAEQKLQQTLrraETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLE----EKNQEL 406
Cdd:TIGR04523 232 DNIEKKQQEINEKtteISNTQTQLNQLK---DEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdlnnQKEQDW 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 407 AR-----VRQREKMNEDHNKRLSDTvDRLLSESNERLQLHLKERMAALEEKNSLMQELESSQRQIEEQQNHKGRLSEEIE 481
Cdd:TIGR04523 309 NKelkseLKNQEKKLEEIQNQISQN-NKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK 387
|
250
....*....|
gi 1926975374 482 KLRQEVDQLK 491
Cdd:TIGR04523 388 NLESQINDLE 397
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
34-495 |
1.99e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.90 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 34 LDEREKLLESLRESQETLVATQGRLQDALHERDQLQRHLN-------------SALPQEFATLTRELSLCREQLLEREEE 100
Cdd:PRK02224 215 LAELDEEIERYEEQREQARETRDEADEVLEEHEERREELEtleaeiedlretiAETEREREELAEEVRDLRERLEELEEE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 101 ISELKAERNNTRL----LLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKAL------KSLFEHHKALD---EK 167
Cdd:PRK02224 295 RDDLLAEAGLDDAdaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADdleeraEELREEAAELEselEE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 168 VRERLRAALQRVSTLEEQLAGAHQQV-----------SALQQAAGVRDGAAEEEGSVDLGLKRLwkDDVVRLEELQELLE 236
Cdd:PRK02224 375 AREAVEDRREEIEELEEEIEELRERFgdapvdlgnaeDFLEELREERDELREREAELEATLRTA--RERVEEAEALLEAG 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 237 K-----QNLE-------LGQARERLATLTAAVAELEEDLgtarrdliksEERSSRHQR--DLREALAQKEDMEERIATLE 302
Cdd:PRK02224 453 KcpecgQPVEgsphvetIEEDRERVEELEAELEDLEEEV----------EEVEERLERaeDLVEAEDRIERLEERREDLE 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 303 KRylAAQREATsIHDLNDKLENELANKESLHRQCEEKARHLQElldvAEQKLQQTLRRAETLPEVEAELAQRIAALTKAE 382
Cdd:PRK02224 523 EL--IAERRET-IEEKRERAEELRERAAELEAEAEEKREAAAE----AEEEAEEAREEVAELNSKLAELKERIESLERIR 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 383 ERHGNIEEHLRQLEgQLEEKNQELArvrqreKMNEDHNKRLSDTVDRllsesneRLQLHLKERMAALEEKNSLMQELESS 462
Cdd:PRK02224 596 TLLAAIADAEDEIE-RLREKREALA------ELNDERRERLAEKRER-------KRELEAEFDEARIEEAREDKERAEEY 661
|
490 500 510
....*....|....*....|....*....|...
gi 1926975374 463 QRQIEeqqnhkgrlsEEIEKLRQEVDQLKGRGG 495
Cdd:PRK02224 662 LEQVE----------EKLDELREERDDLQAEIG 684
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
126-490 |
1.99e-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: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 126 ERSLRMTVVKRQAQSPSGVS-SEVEVLKALKSLFEHHKALDEKVRERLRAALQRVSTLEEQLAGAHQQVSALQQAAGVRD 204
Cdd:TIGR02169 650 EKSGAMTGGSRAPRGGILFSrSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLE 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 205 GAAEEEGSVDLGLKRLWKDDVVRLEELQELLEKQNLELGQARERLATLTAAVAELEEDLGTARRDLIKSEERSSRHQR-- 282
Cdd:TIGR02169 730 QEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVsr 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 283 ----------DLREALAQKEDMEERIATLEK--RYLAAQREA--TSIHDLN---DKLENELANKESLHRQCEEKARHLQE 345
Cdd:TIGR02169 810 iearlreieqKLNRLTLEKEYLEKEIQELQEqrIDLKEQIKSieKEIENLNgkkEELEEELEELEAALRDLESRLGDLKK 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 346 LLDVAEQKLQQTLRRAETLpEVEAELAqriaaltkaeerhgniEEHLRQLEGQLEEKNQELARVrqrekmnEDHNKRLSD 425
Cdd:TIGR02169 890 ERDELEAQLRELERKIEEL-EAQIEKK----------------RKRLSELKAKLEALEEELSEI-------EDPKGEDEE 945
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1926975374 426 TVDRLLSEsnERLQLHLK---ERMAALEEKNSL-MQELESSQRQIEEQQNHKGRLSEEIEKLRQEVDQL 490
Cdd:TIGR02169 946 IPEEELSL--EDVQAELQrveEEIRALEPVNMLaIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
146-476 |
3.45e-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: 57.83 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 146 SEVEVLKALKSLFEHHKALDEKVRERL--RAALQRVSTLEEQLAGAHQQVSALQQAAGVRDGAAEEEGSVDLGLKRLWKD 223
Cdd:pfam17380 266 TENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 224 DVVRLEELQELLEKQNLElgQAR-ERLATLTAAVAELE--------------EDLGTARRDLIKSEERssrhQRDLREal 288
Cdd:pfam17380 346 RERELERIRQEERKRELE--RIRqEEIAMEISRMRELErlqmerqqknervrQELEAARKVKILEEER----QRKIQQ-- 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 289 aQKEDMEERiatlekrylaaqreatsihdlndKLENELANKESLHRQCEEKARHLqELLDVAEQKLQQTLRRaetLPEVE 368
Cdd:pfam17380 418 -QKVEMEQI-----------------------RAEQEEARQREVRRLEEERAREM-ERVRLEEQERQQQVER---LRQQE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 369 AELAQRIAALTKAEERHGNIEEHLRQ-LEGQLEEKNQELARVRQREKM----NEDHNKRLSDTVDRLLSESNERLQLHLK 443
Cdd:pfam17380 470 EERKRKKLELEKEKRDRKRAEEQRRKiLEKELEERKQAMIEEERKRKLlekeMEERQKAIYEEERRREAEEERRKQQEME 549
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1926975374 444 ER-------MAALEEKNSL--MQELESSQRQIEEQQNHKGRL 476
Cdd:pfam17380 550 ERrriqeqmRKATEERSRLeaMEREREMMRQIVESEKARAEY 591
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
244-491 |
4.80e-08 |
|
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: 57.67 E-value: 4.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 244 QARERLATLTAAVAELEEDLGTARRDLIKSEERSSRHQRDLREaLAQKEDMEERIATLEKRYLAAQREATSIHDLNDK-- 321
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQL-KEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEqe 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 322 ----------LENELANKESLHRQCEEKARHLQELLDVAEQKLQQTLRRAETLPEVEAELAQRIaaLTKAEERHGNIEEH 391
Cdd:pfam02463 252 eiesskqeieKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEK--LKESEKEKKKAEKE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 392 LRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERmaalEEKNSLMQELESSQRQIEEQQN 471
Cdd:pfam02463 330 LKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES----ERLSSAAKLKEEELELKSEEEK 405
|
250 260
....*....|....*....|
gi 1926975374 472 hkgRLSEEIEKLRQEVDQLK 491
Cdd:pfam02463 406 ---EAQLLLELARQLEDLLK 422
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
27-492 |
1.06e-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: 56.52 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 27 EQLMVNMLDEREKLLE-SLRESQETLVATQGRL-QDALHERDQLQ-RHLNSALPQEFATLTRELSLCREQLLEREEEISE 103
Cdd:TIGR00618 408 EQATIDTRTSAFRDLQgQLAHAKKQQELQQRYAeLCAAAITCTAQcEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETR 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 104 LKAERNNTRLLLEHLECLVsrhERSLRMTVVKRQAQSPSGVSSEvEVLKALKSLFEHHKALdEKVRERLRAALQRVSTLE 183
Cdd:TIGR00618 488 KKAVVLARLLELQEEPCPL---CGSCIHPNPARQDIDNPGPLTR-RMQRGEQTYAQLETSE-EDVYHQLTSERKQRASLK 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 184 EQLAGAHQQVSALQQ--------AAGVRDgaaEEEGSVDLGLKRLWKDDVVRLEELQELLEKQ--------NLELGQARE 247
Cdd:TIGR00618 563 EQMQEIQQSFSILTQcdnrskedIPNLQN---ITVRLQDLTEKLSEAEDMLACEQHALLRKLQpeqdlqdvRLHLQQCSQ 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 248 RLATLTAAVAELEEDLGTARrdliksEERSSRHQRDLREALAQKEDMEERIATLEKRYLAAQRE--ATSIHDLNDKLENE 325
Cdd:TIGR00618 640 ELALKLTALHALQLTLTQER------VREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEmlAQCQTLLRELETHI 713
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 326 LANKESLHRQCEEKARHLQELL--DVAEQKLQQTLRRA--ETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQ--- 398
Cdd:TIGR00618 714 EEYDREFNEIENASSSLGSDLAarEDALNQSLKELMHQarTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFnrl 793
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 399 LEEKNQELArvrqrEKMNEDHNKRLSDTVDRLLSEsnERLQLHLKERMAALEEKNSLMQELESSQRQIEEQQNHKGRLSE 478
Cdd:TIGR00618 794 REEDTHLLK-----TLEAEIGQEIPSDEDILNLQC--ETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQ 866
|
490
....*....|....
gi 1926975374 479 EIEKLRQEVDQLKG 492
Cdd:TIGR00618 867 EQAKIIQLSDKLNG 880
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
134-451 |
1.57e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 134 VKRQAQSPSGVSSEV-EVLKALKSLFEHHKALDEKVRERLRAALQRVSTLEEQLAGAHQQVSALQQAAGVRDgaAEEEGS 212
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAkKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKK--AEEKKK 1565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 213 VDLglKRLWKDDvvRLEELQELLEKQNLELGQARERLATLTAAVAELEEDLGTARRDLIKSEE-RSSRHQRDLREALAQK 291
Cdd:PTZ00121 1566 AEE--AKKAEED--KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElKKAEEEKKKVEQLKKK 1641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 292 EDMEERIATLEKRylAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLDVAEQKlqqtlRRAETLPEVEAEL 371
Cdd:PTZ00121 1642 EAEEKKKAEELKK--AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA-----KKAEELKKKEAEE 1714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 372 AQRIAALTKAEERHGNIEEHLRQlEGQLEEKNQELARVRQREKmnedhNKrlsdtVDRLLSESNERLQLHLKERMAALEE 451
Cdd:PTZ00121 1715 KKKAEELKKAEEENKIKAEEAKK-EAEEDKKKAEEAKKDEEEK-----KK-----IAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
284-451 |
1.60e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.78 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 284 LREALAQKEDMEERIATLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLDVAeqklqQTLRRAET 363
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-----RNNKEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 364 LpevEAELAQriaaltkAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLK 443
Cdd:COG1579 94 L---QKEIES-------LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
....*...
gi 1926975374 444 ERMAALEE 451
Cdd:COG1579 164 EREELAAK 171
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
283-470 |
2.06e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 283 DLREALAQKEDMEERIATLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLDVAEQKLQQTLRRA- 361
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALy 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 362 ---ETLPEVEA--------ELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRL 430
Cdd:COG3883 97 rsgGSVSYLDVllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1926975374 431 LSESNERLQLHLKERMAALEEKNSLMQELESSQRQIEEQQ 470
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
233-437 |
2.82e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 233 ELLEKQNLELGQARERLATLTAAVAELEEDLGTARRDLIKSEERSSRHQRDLREALAQKEDMEERIATLEKRY----LAA 308
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELaellRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 309 QREAT--------SIHDLNDkLENELANKESLHRQCEEKARHLQELLDVAEQKLQQTLRRAETLPEVEAELAQRIAALTK 380
Cdd:COG4942 114 YRLGRqpplalllSPEDFLD-AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEA 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1926975374 381 AEERHgniEEHLRQLEGQLEEKNQELARVRQREkmnedhnKRLSDTVDRLLSESNER 437
Cdd:COG4942 193 LKAER---QKLLARLEKELAELAAELAELQQEA-------EELEALIARLEAEAAAA 239
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
376-493 |
2.91e-07 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 52.52 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 376 AALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLlsesNERLQLHLK---ERMA--ALE 450
Cdd:COG1842 16 ALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKW----EEKARLALEkgrEDLAreALE 91
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1926975374 451 EKNSLMQELESSQRQIEEQQNHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:COG1842 92 RKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAK 134
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
246-490 |
3.24e-07 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 54.58 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 246 RERLATLTAAVAELEEDLGTARRDLIKSEERSSRHQRdlREALAQKEDMEERIATLEKRYLAAQREATSIHDLND----- 320
Cdd:COG5185 299 AEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETE--TGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVElskss 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 321 -KLENELANKESLHRQCEEKARHLQELLDVAEQKLQQTLRRAEtlpeveaelaqriaalTKAEERHGNIEEHLRQLEgQL 399
Cdd:COG5185 377 eELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAAD----------------RQIEELQRQIEQATSSNE-EV 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 400 EEKNQELAR--VRQREKMNEDHNKRLSDTVDRLLSESNERlqlhlkermaaLEEKNSLMQELESSQRQI-EEQQNHKGRL 476
Cdd:COG5185 440 SKLLNELISelNKVMREADEESQSRLEEAYDEINRSVRSK-----------KEDLNEELTQIESRVSTLkATLEKLRAKL 508
|
250
....*....|....
gi 1926975374 477 SEEIEKLRQEVDQL 490
Cdd:COG5185 509 ERQLEGVRSKLDQV 522
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
136-486 |
3.38e-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: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 136 RQAQSPSGVSSEVEVLKALKSLFEHHKAL----------DEKVRERLRAALQRvstLEEQLAGAHQQVSALQ-QAAGVRD 204
Cdd:pfam01576 160 RISEFTSNLAEEEEKAKSLSKLKNKHEAMisdleerlkkEEKGRQELEKAKRK---LEGESTDLQEQIAELQaQIAELRA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 205 GAAEEEGSVDLGLKRLwkddvvrleelqellEKQNLELGQARERLATLTAAVAELEEDLGTARrdliKSEERSSRHQRDL 284
Cdd:pfam01576 237 QLAKKEEELQAALARL---------------EEETAQKNNALKKIRELEAQISELQEDLESER----AARNKAEKQRRDL 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 285 REAL-AQKEDMEERI-ATLEKRYLAAQREaTSIHDLNDKLENELANKESlhRQCEEKARHLQELLDVAEQkLQQTLRRAE 362
Cdd:pfam01576 298 GEELeALKTELEDTLdTTAAQQELRSKRE-QEVTELKKALEEETRSHEA--QLQEMRQKHTQALEELTEQ-LEQAKRNKA 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 363 TLPE----VEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEE---KNQELARVRQR--EKMN----------------E 417
Cdd:pfam01576 374 NLEKakqaLESENAELQAELRTLQQAKQDSEHKRKKLEGQLQElqaRLSESERQRAElaEKLSklqselesvssllneaE 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 418 DHNKRLSDTVDRL---LSESNERLQ------LHLKERMAALE-EKNSLMQELE---SSQRQIEEQ-QNHKGRLSEEIEKL 483
Cdd:pfam01576 454 GKNIKLSKDVSSLesqLQDTQELLQeetrqkLNLSTRLRQLEdERNSLQEQLEeeeEAKRNVERQlSTLQAQLSDMKKKL 533
|
...
gi 1926975374 484 RQE 486
Cdd:pfam01576 534 EED 536
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
31-489 |
3.48e-07 |
|
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: 54.73 E-value: 3.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 31 VNMLDEREKLL-ESLRESQETLVATQGRLQD-------------ALHERDQLQRHLNSALPQEFATLTRELSlcrEQLLE 96
Cdd:pfam05483 270 ANQLEEKTKLQdENLKELIEKKDHLTKELEDikmslqrsmstqkALEEDLQIATKTICQLTEEKEAQMEELN---KAKAA 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 97 REEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgvsSEVEVLKALKS-----LFEHHKALDEKvrER 171
Cdd:pfam05483 347 HSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS-----SELEEMTKFKNnkeveLEELKKILAED--EK 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 172 LRAALQRVSTLEEQLAGAHQQVSALQQAAGVRDGAAEEEGSVDLGLKRLWKDDVVRLEELQELLEKQNLELGQARERLAT 251
Cdd:pfam05483 420 LLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLL 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 252 LTAAVAELEEDLGTARRdlikseerssRHQRDLREALAQKEDMEERIATLEKRYLaaqreatsihdlndKLENELankES 331
Cdd:pfam05483 500 ENKELTQEASDMTLELK----------KHQEDIINCKKQEERMLKQIENLEEKEM--------------NLRDEL---ES 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 332 LHRQCEEKARHLQELLDVAEqklqqtlrraETLPEVEAELaqriaalTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQ 411
Cdd:pfam05483 553 VREEFIQKGDEVKCKLDKSE----------ENARSIEYEV-------LKKEKQMKILENKCNNLKKQIENKNKNIEELHQ 615
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1926975374 412 REKMNEDHNKRLSDTVDRLLSESNeRLQLHLKERMAALEEKnslmqeLESSQRQIEEQQNHKGRLSEEIEKLRQEVDQ 489
Cdd:pfam05483 616 ENKALKKKGSAENKQLNAYEIKVN-KLELELASAKQKFEEI------IDNYQKEIEDKKISEEKLLEEVEKAKAIADE 686
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
163-414 |
5.12e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.57 E-value: 5.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 163 ALDEKVRERLRAALQRVSTLEEQLAGAHQQVSALQQAAgvrDGAAEEEGSVD--LGLKRLWKDDVVRLEELQELLEKQNL 240
Cdd:COG3096 829 AFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQL---DQLKEQLQLLNklLPQANLLADETLADRLEELREELDAA 905
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 241 ElgQARERLATLTAAVAELEEDLGTARRDLIKSEERssrhQRDLREALAQKEDMEERIATLEkrYLAAQREATSIHD--- 317
Cdd:COG3096 906 Q--EAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQL----QADYLQAKEQQRRLKQQIFALS--EVVQRRPHFSYEDavg 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 318 -------LNDKLENELANKESLHRQCEEKARHLQELLDVAEQKLQQTLRRAETLPEVEAELAQRIAAL-----TKAEERh 385
Cdd:COG3096 978 llgensdLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELgvqadAEAEER- 1056
|
250 260
....*....|....*....|....*....
gi 1926975374 386 gnIEEHLRQLEGQLeekNQELARVRQREK 414
Cdd:COG3096 1057 --ARIRRDELHEEL---SQNRSRRSQLEK 1080
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
258-490 |
5.19e-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: 54.26 E-value: 5.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 258 ELEEDLGTARRDL--IKSEERSSRHQR-DLREALAQKEDMEERIATLEKRYLAAQREATSIHD----LNDKL---ENELA 327
Cdd:TIGR04523 170 ELENELNLLEKEKlnIQKNIDKIKNKLlKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDniekKQQEInekTTEIS 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 328 NKESLHRQCEEKARHLQELLDVAEQKLQQTLRRAETLP----EVEAELA----QRIAALTKA-EERHGNIEEHLRQLEGQ 398
Cdd:TIGR04523 250 NTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEkqlnQLKSEISdlnnQKEQDWNKElKSELKNQEKKLEEIQNQ 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 399 LEEKNQELARVRQ------REKMNEDHNKRlsdTVDRLLSESNERLQLHLKERMAALEEKNSLMQELESSQRQIEEQQNH 472
Cdd:TIGR04523 330 ISQNNKIISQLNEqisqlkKELTNSESENS---EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKL 406
|
250
....*....|....*...
gi 1926975374 473 KGRLSEEIEKLRQEVDQL 490
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELL 424
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
241-493 |
7.49e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.98 E-value: 7.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 241 ELGQARERLATLTAAVAELEEDLGTARRDLIKSEERSSRHQRDLREALAQKEDMEERIATLEKRYLAAQREATSIHDLND 320
Cdd:COG4372 60 ELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 321 KLENELANKESLHRQCEEKARHLQELLDVAEQKLQQTLrraetlpevEAELAQRIAALTKAEERHGNIEEHLRQLEGQLE 400
Cdd:COG4372 140 ELQSEIAEREEELKELEEQLESLQEELAALEQELQALS---------EAEAEQALDELLKEANRNAEKEEELAEAEKLIE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 401 EKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNSLMQELESSQRQIEEQQNHKGRLSEEI 480
Cdd:COG4372 211 SLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290
|
250
....*....|...
gi 1926975374 481 EKLRQEVDQLKGR 493
Cdd:COG4372 291 AALELKLLALLLN 303
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
260-482 |
1.01e-06 |
|
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: 53.20 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 260 EEDLGTARRDLIKSEERssrhQRDLREALAQKEDMEERIATL----EKRYLAAQREATSIHDLNDKLENELANKESLHRQ 335
Cdd:pfam17380 298 QERLRQEKEEKAREVER----RRKLEEAEKARQAEMDRQAAIyaeqERMAMERERELERIRQEERKRELERIRQEEIAME 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 336 CEeKARHLQELLDVAEQK---LQQTLRRAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQL--EEKNQELARVR 410
Cdd:pfam17380 374 IS-RMRELERLQMERQQKnerVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRleEERAREMERVR 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1926975374 411 QREKMNEDHNKRLsdtvdRLLSESNERLQLHL---KERMAALEEKNS--LMQELESSQRQIEEQQNHKGRLSEEIEK 482
Cdd:pfam17380 453 LEEQERQQQVERL-----RQQEEERKRKKLELekeKRDRKRAEEQRRkiLEKELEERKQAMIEEERKRKLLEKEMEE 524
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
334-491 |
1.42e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.21 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 334 RQCEEKARHLQELLDVAEQKLQQTLRRAEtlpEVEAELAQRIAALTKAEERhgnieehLRQLEGQLEEKNQELARVRQRE 413
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELE---QLEEELEQARSELEQLEEE-------LEELNEQLQAAQAELAQAQEEL 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1926975374 414 KMNEDHNKRLSDTVDRLLsesnerlqlhlKERMAALEEKNSLMQELESSQRQIEEQQNHKGRLSEEIEKLRQEVDQLK 491
Cdd:COG4372 104 ESLQEEAEELQEELEELQ-----------KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALE 170
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
33-380 |
1.75e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.76 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 33 MLDEREKLLESLRESQETLVATQGRLQDALHERDQLQRHLNsALPQEFATLTRELSLCREQLLEREEEISELKAErnntr 112
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE-QLEQEEEKLKERLEELEEDLSSLEQEIENVKSE----- 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 113 llLEHLECLVSRHERSLrmtvvkrqaqspsgvsseVEVLKALKSLFEH--HKALDEKVRErLRAALQRVSTLEEQLAGAH 190
Cdd:TIGR02169 760 --LKELEARIEELEEDL------------------HKLEEALNDLEARlsHSRIPEIQAE-LSKLEEEVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 191 QQVSALQQaagvRDGAAEEEGSVDLGLKRLWKDdvvRLEELQELLEKQNLELGQARERLATLTAAVAELEEDLGTARRDL 270
Cdd:TIGR02169 819 QKLNRLTL----EKEYLEKEIQELQEQRIDLKE---QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 271 IKSEERSSRHQRDLREALAQKEDMEERIATLEKRYLAAQREATSIHDLNDKLENELANK---ESLHRQCEEKARHLQELL 347
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEElslEDVQAELQRVEEEIRALE 971
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1926975374 348 DV---AEQKLQQTLRR-------AETLPEVEAELAQRIAALTK 380
Cdd:TIGR02169 972 PVnmlAIQEYEEVLKRldelkekRAKLEEERKAILERIEEYEK 1014
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
320-491 |
2.05e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.69 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 320 DKLENELANKESLHRQCEEKARHLQELLDVAEQKLQQTLRRAetlpeveAELAQRIAALtkaEERHGNIEEHLRQLEGQL 399
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI-------RALEQELAAL---EAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 400 EEKNQELA-RVRQREKMNED-------HNKRLSDTVDRLlsesnERLQLHLKERMAALEEKNSLMQELESSQRQIEEQQN 471
Cdd:COG4942 100 EAQKEELAeLLRALYRLGRQpplalllSPEDFLDAVRRL-----QYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180
....*....|....*....|
gi 1926975374 472 HKGRLSEEIEKLRQEVDQLK 491
Cdd:COG4942 175 ELEALLAELEEERAALEALK 194
|
|
| SAM_superfamily |
cd09487 |
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
966-1017 |
2.47e-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: 45.69 E-value: 2.47e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1926975374 966 EWLPSLGLPQYRSHFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGI 1017
Cdd:cd09487 4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
274-491 |
2.82e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.94 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 274 EERSSRHQRDLREALAQKE---DMEERIATLEKRY--LAAQREA---------TSIHDLNDKLEN---ELANKESLHRQC 336
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNSeikDLTNQDSVKELIIknLDNTRESletqlkvlsRSINKIKQNLEQkqkELKSKEKELKKL 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 337 EEKARHLQELLDVAEQKLQQTLRRAETLpevEAELAQRIAALTKAEERHGNIEEHLR--QLEGQLEEKNQELARVRQREK 414
Cdd:TIGR04523 502 NEEKKELEEKVKDLTKKISSLKEKIEKL---ESEKKEKESKISDLEDELNKDDFELKkeNLEKEIDEKNKEIEELKQTQK 578
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1926975374 415 MNEDHNKRLSDTVDRLLSESNErlqlhLKERMAALEEK-NSLMQELESSQRQIEEQQNHKGRLSEEIEKLRQEVDQLK 491
Cdd:TIGR04523 579 SLKKKQEEKQELIDQKEKEKKD-----LIKEIEEKEKKiSSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
153-493 |
3.29e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 153 ALKSLFEHHKALDEKVRERLRAALQRVSTLEEQLAGAHQQVSALQQAAGVRDGAAEEEGSVDLGLKRLWKDdvvrleelq 232
Cdd:PTZ00121 1333 AAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEED--------- 1403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 233 ellEKQNLELGQARERLATLTAAVAELEEdlgTARRDLIKSEERSSRHQRDLREALAQKEDMEEriatLEKRylaaQREA 312
Cdd:PTZ00121 1404 ---KKKADELKKAAAAKKKADEAKKKAEE---KKKADEAKKKAEEAKKADEAKKKAEEAKKAEE----AKKK----AEEA 1469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 313 TSIHDLNDKLEnELANKESLHRQCEEKARHLQELLDVAEQKLQ-QTLRRAETLPEVE----AELAQRIAALTKAEERHGn 387
Cdd:PTZ00121 1470 KKADEAKKKAE-EAKKADEAKKKAEEAKKKADEAKKAAEAKKKaDEAKKAEEAKKADeakkAEEAKKADEAKKAEEKKK- 1547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 388 iEEHLRQLEGQleEKNQELARVRQREKMNEDHNKRLsdtvdRLLSESNERLQLHLKERMAALEEKNSLMQElessQRQIE 467
Cdd:PTZ00121 1548 -ADELKKAEEL--KKAEEKKKAEEAKKAEEDKNMAL-----RKAEEAKKAEEARIEEVMKLYEEEKKMKAE----EAKKA 1615
|
330 340
....*....|....*....|....*.
gi 1926975374 468 EQQNHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
297-493 |
4.07e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 4.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 297 RIATLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLDVAEQKLQQTLRRAETLPEVEAE------ 370
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEvkelee 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 371 LAQRIAALTKAEE----RHGNIEEHLRQLEGQLEEKNQEL----ARVRQREKMNEDHNK--RLSDTVDRLLSESN--ERL 438
Cdd:PRK03918 236 LKEEIEELEKELEslegSKRKLEEKIRELEERIEELKKEIeeleEKVKELKELKEKAEEyiKLSEFYEEYLDELReiEKR 315
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1926975374 439 QLHLKERMAALEEKnslMQELESSQRQIEEqqnhkgrLSEEIEKLRQEVDQLKGR 493
Cdd:PRK03918 316 LSRLEEEINGIEER---IKELEEKEERLEE-------LKKKLKELEKRLEELEER 360
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
244-493 |
4.13e-06 |
|
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: 51.01 E-value: 4.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 244 QARERLATLTAAVAELEEDLGTARR---DLIKSEERSSRHQRDLREalaqkedmeeRIATLEKRYLAaQREA--TSIhdl 318
Cdd:pfam06160 83 KAKKALDEIEELLDDIEEDIKQILEeldELLESEEKNREEVEELKD----------KYRELRKTLLA-NRFSygPAI--- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 319 nDKLENELANKESLHRQCEE--------KARH----LQELLDVAEQKLQQT---LRRAET-LPEVEAELAQRIAALTKAE 382
Cdd:pfam06160 149 -DELEKQLAEIEEEFSQFEEltesgdylEAREvlekLEEETDALEELMEDIpplYEELKTeLPDQLEELKEGYREMEEEG 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 383 ER--HGNIEEHLRQLEGQLEE-----KNQELARVrqrEKMNEDHNKRLSDTVDRLLSESNERLQLH-----LKERMAALE 450
Cdd:pfam06160 228 YAleHLNVDKEIQQLEEQLEEnlallENLELDEA---EEALEEIEERIDQLYDLLEKEVDAKKYVEknlpeIEDYLEHAE 304
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1926975374 451 EKNS-LMQELES-SQRQI---EEQQNHKGrLSEEIEKLRQEVDQLKGR 493
Cdd:pfam06160 305 EQNKeLKEELERvQQSYTlneNELERVRG-LEKQLEELEKRYDEIVER 351
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
239-490 |
4.28e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.91 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 239 NLELGQARERLATLTAAVAELEEdlgtaRRDLIKSEERSSRHQRD------------LREALAQKEDMEERIATLEKRYL 306
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKE-----KRDELNEELKELAEKRDelnaqvkelreeAQELREKRDELNEKVKELKEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 307 AAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELldvaeQKLQQTlrrAETLPEVEAELAQRIAALTK-AEERh 385
Cdd:COG1340 82 ELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERL-----EWRQQT---EVLSPEEEKELVEKIKELEKeLEKA- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 386 gnieEHLRQLEGQLEEKNQELARVRqrEKMNEDHNKrlsdtvdrlLSESNERLQLHLKERMAALEEKNSLMQELESSQRQ 465
Cdd:COG1340 153 ----KKALEKNEKLKELRAELKELR--KEAEEIHKK---------IKELAEEAQELHEEMIELYKEADELRKEADELHKE 217
|
250 260
....*....|....*....|....*
gi 1926975374 466 IEEQQNHKGRLSEEIEKLRQEVDQL 490
Cdd:COG1340 218 IVEAQEKADELHEEIIELQKELREL 242
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
166-497 |
5.14e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.11 E-value: 5.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 166 EKVRERLRAALQRVSTLEEQLAGAHQQVSALQQAAGVRDGA--AEEEGSVDLGLKRLWKDDVVRLEELQELLEKQNLE-L 242
Cdd:COG3096 378 AEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAvqALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEeV 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 243 GQARERLATLTAAVAELEEDLGTARRdlIKSE-ERSSRHQRdLREALAQKEdmeeriatlEKRYLAAQREAtsihdlndk 321
Cdd:COG3096 458 LELEQKLSVADAARRQFEKAYELVCK--IAGEvERSQAWQT-ARELLRRYR---------SQQALAQRLQQ--------- 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 322 LENELANKESLHRQCEEKARHLQELldvaEQKLQQTLRRAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEE 401
Cdd:COG3096 517 LRAQLAELEQRLRQQQNAERLLEEF----CQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRA 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 402 KNQELarvRQREKMNEDHNKRLsdtvdrllsesnERLQLHLKERMAALEEKNSLMQELESSQRQIEEQQNHkgrLSEEIE 481
Cdd:COG3096 593 RIKEL---AARAPAWLAAQDAL------------ERLREQSGEALADSQEVTAAMQQLLEREREATVERDE---LAARKQ 654
|
330
....*....|....*.
gi 1926975374 482 KLRQEVDQLKGRGGPF 497
Cdd:COG3096 655 ALESQIERLSQPGGAE 670
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
253-491 |
5.30e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.94 E-value: 5.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 253 TAAVAELEEDLGTARR---DLIKS----EERSSRHQRDLREALAQKEDMEER-------IATLEKRYLAAQREATSIHDL 318
Cdd:pfam01576 355 TQALEELTEQLEQAKRnkaNLEKAkqalESENAELQAELRTLQQAKQDSEHKrkklegqLQELQARLSESERQRAELAEK 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 319 NDKLENELANKESLHRQCEEKARHLQELLDVAEQKLQ--QTLRRAETLPEVEaeLAQRIAALtkaeerhgniEEHLRQLE 396
Cdd:pfam01576 435 LSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQdtQELLQEETRQKLN--LSTRLRQL----------EDERNSLQ 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 397 GQLEEknQELARvRQREKMNEDHNKRLSDTvDRLLSESNERLQLHLKERMAALEEKNSLMQELESSQRQIEEQQNHKGRL 476
Cdd:pfam01576 503 EQLEE--EEEAK-RNVERQLSTLQAQLSDM-KKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRL 578
|
250
....*....|....*
gi 1926975374 477 SEEIEKLRQEVDQLK 491
Cdd:pfam01576 579 QQELDDLLVDLDHQR 593
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
20-334 |
6.49e-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: 50.83 E-value: 6.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 20 ADTDANFEQLMVNmLDEREKLLESL----------RESQETLVATQ-----GRLQDALHERDQLQRHLNsALPQEFATLT 84
Cdd:TIGR02168 182 ERTRENLDRLEDI-LNELERQLKSLerqaekaeryKELKAELRELElallvLRLEELREELEELQEELK-EAEEELEELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 85 RELSLCREQLLEREEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKAL 164
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 165 DEK------VRERLRAALQRVSTLEEQLAGAHQQVSALQQAAG-VRDGAAEEEGSVDLGLKRLwkdDVVRLEELQELLEK 237
Cdd:TIGR02168 340 AELeekleeLKEELESLEAELEELEAELEELESRLEELEEQLEtLRSKVAQLELQIASLNNEI---ERLEARLERLEDRR 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 238 QNLELGQARERLATLTAAVAELEEDLGTARRDLIKSEERSSRHQRDLREAlaqkedmEERIATLEKRYLAAQREATSIHD 317
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEEL-------REELEEAEQALDAAERELAQLQA 489
|
330
....*....|....*..
gi 1926975374 318 LNDKLENELANKESLHR 334
Cdd:TIGR02168 490 RLDSLERLQENLEGFSE 506
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
193-527 |
6.89e-06 |
|
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: 50.53 E-value: 6.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 193 VSALQQAAGVRDGAAEEEGSVDLGLKRLwKDDVVRLEELQELLEKQNLELGQARERLATLTAAVAE--LEEDLGTARRDL 270
Cdd:pfam09731 124 QEKEKALEEVLKEAISKAESATAVAKEA-KDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAeaLAEKLKEVINLA 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 271 IKSEERSSRHQRDlrEALAQKEDMEERIATLEKRYLAAQREATSIHDLNDKLEN-------ELANK------ESLHRQCE 337
Cdd:pfam09731 203 KQSEEEAAPPLLD--AAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASerivfqqELVSIfpdiipVLKEDNLL 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 338 EKAR------HLQELLDVAEQKLQQTLRRAETlpEVEAELAQRIAALTKAEER-HGNIEEHLRQLEGQLEEKNQElARVR 410
Cdd:pfam09731 281 SNDDlnsliaHAHREIDQLSKKLAELKKREEK--HIERALEKQKEELDKLAEElSARLEEVRAADEAQLRLEFER-EREE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 411 QREKM-----------NEDHNKRLSDTVDRLLSESNERLQLHLKERMAalEEKNSL---MQELESSQRQIEEQQnhKGRL 476
Cdd:pfam09731 358 IRESYeeklrtelerqAEAHEEHLKDVLVEQEIELQREFLQDIKEKVE--EERAGRllkLNELLANLKGLEKAT--SSHS 433
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1926975374 477 SEEIEKLRqeVDQLkgrggpfvdgvhlrshTGSAVDLRFSLSTAAPGLRRR 527
Cdd:pfam09731 434 EVEDENRK--AQQL----------------WLAVEALRSTLEDGSADSRPR 466
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
320-463 |
7.05e-06 |
|
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: 48.52 E-value: 7.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 320 DKLENELANKESLHRQCEEKARHLQELLDVAEQKLQQTLRRAEtlPEVEAELAQRIAALTKAEERHG-----------NI 388
Cdd:pfam04012 39 VKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGN--EELAREALAEKKSLEKQAEALEtqlaqqrsaveQL 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1926975374 389 EEHLRQLEGQLEEKNQELARVRQREKMNEdHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNSLMQELESSQ 463
Cdd:pfam04012 117 RKQLAALETKIQQLKAKKNLLKARLKAAK-AQEAVQTSLGSLSTSSATDSFERIEEKIEEREARADAAAELASAV 190
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
283-493 |
7.68e-06 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 50.07 E-value: 7.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 283 DLREALAQKEDMEERIATLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLDVAEQkLQQTLRRAE 362
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQ-LQEENFRLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 363 T----------LPEVE-AELAQRIAALTKAeerhgniEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVD--- 428
Cdd:pfam05622 80 TarddyrikceELEKEvLELQHRNEELTSL-------AEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLGDlrr 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1926975374 429 --RLLSESNerlqLHLKERMAALEEK----NSLMQELESSQRQIEEQQnhkGRLSEEI---EKLRQEVDQLKGR 493
Cdd:pfam05622 153 qvKLLEERN----AEYMQRTLQLEEElkkaNALRGQLETYKRQVQELH---GKLSEESkkaDKLEFEYKKLEEK 219
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
1044-1115 |
1.27e-05 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 44.21 E-value: 1.27e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1926975374 1044 VLVWTNEQVVRWVQSVGLRDYAGNLQESGVHGALLALDENFDHsalalALQIPTQNTQARQVMEREFSNLLA 1115
Cdd:smart00454 1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEED-----LKELGITKLGHRKKILKAIQKLKE 67
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
255-493 |
1.61e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 49.06 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 255 AVAELEEDLGTARRDLIKSEERSS--------RHQRDLREALAQKEDMEERI----ATLEKRY-------LAAQREATSI 315
Cdd:PRK04778 166 ALDELEKQLENLEEEFSQFVELTEsgdyvearEILDQLEEELAALEQIMEEIpellKELQTELpdqlqelKAGYRELVEE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 316 H-DL-NDKLENELANKESLHRQCEEkarHLQEL-LDVAEQKLQQTLRRAETLPEV-EAElaqrIAALTKAEERHGNIEEH 391
Cdd:PRK04778 246 GyHLdHLDIEKEIQDLKEQIDENLA---LLEELdLDEAEEKNEEIQERIDQLYDIlERE----VKARKYVEKNSDTLPDF 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 392 LRQLEGQLEEKNQELARVRQREKMNED---HNKRLSDTVDRLlsesnERLQLHLKERMAALEEKNSLMQE-LESSQRQIE 467
Cdd:PRK04778 319 LEHAKEQNKELKEEIDRVKQSYTLNESeleSVRQLEKQLESL-----EKQYDEITERIAEQEIAYSELQEeLEEILKQLE 393
|
250 260 270
....*....|....*....|....*....|...
gi 1926975374 468 EQQNHKGRLSEEIEKLRQE-------VDQLKGR 493
Cdd:PRK04778 394 EIEKEQEKLSEMLQGLRKDelearekLERYRNK 426
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
247-406 |
2.76e-05 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 46.10 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 247 ERLATLTAAVAELEEDLGTARRDLIkseERSSRHQRDLREALAQkeDMEERIATLEKrYLAAQRE--ATSIHDLNDKLEN 324
Cdd:pfam01442 4 DSLDELSTYAEELQEQLGPVAQELV---DRLEKETEALRERLQK--DLEEVRAKLEP-YLEELQAklGQNVEELRQRLEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 325 ELankESLHRQCEEKARHLQELLDVAEQKLQQTLRR---------AETLPEVEAELAQRIAAL-----TKAEERHGNIEE 390
Cdd:pfam01442 78 YT---EELRKRLNADAEELQEKLAPYGEELRERLEQnvdalrarlAPYAEELRQKLAERLEELkeslaPYAEEVQAQLSQ 154
|
170
....*....|....*.
gi 1926975374 391 HLRQLEGQLEEKNQEL 406
Cdd:pfam01442 155 RLQELREKLEPQAEDL 170
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
35-493 |
3.00e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 35 DEREKLLESLRESQETLVATQGRLQ----------DALHERDQLQRHLNS---ALPQEFATLTRELSLCREQLLEREEEI 101
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQeleekleelrLEVSELEEEIEELQKelyALANEISRLEQQKQILRERLANLERQL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 102 SELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSgVSSEVEVLKALKSLFEHHKALDEKVRERLRAALQRVST 181
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE-LEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 182 LEEQLAGAHQQVSALQQAagvRDGAAEEEGSVDLGLKRLWKDDV-VRLEELQELLEKQNLELGQARERLATLTAAVAELE 260
Cdd:TIGR02168 398 LNNEIERLEARLERLEDR---RERLQQEIEELLKKLEEAELKELqAELEELEEELEELQEELERLEEALEELREELEEAE 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 261 EDLGTARRDLIKS----------EERSSRHQRDLREALAQKEDMEERIATL------EKRY------------------- 305
Cdd:TIGR02168 475 QALDAAERELAQLqarldslerlQENLEGFSEGVKALLKNQSGLSGILGVLselisvDEGYeaaieaalggrlqavvven 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 306 LAAQREA-----------------TSIHD--LNDKLENELANKE------SLHRQCEEKARH-LQELLD---VAE----- 351
Cdd:TIGR02168 555 LNAAKKAiaflkqnelgrvtflplDSIKGteIQGNDREILKNIEgflgvaKDLVKFDPKLRKaLSYLLGgvlVVDdldna 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 352 QKLQQTLRRAETLPEVEAELAQRIAALTKAE--------ERHGNIEEH---LRQLEGQLEEKNQELARVR----QREKMN 416
Cdd:TIGR02168 635 LELAKKLRPGYRIVTLDGDLVRPGGVITGGSaktnssilERRREIEELeekIEELEEKIAELEKALAELRkeleELEEEL 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 417 EDHNKRLSDTvDRLLSESNERLQLHLKERMAALEEKNSLMQELESSQRQIEEQ-------QNHKGRLSEEIEKLRQEVDQ 489
Cdd:TIGR02168 715 EQLRKELEEL-SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELeerleeaEEELAEAEAEIEELEAQIEQ 793
|
....
gi 1926975374 490 LKGR 493
Cdd:TIGR02168 794 LKEE 797
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
40-492 |
3.04e-05 |
|
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: 48.68 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 40 LLESLRESQETLVATQGRLQDALHE----RDQLQRHLNSAlpqEFATLTRELSLCREQLLEREEEISELKAERNNTRLLL 115
Cdd:pfam12128 472 RIERAREEQEAANAEVERLQSELRQarkrRDQASEALRQA---SRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWE 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 116 EHLECLVSR---HERSLRMTVVKRQAQSPS---GVSSEVEVLKALKSLFeHHKALDE---KVRERLRAALQRVSTLEEQL 186
Cdd:pfam12128 549 QSIGKVISPellHRTDLDPEVWDGSVGGELnlyGVKLDLKRIDVPEWAA-SEEELRErldKAEEALQSAREKQAAAEEQL 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 187 AGAHQQVSALQqaAGVRDGAAEEEGSvDLGLKRLwkdDVVRLEELQELLEKQNLELGQARERLATLTAAVAELEEDLGTA 266
Cdd:pfam12128 628 VQANGELEKAS--REETFARTALKNA-RLDLRRL---FDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAW 701
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 267 RRDlIKSEERSSRHQRD--LREALAQKEDMEERI-ATLEKRYLAAQREATSIHDLNDkleNELANK-------------- 329
Cdd:pfam12128 702 LEE-QKEQKREARTEKQayWQVVEGALDAQLALLkAAIAARRSGAKAELKALETWYK---RDLASLgvdpdviaklkrei 777
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 330 ESLHRQCEEKARHLQELLD----VAEQKLQQTLRRAETLPEVEAELaqriaaltkaeerhgnieehlRQLEGQLEEKNQE 405
Cdd:pfam12128 778 RTLERKIERIAVRRQEVLRyfdwYQETWLQRRPRLATQLSNIERAI---------------------SELQQQLARLIAD 836
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 406 LARVRQREKMNEDHNKRLSDTVDRLLSESNERLqlhlkERMAALEE---KNSLMQELESSQRQIEEQQNHKGRLSEEIEK 482
Cdd:pfam12128 837 TKLRRAKLEMERKASEKQQVRLSENLRGLRCEM-----SKLATLKEdanSEQAQGSIGERLAQLEDLKLKRDYLSESVKK 911
|
490
....*....|
gi 1926975374 483 lrqEVDQLKG 492
Cdd:pfam12128 912 ---YVEHFKN 918
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
254-499 |
3.10e-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: 47.97 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 254 AAVAELEEDLGTARRDLIKSEERSSRHQRDLREALAQKEDMEERIATLEKRYLAAQREATSIHDLNDKLENELANKESLH 333
Cdd:pfam07888 129 ARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 334 RQCEEKARHLQELLDVAEQK---LQQTLRRAETLPEVeAELAQRIAALTKAEER-------HGNIEEH-----LRQLEGQ 398
Cdd:pfam07888 209 LQLQDTITTLTQKLTTAHRKeaeNEALLEELRSLQER-LNASERKVEGLGEELSsmaaqrdRTQAELHqarlqAAQLTLQ 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 399 LEEKN-----------QELARVRQREKMNEDHNKRLSDTVDRLlsesNERLQLHLKERMAAL----EEKNSLMQELESSQ 463
Cdd:pfam07888 288 LADASlalregrarwaQERETLQQSAEADKDRIEKLSAELQRL----EERLQEERMEREKLEvelgREKDCNRVQLSESR 363
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1926975374 464 RQIEEQ-------QNHKGRLSEEIEKLRQEVDQLKGRGGPFVD 499
Cdd:pfam07888 364 RELQELkaslrvaQKEKEQLQAEKQELLEYIRQLEQRLETVAD 406
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
237-486 |
3.71e-05 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 47.50 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 237 KQNLELGQARERLATltaavaELEEDLGTARRDLIKSEERSSRHQRD--LREALAQKEDMEERIATLEKRYLAAQREATS 314
Cdd:pfam15905 129 KQLLELTRVNELLKA------KFSEDGTQKKMSSLSMELMKLRNKLEakMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQ 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 315 IHDLNDKLENELAnkeslhrqcEEKArHLQELLDvaeqklqqtlrraetlpeveaelaqRIAALTKAEERHGNIEEHLRQ 394
Cdd:pfam15905 203 LEEKLVSTEKEKI---------EEKS-ETEKLLE-------------------------YITELSCVSEQVEKYKLDIAQ 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 395 LEGQLEEKNQELARVRQREKMNEDHnkrLSDTVDRLlsesNERLQLHLKERMAALEEKNSLMQELESSQRQIEEQQNHKg 474
Cdd:pfam15905 248 LEELLKEKNDEIESLKQSLEEKEQE---LSKQIKDL----NEKCKLLESEKEELLREYEEKEQTLNAELEELKEKLTLE- 319
|
250
....*....|..
gi 1926975374 475 rlSEEIEKLRQE 486
Cdd:pfam15905 320 --EQEHQKLQQK 329
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
33-490 |
3.97e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.89 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 33 MLDEREKLLESLRESQETLVATQGRLQDALherDQLQRHLNsALPQEFATLTRELSLCREQLLEREEEISELKAERNNTR 112
Cdd:pfam10174 360 FLNKKTKQLQDLTEEKSTLAGEIRDLKDML---DVKERKIN-VLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTD 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 113 LLLEHLECLVSRHERslrmtVVKRQAQSPSgvSSEVEVLKALKSLFEHHKALDEKVrerlrAALQRVSTLEEQLAGAHQQ 192
Cdd:pfam10174 436 TALTTLEEALSEKER-----IIERLKEQRE--REDRERLEELESLKKENKDLKEKV-----SALQPELTEKESSLIDLKE 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 193 VSALQQAAGVRDGAAEEEGSVDLGLKrlwKDDVVRLEELQELLekQNLELGQARErlATLTAAVAELEEDLGTARRDLIK 272
Cdd:pfam10174 504 HASSLASSGLKKDSKLKSLEIAVEQK---KEECSKLENQLKKA--HNAEEAVRTN--PEINDRIRLLEQEVARYKEESGK 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 273 SEERSSRHQRDLREALAQKEDMEERIATLEKRYLAAQREATSihdlndklenELANKEslHRQCEEKARHLQElldvaeq 352
Cdd:pfam10174 577 AQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNK----------KVANIK--HGQQEMKKKGAQL------- 637
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 353 kLQQTLRRAETLPEVEAE--LAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQ-REKMNEdhnkrlsdtvdr 429
Cdd:pfam10174 638 -LEEARRREDNLADNSQQlqLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAeRRKQLE------------ 704
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1926975374 430 llsesnERLQLHLKERMAALEEKNSLMQELESSQRQIEEQQnhkgrlsEEIEKLRQEVDQL 490
Cdd:pfam10174 705 ------EILEMKQEALLAAISEKDANIALLELSSSKKKKTQ-------EEVMALKREKDRL 752
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
241-504 |
4.76e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.12 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 241 ELGQARERLATLTAAVAELEEDLGTARRDL--IKSEERSSRhqrDLREALAQKEDMEERIATLEKRY--LAAQREATSIH 316
Cdd:TIGR00606 745 EIPELRNKLQKVNRDIQRLKNDIEEQETLLgtIMPEEESAK---VCLTDVTIMERFQMELKDVERKIaqQAAKLQGSDLD 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 317 DLNDKLENELANKESLHRQCEEKARHLQELLDvAEQKLQQTLRraETLPEVEAELAQriaaLTKAEERHGNIEEHLRQLE 396
Cdd:TIGR00606 822 RTVQQVNQEKQEKQHELDTVVSKIELNRKLIQ-DQQEQIQHLK--SKTNELKSEKLQ----IGTNLQRRQQFEEQLVELS 894
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 397 GQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLS---ESNERLQLHLKERMAALEEKNSLMQELESSQR--------- 464
Cdd:TIGR00606 895 TEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISskeTSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQdgkddylkq 974
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1926975374 465 ----------QIEEQQNHKGRLSEEIEKLRQEVDQLKGRGGPFVDGVHLR 504
Cdd:TIGR00606 975 ketelntvnaQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLR 1024
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
361-491 |
4.82e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 4.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 361 AETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQRekmnedhnkrlsdtvdrlLSESNERLQL 440
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE------------------LEELNEQLQA 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1926975374 441 HLKERMAALEEKNSLMQELESSQRQIEEQQNHKGRLSEEIEKLRQEVDQLK 491
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQ 142
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
244-488 |
5.21e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.86 E-value: 5.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 244 QARERLATLTAAVAELEEDLGTARRDLIKSEERSSRHQRDLREALAQKEDMEERIATLEKRYLAAQREATSIHDLNDKLE 323
Cdd:pfam01576 58 EAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 324 NELANKESLHRQCEEKARHLQELLDVAEQKLQQTLRRAETLPEV----EAELAQRIAALTKAEERHGNIEEHLRQLEGQL 399
Cdd:pfam01576 138 EDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLknkhEAMISDLEERLKKEEKGRQELEKAKRKLEGES 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 400 EEKNQELARVRQR----EKMNEDHNKRLSDTVDRLLSESNER--LQLHLKERMAALEEknsLMQELESSQRQIEEQQNHK 473
Cdd:pfam01576 218 TDLQEQIAELQAQiaelRAQLAKKEEELQAALARLEEETAQKnnALKKIRELEAQISE---LQEDLESERAARNKAEKQR 294
|
250
....*....|....*
gi 1926975374 474 GRLSEEIEKLRQEVD 488
Cdd:pfam01576 295 RDLGEELEALKTELE 309
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
274-488 |
5.61e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.59 E-value: 5.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 274 EERSSRHQRDLREALAQKEDMEERIATLEKRYLAAQREATSIHDLNDKLENELANKESLhrqcEEKARHLQELLDVAEQK 353
Cdd:PRK01156 189 EEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSL----EDMKNRYESEIKTAESD 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 354 LQQTLRRAETLPEVEAELAQRIAalTKAEERHGNIEEHLRqLEGQLEEKNQELARVRQREKMNEDHNKRLSD-TVDRLLS 432
Cdd:PRK01156 265 LSMELEKNNYYKELEERHMKIIN--DPVYKNRNYINDYFK-YKNDIENKKQILSNIDAEINKYHAIIKKLSVlQKDYNDY 341
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1926975374 433 ESNERLQLHLKERMAALEEK----NSLMQELESSQRQIEEQQNHKGRLSEEIEKL--RQEVD 488
Cdd:PRK01156 342 IKKKSRYDDLNNQILELEGYemdyNSYLKSIESLKKKIEEYSKNIERMSAFISEIlkIQEID 403
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
1044-1104 |
5.61e-05 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 42.26 E-value: 5.61e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1926975374 1044 VLVWTNEQVVRWVQSVGLRDYAGNLQESGVHGALLALdeNFDHSALAlalQIPTQNTQARQ 1104
Cdd:pfam07647 1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK---RLGITSVGHRR 56
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
166-415 |
7.28e-05 |
|
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: 46.60 E-value: 7.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 166 EKVRERLRAALQRVSTLEEQLAGAHQQVSALQQAAGVRDGAAEEEGSVDLGLKRLWKDDVVRLEELQELLEKQNLELGQA 245
Cdd:pfam19220 107 EELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQ 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 246 RERLATLTAAVAELEEDLGTARRDLIKSE----ERSSRHQRDLREALAQKEDMEERIATLEKRYLAAQREATSIHDLNDK 321
Cdd:pfam19220 187 AAELAELTRRLAELETQLDATRARLRALEgqlaAEQAERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAE 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 322 LENELANKESLHRQCEEKARHLQELLDVAEQKL----QQTLRRAETLPEVE---AELAQRI-----------AALTKAEE 383
Cdd:pfam19220 267 ARNQLRDRDEAIRAAERRLKEASIERDTLERRLagleADLERRTQQFQEMQrarAELEERAemltkalaakdAALERAEE 346
|
250 260 270
....*....|....*....|....*....|....*....
gi 1926975374 384 RHGNIEEHLRQLEGQ-------LEEKNQELARVRQREKM 415
Cdd:pfam19220 347 RIASLSDRIAELTKRfeveraaLEQANRRLKEELQRERA 385
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
32-489 |
8.80e-05 |
|
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: 47.02 E-value: 8.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 32 NMLDEREKLLESLRESQETLVATQGRLQDALHERDQLQRHL---NSAlpqefatlTREL-SLCREQLLEREEEISELKAE 107
Cdd:pfam05483 106 NKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLikeNNA--------TRHLcNLLKETCARSAEKTKKYEYE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 108 RNNTRL----LLEHLECLVSRHERsLRMtvvkrQAQSpsgvsSEVEVLKALKSLFEHHKALDEKVRERLRAALQRVSTLE 183
Cdd:pfam05483 178 REETRQvymdLNNNIEKMILAFEE-LRV-----QAEN-----ARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 184 EQLAGAHQQVSALQ-QAAGVRDGAAEEEGSVDLglkrlwKDDVVRLEELQELLEKQNLElgQARERLATLTAAVAELEED 262
Cdd:pfam05483 247 IQITEKENKMKDLTfLLEESRDKANQLEEKTKL------QDENLKELIEKKDHLTKELE--DIKMSLQRSMSTQKALEED 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 263 LGTARRDLIKSEERSSRHQRDLREALAQKE----DMEERIATLEKRYLAAQREATSIHDLNDKLENELANK----ESLHR 334
Cdd:pfam05483 319 LQIATKTICQLTEEKEAQMEELNKAKAAHSfvvtEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKsselEEMTK 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 335 QCEEKARHLQELLDV--AEQKLQQTLRRAETLPEVEAELAQRIAALTKAEERH-GNIEEHLRQLEGQLEEKNQELARVRQ 411
Cdd:pfam05483 399 FKNNKEVELEELKKIlaEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEiHDLEIQLTAIKTSEEHYLKEVEDLKT 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 412 REKMNEDHNKRLSDTVDRLLSESNERLQ------LHLKERMaalEEKNSLMQELESSQRQIEEQQNHKGRLSEEIEKLRQ 485
Cdd:pfam05483 479 ELEKEKLKNIELTAHCDKLLLENKELTQeasdmtLELKKHQ---EDIINCKKQEERMLKQIENLEEKEMNLRDELESVRE 555
|
....
gi 1926975374 486 EVDQ 489
Cdd:pfam05483 556 EFIQ 559
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
37-490 |
9.77e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 9.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 37 REKL--LESLRESQETLVATQGRLQDaLHERDQLQRHLNSAL----------PQEFATLTRELSLCREQLLEREEEISEL 104
Cdd:PRK04863 499 RELLrrLREQRHLAEQLQQLRMRLSE-LEQRLRQQQRAERLLaefckrlgknLDDEDELEQLQEELEARLESLSESVSEA 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 105 KAERNNTRLLLEHLECLVSRHE------RSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALdEKVRERLRAALQR 178
Cdd:PRK04863 578 RERRMALRQQLEQLQARIQRLAarapawLAAQDALARLREQSGEEFEDSQDVTEYMQQLLEREREL-TVERDELAARKQA 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 179 vstLEEQlagahqqVSALQQAAGVRD----GAAEEEGSVDLGLkrLWKD----D---------------VVRleelqell 235
Cdd:PRK04863 657 ---LDEE-------IERLSQPGGSEDprlnALAERFGGVLLSE--IYDDvsleDapyfsalygparhaiVVP-------- 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 236 ekqnlELGQARERLATL--------------------TAAVAELEEDL--GTARRDL----IKSEERSSRHQRDLR-EAL 288
Cdd:PRK04863 717 -----DLSDAAEQLAGLedcpedlyliegdpdsfddsVFSVEELEKAVvvKIADRQWrysrFPEVPLFGRAAREKRiEQL 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 289 -AQKEDMEERIATLEKRYLAAQR--EATS------------------IHDLNDK---LENELANKESLHRQCEEKARHLQ 344
Cdd:PRK04863 792 rAEREELAERYATLSFDVQKLQRlhQAFSrfigshlavafeadpeaeLRQLNRRrveLERALADHESQEQQQRSQLEQAK 871
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 345 ELLDVAEQKLQQ-TLRRAETLPEVEAELAQRIAALTKAE---ERHGNieeHLRQLEGQ---LEEKNQELARVRQREKMNE 417
Cdd:PRK04863 872 EGLSALNRLLPRlNLLADETLADRVEEIREQLDEAEEAKrfvQQHGN---ALAQLEPIvsvLQSDPEQFEQLKQDYQQAQ 948
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1926975374 418 DHNKRLSDTVdRLLSESNERlQLHLK-ERMAALEEKNSLMQE-LESSQRQIEEQQnhkgrlSEEIEKLRQEVDQL 490
Cdd:PRK04863 949 QTQRDAKQQA-FALTEVVQR-RAHFSyEDAAEMLAKNSDLNEkLRQRLEQAEQER------TRAREQLRQAQAQL 1015
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
225-491 |
9.89e-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: 46.89 E-value: 9.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 225 VVRLEELQELLEKQNLEL-------GQARERLATLTAAVAELEEDLGTARrdlikseersSRHQRDLREALAQKEDMEER 297
Cdd:pfam02463 115 NVTKKEVAELLESQGISPeaynflvQGGKIEIIAMMKPERRLEIEEEAAG----------SRLKRKKKEALKKLIEETEN 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 298 IATLEKRYLAAQREATSIhDLNDKLENELANKESLHRQCEEKARHLQELLDVAEQKLQQTLRRAETLPEVEAELAQRIAA 377
Cdd:pfam02463 185 LAELIIDLEELKLQELKL-KEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKE 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 378 LTKAEERHGNIEEHLRQLEGQLEEKNQeLARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNSLMQ 457
Cdd:pfam02463 264 EEKLAQVLKENKEEEKEKKLQEEELKL-LAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEK 342
|
250 260 270
....*....|....*....|....*....|....
gi 1926975374 458 ELESSQRQIEEQQNHKGRLSEEIEKLRQEVDQLK 491
Cdd:pfam02463 343 ELKELEIKREAEEEEEEELEKLQEKLEQLEEELL 376
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
267-491 |
1.10e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 267 RRDLIKSEERSSRHQRDLREALAQKEDMEERIATlEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARhlqel 346
Cdd:PTZ00121 1498 KADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE-EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKK----- 1571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 347 ldvAEQKLQQTLRRAETLPEVEAelaQRIAALTKAEERHGNIE-EHLRQLEgQLEEKNQELARVRQREKMNEDHNKRLSD 425
Cdd:PTZ00121 1572 ---AEEDKNMALRKAEEAKKAEE---ARIEEVMKLYEEEKKMKaEEAKKAE-EAKIKAEELKKAEEEKKKVEQLKKKEAE 1644
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1926975374 426 TVDRL--LSESNERLQLHLKERMAALEEKNSLMQEL---ESSQRQIEEQQNHKGRLSEEIEKLRQEVDQLK 491
Cdd:PTZ00121 1645 EKKKAeeLKKAEEENKIKAAEEAKKAEEDKKKAEEAkkaEEDEKKAAEALKKEAEEAKKAEELKKKEAEEK 1715
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
158-493 |
1.18e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.50 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 158 FEHHKALDEKvRERLRAALQRVSTLEEQLAGAHQQVSALQQA--AGVRDGAAEEEGSvdlglkrLWKddVVRLEELQELL 235
Cdd:TIGR00618 186 FAKKKSLHGK-AELLTLRSQLLTLCTPCMPDTYHERKQVLEKelKHLREALQQTQQS-------HAY--LTQKREAQEEQ 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 236 EKQNLELGQARERLATLTAAVAELEEdlGTARRDLIKSEERSSRHQRDLREALAQ--------KEDMEERIATLEKRYLA 307
Cdd:TIGR00618 256 LKKQQLLKQLRARIEELRAQEAVLEE--TQERINRARKAAPLAAHIKAVTQIEQQaqrihtelQSKMRSRAKLLMKRAAH 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 308 AQREATsihdlndkLENELANKESLHRQCEEKARHLQELLDVAEQKLQQTlrraeTLPEVEAELAQRIAALTKAEERHGN 387
Cdd:TIGR00618 334 VKQQSS--------IEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQH-----TLTQHIHTLQQQKTTLTQKLQSLCK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 388 IEEHLRQLEGQLEEKNQELARVRQRekmnedhnKRLSDTVDRLLSESNERLQLHLKERMAALEEKNSLMQELESSQRQIE 467
Cdd:TIGR00618 401 ELDILQREQATIDTRTSAFRDLQGQ--------LAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKERE 472
|
330 340
....*....|....*....|....*.
gi 1926975374 468 EQQNHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:TIGR00618 473 QQLQTKEQIHLQETRKKAVVLARLLE 498
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
137-490 |
1.20e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.44 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 137 QAQSPSGVSSEVEV---LKALKSLfEHHKALDEKVRERLRAALQRVSTLEEQlagaHQQVSALQQAAgvrDGAAEEEGSV 213
Cdd:PRK11281 28 RAASNGDLPTEADVqaqLDALNKQ-KLLEAEDKLVQQDLEQTLALLDKIDRQ----KEETEQLKQQL---AQAPAKLRQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 214 DLGLKRLwKDDVVRLEELQEllekQNLELGQARERLATLTAAVAELEEDLGTARRDLIKSEERSSRHQRDLREALAQKed 293
Cdd:PRK11281 100 QAELEAL-KDDNDEETRETL----STLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRL-- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 294 meERIATLEKRYLAAQReaTSIHDLNDKLENELA---NKESLHRQCEEKARHLQELL----DVAEQKLQQTLRRAETLPE 366
Cdd:PRK11281 173 --QQIRNLLKGGKVGGK--ALRPSQRVLLQAEQAllnAQNDLQRKSLEGNTQLQDLLqkqrDYLTARIQRLEHQLQLLQE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 367 V--EAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELAR--VRQREKMNE--DHNKRLSDTVDRLL-SESNerlq 439
Cdd:PRK11281 249 AinSKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLSQrlLKATEKLNTltQQNLRVKNWLDRLTqSERN---- 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1926975374 440 lhLKERMAALeeKNSLmqeLESsqRQIEEQQ-------NHKGrLSEEIEKLR-------QEVDQL 490
Cdd:PRK11281 325 --IKEQISVL--KGSL---LLS--RILYQQQqalpsadLIEG-LADRIADLRleqfeinQQRDAL 379
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
241-413 |
1.89e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 241 ELGQARERLATLTAAVAELEEDLGTARRDLIKSEERSSRHQRDLREAlaqKEDMEERIATLEKRYLAAQR---------- 310
Cdd:COG3883 31 ELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA---EAEIEERREELGERARALYRsggsvsyldv 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 311 --EATSIHDLNDKLEN----ELANKESLHRQCEEKAR--HLQELLDVAEQKLQQTLRRAET--------LPEVEAELAQR 374
Cdd:COG3883 108 llGSESFSDFLDRLSAlskiADADADLLEELKADKAEleAKKAELEAKLAELEALKAELEAakaeleaqQAEQEALLAQL 187
|
170 180 190
....*....|....*....|....*....|....*....
gi 1926975374 375 IAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQRE 413
Cdd:COG3883 188 SAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
250-493 |
1.90e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.05 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 250 ATLTAAVAELEEdlgtARRDLIKSEERSSRHQRDLREALAQKEDMEERIATLEKR--------YLAAQREATSIHDLNDK 321
Cdd:PRK01156 402 IDPDAIKKELNE----INVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcgtTLGEEKSNHIINHYNEK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 322 ---LENELANKESLHRQCEEKARHLQELLD-VAEQKLQQTLRRAETLPEVEAELAQ---RIAALTKAEERHGNIEEHLRQ 394
Cdd:PRK01156 478 ksrLEEKIREIEIEVKDIDEKIVDLKKRKEyLESEEINKSINEYNKIESARADLEDikiKINELKDKHDKYEEIKNRYKS 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 395 LE-GQLEEKNQE-LARVRQREKMNEDHNKRLSDTVDRLLSESNERLQlhlkERMAALEEKNS----LMQELESSQRQIEE 468
Cdd:PRK01156 558 LKlEDLDSKRTSwLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQ----EIEIGFPDDKSyidkSIREIENEANNLNN 633
|
250 260
....*....|....*....|....*
gi 1926975374 469 QQNHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:PRK01156 634 KYNEIQENKILIEKLRGKIDNYKKQ 658
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
292-487 |
1.93e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 44.05 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 292 EDMEERIATLEK---RYLAAQReatsihdlndKLENELANKESLHRQCEEKARhlqELLDVAEQKL-QQTLRRAETLpev 367
Cdd:COG1842 33 RDMEEDLVEARQalaQVIANQK----------RLERQLEELEAEAEKWEEKAR---LALEKGREDLaREALERKAEL--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 368 EAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEdHNKRLSDTVDRLLSESNERLQLHLKERMA 447
Cdd:COG1842 97 EAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAK-AQEKVNEALSGIDSDDATSALERMEEKIE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1926975374 448 ALEEKNSLMQEL---ESSQRQIEEQQNhKGRLSEEIEKLRQEV 487
Cdd:COG1842 176 EMEARAEAAAELaagDSLDDELAELEA-DSEVEDELAALKAKM 217
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
274-488 |
1.96e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 274 EERSSRHQRDLREALA----QKEDMEERIATLEKRyLAAQREATSIHDLNDKLENELANKESLhrqcEEKARHLQELLDV 349
Cdd:COG3206 163 EQNLELRREEARKALEfleeQLPELRKELEEAEAA-LEEFRQKNGLVDLSEEAKLLLQQLSEL----ESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 350 AEQKLQQTLRRAETLPEVEAELAQriaaltkaeerhgniEEHLRQLEGQLEEKNQELARVRQRekMNEDHN--KRLSDTV 427
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQ---------------SPVIQQLRAQLAELEAELAELSAR--YTPNHPdvIALRAQI 300
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1926975374 428 DRLLSESNERLQLHLKERMAALEEKNSLMQELESSQRQIEEQQNHKGRLSEEIEKLRQEVD 488
Cdd:COG3206 301 AALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
313-423 |
1.99e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 313 TSIHDLNDKLENELANKESLHRQCEEKARHLQELLDVAEQKLQQTLRRAETLPEVEAEL---AQRIA--ALTKAEERHGN 387
Cdd:PRK00409 509 KLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLleeAEKEAqqAIKEAKKEADE 588
|
90 100 110
....*....|....*....|....*....|....*....
gi 1926975374 388 IEEHLRQLE--GQLEEKNQELARVRQR-EKMNEDHNKRL 423
Cdd:PRK00409 589 IIKELRQLQkgGYASVKAHELIEARKRlNKANEKKEKKK 627
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
286-493 |
2.01e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.73 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 286 EALAQKEDMEERIATLEKRY----LAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLDVAEQKLQqtlrRA 361
Cdd:TIGR00618 184 MEFAKKKSLHGKAELLTLRSqlltLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLK----KQ 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 362 ETLPEVEAElaqriaaltkaeerhgniEEHLRQLEGQLEEKNQELARVRQREKMNEdHNKRLSDtVDRLLSESNERLQlh 441
Cdd:TIGR00618 260 QLLKQLRAR------------------IEELRAQEAVLEETQERINRARKAAPLAA-HIKAVTQ-IEQQAQRIHTELQ-- 317
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1926975374 442 lkERMAALEEKNSLMQELESSQRQIEEQQNHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:TIGR00618 318 --SKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSI 367
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
325-486 |
2.25e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.50 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 325 ELANKESLHRQCEEKARHLQElldvaeqklQQTLRRAETLPEVEAElaqRIAALTKAEERHGniEEHLRQLEG-QLEEKN 403
Cdd:pfam17380 294 EKMEQERLRQEKEEKAREVER---------RRKLEEAEKARQAEMD---RQAAIYAEQERMA--MERERELERiRQEERK 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 404 QELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHL----------KERMAALEEKNSLMQELESSQ---RQIEEQQ 470
Cdd:pfam17380 360 RELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELeaarkvkileEERQRKIQQQKVEMEQIRAEQeeaRQREVRR 439
|
170
....*....|....*.
gi 1926975374 471 NHKGRlSEEIEKLRQE 486
Cdd:pfam17380 440 LEEER-AREMERVRLE 454
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
237-496 |
2.53e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 237 KQNLELGQARERLATLTAAVAELEEDLGTARRDLIKSEERSSRHQRDLREALAQKEDMEERIATLEKRYLAAQREAtsih 316
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL---- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 317 dlnDKLENElankeslhrqceekarhlQELLDVAEQKLQQTLRraetlpEVEAELAQRIAALTKAEERHGNIEEHLRQLE 396
Cdd:COG4372 118 ---EELQKE------------------RQDLEQQRKQLEAQIA------ELQSEIAEREEELKELEEQLESLQEELAALE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 397 GQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNSLMQELESSQRQIEEQQNHKGRL 476
Cdd:COG4372 171 QELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEE 250
|
250 260
....*....|....*....|
gi 1926975374 477 SEEIEKLRQEVDQLKGRGGP 496
Cdd:COG4372 251 LLEEVILKEIEELELAILVE 270
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
35-491 |
2.88e-04 |
|
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: 45.55 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 35 DEREKLLESLRESQETLVATQGRLQDALHERDQLQRHLNSALpQEFATLTRELSlcreqllereeeiSELKAERNnTRLL 114
Cdd:pfam01576 653 EELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQV-EEMKTQLEELE-------------DELQATED-AKLR 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 115 LE-HLECLVSRHERSLrmtvvkrQAQSPSGVSSEVEVLKALKslfEHHKALDEKVRERLRAALQRvSTLEEQLAGAHQQV 193
Cdd:pfam01576 718 LEvNMQALKAQFERDL-------QARDEQGEEKRRQLVKQVR---ELEAELEDERKQRAQAVAAK-KKLELDLKELEAQI 786
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 194 SALQQAagvRDGAAEEEGSVDLGLKRLWKD-DVVRLEELQEllekqnleLGQARE---RLATLTAAVAELEEDLGTARRD 269
Cdd:pfam01576 787 DAANKG---REEAVKQLKKLQAQMKDLQRElEEARASRDEI--------LAQSKEsekKLKNLEAELLQLQEDLAASERA 855
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 270 LIKSEERSSRHQRDLREALAQKEDMEEriatlEKRYLAAQreatsIHDLNDKLENELANKESLhrqceekarhlqelldv 349
Cdd:pfam01576 856 RRQAQQERDELADEIASGASGKSALQD-----EKRRLEAR-----IAQLEEELEEEQSNTELL----------------- 908
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 350 aEQKLQQTLRRAETLpevEAELAqriaaltkAEERHGNIEEHLRQlegQLEEKNQEL-ARVRQREKMNEDHNKRLSDTVD 428
Cdd:pfam01576 909 -NDRLRKSTLQVEQL---TTELA--------AERSTSQKSESARQ---QLERQNKELkAKLQEMEGTVKSKFKSSIAALE 973
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1926975374 429 RLLSESNERLQLHLKERMAALEEKNSLMQELESSQRQIEEQQNHKGRLSEEIEKLRQEVDQLK 491
Cdd:pfam01576 974 AKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLK 1036
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
261-459 |
3.08e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.28 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 261 EDLGTARRDLIKSeeRSSRHQRDLREALAQKEDMEERIATLEKRylaAQREATSIHDLNDKLENELANKESLHRQCEEKA 340
Cdd:PRK01156 561 EDLDSKRTSWLNA--LAVISLIDIETNRSRSNEIKKQLNDLESR---LQEIEIGFPDDKSYIDKSIREIENEANNLNNKY 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 341 RHLQELlDVAEQKLQQTLrraETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHN 420
Cdd:PRK01156 636 NEIQEN-KILIEKLRGKI---DNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRI 711
|
170 180 190
....*....|....*....|....*....|....*....
gi 1926975374 421 KRLSDTVdrllSESNERLqlhlkERMAALEEKNSLMQEL 459
Cdd:PRK01156 712 NELSDRI----NDINETL-----ESMKKIKKAIGDLKRL 741
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
242-481 |
3.25e-04 |
|
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: 44.67 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 242 LGQARERLATLTAAVAELEEDLGTARRDLIKSEERSSRHQRDLREALAQKEDMEERIATLEKRYLAAQREATSIHDLNDK 321
Cdd:pfam19220 1 IGQRNELLRVRLGEMADRLEDLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 322 LENELANKESLHRQCEEKARHLQELLDVAEQKLQQTLRRAETLPEVEAELAQRIAALTkAEERHgnIEEHLRQLEGQLEE 401
Cdd:pfam19220 81 AEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALE-EENKA--LREEAQAAEKALQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 402 KNQELARVRQREKMNEDHNKRLSDTVDRLLSESNErlqlhLKERMAALEEK-NSLMQELESSQRQIEEQQNHKGRLSEEI 480
Cdd:pfam19220 158 AEGELATARERLALLEQENRRLQALSEEQAAELAE-----LTRRLAELETQlDATRARLRALEGQLAAEQAERERAEAQL 232
|
.
gi 1926975374 481 E 481
Cdd:pfam19220 233 E 233
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
297-491 |
3.67e-04 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 43.44 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 297 RIATLEKRYLAAQREATSIHDLNDKLENELANKESlhrqcEEKARHLQELLDVAEQKLQQ-----------------TLR 359
Cdd:pfam12795 1 KLDELEKAKLDEAAKKKLLQDLQQALSLLDKIDAS-----KQRAAAYQKALDDAPAELRElrqelaalqakaeaapkEIL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 360 RAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTvDRLLSESnerLQ 439
Cdd:pfam12795 76 ASLSLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPP-GEPLSEA---QR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1926975374 440 LHLKERMAALEEKNS-LMQELESSQRQIEEQQNHKGRLSEEIEKLRQEVDQLK 491
Cdd:pfam12795 152 WALQAELAALKAQIDmLEQELLSNNNRQDLLKARRDLLTLRIQRLEQQLQALQ 204
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
241-412 |
3.95e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 44.68 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 241 ELGQARERLATLTAAVAELEedlgtARRDLIkseerssRHQRDLREALAQKEDMEERIATlEKRYLA------------- 307
Cdd:COG0497 166 AWRALKKELEELRADEAERA-----RELDLL-------RFQLEELEAAALQPGEEEELEE-ERRRLSnaeklrealqeal 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 308 ----------------AQREATSIHDLNDKLENELANKESLHRQCEEKARHLQ----------ELLDVAEQKLQQ--TLR 359
Cdd:COG0497 233 ealsggeggaldllgqALRALERLAEYDPSLAELAERLESALIELEEAASELRryldslefdpERLEEVEERLALlrRLA 312
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1926975374 360 R-----AETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQR 412
Cdd:COG0497 313 RkygvtVEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKK 370
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
241-492 |
3.97e-04 |
|
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: 44.78 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 241 ELGQARERLATLTAAVAELeedlgtaRRDLIKSEErssrhqrDLREALAQKEDMEERIATLEKRYlaaqREATS-IHDLN 319
Cdd:pfam01576 216 ESTDLQEQIAELQAQIAEL-------RAQLAKKEE-------ELQAALARLEEETAQKNNALKKI----RELEAqISELQ 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 320 DKLENELANKESLHRQCeekaRHLQELLDVAEQKLQQTLRRAETLPEVEAELAQRIAALTKAEERHGNIEE----HLRQL 395
Cdd:pfam01576 278 EDLESERAARNKAEKQR----RDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEaqlqEMRQK 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 396 EGQ-LEEKNQELARVRqREKMNEDHNKRlsdtvdRLLSESNErLQLHLKERMAALEE----KNSLMQELESSQRQIEEQQ 470
Cdd:pfam01576 354 HTQaLEELTEQLEQAK-RNKANLEKAKQ------ALESENAE-LQAELRTLQQAKQDsehkRKKLEGQLQELQARLSESE 425
|
250 260
....*....|....*....|..
gi 1926975374 471 NHKGRLSEEIEKLRQEVDQLKG 492
Cdd:pfam01576 426 RQRAELAEKLSKLQSELESVSS 447
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
164-376 |
4.04e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 164 LDEKVRERLRAALQRVSTLEEQLAGAHQQVSALQQAagVRDgAAEEEGSVDLGLKRlwKDDVVRLEELQELLEKQNLELG 243
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAA--LEE-FRQKNGLVDLSEEA--KLLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 244 QARERLATLTA----------------AVAELEEDLGTARRDLIKSEERSSRHQRDLREALAQKEDMEERIATLEKRYLA 307
Cdd:COG3206 237 EAEARLAALRAqlgsgpdalpellqspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILA 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1926975374 308 -AQREATSIHDLNDKLENELANKESLHRQCEEKARHLQEL---LDVAEQKLQQTLRRAEtlpEVEAELAQRIA 376
Cdd:COG3206 317 sLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLereVEVARELYESLLQRLE---EARLAEALTVG 386
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
40-492 |
4.17e-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: 44.81 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 40 LLESLRESQETLVATQGRLQdALHERDQLQRHLNSALPQEFATLTRELSLCREQLLEREEEISELKAERNNT-------R 112
Cdd:pfam10174 58 LKEQYRVTQEENQHLQLTIQ-ALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQakelfllR 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 113 LLLEHLECLVSRHERSL--RMTVVKR-----QAQS-PSGVSSEVEVLKALKSLFEHHKA-----LDEKVRE--RLRAALQ 177
Cdd:pfam10174 137 KTLEEMELRIETQKQTLgaRDESIKKllemlQSKGlPKKSGEEDWERTRRIAEAEMQLGhlevlLDQKEKEniHLREELH 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 178 RvstlEEQLAGAHQQVSALQQAAGVRDgaaeeegSVDLGLKRlwkddVVRLEELQELLEKQNLELG--QARERLATLTAA 255
Cdd:pfam10174 217 R----RNQLQPDPAKTKALQTVIEMKD-------TKISSLER-----NIRDLEDEVQMLKTNGLLHteDREEEIKQMEVY 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 256 VAE---LEEDLGTARRDLIKSEERSSRHQRDLREALAQKEDMEERIATLEKRYLAAQREATSIHDLNDKLENELANKES- 331
Cdd:pfam10174 281 KSHskfMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESf 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 332 -------LHRQCEEKA------RHLQELLDVAEQKLQQTLRRAETLPEV-------EAELAQRIAALtkaEERHGNIEEH 391
Cdd:pfam10174 361 lnkktkqLQDLTEEKStlageiRDLKDMLDVKERKINVLQKKIENLQEQlrdkdkqLAGLKERVKSL---QTDSSNTDTA 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 392 LRQLEGQLEEKNQELARVRQ------REKMNE--DHNKRLSDtvdrlLSESNERLQLHLKERMAALEEknslMQELESSQ 463
Cdd:pfam10174 438 LTTLEEALSEKERIIERLKEqreredRERLEEleSLKKENKD-----LKEKVSALQPELTEKESSLID----LKEHASSL 508
|
490 500 510
....*....|....*....|....*....|
gi 1926975374 464 RQ-IEEQQNHKGRLSEEIEKLRQEVDQLKG 492
Cdd:pfam10174 509 ASsGLKKDSKLKSLEIAVEQKKEECSKLEN 538
|
|
| SAM_STIM-1,2-like |
cd09504 |
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ... |
844-902 |
4.94e-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: 40.01 E-value: 4.94e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1926975374 844 WDGPTVVSWLELWVGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNALHRLKLRL 902
Cdd:cd09504 5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
244-493 |
5.62e-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: 44.43 E-value: 5.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 244 QARER---LATLTAAVAELEEDLGTARRDLIKseerssrhqrdLREALAQKEDMEERIAtlEKRYLAAQREATSIHDLND 320
Cdd:pfam10174 409 QLRDKdkqLAGLKERVKSLQTDSSNTDTALTT-----------LEEALSEKERIIERLK--EQREREDRERLEELESLKK 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 321 KLENELANKESLHRQCEEKARHLQELLDVAEQKLQQTLRRAETLPEVEAELAQRIAALTKAEERH-----------GNIE 389
Cdd:pfam10174 476 ENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLkkahnaeeavrTNPE 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 390 --EHLRQLEGQLEEKNQELARVRQ---------REKMNEDHNKrlsdtvDRLLSESNERLQLHLKER---------MAAL 449
Cdd:pfam10174 556 inDRIRLLEQEVARYKEESGKAQAeverllgilREVENEKNDK------DKKIAELESLTLRQMKEQnkkvanikhGQQE 629
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1926975374 450 EEKNSLMQELESSQRQIEEQQNHKGRLSEEI----EKLRQEVDQLKGR 493
Cdd:pfam10174 630 MKKKGAQLLEEARRREDNLADNSQQLQLEELmgalEKTRQELDATKAR 677
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
247-410 |
6.03e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.42 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 247 ERLATLTAAVAELEEDLGTARRdlikseerssrhqrdlrealaQKEDMEERIATLEKRYLAAQREatsihdlNDKLENEL 326
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQ---------------------GNQDLQDSVANLRASLSAAEAE-------RSRLQALL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 327 ANKESLHRQCEEKARHLQELLDVAEQKLQQTLRRAETLPEVEAELAQRIAAL--------TKAEERHGNIEEHLRQLEGQ 398
Cdd:PRK09039 105 AELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALeaaldaseKRDRESQAKIADLGRRLNVA 184
|
170
....*....|..
gi 1926975374 399 LEEKNQELARVR 410
Cdd:PRK09039 185 LAQRVQELNRYR 196
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
257-490 |
6.53e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 43.37 E-value: 6.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 257 AELEEDLGTARRDLIKSEERSSRHQRDLREALAQ--KEDMEERIATLEKRYLAAQREATSIHDLNDKL-ENELANKESLH 333
Cdd:pfam13868 43 RRLDEMMEEERERALEEEEEKEEERKEERKRYRQelEEQIEEREQKRQEEYEEKLQEREQMDEIVERIqEEDQAEAEEKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 334 rqceEKARHLQEllDVAEQKLQQTLRRAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEgqlEEKNQELARVRQRE 413
Cdd:pfam13868 123 ----EKQRQLRE--EIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIE---EEKEREIARLRAQQ 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1926975374 414 KMNEDHNKRLSDTVDRLLSESNERlQLHLKERMAALEEknsLMQELESSQRQIEEQQNHKGRLSEEIEKLRQEVDQL 490
Cdd:pfam13868 194 EKAQDEKAERDELRAKLYQEEQER-KERQKEREEAEKK---ARQRQELQQAREEQIELKERRLAEEAEREEEEFERM 266
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
843-907 |
7.00e-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: 39.17 E-value: 7.00e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1926975374 843 QWDGPTVVSWLElWVGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNALHRLKLRLAIQEM 907
Cdd:pfam00536 2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
348-491 |
7.43e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 7.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 348 DVAEQKLQQTLRRAET-LPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQR-EKMNEDHNKRLSD 425
Cdd:COG3883 15 DPQIQAKQKELSELQAeLEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEiEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 426 ---------TVDRLL-SESNERL--QLHLKERMA-----ALEEKNSLMQELESSQRQIEEQQNHKGRLSEEIEKLRQEVD 488
Cdd:COG3883 95 lyrsggsvsYLDVLLgSESFSDFldRLSALSKIAdadadLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
...
gi 1926975374 489 QLK 491
Cdd:COG3883 175 AQQ 177
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
106-411 |
7.82e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.06 E-value: 7.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 106 AERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPsgvssevEVLKALKSLFehhKALDEKVRERLRAALQRVSTLEEQ 185
Cdd:pfam12128 247 QQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQ-------ETSAELNQLL---RTLDDQWKEKRDELNGELSAADAA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 186 LAGAHQQVSALQQAAGVRDGAAEEEGSVDLGLKRLWKDDVvrleelqellekQNLElgqarERLATLTAAVAELEEDLgT 265
Cdd:pfam12128 317 VAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSEL------------ENLE-----ERLKALTGKHQDVTAKY-N 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 266 ARRDLIKseERSSRHQRDLREALAQKEDMEERIATLEKRYLAAQREAtsihdLNDKLENELANKESLHRQCEEKARHLQE 345
Cdd:pfam12128 379 RRRSKIK--EQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESE-----LREQLEAGKLEFNEEEYRLKSRLGELKL 451
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1926975374 346 LLDVA----EQKLQQT-----LRRA-ETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQ 411
Cdd:pfam12128 452 RLNQAtatpELLLQLEnfderIERArEEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELEL 527
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
291-432 |
1.13e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 291 KEDMEERIATLEKRYLAAQ---REATSIHDLNDKLENELANK-ESLHrqcEEKARHLQElldvAEQKLQQTLRRA-ETLP 365
Cdd:PRK00409 515 KEKLNELIASLEELERELEqkaEEAEALLKEAEKLKEELEEKkEKLQ---EEEDKLLEE----AEKEAQQAIKEAkKEAD 587
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1926975374 366 EVEAELAQRIAALTKAEERHgNIEEHLRQLEGQLEEKNQElarvrQREKMNEDHNKRLSDTVdRLLS 432
Cdd:PRK00409 588 EIIKELRQLQKGGYASVKAH-ELIEARKRLNKANEKKEKK-----KKKQKEKQEELKVGDEV-KYLS 647
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
237-490 |
1.14e-03 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 42.74 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 237 KQNLELGQARERLATLTAAVAELE---EDLGTARRDL---IKSEERSSRHQRDLREALAQKEdmeERIATLEKRYLAAQR 310
Cdd:pfam15742 59 KIKAELKQAQQKLLDSTKMCSSLTaewKHCQQKIRELeleVLKQAQSIKSQNSLQEKLAQEK---SRVADAEEKILELQQ 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 311 EATSIHDLN---------DKLE---NELANKESLHRQCEEKARHLQELLDVAEQKLQQ---TLRRAE-----TLPEVEAE 370
Cdd:pfam15742 136 KLEHAHKVCltdtcilekKQLEeriKEASENEAKLKQQYQEEQQKRKLLDQNVNELQQqvrSLQDKEaqlemTNSQQQLR 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 371 LAQRIAALTKAEERHGNIEEHLR---QLEGQLEEKNQELARVRQRekmnedhNKRLSDTVDRLLSESNERlQLHLKERMA 447
Cdd:pfam15742 216 IQQQEAQLKQLENEKRKSDEHLKsnqELSEKLSSLQQEKEALQEE-------LQQVLKQLDVHVRKYNEK-HHHHKAKLR 287
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1926975374 448 ALeeKNSLMQELESSQRQIEEQQNHKGRLSEEIEKLRQEVDQL 490
Cdd:pfam15742 288 RA--KDRLVHEVEQRDERIKQLENEIGILQQQSEKEKAFQKQV 328
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
307-469 |
1.33e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 307 AAQREATSIhdlndKLENELANKESLHRQceeKARHLQELLDvAEQKLQQTLRRaetLPEVEAELAQRIAALTKAEERHG 386
Cdd:PRK12704 46 EAKKEAEAI-----KKEALLEAKEEIHKL---RNEFEKELRE-RRNELQKLEKR---LLQKEENLDRKLELLEKREEELE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 387 NIEEHLRQLEGQLEEKNQELarvrqrekmnedhnkrlsdtvDRLLSESNERLqlhlkERMAAL---EEKNSLMQELESSQ 463
Cdd:PRK12704 114 KKEKELEQKQQELEKKEEEL---------------------EELIEEQLQEL-----ERISGLtaeEAKEILLEKVEEEA 167
|
170
....*....|....
gi 1926975374 464 R--------QIEEQ 469
Cdd:PRK12704 168 RheaavlikEIEEE 181
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
237-383 |
1.52e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 237 KQNLELgQARERLATLTAavaELEEDLGTARRDLIKSEERssrhqrdlreaLAQKEDM-EERIATLEKRylaaQREATSI 315
Cdd:PRK12704 55 KKEALL-EAKEEIHKLRN---EFEKELRERRNELQKLEKR-----------LLQKEENlDRKLELLEKR----EEELEKK 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1926975374 316 HDLNDKLENELANKESlhrQCEEK-ARHLQELLDVAEqkLQQTLRRAETLPEVEAELAQRIAALTKAEE 383
Cdd:PRK12704 116 EKELEQKQQELEKKEE---ELEELiEEQLQELERISG--LTAEEAKEILLEKVEEEARHEAAVLIKEIE 179
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
966-1021 |
1.63e-03 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 38.02 E-value: 1.63e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1926975374 966 EWLPSLGLPQYRSHFMECLVD-ARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1021
Cdd:pfam07647 11 DWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLK-RLGITSVGHRRKILKKIQELK 66
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
350-489 |
1.91e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 350 AEQKLQQTLRRAETlpevEAELAQRIAALTKAEERHgnieEHLRQLEGQLEEKNQELARVRQREKMNEDHnkrlsdtvdr 429
Cdd:PRK12704 36 AEEEAKRILEEAKK----EAEAIKKEALLEAKEEIH----KLRNEFEKELRERRNELQKLEKRLLQKEEN---------- 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 430 llsesnerlqlhLKERMAALEEKNslmQELESSQRQIEEQQNHKGRLSEEIEKLRQEVDQ 489
Cdd:PRK12704 98 ------------LDRKLELLEKRE---EELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
260-489 |
1.97e-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: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 260 EEDLGTARRDLIKSEERSSRHQRDLRE-ALAQKEDMEERIATLEK----------------RYLAAQREATSI-HDLNDK 321
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKElEKKHQQLCEEKNALQEQlqaetelcaeaeemraRLAARKQELEEIlHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 322 LENELANKESLHRQCEEKARHLQEL---LD---VAEQKLQQTLRRAET-LPEVEAELAQRIAALTKAEERHGNIEEHLRQ 394
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLeeqLDeeeAARQKLQLEKVTTEAkIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 395 LEGQLEEknqELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLH-LKERMAAleEKNSLMQELESSQRQIEEQQNHK 473
Cdd:pfam01576 164 FTSNLAE---EEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEkAKRKLEG--ESTDLQEQIAELQAQIAELRAQL 238
|
250
....*....|....*.
gi 1926975374 474 GRLSEEIEKLRQEVDQ 489
Cdd:pfam01576 239 AKKEEELQAALARLEE 254
|
|
| PRK14160 |
PRK14160 |
heat shock protein GrpE; Provisional |
413-493 |
2.09e-03 |
|
heat shock protein GrpE; Provisional
Pssm-ID: 237629 [Multi-domain] Cd Length: 211 Bit Score: 40.89 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 413 EKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNSLMQELESSQRQIEEQQNHKGRLSEEIEKLRQEVDQLKG 492
Cdd:PRK14160 3 KECKDAKHENMEEDCCKENENKEEDKGKEEDLEFEEIEKEEIIEDSEESNEVKIEELKDENNKLKEENKKLENELEALKD 82
|
.
gi 1926975374 493 R 493
Cdd:PRK14160 83 R 83
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
388-491 |
2.14e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 388 IEEHLRQLEGQLEEKNQELARVRQREK-MNEDHNKRLSDTVDRLLSEsNERLQLHLKERMAALEEknsLMQELESSQRQI 466
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELtEEEEEIRRLEEQVERLEAE-VEELEAELEEKDERIER---LERELSEARSEE 457
|
90 100
....*....|....*....|....*
gi 1926975374 467 EEqqnhKGRLSEEIEKLRQEVDQLK 491
Cdd:COG2433 458 RR----EIRKDREISRLDREIERLE 478
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
249-483 |
2.15e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 41.24 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 249 LATLTAAVAELEEDLGTARRDLIKSEERSSRHQRDLREALAQKEDMEERIATLEKRylaAQREATSIHDLNDKLENELAN 328
Cdd:pfam06008 7 LTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKK---ATQTLAKAQQVNAESERTLGH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 329 KESLHRQCEEKARHLQELLDVAEQKLQQTLRRAETLPEVEAELAQRIAAltkaEERHGNIEEHLRQLEGQLEEKNQELAR 408
Cdd:pfam06008 84 AKELAEAIKNLIDNIKEINEKVATLGENDFALPSSDLSRMLAEAQRMLG----EIRSRDFGTQLQNAEAELKAAQDLLSR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1926975374 409 VRQREKMNEDHNKRLSDTVDRLLSESNERLQ---LHLKERMAALEEKNSLMQELESSQRQIEEQQNHKGRLSEEIEKL 483
Cdd:pfam06008 160 IQTWFQSPQEENKALANALRDSLAEYEAKLSdlrELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEET 237
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
237-491 |
2.23e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.83 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 237 KQNLELGQARERLATLTAAVAELEEDLGTARRDLIKSEERSSRHQRDLREALAQKEDMEERIATLEKRYLAAQREatsih 316
Cdd:pfam13868 89 RQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKE----- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 317 dlndKLENELANKESLHRQCEEKARHLQELLdvaeQKLQQTLRRAETLPEVEAELAQ-------RIAALTKAEERHGNIE 389
Cdd:pfam13868 164 ----KAEREEEREAEREEIEEEKEREIARLR----AQQEKAQDEKAERDELRAKLYQeeqerkeRQKEREEAEKKARQRQ 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 390 EHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNErlqlhlKERMAALEEKNSLmqelessQRQIEEQ 469
Cdd:pfam13868 236 ELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAE------KRRMKRLEHRREL-------EKQIEER 302
|
250 260
....*....|....*....|....*.
gi 1926975374 470 QNHK----GRLSEEIEKLRQEVDQLK 491
Cdd:pfam13868 303 EEQRaaerEEELEEGERLREEEAERR 328
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
34-491 |
2.32e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.63 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 34 LDEREKLLESLRESQETLVATQGRLQDALHERDQLQRHLnSALPQEFATLTRELSlcreqllereeeisELKAERNNTRL 113
Cdd:COG3096 521 LAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELL-AELEAQLEELEEQAA--------------EAVEQRSELRQ 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 114 LLEHLECLVSRHE------RSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALdEKVRERLRAALQRvstLEeqla 187
Cdd:COG3096 586 QLEQLRARIKELAarapawLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREA-TVERDELAARKQA---LE---- 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 188 gahQQVSALQQAAGVRD----GAAEEEGSVdlgLKRLWKDD--------------------VVRleelqellekqnlELG 243
Cdd:COG3096 658 ---SQIERLSQPGGAEDprllALAERLGGV---LLSEIYDDvtledapyfsalygparhaiVVP-------------DLS 718
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 244 QARERLATLT-----------------AAVAELEEdlgTARRDLIKSEERSSRHQRDLREALAQKEDMEERIATLEkryl 306
Cdd:COG3096 719 AVKEQLAGLEdcpedlyliegdpdsfdDSVFDAEE---LEDAVVVKLSDRQWRYSRFPEVPLFGRAAREKRLEELR---- 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 307 aAQREAtsIHDLNDKLENELANKESLHRQCEE-KARHLQELLDvaeqklqqtlrraetlPEVEAELAQriaaltkAEERH 385
Cdd:COG3096 792 -AERDE--LAEQYAKASFDVQKLQRLHQAFSQfVGGHLAVAFA----------------PDPEAELAA-------LRQRR 845
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 386 GNIEEHLRQLEGQLEEKNQELARVRQREkmnedhnkrlsDTVDRLLSESNERLQLHLKERMAALEEKnslMQELESSQRQ 465
Cdd:COG3096 846 SELERELAQHRAQEQQLRQQLDQLKEQL-----------QLLNKLLPQANLLADETLADRLEELREE---LDAAQEAQAF 911
|
490 500
....*....|....*....|....*....
gi 1926975374 466 IEEQQNHKGRLSEEIEKLR---QEVDQLK 491
Cdd:COG3096 912 IQQHGKALAQLEPLVAVLQsdpEQFEQLQ 940
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
320-491 |
2.59e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 320 DKLENELANKESLHRQCEEKARHLQELLDVAEQKLQQTLRRAETLpevEAELAQRIAALTKAEERhgnIEEHLRQLEgql 399
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL---QAEIDKLQAEIAEAEAE---IEERREELG--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 400 eeknqELARVRQREKMNEDH------NKRLSDTVDRL-----LSESNERLQLHLKERMAALEE-KNSLMQELESSQRQIE 467
Cdd:COG3883 90 -----ERARALYRSGGSVSYldvllgSESFSDFLDRLsalskIADADADLLEELKADKAELEAkKAELEAKLAELEALKA 164
|
170 180
....*....|....*....|....
gi 1926975374 468 EQQNHKGRLSEEIEKLRQEVDQLK 491
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLS 188
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
241-490 |
2.68e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.34 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 241 ELGQARERLATLTAAVAELEEDLGTARRDLIKSEERSSRHQRDLREALAQkEDMEERIATLEKRYLAAQRE------ATS 314
Cdd:TIGR00606 585 EINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS-QDEESDLERLKEEIEKSSKQramlagATA 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 315 IHDlnDKLENELANKESLHRQCEEKARHLQELLDVAeQKLQQTLRRAET-LPEVEAELA----QRIAALTKAEERHGNIE 389
Cdd:TIGR00606 664 VYS--QFITQLTDENQSCCPVCQRVFQTEAELQEFI-SDLQSKLRLAPDkLKSTESELKkkekRRDEMLGLAPGRQSIID 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 390 EHLRQLEgQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESN---------ERLQLHLKE---RMAAL-------- 449
Cdd:TIGR00606 741 LKEKEIP-ELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKvcltdvtimERFQMELKDverKIAQQaaklqgsd 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 450 ---------------------------------EEKNSLMQ-------ELESSQRQIEEQQNHKGRLSEEIEKLRQEVDQ 489
Cdd:TIGR00606 820 ldrtvqqvnqekqekqheldtvvskielnrkliQDQQEQIQhlksktnELKSEKLQIGTNLQRRQQFEEQLVELSTEVQS 899
|
.
gi 1926975374 490 L 490
Cdd:TIGR00606 900 L 900
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
241-355 |
3.07e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 40.78 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 241 ELGQARERLATLTAAVAELEEDL---GTARRDLIKSEERSSRHQRDLREALaqkEDMEERIATLEKRYLAAQREATSIHD 317
Cdd:pfam00261 128 DLERAEERAELAESKIVELEEELkvvGNNLKSLEASEEKASEREDKYEEQI---RFLTEKLKEAETRAEFAERSVQKLEK 204
|
90 100 110
....*....|....*....|....*....|....*...
gi 1926975374 318 LNDKLENELankeslhRQCEEKARHLQELLDVAEQKLQ 355
Cdd:pfam00261 205 EVDRLEDEL-------EAEKEKYKAISEELDQTLAELN 235
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
251-486 |
3.46e-03 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 41.16 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 251 TLTAAVAELEEDLGTARrdliksEERSS-RHQRDLREALAQ----KEDMEERIATLEKRYLAAQREATSIHDLN-DKLEN 324
Cdd:pfam04849 98 VLTERNEALEEQLGSAR------EEILQlRHELSKKDDLLQiysnDAEESETESSCSTPLRRNESFSSLHGCVQlDALQE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 325 ELANKESLHRQCEEKARHLQELLDVAEQKLQQTLRraetlpEVEAELA---QRIAALTkaEERHGNIEEHLRQLEgqleE 401
Cdd:pfam04849 172 KLRGLEEENLKLRSEASHLKTETDTYEEKEQQLMS------DCVEQLSeanQQMAELS--EELARKMEENLRQQE----E 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 402 KNQELARVRqrekmneDHNKRLsdtvdRLLSESNERLQLHLkerMAALEEKNSLMQELESSQRQIEEQQNHKGRLSEEIE 481
Cdd:pfam04849 240 ITSLLAQIV-------DLQHKC-----KELGIENEELQQHL---QASKEAQRQLTSELQELQDRYAECLGMLHEAQEELK 304
|
....*
gi 1926975374 482 KLRQE 486
Cdd:pfam04849 305 ELRKK 309
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
35-493 |
3.52e-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: 41.70 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 35 DEREKLLESLRESQETLVATQGRLQDALHERDQLQRHlNSALPQEFATLT--------------RELSLCREQLLEREEE 100
Cdd:pfam01576 622 EERDRAEAEAREKETRALSLARALEEALEAKEELERT-NKQLRAEMEDLVsskddvgknvheleRSKRALEQQVEEMKTQ 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 101 ISELKAERNNT---RLLLE-HLECLVSRHERSLrmtvvkrQAQSPSGVSSEVEVLKALKslfEHHKALDEKVRERLRAAL 176
Cdd:pfam01576 701 LEELEDELQATedaKLRLEvNMQALKAQFERDL-------QARDEQGEEKRRQLVKQVR---ELEAELEDERKQRAQAVA 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 177 QRvSTLEEQLAGAHQQVSALQQAagvRDGAAEEEGSVDLGLKRLWKD-DVVRLEELQEllekqnleLGQARE---RLATL 252
Cdd:pfam01576 771 AK-KKLELDLKELEAQIDAANKG---REEAVKQLKKLQAQMKDLQRElEEARASRDEI--------LAQSKEsekKLKNL 838
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 253 TAAVAELEEDLGTARRdliksEERSSRHQRD-LREALA-----------QKEDMEERIATLEKRYLAAQREATSIHD--- 317
Cdd:pfam01576 839 EAELLQLQEDLAASER-----ARRQAQQERDeLADEIAsgasgksalqdEKRRLEARIAQLEEELEEEQSNTELLNDrlr 913
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 318 ----LNDKLENELANKESlHRQCEEKARHLQElldvaEQKLQQTLRRAETLPEVEAELAQRIAALtkaeerhgniEEHLR 393
Cdd:pfam01576 914 kstlQVEQLTTELAAERS-TSQKSESARQQLE-----RQNKELKAKLQEMEGTVKSKFKSSIAAL----------EAKIA 977
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 394 QLEGQLEEKNQELAR----VRQREK------MNEDHNKRLSDTVDRLLSESNERLQlHLKERMAALEEKNSLMQELESS- 462
Cdd:pfam01576 978 QLEEQLEQESRERQAanklVRRTEKklkevlLQVEDERRHADQYKDQAEKGNSRMK-QLKRQLEEAEEEASRANAARRKl 1056
|
490 500 510
....*....|....*....|....*....|.
gi 1926975374 463 QRQIEEqqnhkgrLSEEIEKLRQEVDQLKGR 493
Cdd:pfam01576 1057 QRELDD-------ATESNESMNREVSTLKSK 1080
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
337-493 |
4.76e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 337 EEKARHLQELLDVAEQKLQQtLRRAETLPEVEAELAQRIAALTKAEERhgnieehLRQLEGQLEEKNQELARVRQREKMN 416
Cdd:COG3206 181 EEQLPELRKELEEAEAALEE-FRQKNGLVDLSEEAKLLLQQLSELESQ-------LAEARAELAEAEARLAALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 417 EDHNKRL--SDTVDRLLSESNErLQLHLKERMAALEEKNSLMQELESSQRQIEEQ------------QNHKGRLSEEIEK 482
Cdd:COG3206 253 PDALPELlqSPVIQQLRAQLAE-LEAELAELSARYTPNHPDVIALRAQIAALRAQlqqeaqrilaslEAELEALQAREAS 331
|
170
....*....|.
gi 1926975374 483 LRQEVDQLKGR 493
Cdd:COG3206 332 LQAQLAQLEAR 342
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
281-493 |
7.36e-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: 39.35 E-value: 7.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 281 QRDLREALAQKEDMEERIATLEkrYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLDVAEQKLQQTLrr 360
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTD--YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 361 aetlpeveAELAQRIAAL-TKAEERHGNIEEHLRQLegqleeknQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQ 439
Cdd:cd00176 82 --------EELNQRWEELrELAEERRQRLEEALDLQ--------QFFRDADDLEQWLEEKEAALASEDLGKDLESVEELL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1926975374 440 LHLKERMAALEEKNSLMQELESSQRQIEEQQNHKGR--LSEEIEKLRQEVDQLKGR 493
Cdd:cd00176 146 KKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADeeIEEKLEELNERWEELLEL 201
|
|
| PRK03992 |
PRK03992 |
proteasome-activating nucleotidase; Provisional |
444-491 |
7.46e-03 |
|
proteasome-activating nucleotidase; Provisional
Pssm-ID: 179699 [Multi-domain] Cd Length: 389 Bit Score: 40.20 E-value: 7.46e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1926975374 444 ERMAALEEKNS-LMQELESSQRQIEEQQNHKGRLSEEIEKLRQEVDQLK 491
Cdd:PRK03992 1 ERLEALEERNSeLEEQIRQLELKLRDLEAENEKLERELERLKSELEKLK 49
|
|
| Abraxas-like_domain |
cd23519 |
Abraxas-like domain of BRCA1-A complex subunit Abraxas 1, BRISC complex subunit Abraxas 2, ... |
420-491 |
7.59e-03 |
|
Abraxas-like domain of BRCA1-A complex subunit Abraxas 1, BRISC complex subunit Abraxas 2, and similar domains found in insects and plants; BRCA1-A and BRISC complex subunit BRE (also known as BRISC and BRCA1 A complex member 2; BRCC4; BRCC45) is a core component of both the BRCA1-A and BRISC complexes. BRCA1-A and BRISC are separate complexes with diverging function; they use the same core of subunits to perform very distinct biological tasks, and are found in all vertebrates. BRCA1-A complex subunit Abraxas 1, also known as ABRA1, FAM175A, and CCDC98, is involved in DNA damage response and double-strand break (DSB) repair and acts as a central scaffold protein that assembles the various components of the complex and mediates the recruitment of BRCA1. The BRCA1-A complex consists of Abraxas-1, BRCC36, BRE, MERIT40, and RAP80. The BRCA1-A complex specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesion sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at DSBs. This complex also possesses deubiquitinase (DUB) activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. BRCA1-A opposes homologous recombination (HR) by suppressing resection. It has been shown for BIR (break-induced replication), an HR-subtype that involves extensive DNA resection and mutagenic DNA synthesis, that Abraxas inhibits DNA end resection through regulating the levels of SLX4/MUS81 chromatin loading at DSBs in response to Topoisomerase I (TOP1) inhibitor-induced DNA damage. Familial mutations in the BRCA1-A proteins Abraxas-1 and RAP80 predispose carriers to early-onset breast cancer, analogous to mutations in BRCA1 and BRCA2. BRCA1-A requires the tandem ubiquitin (UIM2)- and SUMO-interacting motifs (SIM) in RAP80 and the BRCC36 DUB to function in DNA repair. BRCA1-A recruits BRCA1 by binding its BRCT domains upon phosphorylation of a motif near the C-terminus of Abraxas-1. BRCA1 binding to BRCA1-A sequesters the HR activator BRCA1 about 2-10 kb distal from DNA break sites, which is posited to limit HR. It is currently unclear how BRCA1-A is functionalized and targeted by RAP80 and Abraxas-1, and how BRCA1 is inhibited when bound to the complex. BRISC complex subunit Abraxas 2 is also known as ABRO1, FAM175B or KIAA0157. The BRISC complex consists of BRCC36, MERIT40, BRE, and Abraxas 2, and serves cellular stress response and immune signaling functions; it specifically cleaves 'Lys-63'-linked polyubiquitin, leaving the last ubiquitin chain attached to its substrates; In the BRISC complex, Abraxas 2 binds SHMT2a, a metabolic enzyme enabling cancer growth in hypoxic environments, which prevents the BRCC36 from binding and cleaving ubiquitin chains. BRCC36 is the DUB for both BRCA1-A and BRISC. BRCC36 associates with pseudo-DUB proteins (Abraxas 1 in BRCA1-A, Abraxas 2 in BRISC), which lack the essential Zn2+-coordinating residues required for DUB catalytic function. BRCC36 in BRCA1-A and BRISC is activated by assembly due to interaction between Glu30 of BRCC36 and Asn170 in Abraxas 1 and Asn164 in Abraxas 2, respectively, which structures the activation loop and positions the catalytic Glu33, For the BRISC complex it has been shown that higher-order association of BRCC36 and Abraxas2 into a dimer of heterodimers (superdimer) is required for BRCC36 DUB activity. A BRISC complex (containing of BRE/BRCC45, BRCC36, MERIT40, and Abraxas 2/KIAA0157) has been found in insects (Camponotus floridanus) and shown to efficiently degrade K63-linked chains. Homologs of genes encoding components of BRCA1-A and BRISC complexes have been found in plant genomes, including for BRE/BRCC45; plant homologs of BRCC36 have been shown to be involved in DNA repair, and BRCC36-KIAA0157 complexes have been found in Arabidopsis.
Pssm-ID: 467802 Cd Length: 257 Bit Score: 39.57 E-value: 7.59e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1926975374 420 NKRLSDTVDRLLSESNERLQLHLKERMaaleeKNSLMQELESSQRQIEEQQNHKGRLSEEIEKLRQEVDQLK 491
Cdd:cd23519 191 SSILDSYRSDFVDETGQLQQVDAIEQM-----YKSLLEKLKSLCEEVSKSEAEVGQLEKEVEQLREKVERKK 257
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
241-410 |
7.73e-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: 39.28 E-value: 7.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 241 ELGQARERLATLTAAVAELEEDLGTARRDLIKSEERSSRHQRDLREALAQKedMEERIATLEKRYLAAQREATSIHDLND 320
Cdd:pfam04012 37 ELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEELARE--ALAEKKSLEKQAEALETQLAQQRSAVE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 321 KLENELANKESLHRQCEEKARHLQELLDV--AEQKLQQTLRRAET------LPEVEAELAQRIAALTKAEERHG--NIEE 390
Cdd:pfam04012 115 QLRKQLAALETKIQQLKAKKNLLKARLKAakAQEAVQTSLGSLSTssatdsFERIEEKIEEREARADAAAELASavDLDA 194
|
170 180
....*....|....*....|
gi 1926975374 391 HLRQLEGQLEEKNQELARVR 410
Cdd:pfam04012 195 KLEQAGIQMEVSEDVLARLK 214
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
241-493 |
8.31e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.42 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 241 ELGQARerlATLTAAVAELEEDLGTARR---DLIKSEERSSRHQRDLREALAQKEDMEERIATLEKRYLAAqREATSIHD 317
Cdd:PRK10929 31 ELEQAK---AAKTPAQAEIVEALQSALNwleERKGSLERAKQYQQVIDNFPKLSAELRQQLNNERDEPRSV-PPNMSTDA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 318 LNDKL---ENELANKESLHRQCEEKARHLQELLDVAEQK-------LQQTLRRAETLPEVEAELAQRIAALTKAEE--RH 385
Cdd:PRK10929 107 LEQEIlqvSSQLLEKSRQAQQEQDRAREISDSLSQLPQQqtearrqLNEIERRLQTLGTPNTPLAQAQLTALQAESaaLK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 386 GNIEEhlrqLE-GQLEEKN-QELARVRQrekmnEDHNKRlSDTVDRLLSESNERLQ-LHLKERMAALEEKNSLMQELESS 462
Cdd:PRK10929 187 ALVDE----LElAQLSANNrQELARLRS-----ELAKKR-SQQLDAYLQALRNQLNsQRQREAERALESTELLAEQSGDL 256
|
250 260 270
....*....|....*....|....*....|.
gi 1926975374 463 QRQIEEQQNHKGRLSEEIEKLRQEVDQLKGR 493
Cdd:PRK10929 257 PKSIVAQFKINRELSQALNQQAQRMDLIASQ 287
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
302-493 |
8.71e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 8.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 302 EKRYLAAQREATSIHDLNDKLENELANKESLHRQ-CEEK---ARHLQ---ELLDVAEQKLQQTLRRAETLPEVEAELAQR 374
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQlCEEKnalQEQLQaetELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 375 iaaLTKAEER-------HGNIEEHLRQLEGQLEEknQELARVR-QREKMNEDHN-KRLSDTVdRLLSESNERLQLH---L 442
Cdd:pfam01576 84 ---LEEEEERsqqlqneKKKMQQHIQDLEEQLDE--EEAARQKlQLEKVTTEAKiKKLEEDI-LLLEDQNSKLSKErklL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1926975374 443 KERMAAL-------EEKNSLMQELESSQRQIeeQQNHKGRLSEEiEKLRQEVDQLKGR 493
Cdd:pfam01576 158 EERISEFtsnlaeeEEKAKSLSKLKNKHEAM--ISDLEERLKKE-EKGRQELEKAKRK 212
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
387-622 |
8.76e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 387 NIEEHLRQLEGQLEEKNQE-----LARVRQREKMNEDHNKRLSDTVDRLlSESNERLQLHLKERMAALEEKNSLMQELES 461
Cdd:PRK02224 184 DQRGSLDQLKAQIEEKEEKdlherLNGLESELAELDEEIERYEEQREQA-RETRDEADEVLEEHEERREELETLEAEIED 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 462 SQRQIEEQQNHKGRLSEEIEKLRQEVDQLKGRGGPFVDGVHLRSHTGSAVDLRFS-LSTAAPGLRRRysLREEpakdwep 540
Cdd:PRK02224 263 LRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREeLEDRDEELRDR--LEEC------- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 541 cplpRVRAPTATSAFDSDPE-VSDVDEEgpggpadtvSPGSRSDAQTLALMLQ----------EQLDAIDEEIRMIQEEK 609
Cdd:PRK02224 334 ----RVAAQAHNEEAESLREdADDLEER---------AEELREEAAELESELEeareavedrrEEIEELEEEIEELRERF 400
|
250
....*....|...
gi 1926975374 610 ECTQLRAEELETR 622
Cdd:PRK02224 401 GDAPVDLGNAEDF 413
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
258-491 |
9.34e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 39.58 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 258 ELEEDLGTARRDLIK-SEERSSRHQRDLREALAqkEDMEERIATLEKRYLAAqreatsiHDLNDKLENELANKeslHRQC 336
Cdd:pfam02841 100 ELVELLEAKKDDFLKqNEEASSKYCSALLQDLS--EPLEEKISQGTFSKPGG-------YKLFLEERDKLEAK---YNQV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926975374 337 EEKARHlqelldvAEQKLQQTLRRAETlpeVEAELAQRIAALTKAE----ERHGNIEEHLRQLEGQLEEKNQELARVRQR 412
Cdd:pfam02841 168 PRKGVK-------AEEVLQEFLQSKEA---VEEAILQTDQALTAKEkaieAERAKAEAAEAEQELLREKQKEEEQMMEAQ 237
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1926975374 413 EKMNEDHNKRLsdtVDRLlsESNERLQLHLKERMAALEEKNSLMQELESSQrqieeqqnhkgrlsEEIEKLRQEVDQLK 491
Cdd:pfam02841 238 ERSYQEHVKQL---IEKM--EAEREQLLAEQERMLEHKLQEQEELLKEGFK--------------TEAESLQKEIQDLK 297
|
|
| |
